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Ala-Ser-His-Leu-Gly-Leu-Ala-Arg + H2O
Ala-Ser-His-Leu-Gly-Leu-Ala + Arg
-
reaction is much more efficient than reaction with EC 3.4.17.3
-
?
anaphylatoxin C3a + H2O
?
anaphylatoxin C5a + H2O
?
anisylazoformyl-Lys + H2O
anisylazoformic acid + Lys
-
-
-
?
Arg6-Leu5-enkephalin + H2O
Tyr-Gly-Gly-Phe-Leu + Arg
-
i.e. Tyr-Gly-Gly-Phe-Leu-Arg
-
-
?
Arg6-Met5-enkephalin + H2O
Tyr-Gly-Gly-Phe-Met + Arg
-
i.e. Tyr-Gly-Gly-Phe-Met-Arg
-
-
?
benzoyl-o-cyano-Phe-Arg + H2O
benzoyl-o-cyano-Phe + Arg
-
-
-
?
biotinyl-(epsilon-aminocaproic acid)-(epsilon-aminocaproic acid)-Gly-Leu-Met-Val-Gly-Gly-Val-Val-Arg-OH + H2O
biotinyl-(epsilon-aminocaproic acid)-(epsilon-aminocaproic acid)-Gly-Leu-Met-Val-Gly-Gly-Val-Val-OH + Arg
-
-
-
?
bradykinin + H2O
Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe + Arg
-
i.e. Arg-Pro-Pro-Gly-Phe-Ser-Pro-Phe-Arg
-
-
?
complement component C3a octapeptide + H2O
?
-
removal of terminal arginine, low activity
-
-
?
complement component C5a octapeptide + H2O
?
-
removal of terminal arginine
-
-
?
fibrin + H2O
fibrin + L-Lys
-
-
-
-
?
fibrin + H2O
fibrin + Lys
Fibrin, partially degraded + H2O
?
Fibrin, partially degraded + H2O
Fibrin, partially degraded + L-Lys + L-Arg
Glu-plasminogen + H2O
Glu + plasmin
-
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
hippuryl-arginine + H2O
hippuric acid + L-arginine
-
substrate is used to measure the TAFI activation by plasmin
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
hippuryl-L-arginine + H2O
hippuric acid + L-arginine
-
-
-
-
?
Hippuryl-L-argininic acid + H2O
Hippuric acid + argininic acid
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
hippuryl-L-lysine + H2O
hippuric acid + L-lysine
-
-
-
-
?
His-Lys-Asp-Met-Gln-Leu-Gly-Arg + H2O
His-Lys-Asp-Met-Gln-Leu-Gly + Arg
Lys-plasminogen + H2O
Lys + plasmin
Lys6-Leu5-enkephalin + H2O
Tyr-Gly-Gly-Phe-Leu + Lys
-
i.e. Tyr-Gly-Gly-Phe-Leu-Lys
-
-
?
Lys6-Met5-enkephalin + H2O
Tyr-Gly-Gly-Phe-Met + Lys
-
i.e. Tyr-Gly-Gly-Phe-Met-Lys
-
-
?
N-benzoyl-2'-cyano-L-Phe-L-Arg + H2O
N-benzoyl-2'-cyano-L-Phe + L-Arg
-
selective CPU substrate
-
-
?
N-benzoyl-Gly-L-Arg + H2O
N-benzoyl-Gly + L-Arg
-
-
-
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Arg + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Arg
-
-
-
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
p-anisylazoformyl-L-arginine + H2O
p-anisylazoformic acid + L-arginine
-
substrate is used to measure the TAFI activation by thrombin and thrombin-thrombomodulin
-
-
?
[3-(2-furylacryloyl)]-L-alanyl-L-arginine + H2O
[3-(2-furylacryloyl)]-L-alanine + L-arginine
-
-
-
-
?
[3-(2-furylacryloyl)]-L-phenylalanyl-L-phenylalanine + H2O
[3-(2-furylacryloyl)]-L-phenylalanine + L-phenylalanine
-
-
-
-
?
additional information
?
-
anaphylatoxin C3a + H2O
?
-
-
-
-
?
anaphylatoxin C3a + H2O
?
-
inactivation of the inflammatory mediator
-
-
?
anaphylatoxin C5a + H2O
?
-
-
-
-
?
anaphylatoxin C5a + H2O
?
