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ATP + catenated DNA
ADP + phosphate + decatenated DNA
-
-
-
-
?
ATP + catenated kinetoplast DNA
ADP + phosphate + decatenated kinetoplast DNA
ATP + decatenated DNA
ADP + phosphate + catenated DNA
ATP + H2O
ADP + phosphate
ATP + kinetoplast DNA
?
-
-
-
-
?
ATP + knotted supercoiled DNA
ADP + phosphate + unknotted relaxed DNA
-
-
-
-
?
ATP + negatively supercoiled pBR322 DNA
ADP + phosphate + relaxed pBR322 DNA
-
-
-
-
?
ATP + negatively supercoiled pER8:hemagglutinin plasmid DNA
ADP + phosphate + relaxed pER8:hemagglutinin plasmid DNA
ATP + negatively supercoiled pUC19 DNA
ADP + phosphate + relaxed pUC19 DNA
-
-
-
?
ATP + relaxed pBR322 DNA
ADP + phosphate + supercoiled pBR322 DNA
ATP + relaxed pUC18 DNA
ADP + phosphate + supercoiled pUC18 DNA
-
enzyme that binds and hydrolyzes only one ATP undergoes nucleotide-induced N-gate closure and supercoils DNA
-
-
?
ATP + supercoiled pBR322 DNA
ADP + phosphate + relaxed pBR322 DNA
ATP + supercoiled pBR322 plasmid DNA
ADP + phosphate + relaxed pBR322 plasmid DNA
-
-
-
?
ATP + supercoiled plasmid pNO1
ADP + phosphate + relaxed plasmid pNO1
-
-
-
-
?
ATP + supercoiled pUC18 DNA
ADP + phosphate + relaxed pUC18 DNA
-
-
-
-
?
ATP + supercoiled pUC18 plasmid
ADP + phosphate + relaxed pUC18 plasmid
-
-
-
-
?
ATP + supercoiled pUC19 DNA
ADP + phosphate + nicked pUC19 DNA
ATP + supercoiled pUC19 DNA
ADP + phosphate + relaxed pUC19 DNA
catenated DNA + ATP + H2O
minicircular DNA + ADP + phosphate
decatenation
-
-
?
catenated kDNA + ATP + H2O
decatenated kDNA + ADP + phosphate
catenated kDNA + ATP + H2O
unlinked monomer kDNA + ADP + phosphate
-
-
-
?
closed circular DNA + ATP
positively supercoiled DNA + ADP + phosphate
CVM-1 viral DNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of CVM-1 viral DNA, viral DNA contains 10% N6-methyladenine and 42% 5-methylcytosine, 4fold decreased activity compared to unmodified DNA
-
-
?
dATP + negatively supercoiled circular DNA
dADP + phosphate + relaxed circular DNA
DNA
?
-
the enzyme is capable of introducing positive supercoils into closed-circular DNA. It catalyzes positive supercoiling both in negatively supercoiled DNA and in relaxed DNA. The reactions require the presence of ATP
-
-
?
DNA
positively supercoiled DNA
positively supercoils DNA, the enzyme requires ATP, which is bound and hydrolysed by a helicase-like domain
-
-
?
DNA + ATP + H2O
DNA + ADP + phosphate
double-stranded DNA + ATP + H2O
?
double-stranded M13 DNA + ATP + H2O
?
breakage, passage, and rejoining of double-stranded M13 DNA, including ATPase activity
-
-
?
form I DNA + ATP + H2O
form IV DNA + ADP + phosphate
-
-
-
?
four-way junction DNA + ATP + H2O
?
-
binds and cleaves four-way junction DNA in vitro, topoisomerase IIbeta has a 4fold higher affinity for the four-way junction than for the linear duplex, the enzyme binds to the centre of the duplex, the four-way junction contains the sequence of a 40 bp linear duplex (containing a single topoisomerase cleavage site) along to adjacent arms, with the cleavage site straddling the point of strand exchange, the remaining two arms are comprised of sequences which do not contain topoisomerase cleavage sites, except that a potential m-AMSA-inducible cleavage site is introduced across the junction of these two arms
-
?
kDNA + ATP + H2O
?
-
decatenation
-
?
kinetoplast DNA + ATP
?
-
decatenation
-
?
kinetoplast DNA + ATP + H2O
?
linear DNA fragments of viral SSV1 DNA + ATP + H2O
?
negatively supercoiled DNA
positively supercoiled DNA
the enzyme catalyzes a ATP-dependent DNA-positive supercoiling reaction of closed DNA plasmids. ATP is required for a correct coordination of DNA cleavage. The enzyme is able to induce positive supercoiling with ATP concentrations of 0.0001 mM. The efficiency of the reaction increases with increasing nucleotide concentrations, with an optimum between 0.1 and 1.0 mM. In the absence of ATP, the enzyme shows weak type I topoisomerase-like DNA relaxation activity. At all temperatures, relaxed and/or positive topoisomers are produced when a certain amount of the negative substrate is still present, thus suggesting that the enzyme is highly processive, i.e. it performs multiple supercoiling cycles before detaching from DNA and attacking a new substrate molecule. In the absence of ATP the enzyme shows weak type I topoisomerase-like DNA relaxation activity
-
-
?
negatively supercoiled DNA + ATP + H2O
?
negatively supercoiled DNA + ATP + H2O
highly positively supercolied DNA + ADP + phosphate
-
activity of TopR2 of is strictly dependent on the presence of ATP. The enzyme exhibits an high intrinsic processivity. It is able to introduce a very high number of positive superturns in DNA
-
-
?
negatively supercoiled DNA + ATP + H2O
positively supercoil DNA + ADP + phosphate
negatively supercoiled DNA + ATP + H2O
positively supercoiled DNA + ADP + phosphate
negatively supercoiled pBR322 DNA
?
negatively supercoiled pBR322 DNA + ATP + H2O
?
negatively supercoiled pHOTI plasmid DNA + ATP + H2O
?
-
-
-
?
negatively supercoiled plasmid DNA + ATP + H2O
negatively supercoiled plasmid DNA + ADP + phosphate
-
the full-length recombinant enzyme sustains ATP-dependent positive supercoiling. The C-terminal half of Sulfolobus reverse gyrase, expressed in Escherichia coli, exhibits a topoisomerase I activity, independent of the presence of ATP and specific of negative supercoils.The N-terminal domain does not directly unwind DNA but acts more likely by driving ATP-dependent conformational changes within the whole enzyme, reminiscent of a protein motor
-
-
?
negatively supercoiled plasmid pBR322 DNA + ATP + H2O
relaxed plasmid pBR322 DNA + ADP + phosphate
negatively supercoiled pUC18 plasmid DNA + ATP + H2O
relaxed pUC18 plasmid DNA + ADP + phosphate
-
-
-
?
network of DNA rings + ATP + H2O
monomer DNA circles + ADP + phosphate
-
-
-
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
PBCV-1 viral DNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of PBCV-1 viral DNA, viral DNA contains N6-methyladenine and 5-methylcytosine, decreased activity compared to unmodified DNA
-
-
?
plasmid DNA + ATP + H2O
?
-
cleavage of plasmid DNA
-
-
?
plasmid DNA pRYG + ATP + H2O
?
-
cleavage of plasmid DNA pRYG
-
-
?
positively supercoiled plasmid pBR322 DNA + ATP + H2O
relaxed plasmid pBR322 DNA + ADP + phosphate
relaxed DNA + ATP + H2O
positively supercoiled DNA + ADP + phosphate
relaxed pBR322 plasmid + ATP + H2O
supercoiled pBR322 plasmid + ADP + phosphate
supercoiling
-
-
?
supercoiled DNA + ATP
relaxed DNA + ADP + phosphate
-
-
-
?
supercoiled DNA + ATP + H2O
?
substrate is supercoiled scpBR322 plasmid DNA. Topo2a creates transient breaks in supercoiled DNA in an ATP-dependent manner resulting in DNA relaxation
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
supercoiled dsDNA
?
-
relaxation of supercoiled dsDNA, reaction mechanism
-
-
?
supercoiled pBR 322 plasmid DNA + ATP + H2O
relaxed pBR 322 plasmid DNA + ADP + phosphate
-
-
-
-
?
supercoiled pBR322 + ATP
?
-
relaxation
-
?
supercoiled pBR322 DNA
?
-
cleavage of supercoiled pBR322 DNA
-
-
?
supercoiled pBR322 DNA + ATP
?
-
relaxation
-
?
supercoiled pBR322 DNA + ATP + H2O
relaxed pBR322 DNA + ADP + phosphate
-
-
-
?
supercoiled pBR322 plasmid + ATP + H2O
relaxed pBR322 plasmid + ADP + phosphate
relaxation
-
-
?
supercoiled pBR322 plasmid DNA + ATP + H2O
relaxed pBR322 plasmid DNA + ADP + phosphate
-
-
-
-
ir
supercoiled pKMp27 DNA + ATP + H2O
?
-
relaxation of supercoiled pKMp27 DNA
-
-
?
supercoiled plasmid DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
-
-
?
supercoiled plasmid pBR322 DNA + ATP
?
-
relaxation of supercoiled DNA
-
?
supercoiled pRYG DNA + ATP + H2O
?
theta-174 phage DNA + ATP + H2O
?
-
unknotting of theta-174 phage DNA
-
-
?
topoligically relaxed plasmid DNA + ATP
?
-
catenation in presence of a DNA crowding agent
-
?
additional information
?
-
ATP + catenated kinetoplast DNA
ADP + phosphate + decatenated kinetoplast DNA
-
-
-
-
?
ATP + catenated kinetoplast DNA
ADP + phosphate + decatenated kinetoplast DNA
-
-
-
?
ATP + catenated kinetoplast DNA
ADP + phosphate + decatenated kinetoplast DNA
-
-
-
-
?
ATP + catenated kinetoplast DNA
ADP + phosphate + decatenated kinetoplast DNA
-
-
-
-
?
ATP + decatenated DNA
ADP + phosphate + catenated DNA
-
-
-
-
?
ATP + decatenated DNA
ADP + phosphate + catenated DNA
-
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + H2O
ADP + phosphate
-
-
-
?
ATP + negatively supercoiled pER8:hemagglutinin plasmid DNA
ADP + phosphate + relaxed pER8:hemagglutinin plasmid DNA
-
-
-
-
?
ATP + negatively supercoiled pER8:hemagglutinin plasmid DNA
ADP + phosphate + relaxed pER8:hemagglutinin plasmid DNA
-
-
-
-
?
ATP + relaxed pBR322 DNA
ADP + phosphate + supercoiled pBR322 DNA
-
-
-
-
?
ATP + relaxed pBR322 DNA
ADP + phosphate + supercoiled pBR322 DNA
-
-
-
-
?
ATP + relaxed pBR322 DNA
ADP + phosphate + supercoiled pBR322 DNA
-
-
-
-
?
ATP + relaxed pBR322 DNA
ADP + phosphate + supercoiled pBR322 DNA
-
-
-
?
ATP + supercoiled pBR322 DNA
ADP + phosphate + relaxed pBR322 DNA
-
-
-
-
?
ATP + supercoiled pBR322 DNA
ADP + phosphate + relaxed pBR322 DNA
-
-
-
-
?
ATP + supercoiled pBR322 DNA
ADP + phosphate + relaxed pBR322 DNA
-
-
-
-
?
ATP + supercoiled pBR322 DNA
ADP + phosphate + relaxed pBR322 DNA
-
-
-
?
ATP + supercoiled pUC19 DNA
ADP + phosphate + nicked pUC19 DNA
-
-
-
-
?
ATP + supercoiled pUC19 DNA
ADP + phosphate + nicked pUC19 DNA
-
-
-
-
?
ATP + supercoiled pUC19 DNA
ADP + phosphate + relaxed pUC19 DNA
-
-
-
-
?
ATP + supercoiled pUC19 DNA
ADP + phosphate + relaxed pUC19 DNA
-
-
-
-
?
catenated kDNA + ATP + H2O
decatenated kDNA + ADP + phosphate
-
-
-
-
?
catenated kDNA + ATP + H2O
decatenated kDNA + ADP + phosphate
-
very weak decatenation activity
-
-
?
catenated kDNA + ATP + H2O
decatenated kDNA + ADP + phosphate
-
very weak decatenation activity
-
-
?
closed circular DNA + ATP
positively supercoiled DNA + ADP + phosphate
-
-
-
-
?
closed circular DNA + ATP
positively supercoiled DNA + ADP + phosphate
-
-
-
-
?
dATP + negatively supercoiled circular DNA
dADP + phosphate + relaxed circular DNA
-
-
-
-
?
dATP + negatively supercoiled circular DNA
dADP + phosphate + relaxed circular DNA
-
-
-
-
?
DNA + ATP
?
-
cleavage requires coupling to ATP hydrolysis
-
-
?
DNA + ATP
?
DNA topoisomerase VI relaxes both negatively and positively supercoiled DNA in the presence of ATP and has no DNA supercoiling activity
-
-
?
DNA + ATP
?
-
decatenation, the enzyme normally catalyzes DNA transport after it hydrolyzes one ATP and before it hydrolyzes the second
-
?
DNA + ATP + H2O
?
the enzyme helps disentangle chromosomes to facilitate cell division
-
-
?
DNA + ATP + H2O
?
the enzyme helps disentangle chromosomes to facilitate cell division. ATP binding elicits a major structural reorganization that is propagated to the DNA-cleavage center of the enzyme, explaining how ATP is coupled to DNA capture and strand scission
-
-
?
DNA + ATP + H2O
?
the enzyme helps disentangle chromosomes to facilitate cell division
-
-
?
DNA + ATP + H2O
?
the enzyme helps disentangle chromosomes to facilitate cell division. ATP binding elicits a major structural reorganization that is propagated to the DNA-cleavage center of the enzyme, explaining how ATP is coupled to DNA capture and strand scission
-
-
?
DNA + ATP + H2O
?
the enzyme helps disentangle chromosomes to facilitate cell division
-
-
?
DNA + ATP + H2O
?
-
the enzyme catalyzes an ATP-dependent positive DNA supercoiling reaction in vitro
-
-
?
DNA + ATP + H2O
?
the enzyme helps disentangle chromosomes to facilitate cell division. ATP binding elicits a major structural reorganization that is propagated to the DNA-cleavage center of the enzyme, explaining how ATP is coupled to DNA capture and strand scission
-
-
?
DNA + ATP + H2O
?
-
the enzyme catalyzes an ATP-dependent positive DNA supercoiling reaction in vitro
-
-
?
DNA + ATP + H2O
?
-
reverse gyrase is a DNA topoisomerase endowed with ATP-dependent positive supercoiling activity. It is typical of microorganisms living at high temperature and might play a role in maintenance of genome stability and repair
-
-
?
DNA + ATP + H2O
?
-
reverse gyrase is a DNA topoisomerase endowed with ATP-dependent positive supercoiling activity
-
-
?
DNA + ATP + H2O
?
-
binding of the enzyme on double-stranded DNA alters the DNA structure in two ways: (I) reduction of the linking number in a circular duplex after covalent closure by a ligase; (II) singe-stranded DNA cleavage. Positive supercoiling of DNA in the presence of ATP. Catalyzes ATP-dependent positive supercoiling and its stoichiometric binding to DNA
-
-
?
DNA + ATP + H2O
DNA + ADP + phosphate
-
-
-
-
?
DNA + ATP + H2O
DNA + ADP + phosphate
-
cleavage, relaxation, decatenation, and religation of DNA
-
-
?
DNA + ATP + H2O
DNA + ADP + phosphate
-
decatenation of DNA
-
-
?
DNA + ATP + H2O
DNA + ADP + phosphate
-
relaxation and cleavage of DNA, cleavage requires coupling to ATP hydrolysis
-
-
?
double-stranded DNA + ATP + H2O
?
-
ATP-dependent breakage, passage, and rejoining of double-stranded DNA
-
-
?
double-stranded DNA + ATP + H2O
?
the enzyme generates ATP-dependent double-strand breaks with two-nucleotide overhangs on supercoiled or linear DNA. topoVI is covalently attached to the 5'-ends of the broken DNA
-
-
?
dsDNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of dsDNA
-
-
?
dsDNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of dsDNA, enzyme is required for control of DNA topology
-
-
?
dsDNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of dsDNA, very high DNA cleavage activity and high strand passage activity of the viral type enzyme, tight DNA binding, mapping of DNA cleavage sites
-
-
?
dsDNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of dsDNA, very high DNA cleavage activity of the viral type enzyme
-
-
?
dsDNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of dsDNA
-
-
?
dsDNA + ATP + H2O
?
-
cleavage of dsDNA, religation of dsDNA, ligation by the enzyme of the two strands of a double helix in a nonconcerted fashion, ligation of a nicked oligonucleotide in which the 5'-terminal phosphate at the nick is activated by covalent attachment to 4-nitrophenol, the active site Tyr805 is not important for catalysis of ligation
-
-
?
dsDNA + ATP + H2O
?
-
decatenation of dsDNA
-
-
?
dsDNA + ATP + H2O
?
-
dsDNA relaxation, breakage, decatenation, and cleavage, isozyme IIalpha relaxes positively supercoiled DNA 10times faster than negatively supercoiled DNA, isozyme IIbeta has no preference, the enzyme creates transient single- and double-stranded breaks, site-specific cleavage of supercoiled DNA
-
-
?
dsDNA + ATP + H2O
?
-
passage of dsDNA
-
-
?
dsDNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of dsDNA
-
-
?
dsDNA + ATP + H2O
?
Paramecium bursaria chlorella virus
-
breakage, passage, decatenation, and rejoining of dsDNA, enzyme is required for conrol of DNA topology
-
-
?
dsDNA + ATP + H2O
?
Paramecium bursaria chlorella virus
-
breakage, passage, decatenation, and rejoining of dsDNA, very high DNA cleavage activity of the viral type enzyme, mapping of DNA cleavage sites
-
-
?
dsDNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of dsDNA
-
-
?
dsDNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of dsDNA, very high DNA cleavage activity of the viral type enzyme
-
-
?
dsDNA + ATP + H2O
?
Tequatrovirus T4
-
cleavage and religation of dsDNA
-
-
?
kinetoplast DNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of kinetoplast DNA, kinetoplast DNA is isolated from Crithidia fasciculata
-
-
?
kinetoplast DNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of kinetoplast DNA, kinetoplast DNA isolated from Crithidia fasciculata, recombinant wild-type and truncation mutant Top2alphaDELTA1175, mechanisms
-
-
?
kinetoplast DNA + ATP + H2O
?
-
decatenation of kinetoplast DNA
-
-
?
kinetoplast DNA + ATP + H2O
?
-
cleavage of kinetoplast DNA
-
-
?
kinetoplast DNA + ATP + H2O
?
-
decatenation of kinetoplast DNA
-
-
?
linear DNA fragments of viral SSV1 DNA + ATP + H2O
?
-
ATP hydrolysis is necessary for DNA resealing
-
-
?
linear DNA fragments of viral SSV1 DNA + ATP + H2O
?
-
ATP hydrolysis is necessary for DNA resealing
-
-
?
negatively supercoiled DNA + ATP + H2O
?
-
relaxation
-
?
negatively supercoiled DNA + ATP + H2O
?
-
relaxation
-
?
negatively supercoiled DNA + ATP + H2O
?
-
ATP-dependent relaxation of negatively supercoiled DNA
-
-
?
negatively supercoiled DNA + ATP + H2O
positively supercoil DNA + ADP + phosphate
-
-
-
-
?
negatively supercoiled DNA + ATP + H2O
positively supercoil DNA + ADP + phosphate
-
TopR1 is able to positively supercoil DNA only at high temperature, and TopR2 is active at both temperatures are consistent with them having different functions within the cells
-
-
?
negatively supercoiled DNA + ATP + H2O
positively supercoil DNA + ADP + phosphate
-
-
-
-
?
negatively supercoiled DNA + ATP + H2O
positively supercoil DNA + ADP + phosphate
-
TopR1 is able to positively supercoil DNA only at high temperature, and TopR2 is active at both temperatures are consistent with them having different functions within the cells
-
-
?
negatively supercoiled DNA + ATP + H2O
positively supercoiled DNA + ADP + phosphate
-
-
-
-
?
negatively supercoiled DNA + ATP + H2O
positively supercoiled DNA + ADP + phosphate
-
the enzyme catalyzes positive supercoiling either from negatively supercoiled, or from relaxed DNA
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent activity. The same enzyme shows both relaxation of negatively supercoiled DNA and positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA
?
-
ATP-dependent positive supercoiling activity
-
-
?
negatively supercoiled pBR322 DNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of negatively supercoiled pBR322 DNA
-
-
?
negatively supercoiled pBR322 DNA + ATP + H2O
?
-
breakage, passage, decatenation, and rejoining of negatively supercoiled pBR322 DNA, recombinant wild-type and truncation mutant Top2alphaDELTA1175, mechanisms
-
-
?
negatively supercoiled pBR322 DNA + ATP + H2O
?
Paramecium bursaria chlorella virus
-
breakage, passage, and rejoining of negatively supercoiled pBR322 DNA
-
-
?
negatively supercoiled plasmid pBR322 DNA + ATP + H2O
relaxed plasmid pBR322 DNA + ADP + phosphate
-
-
-
-
?
negatively supercoiled plasmid pBR322 DNA + ATP + H2O
relaxed plasmid pBR322 DNA + ADP + phosphate
-
-
-
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation of Trypanosoma cruzi kDNA
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
enzyme is more efficient in decatenation than relaxation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
in absence of an DNA-binding protein: decatenation and unknotting of the DNA rings
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
Tequatrovirus T4
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
Tequatrovirus T4
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
Tequatrovirus T4
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation of kDNA networks
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation of kDNA networks
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
network of DNA rings + ATP + H2O
monomeric DNA circles + ADP + phosphate
-
decatenation
-
?
pBR322 DNA + ATP + H2O
?
-
decatenation, relaxation and cleavage of pBR322 DNA
-
-
?
pBR322 DNA + ATP + H2O
?
-
cleavage of pBR322 DNA
-
-
?
positively supercoiled plasmid pBR322 DNA + ATP + H2O
relaxed plasmid pBR322 DNA + ADP + phosphate
-
-
-
-
?
positively supercoiled plasmid pBR322 DNA + ATP + H2O
relaxed plasmid pBR322 DNA + ADP + phosphate
-
-
-
-
?
relaxed DNA + ATP + H2O
positively supercoiled DNA + ADP + phosphate
-
-
-
-
?
relaxed DNA + ATP + H2O
positively supercoiled DNA + ADP + phosphate
-
the enzyme catalyzes positive supercoiling either from negatively supercoiled, or from relaxed DNA
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
in presence of condensing agents like histone H1 or spermidine
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation in presence of the condensing agent histone H1
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
691220, 691245, 691488, 691495, 691529, 691571, 691609, 691777, 691780, 691826, 692160, 692729, 693362, 693540, 693548, 693676, 693921, 694810, 695190 -
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
network of DNA rings that are topologically interlocked
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
in presence of a yeast DNA-binding protein
network of DNA rings that are topologically interlocked
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
covalently closed double-stranded DNA rings
network of DNA rings that are topologically interlocked
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
Tequatrovirus T4
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
Tequatrovirus T4
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
Tequatrovirus T4
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation in absence of ATP
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
-
?
supercoiled DNA + ATP + H2O
catenated DNA networks + ADP + phosphate
-
catenation
in presence of spermine circular DNA is catenated to dimers, trimer and a network
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation in absence of ATP
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
positive supercoils are relaxed in presence of beta,gamma-imido ATP
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
dATP can substitute for ATP
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
-
-
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
ATP-dependent relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
ATP-dependent relaxation of negative and positive supercoils
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
ATP-dependent relaxation of negative and positive supercoils
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
under optimal conditions the enzyme relaxes all supercoils prior to dissociation of the enzyme from DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
under optimal conditions relaxation of negatively supercoiled DNA occurs in a highly processive manner
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
-
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
ATP-dependent relaxation of supercoiled pBR322 DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
ATP-dependent relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
ATP-dependent relaxation of negative and positive supercoils
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
DNA cleavage by topo VI generates two-nucleotide 5'-protruding ends
-
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation of negatively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
ADP is cleaved to ADP and phosphate
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
ATP-dependent relaxation of negative and positive supercoils
ADP is cleaved to ADP and phosphate
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
ADP is cleaved to ADP and phosphate
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
ATP-dependent relaxation of negative and positive supercoils
ADP is cleaved to ADP and phosphate
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
Tequatrovirus T4
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
Tequatrovirus T4
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
Tequatrovirus T4
-
relaxation
ADP is cleaved to ADP and phosphate
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
Tequatrovirus T4
-
relaxation of negatively or positively supercoiled DNA
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
Tequatrovirus T4
-
relaxation of negatively or positively supercoiled DNA
ADP is cleaved to ADP and phosphate
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
Tequatrovirus T4
-
pBR322 plasmid DNA
ADP is cleaved to ADP and phosphate
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled DNA + ATP + H2O
relaxed DNA + ADP + phosphate
-
relaxation
-
?
supercoiled pRYG DNA + ATP + H2O
?
-
cleavage of supercoiled pRYG DNA
-
-
?
supercoiled pRYG DNA + ATP + H2O
?
-
relaxation and cleavage of supercoiled pRYG DNA
-
-
?
supercoiled pRYG DNA + ATP + H2O
?
-
relaxation of supercoiled pRYG DNA
-
-
?
supercoiled pRYG DNA + ATP + H2O
?
-
relaxation of supercoiled pRYG DNA
-
-
?
additional information
?
-
-
the enzyme cannot supercoil relaxed DNA
-
-
?
additional information
?
-
-
substrate specificity
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the only topoisomerase that can introduce negative supercoils in DNA
-
-
?
additional information
?
-
-
ATP hydrolysis
-
-
?
additional information
?
-
-
in contrast to DNA gyrase, eucaryotic type II topoisomerase interacts preferentially with negatively supercoiled DNA over relaxed DNA
-
-
?
additional information
?
-
-
dATP is a poor substitute for ATP
-
-
?
additional information
?
-
-
the following reactions are catalyzed in an ATP-dependent fashion: relaxation of superhelical turns, catenation, decatenation, unknotting of circular duplex DNA
-
-
?
additional information
?
-
-
ATP-dependent generation of negative supercoils
-
-
?
additional information
?
-
-
involvement in the initiation of DNA replication
-
-
?
additional information
?
-
-
biological role of topoisomerase II and DNA gyrase
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
dATP can substitute for ATP. 8-Azidoadenosine 5'-triphosphate is used less efficiently by the enzyme than ATP
-
-
?
additional information
?
-
-
unknotts P4 DNA in an ATP-dependent manner
-
-
?
additional information
?
-
-
DNA stimulated ATPase activity
-
-
?
additional information
?
-
-
characterization of the interaction between topoisomerase II and DNA by transcription footprinting
-
-
?
additional information
?
-
-
enzyme is required for chromosome segregation
-
-
?
additional information
?
-
-
formation of a covalent enzyme-DNA complex is a prerequisite for activity, the intermediate can destabilize the genome
-
-
?
additional information
?
-
-
the enzyme binds unmodified DNA and DNA containing N6-methyladenine and 5-methylcytosine to the same extent
-
-
?
additional information
?
-
DNA topoisomerase II interacts with Lim15/Dmc1 in meiosis, the enzyme suppresses Lim15/Dmc1-dependent strand transfer activity and activates its DNA-dependent ATPase activity in vitro, overview, Lim15 inhibits the topoisomerase II activity in vivo
-
-
?
additional information
?
-
-
DNA topoisomerase II interacts with Lim15/Dmc1 in meiosis, the enzyme suppresses Lim15/Dmc1-dependent strand transfer activity and activates its DNA-dependent ATPase activity in vitro, overview, Lim15 inhibits the topoisomerase II activity in vivo
-
-
?
additional information
?
-
-
the enzyme converts kinetoplast DNA to the decatenated form. Cleavage of pBR322 DNA
-
-
?
additional information
?
-
-
localization of the enzyme within the single mitochondrion suggests an important role of the enzyme in kinetoplast DNA replication
-
-
?
additional information
?
-
-
top2a is required for decatenation but not for condensation in embryonic mitoses
-
-
?
additional information
?
-
-
top2a is required for decatenation but not for condensation in embryonic mitoses
-
-
?
additional information
?
-
-
unknotts knotted P4 DNA
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme can alter the linking number of DNA only in steps of two
-
-
?
additional information
?
-
-
the enzyme can alter the linking number of DNA only in steps of two
-
-
?
additional information
?
-
-
at high concentrations the enzyme can knot circular duplex DNA molecules
-
-
?
additional information
?
-
-
the following reactions are catalyzed in an ATP-dependent fashion: relaxation of superhelical turns, catenation, decatenation, unknotting of circular duplex DNA
-
-
?
additional information
?
-
-
the following reactions are catalyzed in an ATP-dependent fashion: relaxation of superhelical turns, catenation, decatenation, unknotting of circular duplex DNA
-
-
?
additional information
?
-
-
enzyme binds Z-DNA with an affinity 2 orders of magnitude greater than that for B-DNA
-
-
?
additional information
?
-
-
the Z-DNA binding activity of undegraded topoisomerase II may be important in targeting the enzyme both to structural motifs required for chromatin organization and to sites of local supercoiling
-
-
?
additional information
?
-
-
topoisomerase II ensures proper sister chromatid separation through a direct role in centromere resolution and prevents incorrect microtubule-kinetochore attachments by allowing proper activation of Aurora B kinase, TOPO II activity is required to establish amphitelic kinetochore attachment, TOPO II is required for centromere separation independently of the cohesin complex
-
-
?
additional information
?
-
-
Topo II and Mod(mdg4)2.2 proteins directly interact
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
ATP-dependent negative supercoiling of closed circular duplex DNA
-
-
?
additional information
?
-
-
dATP can substitute for ATP in the supercoiling reaction
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme can alter the linking number of DNA only in steps of two
-
-
?
additional information
?
-
-
in contrast to DNA gyrase, eucaryotic type II topoisomerase interacts preferentially with negatively supercoiled DNA over relaxed DNA
-
-
?
additional information
?
-
-
no formation of negative supercoils
-
-
?
additional information
?
-
-
in presence of a 50000 MW protein from the silk gland of Bombyx mori the enzyme introduces unconstrained negative supercoils into DNA
-
-
?
additional information
?
-
-
topoisomerase I works in concert with topoisomerase II to modulate the level of DNA supercoiling
-
-
?
additional information
?
-
-
controls DNA topology by cleaving and rejoining DNA strands and passing other DNA strands through transient gaps. Plays a crucial function in the regulation of the physiological function of the genome
-
-
?
additional information
?
-
-
enzyme plays a key role in DNA replication and transcription. Required for chromosome segregation during meiosis and mitosis
-
-
?
additional information
?
-
-
involvement in RNA polymerase II transcription
-
-
?
additional information
?
-
-
biological role of topoisomerase II and DNA gyrase
-
-
?
additional information
?
-
-
changes the topology of DNA by coupling binding and hydrolysis of two ATP molecules to the transport of one DNA duplex through a temporary break introduced in another
-
?
additional information
?
-
-
isoenzyme IIalpha is expressed at the highest level during rapid proliferation, isoenzyme IIbeta is expressed maximally in cells that have reached the plateau phase of growth
-
-
?
additional information
?
-
-
the enzyme is essential for DNA metabolism and chromosome dynamics. It changes the topology of DNA by coupling binding and hydrolysis of two ATP molecules to the transport of one DNA duplex through a temporary break introduced in another
-
?
additional information
?
-
-
isozyme IIbeta is no required for DNA replication
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?
additional information
?
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the amount of isozyme IIalpha in cells influences directly the cell cycle kinetics in G2 and early mitosis as well as the resistance to nocodazole
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?
additional information
?
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the enzyme is essential for controlling the conformation of both DNA and whole chromosomes, e.g. for shortening of the chromosome axes, isozyme IIbeta can partially substitute for isozyme IIalpha
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?
additional information
?
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-
the enzyme is essential for genomic integrity
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?
additional information
?
-
-
the enzyme is important in chromosome segregation
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?
additional information
?
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activity is measured using the decatenation assay with kinetoplast DNA as a substrate
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?
additional information
?
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isozyme IIalpha has the potential to alleviate torsional stress ahead of replication forks in an efficient and safe manner
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?
additional information
?
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isozyme IIalpha interacts with the microtubule-directed agent nocodazole, overview
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?
additional information
?
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the enzyme enhances the activity of psorospermin, O5-methyl-psorospermin, and gemcitabine, alkylating DNA through an epoxide-mediated electrophilic attack, at some DNA sites, overview
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-
?
additional information
?
-
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the enzyme has intrinsic ATPase activity
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?
additional information
?
-
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the enzyme performs ATP hydrolysis activity
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?
additional information
?
-
-
the enzyme reaction is modulated by the C-terminus of the enzyme, which is also responsible for sensitivity to anti-cancer drugs
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?
additional information
?
-
-
indirect involvement of topoisomerase II alpha in the formation of radiation-induced chromatid breaks from DNA double-strand breaks, topoisomerase II alpha is a possible factor in the inter-individual variation in chromatid radiosensitivity
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?
additional information
?
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RNA binding influences the catalytic function of topoisomerase IIalpha to regulate DNA topology, topoisomerase II sequentially interacts with the (G/U)-rich region and poly(A)+ tail of the transcript to regulate the template DNA topology in coordination with transcription termination and poly(A)+ RNA export
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?
additional information
?
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topoisomerase IIalpha is a multifunctional enzyme that catalyzes the relaxation of supercoiled DNA, decatenation of interlinked DNA and unknotting of intramolecularly linked DNA by passing a DNA helix through a transient double-strand break in a second helix
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?
additional information
?
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human cells can rapidly activate and deactivate DNA topoisomerase II in response to a signal molecule, the activity of DNA topoisomerase I is highly regulated in HuT 78 cells upon treatment with interleukin-2, overview
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-
?
additional information
?
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the enzyme introduces transient double strand breaks to alter DNA topology, generation of a transient double strand break, with each subunit breaking one DNA strand. The mechanism of DNA cleavage provides several distinct advantages including the protection of DNA ends and the ability to quickly and efficiently religate the DNA strand break. The positively supercoiled DNA at the replication fork can isomerize by migration of the positive supercoiling into wrapping of the two replicated strands. This structure called a precatenane, is a substrate for Top2 mediated DNA catenation, and may represent a plausible mechanism for Top2 action during replication elongation
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-
?
additional information
?
-
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catalytic cycle of topoisomerase II, overview
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-
?
additional information
?
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decatenation assay with substrate kinetoplast DNA from protozoa Crithidia fasciculata, and DNA relaxation assay using pRYG plasmid DNA as substrate
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-
?
additional information
?
-
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DNA cleavage, aperture, closure and religation are critical steps in the topo II reaction cycle, topo II DNA gate dynamics, single-molecule FRET experiments, role of T-segment in gate opening, overview
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-
?
additional information
?
-
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DNA intercalating, relaxation, and decantenation of supercoiled pBR322 DNA
-
-
?
additional information
?
-
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reaction mechanism, DNA cleavage by Top2 uses a tyrosine that is activated to attack the phosphodiester backbone of DNA and form a phosphotyrosine linkage. Topological changes in DNA require the introduction of DNA strand breaks, and topoisomerases provide a safe mechanism for introducing these changes, overview
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?
additional information
?
-
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structure-activity relationship study, overview
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?
additional information
?
-
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structure-activity relationship, structure modelling and modelling of ligand docking in the ATP binding pocket, binding mechanism, overview
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-
?
additional information
?
-
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substrate is kinetoplast DNA for decantenation by TOPOIIalpha
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-
?
additional information
?
-
-
substrate is pBR322 supercoiled DNA
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?
additional information
?
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substrate is supercoiled pBR322 DNA
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-
?
additional information
?
-
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topoisomerase II modulates DNA topology by generating double-stranded breaks in DNA. The presence of a nick at one scissile bond dramatically increases the rate of cleavage by human topoisomerase IIalpha at the scissile bond on the opposite strand, mechanism, overview
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-
?
additional information
?
-
-
the C-terminal domain of topoisomerase IIbeta but not topoisomerase IIalpha affects the binding of the enzyme to the DNA. It alters the enzyme's KD for DNA binding. Differential modes of action of the two isoforms in vivo, overview
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-
?
additional information
?
-
-
cleavage of negatively supercoiled pBR322 plasmid DNA and of pRYG supercoiled DNA by topoisomerase IIalpha
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-
?
additional information
?
-
-
cleavage of negatively supercoiled pBR322 plasmid DNA by topoisomerase IIalpha
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-
?
additional information
?
-
-
cleavage of negatively supercoiled pBR322 plasmid DNA by topoisomerase IIalpha
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-
?
additional information
?
-
kinetoplast DNA is used as a substrate in a decatenation assay
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-
?
additional information
?
-
-
kinetoplast DNA is used as a substrate in a decatenation assay
-
-
?
additional information
?
-
-
substrate for DNA topo IIalpha is supercoiled pBR322 plasmid DNA
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-
?
additional information
?
-
-
substrate for DNA topo IIalpha is supercoiled pBR322 plasmid DNA
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-
?
additional information
?
-
-
substrate for topo IIalpha is supercoiled pBR322 plasmid DNA. Topo II-mediated DNA strand passage requires ATP binding, so reactions in the absence of ATP represent the cleavage and relegation events that take place prior to topo II catalyzed DNA strand passage
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-
?
additional information
?
-
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substrate for topo IIbeta is kinetoplast DNA. Topoisomerase II catalyzes topological changes in DNA and decatenation reaction. Residue Tyr656 of topoisomerase IIbeta is important for its catalytic activity, overview
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-
?
additional information
?
-
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substrate is negatively supercoiled pBR322 plasmid DNA
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?
additional information
?
-
-
substrate is plasmid DNA
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?
additional information
?
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substrate is supercoiled plasmid DNA
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?
additional information
?
-
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the enzyme contains an active site tyrosine within the winged helix domain, role of the C-terminal domain in the topoisomerase II-DNA interaction, overview
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-
?
additional information
?
-
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transport of the T-segment through the transiently cleaved G-DNA segment and the opened C-gate is via a free diffusion mechanism, opening and closing dynamics of the C-gate, two-gate model for chemomechanical coupling of topoisomerase II, detailed overview
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-
?
additional information
?
-
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decatenation assay with kinetoplast DNA, DNA strand break analysis using supercoiled plasmid DNA pBR322 or pRYG
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-
?
additional information
?
-
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DNA strand breakage formation in vitro assay using RF-f1p supercoiled DNA
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?
additional information
?
-
-
TopoIIalpha-mediated catenation of plasmid DNA and kinetoplast DNA comprising small interlocked supercoiled circular DNA
-
-
?
additional information
?
-
-
topoisomerase II action on supercoiled DNA
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-
?
additional information
?
-
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the enzyme creates ATP-dependent transient double strand breaks in a segment of DNA, passage of un-broken segment of DNA though these transient breaks followed by re-ligation of broken-ends
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-
?
additional information
?
-
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ATPase activity is shown by the wild-type enzyme and the truncation mutant comprising residues 1-1058, the enzyme changes the DNA topology by coupling ATP hydrolysis to the transport of one DNA helix through a transient double-stranded break in another
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-
?
additional information
?
-
-
functions in chromosome condensation and segregation
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?
additional information
?
-
-
reconstitution of the heterodimeric active reverse gyrase from the two recombinant proteins overexpressed in Escherichia coli and purification. Subunit RgyB has a DNA-dependent ATPase activity at high temperature (80 °C) and is independent of the presence of subunit RgyA. Subunit RgyA alone has no detectable activity. The addition of subunit RgyA to subunit RgyB reconstitutes positive supercoiling activity
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-
?
additional information
?
-
-
dATP can substitute for ATP. ITP is slightly effective at 5-10 mM
-
-
?
additional information
?
-
-
the enzyme induces the activity of psorospermin, O5-methyl-psorospermin, and gemcitabine alkylating DNA through an epoxide-mediated electrophilic attack, at some DNA sites leading to increased antitumor activity of the alkylating reagents
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-
?
additional information
?
-
-
role of enzyme in activation/repression of developmentally regulated genes at late stages of neuronal differentiation
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?
additional information
?
-
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TopoIIalpha is essential for chromosome segregation performing the DNA surgery necessary to decatenate replicated chromosomes
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-
?
additional information
?
-
-
topoisomerase II is an enzyme that alters the topological state of DNA via a transient covalent enzyme-bridged double strand break in the DNA, through which a second DNA helix can pass
-
-
?
additional information
?
-
negative DNA supercoiling activity assays using relaxed pBR322 DNA as substrate, and ATPase assays
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-
-
additional information
?
-
-
negative DNA supercoiling activity assays using relaxed pBR322 DNA as substrate, and ATPase assays
-
-
-
additional information
?
-
negative DNA supercoiling activity assays using relaxed pBR322 DNA as substrate, and ATPase assays
-
-
-
additional information
?
-
negative DNA supercoiling activity assays using relaxed pBR322 DNA as substrate, and ATPase assays
-
-
-
additional information
?
-
-
the enzyme introduces positively supercoils in both relaxed and negatively supercoiled DNA in an ATP-dependent manner
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-
?
additional information
?
-
Paramecium bursaria chlorella virus
-
formation of a covalent enzyme-DNA complex is a prerequisite for activity, the intermediate can destabilize the genome
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-
?
additional information
?
-
-
the enzyme binds unmodified DNA and DNA containing N6-methyladenine and 5-methylcytosine to the same extent
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-
?
additional information
?
-
-
enzyme is able to discern the handedness of supercoils during the cleavage and preferentially cut negatively supercoiled DNA. Bimodal recognition of DNA geometry in which topoisomerase II uses elements in the C-terminal domain to sense the handedness of supercoils during DNA relaxation and elements in the conserved N-terminal domain or central domain during DNA cleavage
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-
?
additional information
?
-
Paramecium bursaria Chlorella virus-1
-
enzyme is able to discern the handedness of supercoils during the cleavage and preferentially cut negatively supercoiled DNA. Bimodal recognition of DNA geometry in which topoisomerase II uses elements in the C-terminal domain to sense the handedness of supercoils during DNA relaxation and elements in the conserved N-terminal domain or central domain during DNA cleavage
-
-
?
additional information
?
-
the enzyme also catalyzes ATP-dependent unwinding of synthetic Holliday junctions and ATP-stimulated annealing of unconstrained single-stranded oligonucleotides
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-
?
additional information
?
-
-
the enzyme also catalyzes ATP-dependent unwinding of synthetic Holliday junctions and ATP-stimulated annealing of unconstrained single-stranded oligonucleotides
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-
?
additional information
?
-
-
-
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?
additional information
?
-
-
-
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?
additional information
?
-
-
possible involvement in DNA replication
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-
?
additional information
?
-
-
dual role for the topoisomerase IIalpha in vivo consistent with the notion that its sequestration to the chromatin might play a role in chromosome condensation and decondesation during spermatogenesis
-
?
additional information
?
-
-
enzyme shows ATPase activity
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?
additional information
?
-
-
isozyme topo IIbeta substrate is plasmid DNA
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-
?
additional information
?
-
-
changes the linking number of a closed circular molecule by an increment of two
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-
?
additional information
?
-
-
the enzyme induces positive supercoiling into DNA molecules in an ATP-dependent reaction. The isolated ATPase and topoisomerase domains of reverse gyrase form specific physical interactions, retain their own DNA binding and enzymatic activities, and when combined cooperate to achieve the unique ATP-dependent positive supercoiling activity
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-
?
additional information
?
-
-
the enzyme induces positive supercoiling into DNA molecules in an ATP-dependent reaction. The isolated ATPase and topoisomerase domains of reverse gyrase form specific physical interactions, retain their own DNA binding and enzymatic activities, and when combined cooperate to achieve the unique ATP-dependent positive supercoiling activity
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
dATP can substitute for ATP
-
-
?
additional information
?
-
-
changes the linking number of a closed circular molecule by integers
-
-
?
additional information
?
-
-
does not catalyze DNA supercoiling
-
-
?
additional information
?
-
-
characterization of the interaction of topoisomerase II with DNA and identification of a DNA-binding domain, conserved DNA-binding mechanism
-
-
?
additional information
?
-
-
the enzyme performs ATP hydrolysis activity
-
-
?
additional information
?
-
-
topoisomerase II relaxes nucleosomal DNA much faster than topoisomerase I, and the DNA cross-inversion mechanism of topomerase II is facilitated in chromatin. Enzyme is the main modulator of DNA topology in chromatin fibers
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-
?
additional information
?
-
-
G-DNA binds with higher affinity than T-DNA. enzyme with only G-DNA bound is competent to cleave DNA and the ATPase activity of enzyme solely bound to G-DNA is partially stimulated. Full stimulation requires binding of T-DNA
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-
?
additional information
?
-
-
the sequence that defines a cleavage site resides within the central 20 bp of a dNA duplex. The DNA affinity does not correlate with the ability of the enzyme to cleave DNA. The binding step does not contribute significantly to the selection mechanism
-
-
?
additional information
?
-
-
Top2 plays a role in centromeric chromatin compaction
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-
?
additional information
?
-
-
the enzyme introduces transient double strand breaks to alter DNA topology, generation of a transient double strand break, with each subunit breaking one DNA strand. The mechanism of DNA cleavage provides several distinct advantages including the protection of DNA ends and the ability to quickly and efficiently religate the DNA strand break. The positively supercoiled DNA at the replication fork can isomerize by migration of the positive supercoiling into wrapping of the two replicated strands. This structure called a precatenane, is a substrate for Top2 mediated DNA catenation, and may represent a plausible mechanism for Top2 action during replication elongation
-
-
?
additional information
?
-
DNA cleavage, aperture, closure and religation are critical steps in the topo II reaction cycle, topo II DNA gate dynamics, single-molecule FRET experiments, role of T-segment in gate opening, overview
-
-
?
additional information
?
-
-
reaction mechanism, DNA cleavage by Top2 uses a tyrosine that is activated to attack the phosphodiester backbone of DNA and form a phosphotyrosine linkage, overview
-
-
?
additional information
?
-
-
substrate is negatively-supercoiled plasmid DNA
-
-
?
additional information
?
-
-
cleavage of supercoiled pBR322 DNA
-
-
?
additional information
?
-
-
the top2-191 allele acts in a dominant manner to suppress mutant taz1DELTA cold sensitivity. This suppression does not rely on the decatenation activity of Top2 and is independent of its DNA strand-passage activity. Taz1 binds telomeres, which promotes smooth replication fork progression through the repetitive telomeric sequences. The enhanced presence of reaction intermediates in which Top2 is clamped around DNA, promotes the removal of telomeric entanglements in vivo, independently of catalytic cycle completion. Modelling of how the clamped enzyme-DNA complex promotes proper chromosomal segregation, overview
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-
?
additional information
?
-
for DNA cleavage, the correct positioning of the catalytic tyrosine on the CAP domain with respect to the topoisomerase/primase domain seems to be achieved by a rigid body-domain movement, catalytic mechanism and role of the metal-binding TOPRIM domains in catalysis, overview
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-
?
additional information
?
-
for DNA cleavage, the correct positioning of the catalytic tyrosine on the CAP domain with respect to the topoisomerase/primase domain seems to be achieved by a rigid body-domain movement, catalytic mechanism and role of the metal-binding TOPRIM domains in catalysis, overview
-
-
?
additional information
?
-
-
for DNA cleavage, the correct positioning of the catalytic tyrosine on the CAP domain with respect to the topoisomerase/primase domain seems to be achieved by a rigid body-domain movement, catalytic mechanism and role of the metal-binding TOPRIM domains in catalysis, overview
-
-
?
additional information
?
-
-
helicase activity for both the N-terminal domain and the full-length reverse gyrase
-
-
?
additional information
?
-
Tequatrovirus T4
-
-
-
-
?
additional information
?
-
Tequatrovirus T4
-
enzyme also cleaves single-stranded DNA in a site-specific fashion, but this cleavage is mechanistically distinct from the double-strand DNA cleavage
-
-
?
additional information
?
-
Tequatrovirus T4
-
DNA-dependent ATPase activity
-
-
?
additional information
?
-
Tequatrovirus T4
-
the linking number of a DNA molecule changes by one to two units for each ATP molecule hydrolyzed
-
-
?
additional information
?
-
Tequatrovirus T4
-
cannot supercoil various E. coli plasmid DNAs in vitro
-
-
?
additional information
?
-
Tequatrovirus T4
-
when large amounts of enzyme are incubated with circular duplex DNA in absence of ATP, knotted molecules of varying complexity are formed
-
-
?
additional information
?
-
Tequatrovirus T4
-
increased expression of the enzyme causes neoplasia
-
-
?
additional information
?
-
-
mitochondrial topoisomerase II maintains kinetoplast DNA network topology by constantly remodeling the network during replication to maintain a proper minicircle density and network structure
-
-
?
additional information
?
-
-
the enzyme can alter the linking number of DNA only in steps of two
-
-
?
additional information
?
-
-
unknotting activity
-
-
?
additional information
?
-
-
no ATPase activity
-
-
?
additional information
?
-
-
activity is essential for kinetoplast DNA minicircle segregation
-
-
?
additional information
?
-
-
ATP hydrolysis
-
-
?
additional information
?
-
-
ATP hydrolysis
-
-
?