-
inactivation of the inflammatory mediator
-
-
?
fibrin + H2O
fibrin + Lys
-
anti-fibrinolytic activity
-
-
?
fibrin + H2O
fibrin + Lys
-
cleavage of C-terminal Lys, regulation, overview
the cleaved fibrin cannot be bound by plasminogen and the plasminogen activator in contrast to the uncleaved fibrin, fibrinolysis and plasmin regulation cycle involving the enzyme, overview
-
?
fibrin + H2O
fibrin + Lys
-
partially degraded fibrin in fibrin clots, cleavage of C-terminal Lys
-
-
?
fibrin + H2O
fibrin + Lys
-
cleavage of C-terminal Lys
-
-
?
fibrin + H2O
fibrin + Lys
-
cleavage of C-terminal Lys, regulation, overview
the cleaved fibrin cannot be bound by plasminogen and the plasminogen activator in contrast to the uncleaved fibrin, fibrinolysis and plasmin regulation cycle involving the enzyme, overview
-
?
fibrin + H2O
fibrin + Lys
-
cleavage of C-terminal Lys
-
-
?
fibrin + H2O
Lys + ?
-
-
-
?
fibrin + H2O
Lys + ?
-
attenuates clot lysis by removing lysine residues from a fibrin clot
-
?
Fibrin, partially degraded + H2O
?
-
-
-
-
?
Fibrin, partially degraded + H2O
?
-
the enzyme suppresses the ability of fibrin to catalyze plasminogen activation and thus delays clot lysis
-
-
?
Fibrin, partially degraded + H2O
?
-
inhibition of fibrinolysis
-
-
?
Fibrin, partially degraded + H2O
?
-
molecular connection between coagulation and fibrinolysis
-
-
?
Fibrin, partially degraded + H2O
Fibrin, partially degraded + L-Lys + L-Arg
-
-
-
?
Fibrin, partially degraded + H2O
Fibrin, partially degraded + L-Lys + L-Arg
-
-
-
?
Fibrin, partially degraded + H2O
Fibrin, partially degraded + L-Lys + L-Arg
-
-
-
?
Fibrin, partially degraded + H2O
Fibrin, partially degraded + L-Lys + L-Arg
-
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
hippuryl-Arg + H2O
hippuric acid + Arg
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
?
Hippuryl-L-Arg + H2O
Hippuric acid + L-Arg
-
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
-
-
-
?
Hippuryl-L-Lys + H2O
Hippuric acid + L-Lys
-
-
-
-
?
His-Lys-Asp-Met-Gln-Leu-Gly-Arg + H2O
His-Lys-Asp-Met-Gln-Leu-Gly + Arg
-
i.e. C5a, reaction is much more efficient than reaction with EC 3.4.17.3
-
?
His-Lys-Asp-Met-Gln-Leu-Gly-Arg + H2O
His-Lys-Asp-Met-Gln-Leu-Gly + Arg
-
i.e. C5a, the enzyme significantly contributes to the inactivation of C5a, the most potent of the complement derived anaphylatoxins
-
?
Lys-plasminogen + H2O
Lys + plasmin
-
-
-
-
?
Lys-plasminogen + H2O
Lys + plasmin
-
preferred substrate
-
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
-
-
-
?
N-[3-(2-Furylacryloyl)]-L-Ala-L-Lys + H2O
N-[3-(2-Furylacryloyl)]-L-Ala + L-Lys
-
-
-
-
?
osteopontin + H2O
?
-
-
-
-
?
osteopontin + H2O
?
-
thrombin-cleaved substrate
-
-
?
additional information
?
-
TFAI binds heparin
-
-
?
additional information
?
-
-
TFAI binds heparin
-
-
?
additional information
?
-
-
inhibition of the enzyme leads to facilitated induction of coronary artery thrombolysis involving the plasminogen activator
-
-
?
additional information
?
-
-
no substrates are hippuryl-L-Phe, hippurylphenyllactic acid, hippuryl-Gly-Phe
-
-
?
additional information
?
-
-
removal of Lys or Arg from carboxy-terminus of peptides, specific for basic amino acids at carboxy-terminus
-
-
?
additional information
?
-
-
the activated enzyme shows anti-fibrinolytic and fibrin clot lysis activity
-
-
?
additional information
?
-
-
the enzyme circulates as inactive zymogen in the blood stream becoming activated upon blood clotting, the enzyme inhibits fibrinolysis by cleaving C-terminal lysine from the surface of partially degraded fibrin, which stimulates the tissue-type plasminogen activator-mediated conversion of plasminogen to plasmin, the enzyme might also be involved in regulation of inflammation and tissue repair, enzyme regulation overview
-
-
?
additional information
?
-
-
the enzyme down-regulates fibrinolysis by removing carboxy-terminal lysine residues, which are ligands for plasminogen and tissue-type plasminogen activator, from partially degraded fibrin, pharmacological profile and pathphysiological role of the enzyme in rat thrombolysis
-
-
?
additional information
?