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(+)-(S)-4,4'-propylenedi-2,6-piperazinedione
-
i.e. dexrazoxane, ICRF-187
(-)-epigallocatechin gallate
(-)-epigallocatechin-3-gallate
-
-
(1,1',1''-[(6,9-dihydroporphyrin-5,10,15-triyl-k2N22,N24)tris(benzene-4,1-diyloxyethane-2,1-diyl)]tris[1-methylpiperidiniumato(2-)])copper(3+)
-
strong inhibition
(1R,1'R,6S,6'S,7R,7'R,11bR,11b'R)-1,1',7,7'-tetrakis(4-hydroxyphenyl)-1,1',6,6',7,7',11b,11b'-octahydro-6,6'-bi-2-oxadibenzo[cd,h]azulene-4,4',8,8',10,10'-hexol
-
comparison with inhibition of HindIII enzyme
(1R,1'R,6S,6'S,7S,7'S,11bR,11b'R)-1,1',7,7'-tetrakis(4-hydroxyphenyl)-1,1',6,6',7,7',11b,11b'-octahydro-6,6'-bi-2-oxadibenzo[cd,h]azulene-4,4',8,8',10,10'-hexol
-
comparison with inhibition of HindIII enzyme
(1R,3R)-8-methoxy-1-methyl-5,10-dioxo-3,4,5,10-tetrahydro-1H-benzo[g]isochromene-3-carboxylic acid
(1R,3S)-1,3,8-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
(1R,3S)-7,9-dimethoxy-1,3,6-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
(1S,3S)-3-acetyl-3,5,12-trihydroxy-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 3-amino-2,3,6-trideoxy-alpha-L-lyxo-hexopyranoside
-
-
(2E)-1,3-bis[4-(oxiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1,3-bis[4-(thiiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1-(4-methoxyphenyl)-3-[4-(oxiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1-(4-methoxyphenyl)-3-[4-(thiiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1-[2,4-bis(thiiran-2-ylmethoxy)phenyl]-3-(4-methoxyphenyl)prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-1-[4-(3-chloro-2-hydroxypropoxy)phenyl]-3-(4-methoxyphenyl)prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-2-(1,3-benzothiazol-2-ylmethylidene)-N,N-dimethylhydrazinecarbothioamide
-
-
(2E)-2-(1,3-benzothiazol-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(1,8-naphthyridin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(1-benzothiophen-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(benzo[h][1,6]naphthyridin-5-ylmethylidene)-N,N-dimethylhydrazinecarbothioamide
-
-
(2E)-2-(benzo[h][1,6]naphthyridin-5-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(quinolin-2-ylmethylidene)-N-[2-(trifluoromethyl)phenyl]hydrazinecarbothioamide
-
-
(2E)-2-(quinolin-2-ylmethylidene)-N-[4-(trifluoromethyl)phenyl]hydrazinecarbothioamide
-
-
(2E)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(quinoxalin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-(thieno[2,3-b]pyridin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-2-[(3,4-dimethylthieno[2,3-b]thiophen-2-yl)methylidene]hydrazinecarbothioamide
-
-
(2E)-3-(4-methoxyphenyl)-1-[4-(oxiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-3-(4-methoxyphenyl)-1-[4-(thiiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-3-[2-methoxy-4-(oxiran-2-ylmethoxy)phenyl]-1-[4-(oxiran-2-ylmethoxy)phenyl]prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-3-[4-(3-chloro-2-hydroxypropoxy)phenyl]-1-(4-methoxyphenyl)prop-2-en-1-one
-
inhibition in vivo in cancer cells, IC50 values, overview
(2E)-N,N-dimethyl-2-(1,8-naphthyridin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N,N-dimethyl-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
exhibits broad antiproliferative activity arresting synchronized cells at the M-phase, also exhibits iron chelator activity, and topoisomerase IIalpha catalytic inhibition, the latter due to direct interaction with the ATPase domain, blocks of ATP hydroly
(2E)-N,N-dimethyl-2-(quinoxalin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N,N-dimethyl-2-(thieno[2,3-b]pyridin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-bromophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-fluorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-methoxy-5-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-methoxyphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(2-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-bromophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-chlorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-fluorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-methoxyphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(3-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-bromophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-chlorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-cyanophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-fluorophenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-methoxyphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-(4-methylphenyl)-2-(quinolin-2-ylmethylidene)hydrazinecarboxamide
-
-
(2E)-N-benzyl-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-phenyl-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2E)-N-[2',6'-di(propan-2-yl)biphenyl-4-yl]-2-(quinolin-2-ylmethylidene)hydrazinecarbothioamide
-
-
(2R)-2-[(5Z)-5-[[3-(4-fluorophenoxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2R,2'S,3'S)-3'-(3,5-dihydroxyphenyl)-2,2'-bis(4-hydroxyphenyl)-4-[(E)-2-(4-hydroxyphenyl)ethenyl]-2,2',3,3'-tetrahydro-3,4'-bi-1-benzofuran-6,6'-diol
-
comparison with inhibition of HindIII enzyme
(2R,3S)-2-(3,5-dihydroxyphenyl)-1-[(S)-hydroxy(4-hydroxyphenyl)methyl]-3-(4-hydroxyphenyl)-2,3-dihydro-1H-indene-4,6-diol
-
comparison with inhibition of HindIII enzyme
(2S)-2-(2-hydroxypropan-2-yl)-2,5-dimethyl-8,10-bis[(2-methyloxiran-2-yl)methoxy]-1,2-dihydro-11H-furo[3,2-a]xanthen-11-one
-
-
(2S)-2-[(5Z)-4-oxo-5-[(3-phenoxyphenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S)-2-[(5Z)-4-oxo-5-[(3-[[(2Z)-3-phenylprop-2-en-1-yl]oxy]phenyl)methylidene]-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S)-2-[(5Z)-5-([3-[(3,4-dichlorophenyl)methyl]phenyl]methylidene)-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S)-2-[(5Z)-5-[(3',4'-dichloro[1,1'-biphenyl]-3-yl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S)-2-[(5Z)-5-[(3-benzoylphenyl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S)-2-[(5Z)-5-[(3-benzylphenyl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S)-2-[(5Z)-5-[([1,1'-biphenyl]-3-yl)methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S)-2-[(5Z)-5-[[3-(3,4-dichlorophenoxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S)-2-[(5Z)-5-[[3-(3-chlorophenoxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S)-2-[(5Z)-5-[[3-(benzyloxy)phenyl]methylidene]-4-oxo-2-sulfanylidene-1,3-thiazolidin-3-yl]-3-phenylpropanoic acid
-
(2S,3R,4S,6R)-4-amino-2-methyl-6-((3-(2-phenyl-1-tosyl-1H-indol-3-yl)prop-2-yn-1-yl)oxy)tetrahydro-2H-pyran-3-ol
-
103% inhibition at 0.1 mM
(2S,3R,4S,6R)-4-amino-2-methyl-6-((3-(2-phenylbenzofuran-3-yl)prop-2-yn-1-yl)oxy)tetrahydro-2H-pyran-3-ol
-
5.5% inhibition at 0.1 mM
(2S,3R,4S,6R)-4-amino-2-methyl-6-((3-(2-phenylbenzo[b]thiophen-3-yl)prop-2-yn-1-yl)oxy)tetrahydro-2H-pyran-3-ol
-
22.2% inhibition at 0.1 mM
(2S,3R,4S,6R)-4-amino-2-methyl-6-(3-(2-phenyl-1H-indol-3-yl)prop-2-ynyloxy)tetrahydro-2H-pyran-3-ol
-
55.5% inhibition at 0.1 mM
(2S,3S,6R)-2-methyl-6-(3-(2-phenyl-1-tosyl-1H-indol-3-yl)prop-2-ynyloxy)tetrahydro-2H-pyran-3-amine
-
86.2% inhibition at 0.1 mM
(2S,3S,6R)-2-methyl-6-(3-(2-phenyl-1H-indol-3-yl)prop-2-ynyloxy)tetrahydro-2H-pyran-3-amine
-
39.5% inhibition at 0.1 mM
(2S,3S,6R)-2-methyl-6-(3-(2-phenylbenzo[b]thiophen-3-yl)prop-2-ynyloxy)tetrahydro-2H-pyran-3-amine
-
16.4% inhibition at 0.1 mM
(3,3',3''-[(6,9-dihydroporphyrin-5,10,15-triyl-k2N22,N24)tris(benzene-4,1-diyloxy)]tris(N,N,N-trimethylpropan-1-aminiumato)(2-))copper(3+)
-
strong inhibition
(3,5-dimethoxybenzene)-propynoic acid
-
-
(3,5-dimethoxybenzene)-propynoic acid methyl ester
-
-
(3-(6-methoxynaphthalen-2-yl)phenyl)methanol
-
(3E)-3-[1-[(2-aminoethyl)amino]ethylidene]-2H-1-benzopyran-2,4(3H)-dione
-
(3E)-3-[1-[(2-hydroxyethyl)amino]ethylidene]-2H-1-benzopyran-2,4(3H)-dione
-
(3E,3'E)-3,3'-(1,1'-(ethane-1,2-diylbis(azanediyl))bis(ethan-1-yl-1-ylidene))dichroman-2,4-dione
-
(3E,3'E)-3,3'-(1,1'-(propane-1,3-diylbis(azanediyl))bis(ethan-1-yl-ylidene))dichroman-2,4-dione
-
(3R,4R,4aS,5S,9bS,10S)-4-(3,5-dihydroxyphenyl)-3,5,10-tris(4-hydroxyphenyl)-3,4,4a,5,9b,10-hexahydro-11-oxabenzo[5,6]cyclohepta[1,2,3,4-jkl]-as-indacene-2,6,8-triol
-
comparison with inhibition of HindIII enzyme
(3S)-3-methyl-7,9-bis(propan-2-yloxy)-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
(3S)-7,9-dihydroxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
(3S)-7,9-dimethoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
(3S)-9-hydroxy-7-methoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
(3S,4S,4aR,5S,9bS,10S)-4-(3,5-dihydroxyphenyl)-3,5,10-tris(4-hydroxyphenyl)-3,4,4a,5,9b,10-hexahydro-11-oxabenzo[5,6]cyclohepta[1,2,3,4-jkl]-as-indacene-2,6,8-triol
-
comparison with inhibition of HindIII enzyme
(4-(6-methoxynaphthalen-2-yl)phenyl)methanol
-
(4bR,5R,9S,10S,11R,12R)-10-(3,5-dihydroxyphenyl)-5,9,12-tris(4-hydroxyphenyl)-4b,5,9,10,11,12-hexahydrobenzo[6,7]cyclohepta[1,2,3-cd]furo[3,2-f][1]benzofuran-1,3,11-triol
-
comparison with inhibition of HindIII enzyme
(4Z,7Z,10Z,13Z,16Z,19Z)-henicosa-4,7,10,13,16,19-hexaenoic acid
-
IC50 is 0.05 mM for inhibition of decatenation of kinetoplast DNA
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-(1H-pyrrolo[2,3-b]pyridin-6-ylamino)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-(4H-1,2,4-triazol-3-ylamino)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-(9H-purin-6-ylamino)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-(imidazo[1,2-a]pyridin-8-ylamino)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[3-(methylamino)pyridin-2-yl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[3-(piperidin-1-ylmethyl)phenyl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
molecular docking to MDR protein
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[3-(pyrrolidin-1-ylmethyl)phenyl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[4-(piperidin-1-ylmethyl)phenyl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-5-(4-hydroxy-3,5-dimethoxyphenyl)-9-{[4-(pyrrolidin-1-ylmethyl)phenyl]amino}-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-9-({3-[(diethylamino)methyl]phenyl}amino)-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-9-({4-[(diethylamino)methyl]phenyl}amino)-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-9-[(5,6-diphenyl-1,2,4-triazin-3-yl)amino]-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5R,5aR,8aS,9S)-9-[(6-aminopyridin-2-yl)amino]-5-(4-hydroxy-3,5-dimethoxyphenyl)-5,8,8a,9-tetrahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-6(5aH)-one
-
-
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoic acid
-
irreversible inhibition, IC50 is 0.01 mM for inhibition of decatenation of kinetoplast DNA, effects on thermal transition of dsDNA, overview
(6aR,12aR)-11-(2,3-dihydroxypropoxy)-12a-hydroxy-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-11-(3-chloro-2-hydroxypropoxy)-12a-hydroxy-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-11-[3-(benzylamino)-2-hydroxypropoxy]-12a-hydroxy-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-11-[3-[bis(2-hydroxyethyl)amino]-2-hydroxypropoxy]-12a-hydroxy-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-(2-hydroxy-3-methoxypropoxy)-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-(2-hydroxy-3-[[2-(morpholin-4-yl)ethyl]amino]propoxy)-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-[2-hydroxy-3-(morpholin-4-yl)propoxy]-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-[2-hydroxy-3-[(2-hydroxy-2-phenylethyl)amino]propoxy]-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-11-[2-hydroxy-3-[(2-phenylethyl)amino]propoxy]-2,3,9-trimethoxy-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(6aR,12aR)-12a-hydroxy-2,3,9-trimethoxy-11-(oxiran-2-ylmethoxy)-6a,12a-dihydrochromeno[3,4-b]chromen-12(6H)-one
-
-
(9-([2-(1H-indol-3-yl)ethyl]amino)acridin-3-yl)(4-methylpiperazin-1-yl)methanone
-
-
(9-([2-(1H-indol-3-yl)ethyl]amino)acridin-4-yl)(4-methylpiperazin-1-yl)methanone
-
-
(9-[(1-benzylpiperidin-4-yl)amino]acridin-3-yl)(4-methylpiperazin-1-yl)methanone
-
-
(9S,12S,13S)-trihydroxy-(10E)-octadecenoic acid
-
97% inhibition at 0.1 mM
(beta,gamma-Imido)adenosine triphosphate
-
inhibits ATP-driven supercoiling
(E)-3-(1-(2-(methylamino)ethylamino)ethylidene)chroman-2,4-dione
-
(E)-3-(1-(2-mercaptoethylamino)ethylidene)chroman-2,4-dione
-
1,2-bis(3,5-dioxopiperazin-1-yl)ethane
-
i.e. ICRF-154
1,3,5-trihydroxy-4-methoxy-9H-xanthen-9-one
-
-
1,3-benzodioxole-5-carbaldehyde
-
-
1,3-bis(2-chloroethyl)-1-nitroso-urea
-
P388/F11782 cell enzyme, high inhibition
1,3-bis(oxiran-2-ylmethoxy)-9H-xanthen-9-one
-
inhibition in vivo in cancer cells, IC50 values, overview
1,5-dihydroxy-3-methoxy-2,4-bis(3-methylbut-2-en-1-yl)-9H-xanthen-9-one
-
-
1,7-dihydroxy-9H-xanthen-9-one
-
-
1-(-(5-nitrothiazol-2-yl)piperidin-4-yl)-3-phenylthiourea
-
-
1-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)-3-phenylurea
-
-
1-(2,2-dibromoethenyl)-3,5-dimethoxybenzene
-
-
1-(2,2-dibromoethenyl)-4-methoxybenzene
-
-
1-(2-hydroxy-3-[[(6aR,12aR)-12a-hydroxy-2,3,9-trimethoxy-12-oxo-6,6a,12,12a-tetrahydrochromeno[3,4-b]chromen-11-yl]oxy]propyl)piperidin-4-one
-
-
1-(2-hydroxy-5-(6-hydroxynaphthalen-2-yl)-3-nitrophenyl)ethanone
-
1-(2-hydroxy-5-(6-methoxynaphthalen-2-yl)-3-nitrophenyl)ethanone
-
1-(4-(6-methoxynaphthalen-2-yl)phenyl)ethanol
-
-
1-(4-acetylphenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-(4-acetylphenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-(4-chlorobenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-(4-chlorobenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-(4-chlorophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-(4-chlorophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-(4-fluorobenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-(4-fluorobenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-(4-fluorophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-(4-fluorophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-(4-methoxybenzyl)-1H-[1,2,3]triazolo[4,5-g]-phthalazine-4,9-dione
-
-
1-(4-methoxybenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-(4-methoxybenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-(4-methoxyphenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-(4-methoxyphenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-(4-nitrobenzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide
1-(4-nitrophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-(4-nitrophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-(4-tolyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-(4-tolyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-(5-nitrothiazol-2-yl)-N-phenylpiperidin-4-amine
-
-
1-(benzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide
-
-
1-(hydroxymethyl)-3-(2-hydroxypropan-2-yl)-2-(5-methoxy-9H-beta-carbolin-1-yl)-cyclopentanol
-
1-benzenesulfonyl-3-chloropropenyl-1H-indole
-
-
1-benzenesulfonyl-5-benzyloxy-3-chloropropenyl-1H-indole
-
-
1-benzyl-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
-
-
1-benzyl-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
-
-
1-ethoxycarbonyl-naphthoquinone-[2,3-d]indolizidine-6,11-dione
-
0.1 mg/ml, 32.1% inhibition of relaxation
1-ethyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-ethyl-3-(benzimidazol-2-yl)-6,8-difluoro-7-(3-methylpiperazin-1-yl)-4(1H)-quinolone
-
18% and 13% inhibition at 0.1 mM and 0.02 mM, respectively
1-ethyl-3-(benzimidazol-2-yl)-6-fluoro-7-(1-piperazin-1-yl)-1,8-naphthyridine-4(1H)-one
-
8% and 30% inhibition at 0.02 mM and 0.1 mM, respectively
1-ethyl-3-(benzimidazol-2-yl)-6-fluoro-7-(piperazin-1-yl)-4(1H)-quinolone
-
8.5% and 7% inhibition at 0.02 mM and 0.1 mM, respectively
1-hydroxy-3-(2',3'-epoxypropoxy)thioxanthone
-
21% inhibition at 0.1 mM
1-hydroxy-3-(3'-chloro-2'-hydroxy-1'-propoxy)thioxanthone
-
84% inhibition at 0.1 mM
1-hydroxy-3-(3'-chloro-2'-thioyl-1'-propoxy)thioxanthone
-
16% inhibition at 0.1 mM
1-hydroxy-3-(oxiran-2-ylmethoxy)-9H-xanthen-9-one
-
-
1-hydroxy-3-[2-hydroxy-3-(2-hydroxyethoxy)propoxy]-9H-xanthen-9-one
-
89.25% inhibition at 0.1 mM
1-hydroxy-3-[2-hydroxy-3-(propylamino)propoxy]-9H-xanthen-9-one
-
100% inhibition at 0.1 mM. ATPase inhibitory activity, molecular docking, overview. The compound shows a stable binding pattern to the ATP-binding domain of topo II
1-hydroxy-3-[2-hydroxy-3-[(2-hydroxyethyl)amino]propoxy]-9H-xanthen-9-one
-
100% inhibition at 0.1 mM
1-hydroxy-3-[2-hydroxy-3-[(2-hydroxyethyl)sulfanyl]propoxy]-9H-xanthen-9-one
-
63.75% inhibition at 0.1 mM
1-hydroxy-3-[2-hydroxy-3-[(3-hydroxypropyl)amino]propoxy]-9H-xanthen-9-one
-
100% inhibition at 0.1 mM
1-hydroxy-3-[2-hydroxy-3-[(3-hydroxypropyl)sulfanyl]propoxy]-9H-xanthen-9-one
-
68% inhibition at 0.1 mM
1-iso-butyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-iso-propyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-methyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-methyl-3-(2-hydroxypropan-2-yl)-2-(5-methoxy-9H-beta-carbolin-1-yl)-cyclopentanol
-
1-n-butyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-n-propyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
1-[(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)(ethyl)amino]-1-oxopropan-2-yl 1H-indazole-3-carboxylate
-
-
1-[4-[(methanesulfonyl)amino]phenyl]-1-oxopropan-2-yl 1H-indazole-3-carboxylate
-
-
10'(Z),13'(E),15'(E)-heptadecatrienyl hydroquinone
-
i.e. HQ17(3), the cysteine-reactive alkyl hydroquinone modifies topoisomerase IIalpha, enhances DNA breakage, and induces apoptosis in cancer cells, it is attributed to topoisomerase IIalpha poisoning and the induction of oxidative damage. Irreversibly inhibits Topo IIalpha activity in vitro and is more cytotoxic in leukemia HL-60 cells than in Topo IIalpha-deficient variant HL-60/MX2 cell. HQ17(3) reacts with Cys427, Cys733, and Cys997 of recombinant Topo IIalpha in vitro, whereas it reacts with Cys427 of cellular Topo IIalpha in Huh7 hepatoma cells. The cells, HQ17(3) treatment causes prompt inhibition of DNA synthesis and consequently induces the expression of DNA damage-related genes DDIT3, GADD45A, and GADD45G. Topo IIalpha inhibition, apoptosis, and oxidative stress account for cytotoxicity caused by HQ17(3). Pretreatment of Huh7 cells with N-acetylcysteine partially attenuates mitochondrial membrane damage, DNA breakage, and caspase activation, but does not diminish HQ17(3)-induced cell death
10-chloro-7-(3-(dimethylamino)propyl)-3-methoxybenzo[a]phenazin-5(7H)- one
-
10-chloro-7-(3-(dimethylamino)propyl)benzo[a]phenazin-5(7H)-one
-
11-(4-Cyanoanilino)azatoxin
-
-
11beta-(2''-N,N-dimethylaminoethyl)-amino-azatoxin
-
belongs to the epipodophyllotoxins, inhibitors of eukaryotic enzymes, inhibits the S83W mutant enzyme, but not the wild-type bacterial enzyme
1H-[1,2,3]triazolo[4,5,-g]phthalazine-4,9-dione
-
-
2,2'-(4-phenylpyridine-2,6-diyl)diphenol
-
42.7% inhibition at 0.1 mM
2,2'-bis(8-formyl-1,6,7-trihydroxy-5-isopropyl-3-methylnaphthalene)
-
i.e. gossypol, belongs to the class II compounds which interfere with the catalytic function of topoisomerases without generating strand breaks
2,3-dimethoxy-9-(2-dimethylaminoethoxy)-6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
2,3-dimethoxy-9-(2-dimethylaminoethoxy)-6-(3-dimethylaminopropyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
2,4-di(furan-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2,4-di(furan-2-yl)-5H-chromeno[4,3-b]pyridine
-
11.6% inhibition at 0.1 mM
2,4-di(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2,4-di(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
-
10.6% inhibition at 0.1 mM
2,4-di(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2,4-di(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
-
7.9% inhibition at 0.1 mM
2,4-di(thiophen-3-yl)-5H-chromeno[4,3-b]pyridine
-
-
2,4-diphenyl-5,6-dihydrobenzo[h]quinoline
-
-
2,4-diphenyl-5H-chromeno[4,3-b]pyridine
-
15.4% inhibition at 0.1 mM
2-(2,6-diphenylpyridin-4-yl)phenol
-
-
2-(2-chlorophenyl)-4-(furan-2-yl)-6-(3-methylthiophen-2-yl) pyridine
-
33.2% inhibition at 0.1 mM
2-(2-chlorophenyl)-6-(5-chlorothiophen-2-yl)-4-(furan-3-yl) pyridine
-
38% inhibition at 0.02 mM
2-(2-chlorophenyl)benzo-1,4-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
2-(2-hydroxy-5-(6-hydroxynaphthalen-2-yl)phenyl)acetic acid
-
2-(2-hydroxyethyl)-5-(6-methoxynaphthalen-2-yl)phenol
-
2-(3,4-dimethoxyphenyl)-6-methoxynaphthalene
-
2-(3,5-dichlorophenyl)benzo-1,4-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
2-(3-(2-(dimethylamino)ethylamino)propyl)-6-(dodecylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-(2-(dimethylamino)ethylamino)propyl)-6-(octylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-(4-methylpiperazin-1-yl)propyl)-6-(octylamino)-1H-benzo-[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-(dimethylamino)propyl)-6-(methylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-(dimethylamino)propyl)-6-(octylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-(3-chlorophenyl)-6-(5-chlorothiophen-2-yl)-4-(furan-3-yl) pyridine
-
51% inhibition at 0.02 mM
2-(3-chlorophenyl)benzo-1,4-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
2-(3-fluorophenylamino)-5-(3-hydroxyphenyl)-1,3,4-thiadiazole
-
DNA topoisomerase II catalytic inhibitor
2-(4,6-diphenylpyridin-2-yl)phenol
-
-
2-(4-(6-methoxynaphthalen-2-yl)phenyl)acetic acid
-
2-(4-bromophenylamino)-5-(2,4-dichlorophenyl)-1,3,4-thiadiazole
-
DNA topoisomerase II poison
2-(4-chlorophenyl)-4-(furan-2-yl)-6-(3-methylthiophen-2-yl) pyridine
-
18% inhibition at 0.02 mM
2-(4-chlorophenyl)-4-(furan-3-yl)-6-(3-methylthiophen-2-yl) pyridine
-
33.8% inhibition at 0.1 mM
2-(4-chlorophenyl)-6-(5-chlorothiophen-2-yl)-4-(furan-2-yl) pyridine
-
48.4% inhibition at 0.02 mM
2-(4-chlorophenyl)-6-(5-chlorothiophen-2-yl)-4-(furan-3-yl) pyridine
-
57% inhibition at 0.02 mM
2-(4-chlorophenyl)-N-cyclohexylimidazo[1,2-a]pyrazin-3-amine
-
2-(4-chlorophenyl)benzo-1,4-quinone
2-(4-chlorophenyl)imidazo[1,2-a]pyrazin-3-amine
-
2-(4-chlorophenyl)imidazo[1,2-a]pyridin-3-amine
-
2-(4-fluorophenylamino)-5-(2,4-dichlorophenyl)-1,3,4-thiadiazole
-
DNA topoisomerase II poison
2-(4-hydroxy-3-methoxyphenyl)chromenylium-3,5,7-triol
-
anthocyanidin, inhibition of isozyme IIbeta decatenation activity
2-(4-methoxyphenyl)imidazo[1,2-a]pyrazin-3-amine
-
2-(4-phenyl-2,2'-bipyridin-6-yl)phenol
-
-
2-(4-phenyl-2,3'-bipyridin-6-yl)phenol
-
-
2-(4-phenyl-2,4'-bipyridin-6-yl)phenol
-
-
2-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-6-(5-methylfuran-2-yl) pyridine
-
54% inhibition at 0.02 mM
2-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-6-m-tolylpyridine
-
38% inhibition at 0.02 mM
2-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-6-o-tolylpyridine
-
49% inhibition at 0.02 mM
2-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-6-p-tolylpyridine
-
54% inhibition at 0.02 mM
2-(5-chlorothiophen-2-yl)-6-(furan-2-yl)-4-(furan-3-yl)pyridine
-
48.6% inhibition at 0.02 mM
2-(6-hydroxynaphthalen-2-yl)-4-methylbenzoic acid
-
2-(6-phenyl-2,2'-bipyridin-4-yl)phenol
-
-
2-(6-phenyl-2,3'-bipyridin-4-yl)phenol
-
-
2-(6-phenyl-2,4'-bipyridin-4-yl)phenol
-
-
2-(furan-2-yl)-3-[2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxyacetamido]-thiazolidin-4-one
2-(furan-2-yl)-4-(furan-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-(furan-3-yl)-6-(3-methylthiophen-2-yl)pyridine
-
36% inhibition at 0.02 mM
2-(furan-2-yl)-4-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
-
2.0% inhibition at 0.1 mM
2-(furan-2-yl)-4-(pyridin-3-yl)-5H-chromeno[4,3-b]pyridine
-
5.6% inhibition at 0.1 mM
2-(furan-2-yl)-4-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
-
6.8% inhibition at 0.1 mM
2-(furan-2-yl)-4-(thiophen-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-phenyl-5,6-dihydrobenzo[h]quinoline
-
-
2-(furan-2-yl)-4-phenyl-5H-chromeno[4,3-b]pyridine
-
28.4% inhibition at 0.1 mM
2-(p-nitrobenzyl)benzoxazole
-
2-(pyridin-2-yl)-4-(pyridin-3-yl)-5H-chromeno[4,3-b]pyridine
-
8.6% inhibition at 0.1 mM
2-(pyridin-2-yl)-4-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(pyridin-2-yl)-4-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
-
19.4% inhibition at 0.1 mM
2-(pyridin-2-yl)-4-(thiophen-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-(thiophen-2-yl)-4-(thiophen-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
-
-
2-acetoxy-5-(6-methoxynaphthalen-2-yl)benzyl acetate
-
2-Amino-1-(1-benzyl-piperidin-4-yl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 17.0% inhibition of relaxation
2-Amino-1-(2-bromo-ethyl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 43.4% inhibition of relaxation
2-Amino-1-(2-hydroxy-ethyl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 7.8% inhibition of relaxation
2-Amino-1-(4-amino-phenyl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 7.8% inhibition of relaxation
2-Amino-1-(4-fluoro-phenyl)-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 28.3% inhibition of relaxation
2-Amino-1-benzyl-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 9.4% inhibition of relaxation
2-Amino-1-cyclohexyl-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 7.8% inhibition of relaxation
2-Amino-1-isopropyl-4,9-dioxo-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 5.9% inhibition of relaxation
2-amino-3-ethoxycarbonyl-N-(4-fluorophenyl)benz[f]indole-4,9-dione
-
potent inhibitor
2-amino-3-ethoxycarbonyl-N-methyl-benz[f]indole-4,9-dione
-
0.1 mg/ml, 9.8% inhibition of relaxation
2-Amino-4,9-dioxo-1-p-tolyl-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 41.2% inhibition of relaxation
2-Amino-4,9-dioxo-1-phenyl-3a,4,9,9a-tetrahydro-1H-benzo[f]indole-3-carboxylic acid ethyl ester
-
0.1 mg/ml, 21.6% inhibition of relaxation
2-chloro-3-[2-(dimethylamino)isopropoxy]benzo-[b]naphtho[2,3-d]furan-6,11-dione
-
0.05 mM, 88% inhibition. Comparison of cytotoxicity against various human cancer cells
2-dodecyl-6-(2-(4-methylpiperazin-1-yl)ethylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-dodecyl-6-(octylamino)-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
2-ethyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-hydroxy-3-ethoxycarbonyl-N-(3,4-dimethylphenyl)-benz[f]indole-4,9-dione
-
0.1 mg/ml, 17.0% inhibition of relaxation
2-hydroxy-3-methoxy-5-(6-methoxynaphthalen-2-yl)benzaldehyde
-
2-hydroxy-4-(6-hydroxynaphthalen-2-yl)benzoic acid
-
2-hydroxy-5-(6-hydroxynaphthalen-2-yl )-3-methoxybenzaldehyde
-
2-hydroxy-5-(6-hydroxynaphthalen-2-yl)benzaldehyde
-
2-hydroxy-5-(6-hydroxynaphthalen-2-yl)benzoic acid
-
2-hydroxy-5-(6-methoxynaphthalen-2-yl)benzoic acid
-
2-iso-butyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-iso-propyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-methoxy-5-(6-methoxynaphthalen-2-yl)benzaldehyde
-
2-methoxy-6-(3-(trifluoromethyl)phenyl)naphthalene
-
2-methoxy-6-(4-(trifluoromethyl)phenyl)naphthalene
-
2-methoxy-6-(4-nitro-3-(trifluoromethyl)phenyl)naphthalene
-
2-methyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-methyl-N-methyl-5-demethyl ellipticinium iodide
the compound inhibits DNA cleavage without altering the ability of topoisomerase IIalpha to bind its DNA substrate
2-n-butyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-n-propyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
-
-
2-oxo-2-(3-sulfamoylanilino)ethyl 1H-indazole-3-carboxylate
-
-
2-phenyl-4-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-phenyl-4-(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
-
8.6% inhibition at 0.1 mM
2-phenyl-4-(pyridin-3-yl)-5H-chromeno[4,3-b]pyridine
-
14.0% inhibition at 0.1 mM
2-phenyl-4-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-phenyl-4-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
-
10.8% inhibition at 0.1 mM
2-phenyl-4-(thiophen-3-yl)-5,6-dihydrobenzo[h]quinoline
-
-
2-phenyl-4-(thiophen-3-yl)-5H-chromeno[4,3-b]pyridine
-
17.6% inhibition at 0.1 mM
2-[(1,1-dioxo-1l6-thiolan-3-yl)(ethyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(1,1-dioxo-1l6-thiolan-3-yl)(methyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(1,1-dioxo-1l6-thiolan-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)(2-methylpropyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(10Z,13E,15E)-heptadeca-10,13,15-trien-1-yl]benzene-1,4-diol
-
irreversible inhibition of Topo IIalpha activity through the accumulation of Topo II-DNA cleavable complexes
2-[(3-carbamoylthiophen-2-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[(butan-2-yl)(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[4-(methanesulfonyl)piperazin-1-yl]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
2-[4-phenyl-6-(thiophen-2-yl)pyridin-2-yl]phenol
-
-
2-[4-phenyl-6-(thiophen-3-yl)pyridin-2-yl]phenol
-
-
2-[6-(furan-2-yl)-4-phenylpyridin-2-yl]phenol
-
-
2-[benzyl(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
-
-
25,26,27-tris-nor-3beta-methoxylanost-9(11)-en-24-oic acid
-
-
3,3'-(4-phenylpyridine-2,6-diyl)diphenol
-
86.5% inhibition at 0.1 mM
3,4,5-trimethoxybenzaldehyde
-
-
3,4,5-trimethoxyphenylpropynoic-3-(1-benzenesulfonyl-1H-indol-3-yl)-allyl ester
-
-
3,4-dimethoxybenzaldehyde
-
-
3,4-dimethoxyphenylpropynoic-3-(1-benzenesulfonyl-1Hindol-3-yl)-allyl ester
-
-
3,4-methylenedioxyphenylpropynoic-3-(1-benzenesulfonyl-1H-indol-3-yl)-allyl ester
-
-
3,5-dimethoxybenzaldehyde
-
-
3,5-dimethoxyphenylpropynoic-3-(1-benzenesulfonyl-1H-indol-3-yl)-allyl ester
-
-
3,8-dimethyl-5-(propan-2-yl)-6-[(prop-2-en-1-yl)oxy]naphthalene-1,2-dione
-
3,8-dimethyl-6-(octyloxy)-5-(propan-2-yl)naphthalene-1,2-dione
-
3,8-dimethyl-6-[(3-methylbut-2-en-1-yl)oxy]-5-(propan-2-yl)naphthalene-1,2-dione
-
3,8-dimethyl-6-[[(2Z)-3-phenylprop-2-en-1-yl]oxy]-5-(propan-2-yl)naphthalene-1,2-dione
-
3-(1,3-benzodioxol-5-yl)prop-2-ynoic acid
-
-
3-(2,6-diphenylpyridin-4-yl)phenol
-
68.2% inhibition at 0.1 mM
3-(2-dimethylaminoethoxy)-6-(2-dimethylaminoethylamino)indeno[2,1-c]quinolin-7-one
-
-
3-(2-phenyl-1-benzofuran-3-yl)prop-2-yn-1-yl 3-amino-2,3,6-trideoxy-b-D-arabino-hexopyranoside
-
6.5% inhibition at 0.1 mM
3-(2-phenyl-1-benzothiophen-3-yl)prop-2-yn-1-yl 3-amino-2,3,6-trideoxy-b-D-arabino-hexopyranoside
-
5.8% inhibition at 0.1 mM
3-(2-phenyl-1H-indol-3-yl)prop-2-yn-1-yl 3-amino-2,3,6-trideoxy-b-D-arabino-hexopyranoside
-
7.1% inhibition at 0.1 mM
3-(2-pyrrolidin-1-ylethoxy)-6-(2-pyrrolidin-1-ylethylamino)indeno[2,1-c]quinolin-7-one
-
-
3-(3,4,5-trimethoxyphenyl)prop-2-ynoic acid
-
-
3-(3,4-dimethoxyphenyl)prop-2-ynoic acid
-
-
3-(3-dimethylaminopropoxy)-6-(3-dimethylaminopropylamino)indeno[2,1-c]quinolin-7-one
-
-
3-(4,6-diphenylpyridin-2-yl)phenol
-
48.4% inhibition at 0.1 mM
3-(4-chlorophenyl)benzo-1,2-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
3-(4-methoxyphenyl)prop-2-ynoic acid
-
-
3-(4-phenyl-2,2'-bipyridin-6-yl)phenol
-
-
3-(4-phenyl-2,3'-bipyridin-6-yl)phenol
-
-
3-(4-phenyl-2,4'-bipyridin-6-yl)phenol
-
3.6% inhibition at 0.1 mM
3-(6-phenyl-2,2'-bipyridin-4-yl)phenol
-
48.1% inhibition at 0.1 mM
3-(6-phenyl-2,3'-bipyridin-4-yl)phenol
-
37.1% inhibition at 0.1 mM
3-(6-phenyl-2,4'-bipyridin-4-yl)phenol
-
42.8% inhibition at 0.1 mM
3-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
-
-
3-acetyl-2-(4-methoxyphenyl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole
-
-
3-chloro-4-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] azetidin-2-one
3-chloro-4-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]azetidin-2-one
-
-
3-hydroxy-6-(2-dimethylaminoethylamino)indeno[2,1-c]quinolin-7-one
-
-
3-hydroxy-6-(2-pyrrolidin-1-ylethylamino)indeno[2,1-c]quinolin-7-one
-
-
3-hydroxy-6-(3-dimethylaminopropylamino)indeno[2,1-c]quinolin-7-one
-
-
3-Methoxy-5-(6-oxo-5,8,8a,9-tetrahydro-1,3,7-trioxa-5a-aza-dicyclopenta[b,g]naphthalen-5-yl)-[1,2]benzoquinone
-
inhibits decatenation, inhibition due to stabilization of the topoisomerase II-DNA covalent binary complex, the nonintercalative specific inhibitor stabilizes the cleavable complex
3-oxolanost-9(11)-ene-24S,25-diol
-
IC50: 0.186 mM
3-thiiranylmethyloxy-1-hydroxy-5-azaxanthone
-
19.5% and 9% inhibition at 0.1 mM and 0.02 mM, respectively
3-[(10-methoxybenzo[a]phenazin-5-yl)oxy]-N,N-dimethylpropan-1-amine
-
3-[(1E)-3-chloroprop-1-en-1-yl]-1-(phenylsulfonyl)-1H-indole
-
-
3-[1-[(4-methylphenyl)sulfonyl]-2-phenyl-1H-indol-3-yl]prop-2-yn-1-yl 3-amino-2,3,6-trideoxy-b-D-arabino-hexopyranoside
-
101% inhibition at 0.1 mM
3-[2-(diethylamino)ethoxy]benzo[b]naphtho[2,3-d]-furan-6,11-dione
-
0.05 mM, 91% inhibition. Comparison of cytotoxicity against various human cancer cells
3-[2-(dimethylamino)isopropoxy]benzo[b]naphtho[2,3-d]furan-6,11-dione
-
0.05 mM, 84% inhibition. Comparison of cytotoxicity against various human cancer cells
3-[2-(dimethylamino)propoxy]benzo[b]naphtho[2,3-d]furan-6,11-dione
-
0.05 mM, 100% inhibition. Comparison of cytotoxicity against various human cancer cells
3-[2-(furan-2-yl)-6-phenylpyridin-4-yl]phenol
-
47.5% inhibition at 0.1 mM
3-[2-phenyl-6-(thiophen-2-yl)pyridin-4-yl]phenol
-
57.5% inhibition at 0.1 mM
3-[2-phenyl-6-(thiophen-3-yl)pyridin-4-yl]phenol
-
52.6% inhibition at 0.1 mM
3-[3-[(2-chloroethyl)sulfanyl]-2-hydroxypropoxy]-1-hydroxy-9H-xanthen-9-one
-
45.33% inhibition at 0.1 mM
3-[3-[bis(2-hydroxyethyl)amino]-2-hydroxypropoxy]-1-hydroxy-9H-xanthen-9-one
-
100% inhibition at 0.1 mM
3-[4-phenyl-6-(thiophen-2-yl)pyridin-2-yl]phenol
-
53.8% inhibition at 0.1 mM
3-[4-phenyl-6-(thiophen-3-yl)pyridin-2-yl]phenol
-
51.8% inhibition at 0.1 mM
3-[6-(furan-2-yl)-4-phenylpyridin-2-yl]phenol
-
51.6% inhibition at 0.1 mM
3alpha-corosolic acid
-
IC50: 0.083 mM; IC50: 0.089 mM
3beta-corosolic acid
-
IC50: 0.049 mM
4'-(9-acridinylamine)methanesulfon-m-anisidide
-
0.003 mM, 50% inhibition
4'-(9-acridinylamino)methansulfon-m-anisidide
4'-(9-acridinylamino)methansulfon-o-anisidide
-
-
4'-chlorobiphenyl-2,5-diol
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
4,4'-(1,2-dimethyl-1,2-ethanediyl)bis-2,6-piperazinedione
-
i.e.ICRF-193
4,4'-(4-phenylpyridine-2,6-diyl)diphenol
-
76.8% inhibition at 0.1 mM
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl 2-chlorobenzoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl 2-methoxybenzoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl 4-methoxybenzoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl benzoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl butanoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl decanoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl hexanoate
-
4,7-dimethyl-5,6-dioxo-1-(propan-2-yl)-5,6-dihydronaphthalen-2-yl octanoate
-
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-2-yl)thiazole-5-carboxylic acid
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxamide
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxylic acid
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-phenylthiazole-5-carboxylic acid
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-2-yl)thiazole-5-carboxylic acid
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxamide
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxylic acid
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-phenylthiazole-5-carboxylic acid
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-2-yl)thiazole-5-carboxylic acid
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxamide
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxylic acid
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-phenylthiazole-5-carboxylic acid
4-(2,2-dibromoethenyl)-1,2-dimethoxybenzene
-
-
4-(2,6-diphenylpyridin-4-yl)phenol
-
-
4-(3,4,5-trimethoxyphenyl)-1,5-dihydro-3H-furo[3,4-b]carbazol-3-one
-
-
4-(3-amino-6-bromoimidazo[1,2-a]pyridin-2-yl)benzonitrile
-
4-(4,6-diphenylpyridin-2-yl)phenol
-
27.6% inhibition at 0.1 mM
4-(4-chlorophenyl)benzo-1,2-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
4-(4-phenyl-2,2'-bipyridin-6-yl)phenol
-
-
4-(4-phenyl-2,3'-bipyridin-6-yl)phenol
-
18.6% inhibition at 0.1 mM
4-(4-phenyl-2,4'-bipyridin-6-yl)phenol
-
-
4-(5-chlorofuran-2-yl)-2-(3-chlorophenyl)-6-(3-methylthiophen-2-yl) pyridine
-
36% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(3-chlorophenyl)-6-(5-chlorothiophen-2-yl) pyridine
-
41% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(4-chlorophenyl)-6-(3-methylthiophen-2-yl) pyridine
-
40% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(4-chlorophenyl)-6-(5-chlorothiophen-2-yl) pyridine
-
43% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(5-chlorothiophen-2-yl)-6-(furan-2-yl) pyridine
-
40% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(5-chlorothiophen-2-yl)-6-p-tolylpyridine
-
41% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-2-(furan-2-yl)-6-(3-methylthiophen-2-yl) pyridine
-
31% inhibition at 0.02 mM
4-(5-chlorofuran-2-yl)-6-(3-methylthiophen-2-yl)-2,3'-bipyridine
-
25.5% inhibition at 0.02 mM
4-(6-hydroxynaphthalen-2-yl)benzene-1,2-diol
-
4-(6-methoxynaphthalen-2-yl)-2-methylaniline
-
4-(6-methoxynaphthalen-2-yl)aniline
-
4-(6-methoxynaphthalen-2-yl)phenol
-
4-(6-phenyl-2,2'-bipyridin-4-yl)phenol
-
-
4-(6-phenyl-2,3'-bipyridin-4-yl)phenol
-
-
4-(6-phenyl-2,4'-bipyridin-4-yl)phenol
-
8.4% inhibition at 0.1 mM
4-(benzylsulfanyl)-6-[[(2-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
4-(benzylsulfanyl)-6-[[(3-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
4-(furan-2-yl)-2-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-2-yl)-2-(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
-
23.4% inhibition at 0.1 mM
4-(furan-2-yl)-2-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-2-yl)-2-(thiophen-2-yl)-5H-chromeno [4,3-b]pyridine
-
14.1% inhibition at 0.1 mM
4-(furan-2-yl)-2-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
-
-
4-(furan-2-yl)-2-phenyl-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-2-yl)-2-phenyl-5H-chromeno[4,3-b]pyridine
-
11.5% inhibition at 0.1 mM
4-(furan-3-yl)-2-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-3-yl)-2-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-3-yl)-2-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
-
8.4% inhibition at 0.1 mM
4-(furan-3-yl)-2-phenyl-5,6-dihydrobenzo[h]quinoline
-
-
4-(furan-3-yl)-2-phenyl-5H-chromeno[4,3-b]pyridine
-
10.5% inhibition at 0.1 mM
4-(furan-3-yl)-6-(thiophene-2-yl)-[2,4']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
4-(furan-3-yl)-6-(thiophene-3-yl)-[2,4']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
4-(pyridin-2-yl)-2-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-(pyridin-2-yl)-2-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
-
8.5% inhibition at 0.1 mM
4-(pyridin-2-yl)-2-(thiophen-3-yl)-5H-chromeno[4,3-b]pyridine
-
25.3% inhibition at 0.1 mM
4-(thiophene-3-yl)-6-(thiophene-2-yl)-[2,2']-bipyridyl
-
weak inhibitory effects on human DNA Topo II compared to etoposide
4-(thiophene-3-yl)-6-(thiophene-2-yl)-[2,4']-bipyridyl
-
weak inhibitory effects on human DNA Topo II when compared to etoposide
4-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)-3-fluorobenzonitrile
-
-
4-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
-
-
4-chloro-5-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one
-
-
4-chloro-5-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]pyrrolidin-2-one
-
-
4-chloro-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzamide
-
-
4-chloro-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzenesulfonamide
-
-
4-fluoro-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzamide
-
-
4-fluoro-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzenesulfonamide
-
-
4-hydroxy-3-(6-hydroxynaphthalen-2-yl)benzaldehyde
-
4-hydroxy-3-(6-methoxynaphthalen-2-yl)benzaldehyde
-
4-hydroxy-3-[(1E)-1-([[(1E)-1-(4-hydroxy-2-oxo- 2H-chromen-3yl)ethylidene]sulfamoyl]imino)ethyl]-2H-chromen-2-one
-
4-methoxy-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzamide
-
-
4-methoxy-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzenesulfonamide
-
-
4-methoxybenzaldehyde
-
-
4-methoxyphenylpropynoic-3-(1-benzenesulfonyl-1Hindol-3-yl)-allyl ester
-
-
4-N-(2-pyrazinecarboxylic) amino-4'-demethylepipodophyllotoxin
-
-
4-N-(3,4,5-trihydroxybenzoic) amino-4'-demethylepipodophyllotoxin
-
-
4-N-(5-methylpyrazine-2-carboxylic)amino-4'-demethylepipodophyllotoxin
-
-
4-N-(theophylline-7-acetic) amino-4'-demethylepipodophyllotoxin
-
-
4-O-(2-pyrazinecarboxylic)-4'-demethylepipodophyllotoxin
-
-
4-O-(2-quinoline carboxylic)-4'-demethylepipodophyllotoxin
-
-
4-O-(5-methylpyrazine-2-carboxylic)-4'-demethylepipodophyllotoxin
-
-
4-O-(fluoroquinolonic)-4'-demethylepipodophyllotoxin
-
-
4-O-(theophylline-7-acetic)-4'-demethylepipodophyllotoxin
-
-
4-phenyl-2-(pyridin-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-phenyl-2-(pyridin-2-yl)-5H-chromeno[4,3-b]pyridine
-
7.2% inhibition at 0.1 mM
4-phenyl-2-(thiophen-2-yl)-5,6-dihydrobenzo[h]quinoline
-
-
4-phenyl-2-(thiophen-2-yl)-5H-chromeno[4,3-b]pyridine
-
7.5% inhibition at 0.1 mM
4-[2-(furan-2-yl)-6-phenylpyridin-4-yl]phenol
-
30.2% inhibition at 0.1 mM
4-[2-(tert-butylamino)imidazo[1,2-a]pyrimidin-3-yl]benzonitrile
-
4-[2-phenyl-6-(thiophen-2-yl)pyridin-4-yl]phenol
-
-
4-[2-phenyl-6-(thiophen-3-yl)pyridin-4-yl]phenol
-
-
4-[3-(tert-butylamino)imidazo[1,2-a]pyrazin-2-yl]benzoic acid
-
4-[3-(tert-butylamino)imidazo[1,2-a]pyridin-2-yl]benzoic acid
-
4-[3-(tert-butylamino)imidazo[1,2-a]pyridin-2-yl]benzonitrile
-
4-[3-[ethyl(methyl)amino]propyl]furo[3,2-c]phenanthridine-5,10,11(4H)-trione
-
-
4-[4-phenyl-6-(thiophen-2-yl)pyridin-2-yl]phenol
-
35.4% inhibition at 0.1 mM
4-[4-phenyl-6-(thiophen-3-yl)pyridin-2-yl]phenol
-
38.3% inhibition at 0.1 mM
4-[6-(furan-2-yl)-4-phenylpyridin-2-yl]phenol
-
35.2% inhibition at 0.1 mM
4-[[1-(2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-(pyridin-2-yl)-1,3-thiazole-5-carboxamide
4-[[1-(2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-phenyl-1,3-thiazole-5-carboxamide
4-[[1-(7-hydroxy-2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-(pyridin-2-yl)-1,3-thiazole-5-carboxamide
4-[[1-(7-hydroxy-2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-phenyl-1,3-thiazole-5-carboxamide
4-[[1-(7-methoxy-2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-(pyridin-2-yl)-1,3-thiazole-5-carboxamide
4-[[1-(7-methoxy-2-oxo-2H-1-benzopyran-3-yl)-4,5-dihydro-1H-1,2,3-triazol-5-yl]methoxy]-2-phenyl-1,3-thiazole-5-carboxamide
5,8-dihydroxy-4-methoxy-3,6-bis(3-methylbut-2-en-1-yl)-4a,9a-dihydro-1H-xanthene-1,2,9-trione
-
-
5-(2,2-dibromoethenyl)-1,2,3-trimethoxybenzene
-
-
5-(2,2-dibromoethenyl)-1,3-benzodioxole
-
-
5-amino-2-(4-fluorophenyl)benzoxazole
-
5-amino-2-(4-methylbenzyl)benzoxazole
-
5-amino-2-(p-methylbenzyl)benzoxazole
-
5-amino-2-phenylbenzoxazole
-
5-chloro-2-(4-methylphenyl)benzoxazole
-
5-chloro-2-(p-methylphenyl)benzoxalzole
-
5-fluorouracil
-
P388/F11782 cell enzyme, high inhibition
5-methoxy-1,3-bis[(2-methyloxiran-2-yl)methoxy]-7-(oxiran-2-ylmethyl)-9H-xanthen-9-one
-
-
5-methoxy-1,3-bis[(2-methyloxiran-2-yl)methoxy]-7-(propan-2-yl)-9H-xanthen-9-one
-
-
5-nitro-2-(4-nitrobenzyl)benzoxazole
-
5-nitro-2-(p-nitrobenzyl)benzoxazole
-
5-nitro-2-phenoxymethyl-benzimidazole
-
6'-(thiophene-2-yl)-[3,4',2',4'']-terpyridine
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6'-(thiophene-2-yl)-[4,2',4',4'']-terpyridine
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6,11-dihydroxy-3,3-dimethyl-5-(3-methylbut-2-en-1-yl)-3H,7H-pyrano[2,3-c]xanthen-7-one
-
-
6,8-bis(oxiran-2-ylmethoxy)benzo[b][1,8]naphthyridin-5(10H)-one
-
9% and 13% inhibition at 0.02 mM and 0.1 mM, respectively
6,8-bis(thiiran-2-ylmethoxy)benzo[b][1,8]naphthyridin-5(10H)-one
-
8.5% and 7% inhibition at 0.02 mM and 0.1 mM, respectively
6-(2-(2-(dimethylamino)ethylamino)ethylamino)-2-dodecyl-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
6-(2-(2-(dimethylamino)ethylamino)ethylamino)-2-octyl-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
6-(2-(4-methylpiperazin-1-yl)ethylamino)-2-octyl-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
6-(2-(dimethylamino)ethylamino)-2-dodecyl-1H-benzo[de]isoquinoline-1,3(2H)-dione
-
-
6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
6-(3,4-dimethoxyphenyl)naphthalen-2-ol
-
6-(3,4-dimethylphenyl)-3-[[4-[3-(4-methylpiperazin-1-yl)propoxy]phenyl]amino]pyrazine-2-carboxamide
-
-
6-(3-(hydroxymethyl)phenyl)naphthalen-2-ol
-
6-(3-dimethylaminopropyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
6-(4-(1-hydroxyethyl)phenyl)naphthalen-2-ol
-
6-(4-(hydroxymethyl)phenyl)naphthalen-2-ol
-
6-(4-amino-3-methylphenyl)naphthalen-2-ol
-
6-(4-aminophenyl)naphthalen-2-ol
-
6-(4-hydroxy-3-(2-hydroxyethyl)phenyl)naphthalen-2-ol
-
6-(4-hydroxy-3-(hydroxymethyl)phenyl)naphthalen-2-ol
-
6-(4-hydroxyphenyl)naphthalen-2-ol
-
6-(4-nitro-3-(trifluoromethyl)phenyl)naphthalen-2-ol
-
6-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-2,2'-bipyridine
-
39% inhibition at 0.02 mM
6-(5-chlorothiophen-2-yl)-4-(furan-3-yl)-2,3'-bipyridine
-
41% inhibition at 0.02 mM
6-(benzyloxy)-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-(benzylsulfanyl)-4-(butylsulfanyl)-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-(phenylsulfanyl)-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-(propylsulfanyl)-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[(cyclobutylmethyl)sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[(cyclopropylmethyl)sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(2-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(2-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(2-methoxyphenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(2-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(3-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(3-methoxyphenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(3-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(4-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(4-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(benzylsulfanyl)-4-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
-
-
6-(dodecylamino)-2-(3-(4-methylpiperazin-1-yl)propyl)-1H-benzo-[de]isoquinoline-1,3(2H)-dione
-
-
6-(dodecyloxy)-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-(furan-2-yl)-4-(furan-3-yl)-[2,2']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6-(furan-2-yl)-4-(furan-3-yl)-[2,4']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6-(furan-2-yl)-4-(thiophene-2-yl)-[2,4']-bipyridyl
-
weak inhibitory effects on human DNA Topo II compared to etoposide
6-(furan-2-yl)-4-(thiophene-3-yl)-[2,4']-bipyridyl
-
significant inhibitory effects on human DNA Topo II at 20 microM and 100 microM concentration
6-(furan-2-yl)-[3,4',2',4'']-terpyridine
-
weak inhibitory effects on human DNA Topo II compared to etoposide
6-aminohexanoyl-L-lysyl-6-aminohexanoyl amide
-
-
6-butoxy-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-chloro-2-(pyridin-2-yl)imidazo[1,2-a]pyridin-3-amine
-
6-ethoxy-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-hydroxy-8-(thiiran-2-ylmethoxy)-5H-chromeno[2,3-b]pyridin-5-one
-