-
-
the enzyme inhibits fibrinolysis
-
-
?
additional information
?
-
-
the enzyme inhibits fibrinolysis and has a distinct role in haemostasis and a possible risk factor for thrombotic disease involving the polymorphism at position 325, overview, the plasminogen activation system plays a role in enzyme regulation
-
-
?
additional information
?
-
-
the enzyme is involved and important in control of clot stability determined by clot formation and fibrinolysis, overview
-
-
?
additional information
?
-
-
the enzyme is involved in blood clot lysis
-
-
?
additional information
?
-
-
the enzyme is involved in the regulation of the coagulation and fibrinolytic systems preventing blood loss at sites of vessel wall damage and maintainthe fluidity of the blood in the body
-
-
?
additional information
?
-
-
the enzyme is partially accountable for the antifibrinolytic activity in amniotic fluid
-
-
?
additional information
?
-
-
the enzyme might be the primary in vivo regulator of complement component C5a-mediated inflammation in the circulation, the enzyme cleaves terminal lysine from the surface of fibrin clots preventing the binding and activation of plasminogen and inhibiting whole blood clot lysis
-
-
?
additional information
?
-
-
the enzyme, activated by thrombin, protects the fibrin clot against lysis, altered enzyme activity is involved in bleeding and thrombotic disorders, the enzyme is involved in wound healing and inflammation, overview
-
-
?
additional information
?
-
-
thrombin activatable fibrinolysis inhibitor and its fibrinolytic effect in normal pregnancy
-
-
?
additional information
?
-
-
thrombin activatable fibrinolysis inhibitor, TAFI, plays a role in the delicate balance between coagulation and fibrinolysis, the stability of the fibrin clot, inflammation, thrombosis, and in Behcets disease, vascular involvement pattern in patients, overview
-
-
?
additional information
?
-
-
enzyme assay using a specific chromogenic dipeptide substrate
-
-
?
additional information
?
-
-
the enzyme binds alpha2-macroglobulin and pregnancy zone protein, which does not inhibit the enzyme
-
-
?
additional information
?
-
-
the enzyme binds to plasminogen and fibrinogen
-
-
?
additional information
?
-
-
TFAI binds heparin
-
-
?
additional information
?
-
the effects of the carboxypeptidase U system on the regulation of fibrinolysis is investigated and compared in four different in vitro models of fibrinolysis
-
-
?
additional information
?
-
pro-carboxypeptidase R is an acute phase protein under inflammatory conditions
-
?
additional information
?
-
-
pro-carboxypeptidase R is an acute phase protein under inflammatory conditions
-
?
additional information
?
-
-
the enzyme circulates as inactive zymogen in the blood stream becoming activated upon blood clotting, the enzyme inhibits fibrinolysis by cleaving C-terminal lysine from the surface of partially degraded fibrin, which stimulates the tissue-type plasminogen activator-mediated conversion of plasminogen to plasmin, the enzyme might also be involved in regulation of inflammation and tissue repair, enzyme regulation overview
-
-
?
additional information
?
-
-
the enzyme, activated by thrombin, protects the fibrin clot against lysis, altered enzyme activity is involved in bleeding and thrombotic disorders, the enzyme is involved in wound healing and inflammation, overview
-
-
?
additional information
?
-
-
pro-carboxypeptidase R production is increased under inflammatory conditions
-
?
additional information
?
-
-
the enzyme down-regulates fibrinolysis by removing carboxy-terminal lysine residues, which are ligands for plasminogen and tissue-type plasminogen activator, from partially degraded fibrin, pharmacological profile and pathphysiological role of the enzyme in rat thrombolysis
-
-
?
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(R)-2-(3-guanidinophenyl)-3-mercaptopropanoic acid
-
-
(R)-2-guanidino-3-mercaptopropanoic acid
-
-
(R)-3-(2-aminoethylthio)-2-(3-((R)-3-cyclohexyl-1-oxo-1-((1R,2R,4R)-1,7,7-trimethylbicyclo[2.2.1]heptan-2-ylamino)propan-2-yl)ureido)propanoic acid
-
-
(S)-2,5-dihydroxy-N-(1-hydroxy-3-phenylpropan-2-yl)benzamide
-
-
2-(2-amino-pyridin-4-ylmethyl)-3-mercapto-propionic acid
-
reversible inhibition, IC50: 0.0032 mM
2-(2-guanidinoethylthio)succinic acid
-
-
2-(3-carbamimidamidophenyl)-3-sulfanylpropanoic acid
-
-
2-(6-amino-pyridin-3-ylmethyl)-2-mercaptomethyl-butyric acid
-
reversible inhibition, IC50: 0.25 mM
2-Bromo-4-methylbutan-1,4-olide
-
-
2-Guanidinoethylmercaptosuccinic acid
2-mercaptomethyl-3-(6-amino-pyridin-3-yl)-2-fluoro-propionic acid
-
reversible inhibition, IC50: 0.0005 mM
2-mercaptomethyl-3-(6-amino-pyridin-3-yl)-2-hydroxy-propionic acid
-
reversible inhibition, IC50: 0.0009 mM
2-mercaptomethyl-3-piperidin-4-yl-propionic acid
-
reversible inhibition, IC50: 0.0032 mM
2-mercaptomethyl-3-pyrrolidin-3-yl-propionic acid
-
reversible inhibition, IC50: 0.0016 mM
2-[[(2-carbamimidamidoethyl)sulfanyl]methyl]butanedioic acid
-
reversible inhibition, IC50: 0.27 mM
3-(2-amino-thiazol-5-yl)-2-mercaptomethyl-propionic acid
-
reversible inhibition, IC50: 0.0013 mM
3-(2-guanidinoethylthio)-2-(mercaptomethyl)propanoic acid
-
-
3-(6-amino-2-methyl-pyridin-3-yl)-2-mercaptomethyl-propionic acid
-
reversible inhibition, IC50: 0.0063 mM
3-(6-amino-4-methyl-pyridin-3-yl)-2-mercaptomethyl-propionic acid
-
reversible inhibition, IC50: 0.0079 mM
3-(6-amino-5-chloro-pyridin-3-yl)-2-mercaptomethyl-propionic acid
-
reversible inhibition, IC50: 0.010 mM
3-(6-amino-5-hydroxymethyl-pyridin-3-yl)-2-mercaptomethyl-propionic acid
-
reversible inhibition, IC50: 0.013 mM
3-(6-amino-5-methyl-pyridin-3-yl)-2-(hydroxymethyl)-2-mercaptomethyl-propionic acid
-
reversible inhibition, IC50: 0.083 mM
3-(6-amino-5-methyl-pyridin-3-yl)-2-mercaptomethyl-2-methyl-propionic acid
-
reversible inhibition, IC50: 0.0016 mM; reversible inhibition, IC50: 0.001 mM
3-(6-amino-pyridin-3-yl)-2-mercaptomethyl-2-methyl-propionic acid
-
reversible inhibition, IC50: 0.0006 mM
3-(6-amino-pyridin-3-yl)-2-mercaptomethyl-propionic acid
-
reversible inhibition, IC50: 0.0002 mM
3-(6-aminopyridin-3-yl)-2-(1-((5-(5-chlorothiophen-2-yl)isoxazol-3-yl)methyl)-1H-imidazol-4-yl)propanoic acid
-
-
3-(6-aminopyridin-3-yl)-2-(1-isopentyl-1H-imidazol-4-yl)propanoic acid
-
-
3-(6-aminopyridin-3-yl)-2-(1H-imidazol-4-yl)propanoic acid
-
IC50: 0.000001 mM
3-(6-aminopyridin-3-yl)-2-(mercaptomethyl)propanoic acid
-
-
3-(6-aminopyridin-3-yl)-2-(sulfanylmethyl)propanoic acid
-
-
3-(6-aminopyridin-3-yl)-2-[1-(3-methylbutyl)-1H-imidazol-4-yl]propanoic acid
-
-
3-(cis-4-amino-cyclopent-2-yl)-2-mercaptomethyl-propionic acid
-
reversible inhibition, IC50: 0.001 mM
3-[(2-carbamimidamidoethyl)sulfanyl]-2-(sulfanylmethyl)propanoic acid
-
reversible inhibition, IC50: 0.02 mM
4-chloromercuribenzoate
-
-
5-amino-2-[(1-propyl-1H-imidazol-4-yl)methyl]pentanoic acid
-
-
anabaenopeptin-type cyclic peptide
-
-
-
BX-528
-
i.e. (S)-2-[3-(aminomethyl)phenyl]-3-hydroxy[(R)-2-methyl-1-[(3-phenylpropyl)sulfonyl]aminopropyl]phosphoryl propanoic acid
DL-2-mercapto methyl-3-guanidinoethyl-thiopropanoic acid
-
-
DL-2-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
-
DL-mercaptomethyl-3-guanidinoethylthiopropanoic acid
-
i.e. Plummer's inhibitor, IC50: 0.029 mM
EF-6265
-
i.e. (2S)-7-amino-2-((hydroxyl((R)-2-methyl-1-(3-phenylpropanamido)propyl)phosphoryl)methyl)heptanoic acid
epsilon-amino caproic acid
-
-
epsilon-aminocaproic acid
-
-
glycyl-glycyl-L-cysteine
-
-
guanidinoethyl-mercaptosuccinic acid
-
-
Guanidinoethylmercaptosuccinic acid
-
-
guanidinyl-L-cysteine
-