inhibition in vivo in cancer cells, IC50 values, overview
6-hydroxy-8-(thiiran-2-ylmethoxy)benzo[b][1,8]naphthyridin-5(10H)-one
-
8% and 9% inhibition at 0.02 mM and 0.1 mM, respectively
6-methoxy-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-methoxy-4-(2-[4-[([1,3]oxathiolo[5,4-c]pyridin-6-ylmethyl)amino]piperidin-1-yl]ethyl)quinoline-3-carbonitrile
i.e. GSK299423, it shows potent inhibition of supercoiling by DNA gyrase, enzyme binding mode and structure, overview. The inhibitor bridges the DNA and a transient non-catalytic pocket on the 2fold axis at the GyrA dimer interface, and is close to the active sites and luoroquinolone binding sites. In the inhibitor complex the active site seems poised to cleave the DNA, with a single metal ion observed between the topoisomerase/primase domain and the scissile phosphate; i.e. GSK299423, it shows potent inhibition of supercoiling by DNA gyrase, enzyme binding mode and structure, overview. The inhibitor bridges the DNA and a transient non-catalytic pocket on the 2fold axis at the GyrA dimer interface, and is close to the active sites and luoroquinolone binding sites. In the inhibitor complex the active site seems poised to cleave the DNA, with a single metal ion observed between the topoisomerase/primase domain and the scissile phosphate
6-methoxy-7,8-methylenedioxycoumarin
-
57% inhibition at 0.1 mM
6-[(2-phenylethyl)sulfanyl]-9H-purin-2-amine
6-[(cyclopentylsulfanyl)methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
-
6-[2-(dimethylamino)ethyl]-8-hydroxy-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
moderate inhibition
6-[2-(dimethylamino)ethyl]-8-[3-(dimethylamino)propoxy]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
strong inhibition
6-[3-(dimethylamino)propyl]-8-hydroxy-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
moderate inhibition
6-[4-(dimethylamino)butyl]-8-[2-(dimethylamino)ethoxy]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
weak inhibition
6-[4-(dimethylamino)butyl]-8-[3-(dimethylamino)propoxy]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
weak inhibition
6-[[(1-cyclopentyl-1H-tetrazol-5-yl)sulfanyl]methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
-
6-[[(2E)-3,7-dimethylocta-2,6-dien-1-yl]oxy]-3,8-dimethyl-5-(propan-2-yl)naphthalene-1,2-dione
-
6-[[(5-cyclopropyl-1,3,4-oxadiazol-2-yl)sulfanyl]methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
-
7-(2-(4-methylpiperazin-1-yl)ethyl)benzo[a]phenazin-5(7H)-one
-
7-(2-(diethylamino)ethyl)benzo[a]phenazin-5(7H)-one
-
7-(2-(dimethylamino)ethyl)-3-methoxybenzo[a]phenazin-5(7H)-one
-
7-(2-(dimethylamino)ethyl)benzo[a]phenazin-5(7H)-one
-
7-(2-(piperidin-1-yl)ethyl)benzo[a]phenazin-5(7H)-one
-
7-(2-morpholinoethyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(4-methylpiperazin-1-yl)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(diethylamino)propyl)-3-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(diethylamino)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-10-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-2-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-3,10-dimethoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-3,9-dimethoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-3-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)-9-methoxybenzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(dimethylamino)propyl)benzo[f]pyrido[2,3-b]quinoxalin-5(7H)-one
-
7-(3-(piperidin-1-yl)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-(piperidin-1-yl)propyl)benzo[f]pyrido[2,3-b]quinoxalin-5(7H)-one
-
7-(3-(pyrrolidin-1-yl)propyl)benzo[a]phenazin-5(7H)-one
-
7-(3-morpholinopropyl)benzo[a]phenazin-5(7H)-one
-
7-(4-(diethylamino)butyl)benzo[a]phenazin-5(7H)-one
-
7-(4-(dimethylamino)butyl)benzo[a]phenazin-5(7H)-one
-
7-chloro-1,3-dihydroxyacridone
-
at both 0.2 mM and 0.1 mM, preincubation with the enzyme prior to the addition of DNA leads to the complete loss of DNA binding
7-propylbenzo[a]phenazin-5(7H)-one
-
8-(2-(diethylamino)ethoxy)benzofuro[3,2-g]quinoline-5,11-dione
-
0.05 mM, 100% inhibition. Comparison of cytotoxicity against various human cancer cells
8-(2-dimethylaminoethoxy)-6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
8-(2-dimethylaminoethoxy)-6-(3-dimethylaminopropyl)-6Hindeno[1,2-c]isoquinolin-5,11-dione
-
-
8-[2-(dimethylamino)ethoxy]-6-[2-(dimethylamino)ethyl]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
very strong inhibition
8-[3-(dimethylamino)propoxy]-6-[3-(dimethylamino)propyl]-5H-indeno[1,2-c]isoquinoline-5,11(6H)-dione
-
strong inhibition
9-(2-dimethylaminoethoxy)-6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
9-(2-dimethylaminoethoxy)-6-(3-dimethylaminopropyl)-6Hindeno[1,2-c]isoquinolin-5,11-dione
-
-
9-(2-pyrrolidin-1-ylethoxy)-6-(2-pyrrolidin-1-ylethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
9-(4-hydroxy-3,5-dimethoxyphenyl)-8-oxo-5,5a,6,8,8a,9-hexahydro-2H-furo[3',4':6,7]naphtho[2,3-d][1,3]dioxol-5-yl 4,6-O-ethylidenehexopyranoside
-
-
9-benzenesulfonyl-4-(3,4,5-trimethoxyphenyl)-1,5-dihydro-H-furo[3,4-b]carbazol-3-one
-
-
9-benzenesulfonyl-4-(3,4-dimethoxyphenyl)-1,5-dihydro-3H-furo[3,4-b]carbazol-3-one
-
-
9-benzenesulfonyl-4-(3,4-methylenedioxyphenyl)-1,5-dihydro-3H-furo[3,4-b]carbazol-3-one
-
-
9-benzenesulfonyl-4-(3,5-dimethoxyphenyl)-1,5-dihydro-3H-furo[3,4-b]carbazol-3-one
-
-
9-benzenesulfonyl-4-(4-methoxyphenyl)-1,5-dihydro-3Hfuro[3,4-b]carbazol-3-one
-
-
9-hydroxy-6-(2-dimethylaminoethyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
9-hydroxy-6-(3-dimethylaminopropyl)-6H-indeno[1,2-c]isoquinolin-5,11-dione
-
-
9-Hydroxy-isoellipticine
-
-
Acrylamide
-
acrylamide is a catalytic inhibitor, no enzyme poison, it antagonizes the effect of etoposide, a topoisomerase II poison, and inhibits the enzyme in vivo in V-79 cells. Acrylamide reduces the level of catalytically active cellular topoisomerase II available for the action of etoposide. Assay in presence of DTT
Adenylyl imidodiphosphate
-
-
adenylyl(beta,gamma-methylene)diphosphate
-
-
adenylyl-imidodiphosphate
-
i.e. AMP-PNP. In mixtures of AMP-PNP and ATP, the double-strand passage reaction of the enzyme gets blocked and progressively fewer entanglements are relaxed. A total replacement of ATP by AMP-PNP results in a temporal increase in elasticity at higher frequencies, but no transition to an elastic gel with fixed cross-links
alpha-lapachone
-
inhibits initial non-covalent binding of topoisomerase II to DNA and, in addition, induces religation of DNA breaks, irreversible
alpha-viniferin-13-O-beta-glucopyranoside
-
comparison with inhibition of HindIII enzyme
AMP-PNP
-
structure analysis of a fully-catalytic Saccharomyces cerevisiae topoisomerase II homodimer complexed with DNA and the nonhydrolyzable ATP analogue, overview. The enzyme adopts a domain-swapped configuration wherein the ATPase domain of one protomer sits atop the nucleolytic region of its partner subunit. This organization produces an unexpected interaction between the bound DNA and a conformational transducing element in the ATPase domain, which is critical for both DNA-stimulated ATP hydrolysis and global topoisomerase activity. Three dimerization interfaces can each exist in an associated or dissociated state, giving rise to significant conformational variability within a population
anthocyanidins
-
modulate the enzyme activity and affect cellular DNA integrity, high enzyme inhibition by anthocyanidins with vicinal hydroxyl groups like delphinidin or cyanidin, competitive to ethidium bromide in DNA intercalation
Anticancer drug VP16-213
-
-
apigenin
-
inhibition of enzyme-mediated religation of DNA
ATP
inhibition of the ATP hydrolysis reaction at ATP concentrations higher than 0.3 mM
Barminomycin-like anthracyclines
-
-
BAY 50-7950
-
IC50: 15 mg/l, no substantial inhibitory activity
BAY 50-7952
-
IC50: 60 mg/l, no substantial inhibitory activity
BE-10988
-
the inhibitor is produced by a streptomycete
Benzene
-
enzyme inhibition by benzene and its metabolites represents a potential mechanism by which benzene can induce its chromosome-altering and leukemogenic effects
Benzisoquinolinediones
-
-
-
benzoquinone mustard compounds
-
induce the formation of DNA-protein complexes, quantitative structure-activity analysis, inhibition mechanism, overview
-
beta-lapachone
-
inhibits by inducing religation and dissociation of the enzyme from DNA in presence of ATP, irreversible
betulinic acid
-
IC50: 0.08 mM
bis(2,2-dichloro-6-[[2-(hydroxy-kO)benzylidene]amino-kN]-4H-1,3,2-benzodioxastannin-4-onato)copper(2+)
-
-
bis(2-hydroxy-5-[[2-(hydroxy-kO)benzylidene]amino-kN]benzoato)copper(2+)
-
-
bis(acridin-4-ylmethyl)cyanamide
-
comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
Bisantrene
-
efficiency in patients with breast cancer and acute leukemia
C11-substituted derivatives of azaelliptitoxin
-
-
cisplatin
-
P388/F11782 cell enzyme, high inhibition
CJ-12,371
-
inhibits both DNA supercoiling and relaxation without blocking religation, the inhibitor is isolated from the fermentation broth of an unidentified fungus
CJ-12,372
-
inhibits both DNA supercoiling and relaxation without blocking religation, the inhibitor is isolated from the fermentation broth of an unidentified fungus
colchiceinamide
-
and analogues, 0.1 mM
Colchicine
-
P388/F11782 cell enzyme, high inhibition
conjugated docosahexanoic acid
-
IC50 is 0.01 mM for inhibition of decatenation of kinetoplast DNA
-
conjugated eicosapentaenoic acid
-
irreversible inhibition, IC50 is 0.0025 mM for inhibition of decatenation of kinetoplast DNA, effects on thermal transition of dsDNA, overview
corosolic acid
-
IC50: 0.043 mM
curcumin sulfate
i.e. diferuloylmethane sulfate
cyanidin
-
anthocyanidin, complete inhibition of enzyme, isozyme IIalpha and IIbeta, decatenation activity at 0.01 mM, no stabilization of the DNA-enzyme intermediate in contrast to topoisomerase poisons
cyclophosphamide
-
P388/F11782 cell enzyme, high inhibition
dactinomycin
-
i.e. actinomycin D
daunomycin
-
i.e. daunorubicin
delphinidin
-
anthocyanidin, complete inhibition of enzyme, isozyme IIalpha and IIbeta, decatenation activity at 0.01 mM, no stabilization of the DNA-enzyme intermediate in contrast to topoisomerase poisons
Demethylepipodophyllotoxins
-
-
DMP 840
-
synonym bisnafide
doxorubin
-
i.e. adriamycin
EO9
-
inhibition mechanism
ethyl 2-(4-chlorophenyl)-3-(cyclohexylamino)-1H-imidazo[1,2-b]pyrazole-7-carboxylate
-
ethyl 3-(tert-butylamino)-2-(4-chlorophenyl)-1H-imidazo[1,2-b]pyrazole-7-carboxylate
-
ethyl 3-amino-2-(4-chlorophenyl)-1H-imidazo[1,2-b]pyrazole-7-carboxylate
-
etopophos
-
P388/F11782 cell enzyme, high inhibition
etoposide quinone
-
etoposide quinone inhibits ATP hydrolysis by topoisomerase IIalpha
F11782
-
inhibition of the P388 cell enzyme, mechanism, in vitro resistance of the P388/F11782 cell enzyme to the inhibitor is not associated with a classic multidrug resistance profile, resistant cells show cross-resistance to merbarone and doxorubicin, resistance mechanism
F14512
-
potent inhibitor, decreased sensitivity of L-1210 cells to F14512 in the presence of putrescine, spermidine, and spermine
FEITPEKNPQ
-
inhibits human topoisomerase II activity through binding to the active site of the CTD domain
fluoroquinolones
-
broad-spectrum antimicrobial agents, Ser83 is responsible for sensitivity, mutation S83W and S83L lead to resistance against the agents
-
fomitellic acid A
-
0.1 mM, 95% inhibition
fomitellic acid B
-
0.1 mM, 95% inhibition
GTP-gamma-S
-
allosteric inhibition
hemsleyanol
-
comparison with inhibition of HindIII enzyme
Hoechst 33258
-
bis-imidazole derivative
Hoechst 33342
-
bis-imidazole derivative
hydroquinone
-
hydroquinone inhibits topoII at the DNA binding stage as well as in the closed clamp stage in the catalytic cycle, thereby interfering with either the binding to, or the release of, DNA from the enzyme, inhibition mechanism, overview
hypericin
-
inhibits DNA relaxation activity, potent antagonist of cleavage complex stabilization by chemotherapeutics etoposide and amsacrine
ICRF 187
-
inhibits ATP hydrolysis
ICRF 193
-
inhibits ATP hydrolysis
ICRF187
-
catalytic inhibitor
ICRF193
-
catalytic inhibitor
IETWNPNNKP
-
inhibits human topoisomerase II activity through binding to the active site of the CTD domain
intoplicine
-
molecular interactions of the inhibitor with DNA and topoisomerase II in ternary complexes. Binding modes and biological effects of Intoplicine derivatives
irinotecan
-
P388/F11782 cell enzyme, high inhibition
Isochroman carboxylic acid
-
CJ-12,373, isolated from Penicillium sp. CL22557
-
Lim15/Dmc1
from Coprimus cinereus, a meiosis-specific RecA-like protein, Lim15 inhibits the topoisomerase II activity in vivo, but activates the DNA relaxation and decatenation activity of topoisomerase II in vitro
-
lithocholic acid
-
IC50: 0.015 mM, the lithocholic interaction interface has a pocket comprised of three amino acids, Lys720, Leu760 and Thr791
LU 79553
-
synonym elinafide
lyoniside
-
12% inhibition at 0.1 mM
malvidin
-
anthocyanidin, inhibition of isozyme IIbeta decatenation activity
mAMSA
-
inhibits the religation step and traps Top2 as a covalent complex with the enzyme covalently bound to DNA with broken DNA strands
maslinic acid
-
IC50: 0.092 mM
meglumine antimoniate
-
14% inhibition at 0.0033 mM
menadione
-
inhibition mechanism
meso-2,3-Bis(3,5-dioxopiperazine-1-yl)butane
methotrexate
-
P388/F11782 cell enzyme, low inhibition
methyl 2-(2-hydroxy-4-(6-methoxynaphthalen-2-yl)phenyl)acetate
-
methyl 2-(2-hydroxy-5-(6-hydroxynaphthalen-2-yl)phenyl)acetate
-
methyl 2-(4-(6-methoxynaphthalen-2-yl)phenyl)acetate
-
methyl 2-hydroxy-2-(4-(6-methoxynaphthalen-2-yl)phenyl)acetate
-
methyl 2-hydroxy-4-(6-methoxynaphthalen-2-yl)benzoate
-
methyl 2-hydroxy-5-(6-methoxynaphthalen-2-yl)benzoate
-
methyl 3-(1,3-benzodioxol-5-yl)prop-2-ynoate
-
-
methyl 3-(3,4,5-trimethoxyphenyl)prop-2-ynoate
-
-
methyl 3-(3,4-dimethoxyphenyl)prop-2-ynoate
-
-
methyl 3-(4-methoxyphenyl)prop-2-ynoate
-
-
methyl 3-(6-hydroxynaphthalen-2-yl)-4-methylbenzoate
-
methyl 3-(6-methoxynaphthalen-2-yl)-4-methylbenzoate
-
methyl 4-(6-methoxynaphthalen-2-yl)benzoate
-
methyl 4-hydroxy-3-(6-hydroxynaphthalen-2-yl)benzoate
-
methyl 4-hydroxy-3-(6-methoxynaphthalen-2-yl)benzoate
-
methyl N-(4'-(9-acridinylamino)-2-methoxy-phenyl)carbamate hydrochloride
-
methyl N-(4'-(9-acridinylamino)-phenyl) carbamate hydrochloride
-
N,N'-bis[2-(5-nitro-1,3-dioxo-2,3-dihydro-1H-benz[de]-isoquinolin-2-yl)]butylaminoethyl-2-propanediamine
-
-
N,N'-bis[2-(5-nitro-1,3-dioxo-2,3-dihydro-1H-benz[de]-isoquinolin-2-yl)]propane-2-ethanediamine
-
-
N,N'-diphenyl-N-[(2E)-3-phenylprop-2-en-1-yl]-urea
-
-
N,N,N',N'-tetrakis(acridin-4-ylmethyl)butane-1,4-diamine
-
compound shows in addition in vitro proteasome inhibition properties. Comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N,N,N',N'-tetrakis(acridin-4-ylmethyl)ethane-1,2-diamine
-
comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N,N,N',N'-tetrakis[(7-bromo-9-chloroacridin-4-yl)methyl]butane-1,4-diamine
-
comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N,N,N',N'-tetrakis[(9-aminoacridin-4-yl)methyl]ethane-1,2-diamine
-
compound shows in addition in vitro proteasome inhibition properties. Comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N,N-diethyl-9-([2-(1H-indol-3-yl)ethyl]amino)acridine-3-carboxamide
-
-
N,N-dimethyl(6-methyl-10,11-dioxo-10,11-dihydrophenanthro[1,2-b]furan-1-yl)methanaminium (2E)-3-carboxyprop-2-enoate
-
-
-
N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)-1-phenylmethanesulfonamide
-
-
N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)-2-phenylacetamide
-
-
N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzamide
-
-
N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzenesulfonamide
-
-
N-(4'-(9-acridinylamino)-3-methoxy-phenyl) methane sulfonamide
-
N-(4-chlorobenzyl)-1-(5-nitrothiazol-2-yl)piperidin-4-amine
-
-
N-(4-chlorophenyl)-N-[(2E)-3-phenylprop-2-en-1-yl]urea
-
-
N-(4-fluorobenzyl)-1-(5-nitrothiazol-2-yl)piperidin-4-amine
-
-
N-(4-fluorphenyl)-N-[(2E)-3-phenylprop-2-en-1-yl]urea
-
-
N-(4-methoxybenzyl)-1-(5-nitrothiazol-2-yl)piperidin-4-amine
-
-
N-(4-methoxyphenyl)-N-[(2E)-3-phenylprop-2-en-1-yl]urea
-
-
N-(4-methylphenyl)-N-[(2E)-3-phenylprop-2-en-1-yl]urea
-
-
N-(acridin-1-ylmethyl)-N,N',N'-tris(acridin-2-ylmethyl)octane-1,8-diamine
-
comparison with inhibition of calpain, chymotrypsin, cathepsin B, trypsin
N-([3-[(methanesulfonyl)amino]phenyl]methyl)-1H-indazole-3-carboxamide
-
-
N-([4-[(methylsulfamoyl)methyl]phenyl]methyl)-1H-indazole-3-carboxamide
-
-
N-benzyl-1-(5-nitrothiazol-2-yl)piperidin-4-amine
-
-
N-benzyladriamycin
-
inhibits by preventing the initial non-covalent binding of topoisomerase II to DNA
N-methyl-5-demethyl ellipticine
the compound inhibits DNA cleavage without altering the ability of topoisomerase IIalpha to bind its DNA substrate
N-tert-butyl-2-(1H-pyrrol-2-yl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-(2-chlorophenyl)imidazo[1,2-a]pyrazin-3-amine
-
N-tert-butyl-2-(3-methoxyphenyl)imidazo[1,2-a]pyrazin-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)-7-methylimidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)-9H-imidazo[1,2-a]benzimidazol-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)imidazo[1,2-a]pyrazin-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-(4-chlorophenyl)imidazo[1,2-a]pyrimidin-3-amine
-
N-tert-butyl-2-(naphthalen-1-yl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-(pyridin-2-yl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-phenylimidazo[1,2-a]pyrazin-3-amine
-
N-tert-butyl-2-phenylimidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-propylimidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-2-[4-(dimethylamino)phenyl]imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-6-chloro-2-(4-chlorophenyl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butyl-6-chloro-2-(4-fluorophenyl)imidazo[1,2-a]pyridin-3-amine
-
N-tert-butylimidazo[1,2-a]pyrazin-3-amine
-
N-tert-butylimidazo[1,2-a]pyridin-3-amine
-
N-Trifluoroacetyldoxorubicin-14 valerate
-
-
N-[(1E)-1-(4-hydroxy-2-oxo-2H-chromen-3-yl)ethylidene]aminosulfonamide
-
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]methanesulfonamide
-
-
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]methanesulfonohydrazide
-
-
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]propane-1-sulfonamide
-
-
N-[3-[(methanesulfonyl)amino]propyl]-1H-indazole-3-carboxamide
-
-
N-[4-[(methanesulfonyl)amino]-3-methylphenyl]-1H-indazole-3-carboxamide
-
-
N-[4-[(methanesulfonyl)amino]phenyl]-1H-indazole-3-carboxamide
-
-
N2-(1,3-benzothiazol-6-yl)-N6-cycloheptyl-5,9-dihydro-4H-purine-2,6-diamine
-
N2-(1,3-benzothiazol-6-yl)-N6-cyclohexyl-9H-purine-2,6-diamine
-
-
N2-(1,3-benzothiazol-6-yl)-N6-tert-butyl-5,9-dihydro-4H-purine-2,6-diamine
-
N2-(1,3-benzothiazol-6-yl)-N6-tert-butyl-9H-purine-2,6-diamine
-
-
N2-(4-fluorophenyl)-6-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
-
N2-(4-fluorophenyl)-6-[[(1-propyl-1H-imidazol-2-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
-
N2-(4-fluorophenyl)-6-[[(1H-1,2,4-triazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
-
-
N2-(4-fluorophenyl)-6-[[(1H-tetrazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
-
N6-tert-butyl-8-ethyl-N2-[2-[2-(morpholin-4-yl)ethoxy]quinolin-6-yl]-5,9-dihydro-4H-purine-2,6-diamine
neoamphimedine
-
a marine alkaloid from Xestospongia sp., potently inhibits TopoIIalpha-dependent DNA decatenation in the presence of Metnase , circumvents DNA repair protein metnase-enhanced DNA topoisomerase IIalpha activity through ATP-competitive inhibition by binding ata the N-terminal ATPase sites of TopoIIalpha, key interactions observed with neoamphimedine are a network of hydrogen bonds with Ser148, Ser149, and Asn150, and with Asn91 through an ordered water molecule , molecular modeling, oveview
nitric oxide
-
NO, unlike VP-16, preferentially induces the formation of TOP2beta cleavable complexes in cells, induces skin melanomas formation in 7,12-dimethyl-benz[a]anthracene-initiated mice
nudiposide
-
9% inhibition at 0.1 mM
o-Quinone analogues of podophyllotoxin possessing various C-4 beta-aniline moieties
-
-
-
ofloxacin
-
IC50 for the wild-type enzyme is 0.018 mg/ml and 0.4 mg/ml for the mutant 10 enzyme
oleanolic acid
-
IC50: 0.081 mM
pelargonidin
-
anthocyanidin, inhibition of isozyme IIbeta decatenation activity
Peptide fragments of DNA topoisomerase II with helix-forming and coiled-coil-forming properties
-
-
-
potassium antimonyl tartrate
-
10% inhibition at 0.0033 mM
potassium glutamate
-
1 M, inhibition of relaxation activity
procyanidin B2
-
potentiating interactions between procyanidin B2 and epicatechin gallate, myricetin and resveratrol
prodigiosin
-
red pigment of Serratia marcescens with apoptotic activity, anti-tumor drug, induces Cu2+-mediated pH-dependent DNA damage, inhibits the enzyme in vitro and in vivo by binding and intercalation with the DNA
Ro-61-6653
-
IC50: 60 mg/l, no substantial inhibitory activity
ruthenium benzene
-
inhibition of enzyme activity and anti-HIV-1 activity in Sup-T1 cells at nanomolar concentrations. Complete inhibition of proviral DNA synthesis as well as the formation of pre-integration complexes
S-[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl] hydrogen carbonothioate
-
-
S35047
-
a phenyl derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
S35794
-
a derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
S36699
-
a derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
S36888
-
a derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
S36889
-
a derivative of 8-[2-(dialkylamino)ethoxy]-2,3-dimethoxy-5H-10H-indenol[1,2-b]indol-10-one-O-propynyl-oxime core structure, inhibition of topoisomerase II, intercalation with DNA causes cytoxic activity
scopoletin
-
16% inhibition at 0.1 mM
Selenite
-
selenite induces topoisomerase II-DNA complexes in K562 cells
single-stranded DNA
-
strong inhibition of relaxation
sodium antimonyl(III) gluconate
-
IC50 is 0.0028 mM
sodium stibogluconate
-
IC50 is 0.0027 mM
Symadex
-
i.e. C-1311, reduced inhibition of the enzyme in vincristine-resistant cells
tanshinone-1
-
less than 10% inhibition at 0.005 mM
tert-butoxycarbonyl-(L-lysyl-benzyloxycarbonyl)-6-aminohexanoyl amide
-
-
tert-butoxycarbonyl-6-aminohexanoyl-(L-lysyl-benzyloxycarbonyl)-6-aminohexanoyl amide
-
-
tert-butoxycarbonyl-6-aminohexanoyl-(L-lysyl-benzyloxycarbonyl)-methoxy-6-aminohexanoate
-
-
tert-butoxycarbonyl-6-aminohexanoyl-L-lysyl-methoxy-6-aminohexanoate
-
-
tert-butoxycarbonyl-L-lysyl-6-aminohexanoyl amide
-
-
thiomorpholide amido methyl ferrocene
-
topotecan
-
P388/F11782 cell enzyme, high inhibition
vanadate
-
inhibition of wild-type enzyme, no inhibition of mutant R162K, R162Q and Y165S, inhibition mechanism
VFDGEL
-
inhibits human topoisomerase II activity through binding to the active site of the CTD domain
vinblastine
-
P388/F11782 cell enzyme, high inhibition
vinflunine
-
P388/F11782 cell enzyme, high inhibition
vinorelbine
-
P388/F11782 cell enzyme, high inhibition
y, Namen korrigieren: 4-chloro-5-(furan-2-yl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]pyrrolidin-2-one
Z-DNA
-
inhibits relaxation of closed circular supercoiled DNA
-
zinc bis(2-[(E)-[(2,2-dichloro-4-oxo-4H-1,3,2-benzodioxastannin-6-yl)imino]methyl]phenolate)
-
-
zinc bis(2-[(E)-[(3-carboxy-4-hydroxyphenyl)imino]methyl]phenolate)
-
-
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl 4-methylpiperazine-1-carbodithioate
-
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl cyclohexyl(methyl)carbamodithioate
-
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl piperidine-1-carbodithioate
-
{1,1',1'',1'''-[(1,4-dihydroporphyrin-5,10,15,20-tetrayl-k4N21,N22,N23,N24)tetrakis(benzene-4,1-diylmethanediyl)]tetrakis[1-methylpiperidiniumato(2-)]}nickel(4+) tetraiodide
-
strong inhibition
{2,2',2'',2''',2'''',2''''',2'''''',2'''''''-[(5,28-dihydro-29H,31H-tetrabenzoporphine-2,3,9,10,16,17,23,24-octayl-k4N29,N30,N31,N32)octasulfanediyl]octakis(N,N-diethyl-N-methylethanaminiumato)(2-)}zinc(8+) octaiodide
-
strong inhibition
(+)-9-demethyleleutherin
-
-
(+)-9-demethyleleutherin
-
-
(+)-deoxyeleutherin
-
-
(-)-deoxyeleutherin
-
-
(-)-epicatechin
-
-
(-)-epicatechin
-
98% inhibition at 0.1 mM
(-)-epigallocatechin
-
-
(-)-epigallocatechin
-
redox-dependent topoisomerase II poison
(-)-epigallocatechin gallate
-
redox-dependent topoisomerase II poison
(-)-epigallocatechin gallate
-
redox-dependent topoisomerase II poison that acts by covalently adducting to the enzyme, inhibits the DNA cleavage activities of topoisomerase IIalpha and beta when incubated with either enzyme prior to the addition of DNA, exposure of (-)-epigallocatechin gallate to dithiothreitol prior to its addition to DNA cleavage assays abrogates the effects of the catechin on DNA scission
(1R,3R)-8-methoxy-1-methyl-5,10-dioxo-3,4,5,10-tetrahydro-1H-benzo[g]isochromene-3-carboxylic acid
-
-
(1R,3R)-8-methoxy-1-methyl-5,10-dioxo-3,4,5,10-tetrahydro-1H-benzo[g]isochromene-3-carboxylic acid
-
-
(1R,3S)-1,3,8-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(1R,3S)-1,3,8-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(1R,3S)-7,9-dimethoxy-1,3,6-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(1R,3S)-7,9-dimethoxy-1,3,6-trimethyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-3-methyl-7,9-bis(propan-2-yloxy)-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-3-methyl-7,9-bis(propan-2-yloxy)-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-7,9-dihydroxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-7,9-dihydroxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-7,9-dimethoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-7,9-dimethoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-9-hydroxy-7-methoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
(3S)-9-hydroxy-7-methoxy-3-methyl-3,4-dihydro-1H-benzo[g]isochromene-5,10-dione
-
-
1,4-benzoquinone
-
a topoisomerase II poison in vivo and in vitro, enhances cleavage activity, inhibits ligation activity, at 0.025 mM, 1,4-hydroquinone has a higher inhibitory effect on ligation activity but a lower effect on cleavage activity compared to 1,4-benzoquinone
1,4-benzoquinone
-
inhibition by blocking the N-terminal gate of enzyme
1,4-hydroquinone
-
inhibition mechanism
1,4-hydroquinone
-
physiological precursor of 1,4-benzoquinone, a topoisomerase II poison, enhances cleavage activity, inhibits ligation activity, at 0.25 mM, alters the enzyme's cleavage site specificity, 1,4-hydroquinone has a higher inhibitory effect on ligation activity but a lower effect on cleavage activity compared to 1,4-benzoquinone
1-(4-nitrobenzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide
-
-
1-(4-nitrobenzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide
-
-
1-(4-nitrobenzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide
-
1-(4-nitrobenzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide
-
-
2-(4-chlorophenyl)benzo-1,4-quinone
-
inhibits DNA religation by isoform IIalpha by blocking the N-terminal gate of the enzyme by cross-linking cross-linking its two protomer subunits
2-(4-chlorophenyl)benzo-1,4-quinone
-
inhibition by blocking the N-terminal gate of enzyme
2-(furan-2-yl)-3-[2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxyacetamido]-thiazolidin-4-one
-
-
2-(furan-2-yl)-3-[2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxyacetamido]-thiazolidin-4-one
-
3-chloro-4-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] azetidin-2-one
-
3-chloro-4-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] azetidin-2-one
-
-
4'-(9-acridinylamino)methansulfon-m-anisidide
-
epipodophyllotoxin-resistant line, VpmR-5, is not inhibited
4'-(9-acridinylamino)methansulfon-m-anisidide
-
-
4'-(9-acridinylamino)methansulfon-m-anisidide
-
-
4'-(9-acridinylamino)methansulfon-m-anisidide
-
and related quinoline carboxamides
4'-(9-acridinylamino)methansulfon-m-anisidide
-
epipodophyllotoxin-resistant line, VpmR-5, is not inhibited
4'-(9-acridinylamino)methansulfon-m-anisidide
-
-
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-2-yl)thiazole-5-carboxylic acid
-
-
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-2-yl)thiazole-5-carboxylic acid
-
-
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxamide
-
-
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxamide
-
-
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxylic acid
-
-
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxylic acid
-
-
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-phenylthiazole-5-carboxylic acid
-
-
4-((1-(2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-phenylthiazole-5-carboxylic acid
-
-
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-2-yl)thiazole-5-carboxylic acid
-
-
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-2-yl)thiazole-5-carboxylic acid
-
-
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxamide
-
-
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxamide
-
-
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxylic acid
-
-
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxylic acid
-
-
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-phenylthiazole-5-carboxylic acid
-
-
4-((1-(7-hydroxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-phenylthiazole-5-carboxylic acid
-
-
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-2-yl)thiazole-5-carboxylic acid
-
-
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-2-yl)thiazole-5-carboxylic acid
-
-
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxamide
-
-
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxamide
-
-
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxylic acid
-
-
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-(pyridin-3-yl)thiazole-5-carboxylic acid
-
-
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-phenylthiazole-5-carboxylic acid
-
-
4-((1-(7-methoxy-2-oxo-2H-chromen-3-yl)-1H-1,2,3-triazol-5-yl)methoxy)-2-phenylthiazole-5-carboxylic acid
-
-
4-[[1-(2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-(pyridin-2-yl)-1,3-thiazole-5-carboxamide
-
-
4-[[1-(2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-(pyridin-2-yl)-1,3-thiazole-5-carboxamide
-
-
4-[[1-(2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-phenyl-1,3-thiazole-5-carboxamide
-
-
4-[[1-(2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-phenyl-1,3-thiazole-5-carboxamide
-
-
4-[[1-(7-hydroxy-2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-(pyridin-2-yl)-1,3-thiazole-5-carboxamide
-
-
4-[[1-(7-hydroxy-2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-(pyridin-2-yl)-1,3-thiazole-5-carboxamide
-
-
4-[[1-(7-hydroxy-2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-phenyl-1,3-thiazole-5-carboxamide
-
-
4-[[1-(7-hydroxy-2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-phenyl-1,3-thiazole-5-carboxamide
-
-
4-[[1-(7-methoxy-2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-(pyridin-2-yl)-1,3-thiazole-5-carboxamide
-
-
4-[[1-(7-methoxy-2-oxo-2H-1-benzopyran-3-yl)-1H-1,2,3-triazol-5-yl]methoxy]-2-(pyridin-2-yl)-1,3-thiazole-5-carboxamide
-
-
4-[[1-(7-methoxy-2-oxo-2H-1-benzopyran-3-yl)-4,5-dihydro-1H-1,2,3-triazol-5-yl]methoxy]-2-phenyl-1,3-thiazole-5-carboxamide
-
-
4-[[1-(7-methoxy-2-oxo-2H-1-benzopyran-3-yl)-4,5-dihydro-1H-1,2,3-triazol-5-yl]methoxy]-2-phenyl-1,3-thiazole-5-carboxamide
-
-
6-[(2-phenylethyl)sulfanyl]-9H-purin-2-amine
-
-
6-[(2-phenylethyl)sulfanyl]-9H-purin-2-amine
-
7-methoxyeleutherin
-
-
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00025 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00025 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00006 mg/ml
ABT-719
Citrobacter spp.
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00012 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00025 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00012 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00012 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00025 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.000008 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.000003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00025 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.000015 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.016 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.000015 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00025 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00025 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00012 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.000015 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00006 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.000015 mg/ml for strain CiproS, 0.00025 mg/ml for strain CiproR, and 0.001 mg/ml for the methicillin-resistant strain
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml for the wild-type and 0.00025 mg/ml for the methicillin-resistant strain
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00006 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml for the wild-type strain and for the strain Pen I/R
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
ABT-719
-
i.e. A-86719.1 or 8-(3-(S)-aminopyrrolidin-1-yl)-1-cyclopropyl-7-fluoro-9-methyl-4H-4-oxo-quinolizine-3-carboxylic acid hydrochloride monohydrate, in vitro evaluation, 2-pyrisone derivative, MIC90 is 0.00003 mg/ml
Aclarubicin
-
-
Aclarubicin
i.e. NCI0654508
Aclarubicin
-
catalytic topo II inhibitor
Aclarubicin
-
inhibits enzyme binding to the DNA substrate
actinomycins
-
-
-
actinomycins
-
actinomycin D
-
ADP
-
traps the wild-type enzyme in the closed clamp formation, which shows no ATPase activity
ADP
-
traps the wild-type enzyme in the closed clamp formation, which shows no ATPAse hydrolysis activity
adriamycin
-
-
adriamycin
-
enzyme targeting anticancer drug, inhibits in vitro and in vivo, inhibition is 8fold increased by cell transfection with the E1A vector
amsacrine
-
weak inhibition of DNA cleavage at some sites, primarily inhibition of DNA ligation, low sensitivity for the drug
amsacrine
-
reduced inhibition of the enzyme in vincristine-resistant cells
amsacrine
-
topo II poison
aurintricarboxylic acid
-
-
aurintricarboxylic acid
-
-
aurintricarboxylic acid
-
-
azalactone ferrocene
-
inhibition of enzyme activity and anti-HIV-1 activity in Sup-T1 cells at nanomolar concentrations. Complete inhibition of proviral DNA synthesis as well as the formation of pre-integration complexes
-
azalactone ferrocene
-
specific inhibition of DNA passage and ATPase activities of isozyme IIbeta with IC50 of 0.1 mM, inhibition mechanism via complex formation, overview
-
benzoquinone
-
alkylating agent, inhibits isozyme IIalpha via DNA cross-linking, forms cysteine sulfhydryl adducts, inhibits cell growth in vivo, which is 10fold increased in absence of cysteine, quantitative structure-activity analysis, structure of DNA binding, overview, inhibition mechanism
benzoquinone
-
inhibits DNA religation and blocks N-terminal gate of the protein by cross-linking its two protomer subunits. Adduction at C392 and C405 of protein is important for its action
Berenil
-
-
bisdioxopiperazine
-
inhibition of wild-type enzyme and mutant R162K, inhibition mechanism
bisdioxopiperazine
-
inhibits the ATPase activity of the wild-type enzyme
bisdioxopiperazine
-
inhibits the ATPase activity of the wild-type enzyme
Bisdioxopiperazines
-
-
-
Bisdioxopiperazines
-
-
-
camptothecin
-
-
camptothecin
-
34% inhibition at 0.5 mM
camptothecin
-
P388/F11782 cell enzyme, high inhibition
Ciprofloxacin
-
MIC90 is 0.0005 mg/ml
Ciprofloxacin
-
MIC90 is 0.016 mg/ml
Ciprofloxacin
-
MIC90 is 0.032 mg/ml
Ciprofloxacin
-
MIC90 is 0.00012 mg/ml
Ciprofloxacin
Citrobacter spp.
-
MIC90 is 0.00003 mg/ml
Ciprofloxacin
-
MIC90 is 0.016 mg/ml
Ciprofloxacin
-
MIC90 is 0.0005 mg/ml
Ciprofloxacin
-
MIC90 is 0.002 mg/ml
Ciprofloxacin
-
MIC90 is 0.002 mg/ml
Ciprofloxacin
-
MIC90 is 0.064 mg/ml
Ciprofloxacin
-
MIC90 is 0.000015 mg/ml
Ciprofloxacin
-
inhibits wild-type enzyme completely at 0.01 mM, 50% inhibition of the mutant S83W at about 0.065 mM
Ciprofloxacin
-
MIC90 is 0.00003 mg/ml
Ciprofloxacin
-
40fold higher selectivity for Leishmania panamensis enzyme over human macrophage enzyme
Ciprofloxacin
a topoisomerase II inhibitor
Ciprofloxacin
-
MIC90 is 0.00006 mg/ml
Ciprofloxacin
-
MIC90 is 0.00025 mg/ml
Ciprofloxacin
-
40fold higher selectivity for Leishmania panamensis enzyme over human macrophage enzyme
Ciprofloxacin
-
MIC90 is 0.002 mg/ml
Ciprofloxacin
-
MIC90 is 0.00003 mg/ml
Ciprofloxacin
-
MIC90 is 0.00003 mg/ml
Ciprofloxacin
-
MIC90 is 0.016 mg/ml
Ciprofloxacin
-
weak inhibition of TopoNM with IC50 of 0.125 mg/ml
Ciprofloxacin
-
MIC90 is 0.00006 mg/ml
Ciprofloxacin
-
MIC90 is 0.004 mg/ml
Ciprofloxacin
-
MIC90 is 0.016 mg/ml
Ciprofloxacin
-
MIC90 is 0.00006 mg/ml
Ciprofloxacin
-
MIC90 is 0.00006 mg/ml
Ciprofloxacin
-
MIC90 is 0.00012 mg/ml
Ciprofloxacin
-
MIC90 is 0.0005 mg/ml
Ciprofloxacin
-
IC50 for the wild-type enzyme is 0.008 mg/ml and 0.4 mg/ml for the mutant 10 enzyme
Ciprofloxacin
-
MIC90 is 0.00006 mg/ml
Ciprofloxacin
-
MIC90 is 0.00025 mg/ml
Ciprofloxacin
-
MIC90 is 0.0005 mg/ml for strain CiproS, 0.064 mg/ml for strain CiproR, and 0.128 mg/ml for the methicillin-resistant strain
Ciprofloxacin
a fluoroquinolone, enzyme binding mode and structure, overview; a fluoroquinolone, enzyme binding mode and structure, overview
Ciprofloxacin
-
MIC90 is 0.00025 mg/ml for the wild-type and 0.032 mg/ml for the methicillin-resistant strain
Ciprofloxacin
-
MIC90 is 0.002 mg/ml
Ciprofloxacin
-
MIC90 is 0.002 mg/ml for the wild-type strain and for the strain Pen I/R
Ciprofloxacin
-
MIC90 is 0.002 mg/ml
Ciprofloxacin
-
MIC90 is 0.002 mg/ml
clinafloxacin
-
MIC90 is 0.00006 mg/ml
clinafloxacin
-
MIC90 is 0.00025 mg/ml
clinafloxacin
-
MIC90 is 0.0005 mg/ml
clinafloxacin
-
MIC90 is 0.00012 mg/ml
clinafloxacin
Citrobacter spp.
-
MIC90 is 0.00003 mg/ml
clinafloxacin
-
MIC90 is 0.00025 mg/ml
clinafloxacin
-
MIC90 is 0.00025 mg/ml
clinafloxacin
-
MIC90 is 0.00012 mg/ml
clinafloxacin
-
MIC90 is 0.00025 mg/ml
clinafloxacin
-
MIC90 is 0.002 mg/ml
clinafloxacin
-
MIC90 is 0.000015 mg/ml
clinafloxacin
-
MIC90 is 0.000003 mg/ml
clinafloxacin
-
MIC90 is 0.00003 mg/ml
clinafloxacin
-
MIC90 is 0.00012 mg/ml
clinafloxacin
-
MIC90 is 0.00012 mg/ml
clinafloxacin
-
MIC90 is 0.000015 mg/ml
clinafloxacin
-
MIC90 is 0.00003 mg/ml
clinafloxacin
-
MIC90 is 0.064 mg/ml
clinafloxacin
-
MIC90 is 0.000015 mg/ml
clinafloxacin
-
MIC90 is 0.00025 mg/ml
clinafloxacin
-
MIC90 is 0.00025 mg/ml
clinafloxacin
-
MIC90 is 0.00003 mg/ml
clinafloxacin
-
MIC90 is 0.00003 mg/ml
clinafloxacin
-
MIC90 is 0.00003 mg/ml
clinafloxacin
-
MIC90 is 0.00025 mg/ml
clinafloxacin
-
MIC90 is 0.00003 mg/ml
clinafloxacin
-
MIC90 is 0.00006 mg/ml
clinafloxacin
-
MIC90 is 0.00003 mg/ml for strain CiproS, 0.001 mg/ml for strain CiproR, and 0.001 mg/ml for the methicillin-resistant strain
clinafloxacin
-
MIC90 is 0.00003 mg/ml for the wild-type and 0.001 mg/ml for the methicillin-resistant strain
clinafloxacin
-
MIC90 is 0.00025 mg/ml
clinafloxacin
-
MIC90 is 0.00012 mg/ml for the wild-type strain and 0.00025 mg/ml for the strain Pen I/R
clinafloxacin
-
MIC90 is 0.00006 mg/ml
clinafloxacin
-
MIC90 is 0.00006 mg/ml
Clorobiocin
-
-
coralyne
-
potent inhibitor of both human and leishmania panamensis enzyme
coralyne
-
potent inhibitor of both human and leishmania panamensis enzyme
coumermycin
-
coumermycin A1
coumermycin
-
concentration required to observe inhibition with the eukaryotic enzyme is much higher than those needed to inhibit bacterial gyrase
coumermycin
-
coumermycin A1
coumermycin
-
coumermycin A1
coumermycin
-
concentration required to observe inhibition with the eukaryotic enzyme is much higher than those needed to inhibit bacterial gyrase; coumermycin A1
coumermycin
-
coumermycin A1
coumermycin
-
no inhibition
coumermycin
-
coumermycin A
coumermycin
-
coumermycin A2
coumermycin
-
coumermycin A2
CP-115953
-
-
daunorubicin
-
-
daunorubicin
-
comparison with inhibition of HindIII enzyme
deoxynanaomycin A
-
-
dexrazoxane
-
inhibition of wild-type enzyme, no inhibition of mutant enzymes Y50F, Y165S and L169F, partial inhibition of mutant enzymes L169I, R162Q and R162K
dexrazoxane
-
i.e, ICRF-187
doxorubicin
-
-
doxorubicin
-
anti-cancer drug
doxorubicin
-
0.05 mM, 100% inhibition
doxorubicin
-
also called adriamycin
doxorubicin
-
topo II poison
doxorubicin
-
the presence of the formamidino group in the doxorubicin molecule reduced its ability to stimulate DNA cleavage by DNA topoisomerase II
doxorubicin
-
the presence of the formamidino group in the doxorubicin molecule reduced its ability to stimulate DNA cleavage by DNA topoisomerase II
doxorubicin
-
model of binding to enzyme
EDTA
-
-
EDTA
Paramecium bursaria chlorella virus
-
-
eleutherin
-
inhibits by inducing religation and dissociation of the enzyme from DNA in presence of ATP
ellagic acid
-
15.7fold higher selectivity human macrophage for enzyme over Leishmania panamensis enzyme
ellagic acid
-
15.7fold higher selectivity human macrophage for enzyme over Leishmania panamensis enzyme
ellipticine
-
ellipticine
i.e. 5,11-dimethyl-6H-pyrido[4,3-b]carbazole
ellipticines
-
-
ellipticines
-
mechanism of drug action, characterization of the interaction between ellipticine and the enzyme
enoxacin
-
592fold higher selelctivity for Leishmania panamensis enzyme over human macrophage enzyme
enoxacin
-
592fold higher selelctivity for Leishmania panamensis enzyme over human macrophage enzyme
epirubicin
-
a so called topoisomerase poison, which stabilizes the enzyme-linked double-strand break, that is otherwise transient and rapidly religated
epirubicin
-
a so called topoisomerase poison, which stabilizes the enzyme-linked double-strand break, that is otherwise transient and rapidly religated
Ethidium bromide
-
0.6 mg/l, 50% inhibition
etoposide
-
inhibits the enzyme at the DNA relaxation step
etoposide
-
0.07 mM, 50% inhibition
etoposide
-
weak inhibition of DNA cleavage at some sites, primarily inhibition of DNA ligation, low sensitivity for the drug
etoposide
-
belongs to the epipodophyllotoxins, inhibitors of eukaryotic enzymes, inhibits the S83W mutant enzyme, but not the wild-type bacterial enzyme
etoposide
-
IC50: 0.05 mM
etoposide
-
anti-cancer drug, the enzyme inhibition by etoposide is not influenced by the divalent cation
etoposide
-
i.e. VP-16, enzyme targeting anticancer drug, inhibits in vitro and in vivo, inhibition is 16fold increased by cell transfection with the E1A vector
etoposide
-
anti-cancer drug
etoposide
-
inhibition of enzyme-mediated religation of DNA
etoposide
-
geminal protons of the A-ring, the H5 and H8 protons of the B-ring, and the H2 and H6 protons and the 3- and 5-methoxyl protons of the pendent E-ring interact with enzyme in the binary protein-ligand complex. No significant nuclear Overhauser enhancement signals arise from the C-ing, the D-ring, or the C4 glycosidic moiety
etoposide
-
0.05 mM, 100% inhibition
etoposide
-
Topoisomerase II inhibitor added for measuring the inhibition of DNA relaxation
etoposide
-
78% inhibition at 0.1 mM
etoposide
-
70% inhibition at 0.1 mM
etoposide
-
29% inhibition at 0.02 mM, 53% at 0.1 mM
etoposide
-
inhibits ADP and T segment release
etoposide
-
inhibits the religation step and traps Top2 as a covalent complex with the enzyme covalently bound to DNA with broken DNA strands
etoposide
-
etoposide is a widely prescribed anticancer drug that stabilizes covalent topoisomerase II-cleaved DNA complexes. The drug contains a polycyclic ring system, a glycosidic moiety at C4, and a pendant ring at C1. Interactions between topoisomerase IIalpha and etoposide in the binary enzyme-drug complex are mediated by substituents on the A-, B-, and E-rings of etoposide. The D-ring alterations all decrease the ability of etoposide to enhance DNA cleavage mediated by the enzyme in vitro and in cultured cells, and also weaken etoposide binding in the ternary enzyme-drug-DNA complex and altered sites of enzyme-mediated DNA cleavage. NMR spectroscopic interaction analysis, overview
etoposide
-
very strong inhibition
etoposide
-
77.7% inhibition at 0.1 mM
etoposide
-
a so called topoisomerase poison, which stabilizes the enzyme-linked double-strand break, that is otherwise transient and rapidly religated
etoposide
a topoisomerase IIalpha inhibitor
etoposide
-
topoisomerase II inhibitor
etoposide
-
the ATPase inhibitor does not affect the DNA relaxation and catenation activities of the enzyme
etoposide
traps the enzyme in a covalent complex with DNA, competes with ATP for the N-terminal binding site, binding involves N65, V77, Y127, N128, and N96, inhibits the ATPase activity of the recombinant N-terminal domain by 73% at 0.01 mM, molecular docking analysis, overview
etoposide
-
P388/F11782 cell enzyme, low inhibition
etoposide
-
cytotoxicity of inhibitor is mainly dependent on enzyme isoform 2alpha
etoposide
-
a DNA topoisomerase II trapping agent with cytotoxic effect
etoposide
-
etoposide triggers the formation of topoisomerase II-DNA adducts. Enzyme-associated DNA breaks can be stabilised by drugs such as etoposide. The proteasome has a role in converting etoposide-stabilised protein-DNA complexes into frank double-strand breaks
etoposide
-
a so called topoisomerase poison, which stabilizes the enzyme-linked double-strand break, that is otherwise transient and rapidly religated
etoposide
-
VP-16, induces skin melanomas formation in 7,12-dimethyl-benz[a]anthracene-initiated mice
etoposide
-
geminal protons of the A-ring, the H5 and H8 protons of the B-ring, and the H2 and H6 protons and the 3- and 5-methoxyl protons of the pendent E-ring interact with enzyme in the binary protein-ligand complex. No significant nuclear Overhauser enhancement signals arise from the C-ing, the D-ring, or the C4 glycosidic moiety
etoposide
-
the ATPase inhibitor does not affect the DNA relaxation and catenation activities of the enzyme
etoposide
-
mediates inhibition of the DNA ligation step in the Topo-II decatenation reaction
geldanamycin
-
geldanamycin suppresses the ATPase activity of the enzyme
geldanamycin
-
geldanamycin suppresses the ATPase activity of the enzyme
genistein
-
-
genistein
-
inhibition of enzyme-mediated religation of DNA
GTP
-
allosteric inhibition
hexamethyleneimine
-
the presence of the formamidino group in the molecule reduced its ability to stimulate DNA cleavage byDNA topoisomerase II, which is not a primary cellular target for the compound
hexamethyleneimine
-
the presence of the formamidino group in the molecule reduced its ability to stimulate DNA cleavage byDNA topoisomerase II, which is not a primary cellular target for the compound
Hydroxystilbamidine
-
-
ICRF-187
-
reduced inhibition of the enzyme in vincristine-resistant cells
ICRF-193
-
-
ICRF-193
-
a TopoIIalpha inhibitor that binds allosterically in proximity to the N-terminal ATPase site, DNA repair protein metnase increases resistance of the enzyme to ICRF-193
ICRF-193
-
i.e., meso-4,4-(2,3-butanediyl)-bis (2,6-piperazinedione)
idarubicin
-
-
KCl
-
required for DNA cleavage, KCl is inhibitory above 400 mM
Lampit
-
-
luteolin
-
inhibition of enzyme-mediated religation of DNA
luteolin
inhibits the ATPase activity of the recombinant N-terminal domain by 57% at 0.02 mM
m-AMSA
-
inhibits the enzyme at the DNA relaxation step
m-AMSA
Tequatrovirus T4
-
hydrochloride salt of amsacrine, topoisomerase poison
Merbarone
-
-
Merbarone
-
inhibits, ATP binding, dimerization and DNA double strand break, and thus stabilization of the DNA-enzyme complex
meso-2,3-Bis(3,5-dioxopiperazine-1-yl)butane
-
-
meso-2,3-Bis(3,5-dioxopiperazine-1-yl)butane
-
-
meso-2,3-Bis(3,5-dioxopiperazine-1-yl)butane
-
-
meso-2,3-Bis(3,5-dioxopiperazine-1-yl)butane
-
-
meso-2,3-Bis(3,5-dioxopiperazine-1-yl)butane
-
-
meso-2,3-Bis(3,5-dioxopiperazine-1-yl)butane
-
-
mitoxanthrone
-
-
mitoxanthrone
-
P388/F11782 cell enzyme, high inhibition
Mitoxantrone
-
-
Mitoxantrone
-
reduced inhibition of the enzyme in vincristine-resistant cells
morpholine
-
amine derivative of doxorubicin, the presence of the formamidino group in the molecule reduces its ability to stimulate DNA cleavage by DNA topoisomerase II, which is not a primary cellular target for the compound
morpholine
-
amine derivative of doxorubicin, the presence of the formamidino group in the molecule reduces its ability to stimulate DNA cleavage by DNA topoisomerase II, which is not a primary cellular target for the compound
myricetin
-
inhibition of enzyme-mediated religation of DNA
myricetin
-
potentiating interaction between inhibitors myricetin and resveratrol
N6-Methyladenine
-
i.e.6 mA, inhibits DNA scission by the enzyme, 10% content in viral DNA
N6-Methyladenine
-
i.e.6mA, inhibits DNA scission by the enzyme, high content in viral DNA
N6-tert-butyl-8-ethyl-N2-[2-[2-(morpholin-4-yl)ethoxy]quinolin-6-yl]-5,9-dihydro-4H-purine-2,6-diamine
-
-
N6-tert-butyl-8-ethyl-N2-[2-[2-(morpholin-4-yl)ethoxy]quinolin-6-yl]-5,9-dihydro-4H-purine-2,6-diamine
-
NaCl
-
above 100 mM
Nalidixic acid
-
-
Nalidixic acid
-
concentration required to observe inhibition with the eukaryotic enzyme is much higher than that needed to inhibit bacterial gyrase
Nalidixic acid
-
concentration required to observe inhibition with the eukaryotic enzyme is much higher than that needed to inhibit bacterial gyrase
Nalidixic acid
-
the Pseudomonas aeruginosa enzyme shows less sensitivity than the enzyme from Escherichia coli
Nalidixic acid
-
IC50 for the wild-type enzyme and the mutant 10 enzyme is above 0.4 mg/ml, inhibits both the replication of DNA in growing cells and the supercoiling enzyme activity in vitro
Nalidixic acid
-
no inhibition
nanaomycin A
-
-
NEM
-
0.06 mM, 50% inhibition
Norfloxacin
-
-
Norfloxacin
-
IC50 for the wild-type enzyme is 0.017 mg/ml and 0.4 mg/ml for the mutant 10 enzyme
novobiocin
-
concentration required to observe inhibition with the eukaryotic enzyme is much higher than that needed to inhibit bacterial gyrase
novobiocin
-
0.07 mM, 50% inhibition
novobiocin
-
no inhibition
novobiocin
-
no inhibition
novobiocin
-
concentration required to observe inhibition with the eukaryotic enzyme is much higher than that needed to inhibit bacterial gyrase
novobiocin
-
inhibits the ATPase activity
novobiocin
-
potent inhibitor
novobiocin
-
inhibition of TopoNM with IC50 of 0.075 mg/ml
novobiocin
-
IC50 for the wild-type enzyme is 0.0002 mg/ml and 0.0004 mg/ml for the mutant 10 enzyme
novobiocin
-
no inhibition
novobiocin
-
no inhibition
novobiocin
Tequatrovirus T4
-
cumarin-based drug
Oxolinic acid
-
-
Oxolinic acid
-
concentration required to observe inhibition with the eukaryotic enzyme is much higher than that needed to inhibit bacterial gyrase
Oxolinic acid
-
concentration required to observe inhibition with the eukaryotic enzyme is much higher than that needed to inhibit bacterial gyrase
Oxolinic acid
Tequatrovirus T4
-
little or no inhibition
Oxolinic acid
Tequatrovirus T4
-
-
Pefloxacin
-
-
Pentamidine
-
17.6fold higher selectivity for Leishmania panamensis enzyme over human macrophage enzyme
Pentamidine
-
17.6fold higher selectivity for Leishmania panamensis enzyme over human macrophage enzyme
Pirarubicin
-
-
quercetin
-
-
quercetin
-
inhibition of enzyme-mediated religation of DNA
quercetin
-
161fold higher selectivity for Leishmania panamensis enzyme over human macrophage enzyme
quercetin
a topoisomerase IIalpha inhibitor
quercetin
-
161fold higher selectivity for Leishmania panamensis enzyme over human macrophage enzyme
quinolones
-
-
-
quinolones
-
e.g. CP-115,953
-
radicicol
-
radicicol suppresses the ATPase activity of the enzyme
radicicol
inhibits the decatenation and relaxation activities
radicicol
-
radicicol suppresses the ATPase activity of the enzyme
razoxane
-
the ATPase inhibitor does not affect the DNA relaxation and catenation activities of the enzyme
razoxane
-
the ATPase inhibitor does not affect the DNA relaxation and catenation activities of the enzyme
resveratrol
-
-
resveratrol
-
potentiating interaction between inhibitors myricetin and resveratrol
resveratrol
-
is able to inhibit the ability of recombinant human TOPO IIalpha to decatenate kDNA, so that it can be considered a TOPO II poison
salicylic acid
-
salicylic acid suppresses the ATPase and decatenation but not relaxation activity of the enzyme
salicylic acid
-
salicylic acid suppresses the ATPase and decatenation but not relaxation activity of the enzyme
salvicine
diterpenoid quinone from Salvia prionitis, nonintercalative enzyme inhibitor and ATP competitor. Salvicine binds to the ATP pocket in the ATPase domain of enzyme and superimposes on the phosphate and ribose groups. Salvicine shows higher affinity for the ATPase domain than ADP and ATP
salvicine
-
0.001 mM inhibits 40%, 0.005 mM inhibits 90%, IC50: 0.003 mM, inhibits by trapping enzyme-DNA cleavage complexes, which in turn produces anticancer effects
Sitafloxacin
-
-
sodium orthovanadate
-
inhibits the ATPase activity of the wild-type enzyme, 50% inhibition at 0.005 mM, traps the enzyme in a salt-stable closed conformation, i.e. the closed clamp, no inhibition of mutant Y50F
sodium orthovanadate
-
noncompetitive, formation of a ternary enzyme-ADP-vanadate complex, inhibits the ATPase activity of the wild-type enzyme, traps the enzyme in a salt-stable closed conformation, i.e. the closed clamp, no inhibition of mutant Y28F
sparfloxacin
-
MIC90 is 0.00006 mg/ml
sparfloxacin
-
MIC90 is 0.002 mg/ml
sparfloxacin
-
MIC90 is 0.004 mg/ml
sparfloxacin
-
MIC90 is 0.00025 mg/ml
sparfloxacin
Citrobacter spp.
-
MIC90 is 0.00003 mg/ml
sparfloxacin
-
MIC90 is 0.004 mg/ml
sparfloxacin
-
MIC90 is 0.0005 mg/ml
sparfloxacin
-
MIC90 is 0.00025 mg/ml
sparfloxacin
-
MIC90 is 0.0005 mg/ml
sparfloxacin
-
MIC90 is 0.001 mg/ml
sparfloxacin
-
MIC90 is 0.00003 mg/ml
sparfloxacin
-
MIC90 is 0.00003 mg/ml
sparfloxacin
-
MIC90 is 0.00012 mg/ml
sparfloxacin
-
MIC90 is 0.00025 mg/ml
sparfloxacin
-
MIC90 is 0.00025 mg/ml
sparfloxacin
-
MIC90 is 0.000015 mg/ml
sparfloxacin
-
MIC90 is 0.00025 mg/ml
sparfloxacin
-
MIC90 is 0.002 mg/ml
sparfloxacin
-
MIC90 is 0.000015 mg/ml
sparfloxacin
-
MIC90 is 0.0005 mg/ml
sparfloxacin
-
MIC90 is 0.004 mg/ml
sparfloxacin
-
MIC90 is 0.00025 mg/ml
sparfloxacin
-
MIC90 is 0.001 mg/ml
sparfloxacin
-
MIC90 is 0.0005 mg/ml
sparfloxacin
-
MIC90 is 0.001 mg/ml
sparfloxacin
-
MIC90 is 0.00006 mg/ml
sparfloxacin
-
MIC90 is 0.001 mg/ml
sparfloxacin
-
MIC90 is 0.00006 mg/ml for strain CiproS, 0.016 mg/ml for strain CiproR, and 0.008 mg/ml for the methicillin-resistant strain
sparfloxacin
-
MIC90 is 0.00012 mg/ml for the wild-type and 0.008 mg/ml for the methicillin-resistant strain
sparfloxacin
-
MIC90 is 0.001 mg/ml
sparfloxacin
-
MIC90 is 0.0005 mg/ml for the wild-type strain and 0.00025 mg/ml for the strain Pen I/R
sparfloxacin
-
MIC90 is 0.0005 mg/ml
sparfloxacin
-
MIC90 is 0.00025 mg/ml
suramin
-
-
suramin
a topoisomerase IIalpha inhibitor
TAS-103
-
-
TAS-103
-
P388/F11782 cell enzyme, low inhibition
Teniposide
-
-
Teniposide
-
belongs to the epipodophyllotoxins, inhibitors of eukaryotic enzymes, inhibits the S83W mutant enzyme, but not the wild-type bacterial enzyme
Teniposide
-
P388/F11782 cell enzyme, high inhibition
tetracycline
-
-
thiomorpholide amido methyl ferrocene
-
inhibition of enzyme activity and anti-HIV-1 activity in Sup-T1 cells at nanomolar concentrations. Complete inhibition of proviral DNA synthesis as well as the formation of pre-integration complexes
-
thiomorpholide amido methyl ferrocene
-
specific inhibition of DNA passage and ATPase activities of isozyme IIbeta with IC50 of 0.05 mM, inhibition mechanism via complex formation, overview
-
thysanone
-
-
ursolic acid
-
IC50: 0.036 mM
ursolic acid
-
0.1 mM, 20% inhibition
ventiloquinone L
-
-
VP-16
-
4'-Demethlepipodophyllotoxin 9-(4,6-O-ethylidene-beta-D-glucopyranoside)
y, Namen korrigieren: 4-chloro-5-(furan-2-yl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]pyrrolidin-2-one
-
-
y, Namen korrigieren: 4-chloro-5-(furan-2-yl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]pyrrolidin-2-one
-
-
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
-
-
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
-
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
-
-
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
-
additional information
-
not inhibited by 3-chloro-4-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] azetidin-2-one, 4-chloro-5-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]pyrrolidin-2-one, 4-chloro-5-(4-chlorophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 3-acetyl-2-(furan-2-yl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole, 3-acetyl-2-(4-methoxyphenyl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole, and amphotericin B
-
additional information
-
antibacterial agents of the novobiocin-coumermycin family inhibit
-
additional information
-
not inhibited by camptothecin, 2-phenoxymethylbenzimidazole, 5-amino-2-(p-bromophenyl)benzoxazole, and 2-(p-chlorobenzyl)benzoxazole
-
additional information
not inhibited by camptothecin, 2-phenoxymethylbenzimidazole, 5-amino-2-(p-bromophenyl)benzoxazole, and 2-(p-chlorobenzyl)benzoxazole
-
additional information
-
not inhibited by 1-(benzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide, 3-chloro-4-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]azetidin-2-one, 3-chloro-4-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] azetidin-2-one, 4-chloro-5-(furan-2-yl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 4-chloro-5-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]pyrrolidin-2-one, 4-chloro-5-(4-chlorophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 4-chloro-5-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 3-acetyl-2-(furan-2-yl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole, 3-acetyl-2-(4-methoxyphenyl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole, 2-(furan-2-yl)-3-[2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxyacetamido]-thiazolidin-4-one, and tetracycline
-
additional information
-
5-methylcytosine in DNA has a weak effect on enzyme DNA scission activity, 5mC has a 42% content in viral DNA
-
additional information
-
the enzyme is fully active in the presence of oxygen
-
additional information
not inhibited by 1-(benzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide, 3-chloro-4-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]azetidin-2-one, 4-chloro-5-(furan-2-yl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one 4a4-chloro-5-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]pyrrolidin-2-one, 4-chloro-5-(4-chlorophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 4-chloro-5-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 3-acetyl-2-(furan-2-yl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole, 3-acetyl-2-(4-methoxyphenyl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole, and amphotericin B
-
additional information
-
-
-
additional information
-
-
-
additional information
-
triplex regions within 3 bases 5' or 7 bases 3' of cleavage sites blocked DNA cleavage, triplex formation outside of this region has no effect upon cleavage activity
-
additional information
-
antitumor effect of inhibitors
-
additional information
-
cytotoxic effects of inhibitors on K562 and K562adr tumor cells, overview
-
additional information
-
the C-terminus of the enzyme is responsible for sensitivity to anticancer drugs
-
additional information
-
IC50 values, overview
-
additional information
-
cytoplasmic localization of the enzyme is a mechanism to confer drug resistance to cells, cytotoxic affects of drugs on different cell lines, overview
-
additional information
-
inhibitory effect of grape, a Vitis sp. hybrid, cell culture extract fractions on enzyme activity, the fractions contain flavonoids and stilbenes which might be responsible for the inhibition, extract analysis reveals several compounds, overview
-
additional information
combination of molecular modeling and virtual screening for inhibitor identification, structural features for inhibitory effect on the enzyme, inhibitory mechanisms, overview
-
additional information
-
combination of molecular modeling and virtual screening for inhibitor identification, structural features for inhibitory effect on the enzyme, inhibitory mechanisms, overview
-
additional information
-
monocyte cytotoxic effects of inhibitors
-
additional information
-
E1A, an adenovirus type 5-based vector that contains E1A, but lacks E1B and E3, specifically enhances sensitivity to topoisomerase IIa targeting anticancer drugs etoposide and adriamycin, but not to amsacrine and camptothecin, by up-regulating the promoter activity by 3.5fold, which also leads to increased enzyme expression, overview
-
additional information
-
vincristine selection and resistance is accompanied by specific downregulation of isozyme IIalpha, but of isozyme IIbeta, leading to at least 7fold reduced chromosome-associated isozyme IIalpha
-
additional information
-
determination of enzyme inhibition in vitro and DNA damage and apoptosis rate in vivo in HeLa cells and A-549 cells by inhibitory drugs, overview
-
additional information
-
attachment of five derivatives of etoposide to triplex-forming oligonucleotides results in active enzyme poisons. The conjugates induce cleavage 13-14 bp from the triplex end where the drug is attached
-
additional information
-
not inhibited by 1-hydroxy-3-(2',3'-thioepoxypropoxy)thioxanthone
-
additional information
-
not inhibited by (-)-epicatechin gallate and (-)-epicatechin
-
additional information
-
soy protein hydrolysate inhibits 61% of topoisomerase II activity at 0.5 mg/ml
-
additional information
-
cytotoxic activity of anthracyclines toward cancer cells, mechanism of DNA break formation by anthracyclines, overview
-
additional information
-
inhibitory and cytotoxic potencies of inhibitor compounds, in vivo activity in cancer cell lines, overview. No or poor inhibition by compounds 6, 7, 9, 10, and 11
-
additional information
-
no inhibition of Top2 by diverse plant-originated triterpenoids and triterpenoid glycosides, overview
-
additional information
-
the enzyme is inhibited by pyranonaphthoquinone derivatives of eleutherin possessing a diverse topoisomerase II inhibition and cytotoxicity spectrum, the natural products are generally weaker inhibitors than their synthetic counterparts, pyranonaphthoquinones do not unspecifically inactivate enzymatic activity, overview. The nature of the substituents at C1 on the pyran ring and oxygenated substituents on the aryl ring are critical for anti-topoII activity, structure-based mechanism, overview. Synthesis of the dimeric pyranonaphthoquinone core of the cardinalins using a palladium catalysed homocoupling of an aryl triflate as a key step
-
additional information
-
design and synthesis of 60 2-thienyl-4-furyl-6-aryl pyridine derivatives, inhibitory potency and cytotoxicity analysis using human topoisomerase II and human cancer cell lines MCF-7, HeLa, DU145, and K562. The 2-(5-chlorothiophen-2-yl)-4-(furan-3-yl) moiety has an important role in displaying biological activities
-
additional information
-
inhibitor binding and inhibition mechanisms, overview
-
additional information
-
design, synthesis, and inhibitory potencies of 4beta-anilino-podophyllotoxin analogues, derived from etoposide, overview. The compounds stabilize the covalent TopoII-DNA cleavage complex by inhibiting the TopoII-mediated religation reaction, in vitro antiproliferation activities against three drug-resistance tumor cell lines
-
additional information
-
synthesis and inhibitory potencial of bisoxiranylmethoxy- and bisthiiranylmethoxy-chalcone derivatives on topoisomerase II, overview. No inhibition of topoisomerase I, EC 5.99.1.2
-
additional information
-
synthesis, cytotoxicity and topoisomerase inhibition properties of multifarious aminoalkylated indeno[1,2-c]isoquinolin-5,11-diones, overview
-
additional information
-
synthesis, topoisomerase IIalpha inhibitory activity, cytotoxicity in human cancer cell lines, and structure-activity relationship study of hydroxylated 2,4-diphenyl-6-aryl pyridines, overview. Hydroxyl substitution at 3- or 3'-position of phenyl ring on 2,4-diphenyl-6-aryl pyridines might be required in order to show significant topo inhibitory activity
-
additional information
-
topoisomerase IIalpha inhibition of glycosylated 2-phenyl-indoles, 2-phenyl-benzo[b]thiophenes and 2-phenyl-benzo[b]furans, overview. Analysis of cytotoxocity against three human non-tumor cell lines analyzed by the MTS (3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulfophenyl)-2H-tetrazolium) cell viability assay. No inhibition by 9
-
additional information
-
synthesis, topoisomerase II inhibitory activity, cytotoxicity, and structure-activity relationship study of rigid analogues of 2,4,6-trisubstituted pyridine containing 5,6-dihydrobenzo[h]quinoline moiety, overview. No inhibition of topo II by 12, 24, 28, and 29, these compounds are specific for topo I, EC 5.99.1.2
-
additional information
-
DNA binding, topoisomerase inhibition and cytotoxic properties of 1,5-dihydro-4-(substituted phenyl)-3H-furo[3,4-b]carbazol-3-ones, synthesised via a key step Diels-Alder reaction under microwave irradiation, overview
-
additional information
-
molecular docking study, overview
-
additional information
-
synthesis of 2,4-diaryl chromenopyridines and evaluation of their topoisomerase II inhibitory activity, cytotoxicity, and structure-activity relationship, overview. 2-Furyl or 2-thienyl at 2- or 4-position of central pyridine is crucial in displaying topo I or II inhibitory activity and cytotoxicity
-
additional information
-
IC50 values for in vivo inhibition of the enzyme in human cancer cell lines, overview
-
additional information
structure-activity relationship study, molecular docking studies based on 5'-adenylyl-beta,gamma-imidodiphosphate-bound enzyme, PDB ID 1ZXM, and ADP-bound form, PDB 1ZXN, and molecular dynamics simulation analysis for design of structure-based inhibitors, overview. The catalytic mode of inhibition proceeds by blocking the ATP-binding site
-
additional information
-
structure-activity relationship study, molecular docking studies based on 5'-adenylyl-beta,gamma-imidodiphosphate-bound enzyme, PDB ID 1ZXM, and ADP-bound form, PDB 1ZXN, and molecular dynamics simulation analysis for design of structure-based inhibitors, overview. The catalytic mode of inhibition proceeds by blocking the ATP-binding site
-
additional information
-
binding constant values of heterobimetallic complexes including Sn2+ and Cu2+ or Zn2+, and ligand 5-{[(1E)-(2-hydroxyphenyl)methylene]amino}-2-hydroxybenzoic acid with the DNA, NMR and mass spectrometric structure analysis, inhibitory potencies, overview
-
additional information
-
the C-terminal domain of topoisomerase IIbeta acts as a negative regulator
-
additional information
-
no inhibition by tert-butoxycarbonyl-6-aminohexanoiyl-L-lysyl-6-aminohexanoyl amide
-
additional information
-
synthesis of rotenoid derivatives with cytotoxic and topoisomerase II inhibitory activities, overview. Effects of five different 6-deoxyclitoriacetal derivatives on the thermal denaturation of calf thymus DNA
-
additional information
-
rational design strategy of podophyllum topoisomerase II inhibitors for the synthesis of the 4-O-(2-pyrazinecarboxylic)-4-demethylepipodophyllotoxin with antitumor activity by diminishing the relaxation reaction of topoisomerase II-DNA decatenation, overview. The compounds exhibit promising in vitro antitumor activity
-
additional information
-
supercoiled pRYG substrate is relaxed with topoisomerase II without a significant effect by DMSO
-
additional information
-
xanthone derivative inhibitor design, pharmacokinetics parameters , and structure-activity relationship represented by the QSAR model, overview
-
additional information
-
no inhibition by paclitaxel
-
additional information
-
another marine alkaloids from Xestospongia sp., amphimedine, is biologically inactive as an antitumor agent
-
additional information
-
design and synthesis of urea-derived enzyme inhibitors, asymmetrically N,N'-substituted ureas, molecular docking study, overview. No inhibition by N-(4-bromophenyl)-N-[(2E)-3-phenylprop-2-en-1-yl]urea
-
additional information
no inhibition of ATPase activity by dihydrobetulinic acid, a pentacyclic triterpenoid derivative
-
additional information
-
no inhibition of ATPase activity by dihydrobetulinic acid, a pentacyclic triterpenoid derivative
-
additional information
-
P388/F11782 cells, resistant to F11782, show cross-resistance to merbarone and doxorubicin
-
additional information
-
cytotoxic activity of anthracyclines toward L1210 cells, mechanism of DNA break formation by anthracyclines, and role of the stabilization of DNA topoisomerase II in the mechanism of cell killing by the anthracyclines, overview
-
additional information
-
not inhibited by Isoniazid, rifampicin, and afloxacin
-
additional information
-
5-methylcytosine in DNA has a weak effect on enzyme DNA scission activity, 5mC has a high content in viral DNA
-
additional information
-
ciprofloxacin-resistant strain shows increased MIC90 values for the inhibitors compared to the wild-type strains
-
additional information
-
inhibitory potency of diverse ferrocene derivatives, overview
-
additional information
geldanamycin does not inhibit the decatenation and relaxation activities
-
additional information
-
geldanamycin does not inhibit the decatenation and relaxation activities
-
additional information
-
no inhibition by nalidixic acid, oxolinic acid or novobiocin
-
additional information
-
-
-
additional information
-
cytotoxicity of eleutherin and pyranonaphthoquinone derivatives, structure-activity study and mechanism, overview
-
additional information
-
not inhibited by 1-(benzylidene)-2-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetohydrazide, 3-chloro-4-phenyl-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido]azetidin-2-one, 4-chloro-5-(4-chlorophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 4-chloro-5-(4-nitrophenyl)-1-[(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxy)acetamido] pyrrolidin-2-one, 3-acetyl-2-(furan-2-yl)-5-(2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxymethyl)-1,3,4-(2H)-oxadiazole, 2-(furan-2-yl)-3-[2-oxo-4-phenyl-2H-benzo[b]pyran-7-yloxyacetamido]-thiazolidin-4-one, and amphotericin B
-
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0.046
(+)-catechin
Cricetulus griseus
-
-
0.0372
(-)-epicatechin
Cricetulus griseus
-
-
3.61
(-)-epigallocatechin
Cricetulus griseus
-
-
3.78
(-)-epigallocatechin-3-gallate
Cricetulus griseus
-
-
6
(1R,1'R,6S,6'S,7R,7'R,11bR,11b'R)-1,1',7,7'-tetrakis(4-hydroxyphenyl)-1,1',6,6',7,7',11b,11b'-octahydro-6,6'-bi-2-oxadibenzo[cd,h]azulene-4,4',8,8',10,10'-hexol
Homo sapiens
-
pH 7.9, 30°C
4
(1R,1'R,6S,6'S,7S,7'S,11bR,11b'R)-1,1',7,7'-tetrakis(4-hydroxyphenyl)-1,1',6,6',7,7',11b,11b'-octahydro-6,6'-bi-2-oxadibenzo[cd,h]azulene-4,4',8,8',10,10'-hexol
Homo sapiens
-
pH 7.9, 30°C
5
(2R,2'S,3'S)-3'-(3,5-dihydroxyphenyl)-2,2'-bis(4-hydroxyphenyl)-4-[(E)-2-(4-hydroxyphenyl)ethenyl]-2,2',3,3'-tetrahydro-3,4'-bi-1-benzofuran-6,6'-diol
Homo sapiens
-
pH 7.9, 30°C
7
(2R,3S)-2-(3,5-dihydroxyphenyl)-1-[(S)-hydroxy(4-hydroxyphenyl)methyl]-3-(4-hydroxyphenyl)-2,3-dihydro-1H-indene-4,6-diol
Homo sapiens
-
pH 7.9, 30°C
0.00083
(2S)-2-(2-hydroxypropan-2-yl)-2,5-dimethyl-8,10-bis[(2-methyloxiran-2-yl)methoxy]-1,2-dihydro-11H-furo[3,2-a]xanthen-11-one
Homo sapiens
-
pH and temperature not specified in the publication, predicted value
3
(3R,4R,4aS,5S,9bS,10S)-4-(3,5-dihydroxyphenyl)-3,5,10-tris(4-hydroxyphenyl)-3,4,4a,5,9b,10-hexahydro-11-oxabenzo[5,6]cyclohepta[1,2,3,4-jkl]-as-indacene-2,6,8-triol
Homo sapiens
-
pH 7.9, 30°C
6
(3S,4S,4aR,5S,9bS,10S)-4-(3,5-dihydroxyphenyl)-3,5,10-tris(4-hydroxyphenyl)-3,4,4a,5,9b,10-hexahydro-11-oxabenzo[5,6]cyclohepta[1,2,3,4-jkl]-as-indacene-2,6,8-triol
Homo sapiens
-
pH 7.9, 30°C
5
(4bR,5R,9S,10S,11R,12R)-10-(3,5-dihydroxyphenyl)-5,9,12-tris(4-hydroxyphenyl)-4b,5,9,10,11,12-hexahydrobenzo[6,7]cyclohepta[1,2,3-cd]furo[3,2-f][1]benzofuran-1,3,11-triol
Homo sapiens
-
pH 7.9, 30°C
0.05
(4Z,7Z,10Z,13Z,16Z,19Z)-henicosa-4,7,10,13,16,19-hexaenoic acid
Homo sapiens
-
IC50 is 0.05 mM for inhibition of decatenation of kinetoplast DNA
0.01
(5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoic acid
Homo sapiens
-
irreversible inhibition, IC50 is 0.01 mM for inhibition of decatenation of kinetoplast DNA, effects on thermal transition of dsDNA, overview
0.00058
1,3,5-trihydroxy-4-methoxy-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00069
1,5-dihydroxy-3-methoxy-2,4-bis(3-methylbut-2-en-1-yl)-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication
0.00058
1,7-dihydroxy-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication
0.0098
1-(-(5-nitrothiazol-2-yl)piperidin-4-yl)-3-phenylthiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00175
1-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)-3-phenylurea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.02331
1-(4-acetylphenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0157
1-(4-acetylphenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.01305
1-(4-chlorobenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0064
1-(4-chlorobenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.008707
1-(4-chlorophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0098
1-(4-chlorophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0015
1-(4-fluorobenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0036
1-(4-fluorobenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00807
1-(4-fluorophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0026
1-(4-fluorophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0286
1-(4-methoxybenzyl)-1H-[1,2,3]triazolo[4,5-g]-phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0076
1-(4-methoxybenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0015
1-(4-methoxybenzyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.004538
1-(4-methoxyphenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00356
1-(4-methoxyphenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.02151
1-(4-nitrophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0239
1-(4-nitrophenyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.01785
1-(4-tolyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00585
1-(4-tolyl)-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00733
1-(5-nitrothiazol-2-yl)-N-phenylpiperidin-4-amine
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0075
1-benzyl-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)thiourea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.002136
1-benzyl-3-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)urea
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0556
1-ethyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0298
1-iso-butyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0333
1-iso-propyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.039
1-methyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0432
1-n-butyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.049
1-n-propyl-1H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.4767
1-[(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)(ethyl)amino]-1-oxopropan-2-yl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0256
1-[4-[(methanesulfonyl)amino]phenyl]-1-oxopropan-2-yl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0528
1H-[1,2,3]triazolo[4,5,-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0174
2-(p-nitrobenzyl)benzoxazole
Bos taurus
-
0.522
2-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
Homo sapiens
-
at pH 7.9 and 37°C
0.0615
2-ethyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0194
2-iso-butyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0545
2-iso-propyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0556
2-methyl-2H-[1,2,3]triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0648
2-n-butyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0444
2-n-propyl-2H-[1,2,3] triazolo[4,5-g]phthalazine-4,9-dione
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.0268
2-oxo-2-(3-sulfamoylanilino)ethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0242
2-[(1,1-dioxo-1l6-thiolan-3-yl)(ethyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.1963
2-[(1,1-dioxo-1l6-thiolan-3-yl)(methyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0289
2-[(1,1-dioxo-1l6-thiolan-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.2146
2-[(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)(2-methylpropyl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
1
2-[(3-carbamoylthiophen-2-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
IC50 above 1.0 mM, pH and temperature not specified in the publication
1
2-[(butan-2-yl)(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
IC50 above 1.0 mM, pH and temperature not specified in the publication
0.06454
2-[4-(methanesulfonyl)piperazin-1-yl]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.0236
2-[benzyl(1,1-dioxo-2,3-dihydro-1H-1l6-thiophen-3-yl)amino]-2-oxoethyl 1H-indazole-3-carboxylate
Homo sapiens
-
pH and temperature not specified in the publication
0.528
3-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
Homo sapiens
-
at pH 7.9 and 37°C
0.186
3-oxolanost-9(11)-ene-24S,25-diol
Homo sapiens
-
IC50: 0.186 mM
0.00119
3-[2-(dimethylamino)propoxy]benzo[b]naphtho[2,3-d]furan-6,11-dione
Homo sapiens
-
-
0.083 - 0.089
3alpha-corosolic acid
0.049
3beta-corosolic acid
Homo sapiens
-
IC50: 0.049 mM
0.4858
4-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)-3-fluorobenzonitrile
Homo sapiens
-
at pH 7.9 and 37°C
0.1534
4-([[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl]sulfanyl]methyl)benzonitrile
Homo sapiens
-
at pH 7.9 and 37°C
0.0035
4-chloro-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0026
4-chloro-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzenesulfonamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0054
4-fluoro-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0117
4-fluoro-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzenesulfonamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0065
4-methoxy-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00531
4-methoxy-N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzenesulfonamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00071
5,8-dihydroxy-4-methoxy-3,6-bis(3-methylbut-2-en-1-yl)-4a,9a-dihydro-1H-xanthene-1,2,9-trione
Homo sapiens
-
pH and temperature not specified in the publication, predicted value
0.4878
5-amino-4-(p-fluorophenyl)benzoxazole
Bos taurus
-
0.1867
5-amino-4-(p-methylbenzyl)benzoxazole
Bos taurus
-
0.58
5-amino-4-phenylbenzoxazole
Bos taurus
-
0.0223
5-chloro-2-(4-methylphenyl)benzoxazole
Bos taurus
-
0.00079
5-methoxy-1,3-bis[(2-methyloxiran-2-yl)methoxy]-7-(oxiran-2-ylmethyl)-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication, predicted value
0.00075
5-methoxy-1,3-bis[(2-methyloxiran-2-yl)methoxy]-7-(propan-2-yl)-9H-xanthen-9-one
Homo sapiens
-
pH and temperature not specified in the publication, predicted value
0.09141
5-nitro-2-(4-nitrobenzyl)benzoxazole
Bos taurus
-
0.0006
6,11-dihydroxy-3,3-dimethyl-5-(3-methylbut-2-en-1-yl)-3H,7H-pyrano[2,3-c]xanthen-7-one
Homo sapiens
-
pH and temperature not specified in the publication
0.2347
6-(benzylsulfanyl)-4-(butylsulfanyl)-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
1
6-(benzylsulfanyl)-4-(phenylsulfanyl)-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
1
6-(benzylsulfanyl)-4-(propylsulfanyl)-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
1
6-(benzylsulfanyl)-4-[(cyclobutylmethyl)sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.481
6-(benzylsulfanyl)-4-[(cyclopropylmethyl)sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.0941
6-(benzylsulfanyl)-4-[[(2-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.0725
6-(benzylsulfanyl)-4-[[(2-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
1
6-(benzylsulfanyl)-4-[[(2-methoxyphenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
IC50 above 1.0 mM, at pH 7.9 and 37°C
0.3767
6-(benzylsulfanyl)-4-[[(2-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.0576
6-(benzylsulfanyl)-4-[[(3-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.4853
6-(benzylsulfanyl)-4-[[(3-methoxyphenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.4883
6-(benzylsulfanyl)-4-[[(3-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.2193
6-(benzylsulfanyl)-4-[[(4-chlorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.1466
6-(benzylsulfanyl)-4-[[(4-fluorophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.3859
6-(benzylsulfanyl)-4-[[(4-nitrophenyl)methyl]sulfanyl]-1,3,5-triazin-2(1H)-one
Homo sapiens
-
at pH 7.9 and 37°C
0.000014
6-methoxy-4-(2-[4-[([1,3]oxathiolo[5,4-c]pyridin-6-ylmethyl)amino]piperidin-1-yl]ethyl)quinoline-3-carbonitrile
Staphylococcus aureus
pH not specified in the publication, temperature not specified in the publication
1
6-[(cyclopentylsulfanyl)methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
1
6-[[(1-cyclopentyl-1H-tetrazol-5-yl)sulfanyl]methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
1
6-[[(5-cyclopropyl-1,3,4-oxadiazol-2-yl)sulfanyl]methyl]-N2-(4-fluorophenyl)-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.00068
8-(2-(diethylamino)ethoxy)benzofuro[3,2-g]quinoline-5,11-dione
Homo sapiens
-
-
0.002
aclacinomycin A
Homo sapiens
-
-
4
alpha-viniferin-13-O-beta-glucopyranoside
Homo sapiens
-
pH 7.9, 30°C
0.1
azalactone ferrocene
Rattus norvegicus
-
specific inhibition of DNA passage and ATPase activities of isozyme IIbeta with IC50 of 0.1 mM, inhibition mechanism via complex formation, overview
-
0.08
betulinic acid
Homo sapiens
-
IC50: 0.08 mM
0.0065
bis(acridin-4-ylmethyl)cyanamide
Homo sapiens
-
pH 8.0
0.00007 - 0.02645
camptothecin
0.031 - 1.999
Ciprofloxacin
0.01
conjugated docosahexanoic acid
Homo sapiens
-
IC50 is 0.01 mM for inhibition of decatenation of kinetoplast DNA
-
0.0025
conjugated eicosapentaenoic acid
Homo sapiens
-
irreversible inhibition, IC50 is 0.0025 mM for inhibition of decatenation of kinetoplast DNA, effects on thermal transition of dsDNA, overview
0.043
corosolic acid
Homo sapiens
-
IC50: 0.043 mM
8.5
daunorubicin
Homo sapiens
-
pH 7.9, 30°C
0.0000183 - 0.0000314
doxorubicin
0.0263 - 0.413
ellagic acid
0.000029
epicatechin gallate
Homo sapiens
-
pH 8.0, 37°C
0.000194 - 0.17
etoposide
0.00000026 - 0.0087
F14512
2.4
FEITPEKNPQ
Homo sapiens
-
in 50 mM Tris-HCl (pH 8.0)
0.0006
GSK299423
Plasmodium falciparum
-
at pH 8.0 and 26°C
1
hemsleyanol
Homo sapiens
-
pH 7.9, 30°C
0.0000908 - 0.000094
hexamethyleneimin
0.0000908 - 0.000094
hexamethyleneimine
0.0002
ICRF-193
Homo sapiens
-
at 37°C
4
IETWNPNNKP
Homo sapiens
-
in 50 mM Tris-HCl (pH 8.0)
0.015
lithocholic acid
Homo sapiens
-
IC50: 0.015 mM, the lithocholic interaction interface has a pocket comprised of three amino acids, Lys720, Leu760 and Thr791
0.092
maslinic acid
Homo sapiens
-
IC50: 0.092 mM
0.002
Mitoxantrone
Homo sapiens
-
-
0.0000244 - 0.000026
morpholine
0.000039
myricetin
Homo sapiens
-
pH 8.0, 37°C
0.0043
N,N,N',N'-tetrakis(acridin-4-ylmethyl)butane-1,4-diamine
Homo sapiens
-
pH 8.0
0.0057
N,N,N',N'-tetrakis(acridin-4-ylmethyl)ethane-1,2-diamine
Homo sapiens
-
pH 8.0
0.0002
N,N,N',N'-tetrakis[(7-bromo-9-chloroacridin-4-yl)methyl]butane-1,4-diamine
Homo sapiens
-
pH 8.0
0.0009
N,N,N',N'-tetrakis[(9-aminoacridin-4-yl)methyl]ethane-1,2-diamine
Homo sapiens
-
pH 8.0
0.0529
N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)-1-phenylmethanesulfonamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00173
N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)-2-phenylacetamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00023
N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.00105
N-(1-(5-nitrothiazol-2-yl)piperidin-4-yl)benzenesulfonamide
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0199
N-(4-chlorobenzyl)-1-(5-nitrothiazol-2-yl)piperidin-4-amine
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0001496
N-(4-fluorobenzyl)-1-(5-nitrothiazol-2-yl)piperidin-4-amine
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.01742
N-(4-methoxybenzyl)-1-(5-nitrothiazol-2-yl)piperidin-4-amine
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0004
N-(acridin-1-ylmethyl)-N,N',N'-tris(acridin-2-ylmethyl)octane-1,8-diamine
Homo sapiens
-
pH 8.0
0.5
N-([3-[(methanesulfonyl)amino]phenyl]methyl)-1H-indazole-3-carboxamide
Homo sapiens
-
IC50 above 0.5 mM, pH and temperature not specified in the publication
0.5
N-([4-[(methylsulfamoyl)methyl]phenyl]methyl)-1H-indazole-3-carboxamide
Homo sapiens
-
IC50 above 0.5 mM, pH and temperature not specified in the publication
0.00925
N-benzyl-1-(5-nitrothiazol-2-yl)piperidin-4-amine
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.0251
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]methanesulfonamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0139
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]methanesulfonohydrazide
Homo sapiens
-
pH and temperature not specified in the publication
0.5
N-[1-(1H-indazole-3-carbonyl)piperidin-4-yl]propane-1-sulfonamide
Homo sapiens
-
IC50 above 0.5 mM, pH and temperature not specified in the publication
0.3819
N-[3-[(methanesulfonyl)amino]propyl]-1H-indazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.5
N-[4-[(methanesulfonyl)amino]-3-methylphenyl]-1H-indazole-3-carboxamide
Homo sapiens
-
IC50 above 0.5 mM, pH and temperature not specified in the publication
0.0458
N-[4-[(methanesulfonyl)amino]phenyl]-1H-indazole-3-carboxamide
Homo sapiens
-
pH and temperature not specified in the publication
0.0084
N2-(1,3-benzothiazol-6-yl)-N6-cyclohexyl-9H-purine-2,6-diamine
Homo sapiens
-
-
0.0017
N2-(1,3-benzothiazol-6-yl)-N6-tert-butyl-9H-purine-2,6-diamine
Homo sapiens
-
-
1
N2-(4-fluorophenyl)-6-[[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
1
N2-(4-fluorophenyl)-6-[[(1-propyl-1H-imidazol-2-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.337
N2-(4-fluorophenyl)-6-[[(1H-tetrazol-5-yl)sulfanyl]methyl]-1,3,5-triazine-2,4-diamine
Homo sapiens
pH and temperature not specified in the publication
0.0005 - 0.002
neoamphimedine
0.00018
novobiocin
Mycobacterium tuberculosis
-
at pH 7.9 and 37°C
0.081
oleanolic acid
Homo sapiens
-
IC50: 0.081 mM
0.0811 - 1.426
Pentamidine
0.0045
procyanidin B2
Homo sapiens
-
pH 8.0, 37°C
0.0006 - 0.0889
quercetin
0.0657
resveratrol
Homo sapiens
-
pH 8.0, 37°C
1
S-[6-(benzylsulfanyl)-4-oxo-4,5-dihydro-1,3,5-triazin-2-yl] hydrogen carbonothioate
Homo sapiens
-
at pH 7.9 and 37°C
0.003
salvicine
Rattus norvegicus
-
0.001 mM inhibits 40%, 0.005 mM inhibits 90%, IC50: 0.003 mM, inhibits by trapping enzyme-DNA cleavage complexes, which in turn produces anticancer effects
0.0028
sodium antimonyl(III) gluconate
Homo sapiens
-
IC50 is 0.0028 mM
0.0027
sodium stibogluconate
Homo sapiens
-
IC50 is 0.0027 mM
0.02149
tanshinone-1
Homo sapiens
-
at pH 8.0 and 37°C
0.05
thiomorpholide amido methyl ferrocene
Rattus norvegicus
-
specific inhibition of DNA passage and ATPase activities of isozyme IIbeta with IC50 of 0.05 mM, inhibition mechanism via complex formation, overview
-
0.036
ursolic acid
Homo sapiens
-
IC50: 0.036 mM
7.9
VFDGEL
Homo sapiens
-
in 50 mM Tris-HCl (pH 8.0)
1
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl 4-methylpiperazine-1-carbodithioate
Homo sapiens
pH and temperature not specified in the publication
1
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl cyclohexyl(methyl)carbamodithioate
Homo sapiens
pH and temperature not specified in the publication
0.139
[4-amino-6-(4-fluoroanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
Homo sapiens
pH and temperature not specified in the publication
0.229
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl morpholine-4-carbodithioate
Homo sapiens
pH and temperature not specified in the publication
1
[4-amino-6-(4-methoxyanilino)-1,3,5-triazin-2-yl]methyl piperidine-1-carbodithioate
Homo sapiens
pH and temperature not specified in the publication
additional information
additional information
-
0.083
3alpha-corosolic acid
Homo sapiens
-
IC50: 0.083 mM
0.089
3alpha-corosolic acid
Homo sapiens
-
IC50: 0.089 mM
0.00007
camptothecin
Homo sapiens
enzyme from HL-60 cell, at pH 8.0 and 37°C
0.00537
camptothecin
Homo sapiens
enzyme from K-562 cell, at pH 8.0 and 37°C
0.01162
camptothecin
Homo sapiens
enzyme from HeLa cell, at pH 8.0 and 37°C
0.02645
camptothecin
Homo sapiens
enzyme from A-549 cell, at pH 8.0 and 37°C
0.031
Ciprofloxacin
Staphylococcus aureus
pH not specified in the publication, temperature not specified in the publication
0.035
Ciprofloxacin
Plasmodium falciparum
-
at pH 8.0 and 26°C
0.05
Ciprofloxacin
Leishmania panamensis
-
pH 8.0, 37°C
0.1695
Ciprofloxacin
Homo sapiens
inhibition of DNA relaxation activity, pH 8.0, temperature not specified in the publication, recombinant topo2alpha
0.797
Ciprofloxacin
Homo sapiens
inhibition of ATPase activity, pH 8.0, temperature not specified in the publication, recombinant topo2alpha
1.999
Ciprofloxacin
Homo sapiens
-
pH 8.0, 37°C
0.0329
coralyne
Leishmania panamensis
-
pH 8.0, 37°C
0.074
coralyne
Homo sapiens
-
pH 8.0, 37°C
0.0000183
doxorubicin
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells
0.0000314
doxorubicin
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells in presence of inhibitor ICRF-187
0.0263
ellagic acid
Homo sapiens
-
pH 8.0, 37°C
0.413
ellagic acid
Leishmania panamensis
-
pH 8.0, 37°C
0.0026
enoxacin
Leishmania panamensis
-
pH 8.0, 37°C
1.485
enoxacin
Homo sapiens
-
pH 8.0, 37°C
0.000194
etoposide
Cricetulus griseus
-
in CHO-K1 cells
0.000329
etoposide
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells
0.000418
etoposide
Cricetulus griseus
-
in CHO-XRS6 cells
0.000585
etoposide
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells in presence of inhibitor ICRF-187
0.02
etoposide
Plasmodium falciparum
-
at pH 8.0 and 26°C
0.021
etoposide
Homo sapiens
inhibition of ATPase activity, pH 8.0, temperature not specified in the publication, recombinant topo2alpha
0.05
etoposide
Homo sapiens
-
IC50: 0.05 mM
0.0589
etoposide
Homo sapiens
inhibition of DNA relaxation activity, pH 8.0, temperature not specified in the publication, recombinant topo2alpha
0.0784
etoposide
Homo sapiens
-
-
0.0929
etoposide
Homo sapiens
-
in 50 mM Tris-HCl, pH 8, 120 mM KCl, 10 mM MgCl2, 0.5 mM ATP, 0.5 mM dithiothreitol, 0.03 mg/ml bovine serum albumin, at 37°C
0.17
etoposide
Bos taurus
-
0.00000026
F14512
Cricetulus griseus
-
in CHO-XRS6 cells
0.0000109
F14512
Cricetulus griseus
-
in CHO-K1 cells
0.00012
F14512
Cricetulus griseus
-
in CHO cells
0.0087
F14512
Cricetulus griseus
-
in CHO-MG cells
0.0000908
hexamethyleneimin
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells in presence of inhibitor ICRF-187
0.000094
hexamethyleneimin
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells
0.0000908
hexamethyleneimine
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells in presence of inhibitor ICRF-187
0.000094
hexamethyleneimine
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells
0.0000244
morpholine
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells
0.000026
morpholine
Mus musculus
-
pH 7.5, 37°C, cytotoxicity assay in L1210 cells in presence of inhibitor ICRF-187
0.0005
neoamphimedine
Homo sapiens
-
inhibition of DNA catenation, pH 8.0, 39°C
0.002
neoamphimedine
Homo sapiens
-
inhibition of ATPase activity, pH 8.0, 39°C
0.0811
Pentamidine
Leishmania panamensis
-
pH 8.0, 37°C
1.426
Pentamidine
Homo sapiens
-
pH 8.0, 37°C
0.0006
quercetin
Leishmania panamensis
-
pH 8.0, 37°C
0.0036
quercetin
Homo sapiens
inhibition of ATPase activity, pH 8.0, temperature not specified in the publication, recombinant topo2alpha
0.0277
quercetin
Homo sapiens
inhibition of DNA relaxation activity, pH 8.0, temperature not specified in the publication, recombinant topo2alpha
0.0889
quercetin
Homo sapiens
-
pH 8.0, 37°C
0.0003
suramin
Homo sapiens
inhibition of DNA relaxation activity, pH 8.0, temperature not specified in the publication, recombinant topo2alpha
0.021
suramin
Homo sapiens
inhibition of ATPase activity, pH 8.0, temperature not specified in the publication, recombinant topo2alpha
0.00006
VP-16
Homo sapiens
enzyme from HL-60 cell, at pH 8.0 and 37°C
0.00054
VP-16
Homo sapiens
enzyme from HeLa cell, at pH 8.0 and 37°C
0.00164
VP-16
Homo sapiens
enzyme from K-562 cell, at pH 8.0 and 37°C
0.00891
VP-16
Homo sapiens
enzyme from A-549 cell, at pH 8.0 and 37°C
additional information
additional information
Homo sapiens
-
2-thienyl-4-furyl-6-aryl pyridine derivatives, IC50 values in cytotoxicity assays in cancer cell lines, overview
-
additional information
additional information
Homo sapiens
-
in vitro antiproliferation activities against three drug-resistance tumor cell lines of 4beta-anilino-podophyllotoxin analogues, IC50 values
-
additional information
additional information
Homo sapiens
-
in vivo IC50 values of inhibitors in different cancer cell lines in a cytotoxicity assay, overview
-
additional information
additional information
Homo sapiens
-
inhibitor IC50 values in vivo in different cancer cell lines, overview
-
additional information
additional information
Homo sapiens
-
cytotoxic activity of inhibitory compounds, docking study, overview
-
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