IC50: 0.0094 mM in inhibition of plasma fibrin clot lysis
Hirudo medicinalis peptide inhibitor
-
-
-
LCI
-
leech carboxypeptidase inhibitor
leech carboxypeptidase inhibitor
-
-
-
p-chloromercuribenzoate
-
-
PCI-2KR
-
i.e. peptide CKPAKNRC
peptide inhibitor from Hirudo medicinalis
-
-
-
potato carboxypeptidase inhibitor
-
potato tuber carboxypeptidase inhibitor
-
competitive inhibition in the nanomolar range
-
PTCI
-
potato carboxypeptidase inhibitor
tick carboxypeptidase inhibitor
-
[(S)-7-amino-2-[[[(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl]methyl]heptanoic acid]
-
IC50: 8.3 nM, potent and highly selective inhibitor. Systemically administered inhibitor enhances fibrinolysis in a dose- and time-dependent manner
2-Guanidinoethylmercaptosuccinic acid
-
i.e. GEMSA
2-Guanidinoethylmercaptosuccinic acid
-
-
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.00000826 mM, inhibitory effect in vivo, overview
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.000001 mM
EF6265
-
i.e. (S)-7-amino-2-[([(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl)methyl]heptanoic acid, IC50: 0.00000389 mM, inhibitory effect in vivo, overview
EF6265
-
specific inhibitor of activated form of TAFIa. A pharmacologic study to assess the effect of EF6265 on rat sepsis-induced organ dysfunction models is performed. In the endotoxemia model, posttreatment with EF6265 reduces fibrin deposits in the kidney and liver accompanied by no significant changes in platelet count and fibrinogen concentration in plasma. EF6265 also significantly decreases levels of plasma lactate dehydrogenase and aspartate aminotransferase, markers of organ dysfunction. In the sepsis model, EF6265, simultaneously administered with ceftazidime (CAZ) 2 h after Pseudomonas aeruginosa injection dramatically potentiates the interleukin-6-reducing effect of CAZ in plasma. This combined treatment also lowers plasma lactate dehydrogenase and blood urea nitrogen more potently than single treatment with CAZ
GEMSA
-
reversible, mechanism, reduces enzyme activity 10fold
GEMSA
-
i.e. guanidinoethyl-thiopropanoic acid
MERGETPA
-
D,L-2-mercaptomethyl-3-guanidinoethyl-thipropanoic acid, a carboxypeptidase inhibitor
MERGETPA
-
D,L-2-mercaptomethyl-3-guanidinoethyl-thipropanoic acid
potato carboxypeptidase inhibitor
-
-
-
potato carboxypeptidase inhibitor
-
-
potato carboxypeptidase inhibitor
-
inhibition mechanism
-
potato carboxypeptidase inhibitor
-
fibrinolytic vulnerability and the contribution of thrombin activatable fibrinolysis inhibitor to fibrinolytic defenses in normal subjects are analysed: Plasma from 30 normal subjects is exposed to tissue factor/kaolin and tissue-type plasminogen activator. Prior to activation of coagulation, samples are either not exposed or exposed to potato carboxypeptidase inhibitor (25 microg/ml, a thrombin activatable fibrinolysis inhibitor). Thrombin activatable fibrinolysis inhibitor's inhibition decreases the time to onset of maximum fibrinolysis by 45%, increases the rate of maximum lysis by 50%, and decreases clot lysis time by 45%
-
potato carboxypeptidase inhibitor
-
-
tick carboxypeptidase inhibitor
proteinaceous inhibitor TCI which is found in in the hematophagous ixodid tick Rhipicephalus bursa consists of tandem structurally similar small modules, an N-terminal and a C-terminal domain. TCI inhibits TFAIa mainly through its C-terminal domain. The C-terminal residue His75 is cleaved and the new C-terminus Leu74 approaches and contacts the TAFIa catalytic zinc ion through its carboxylate atoms. In addition to this contact, the C-terminal domain of TCI itneracts with TFAIa through 15 hydrogen bonds and 5 hydrophobic contacts
-
tick carboxypeptidase inhibitor
-
-
-
UK-396082
-
i.e. (S)-5-amino-2-((1-propyl-1H-imidazol-4-yl)methyl)pentanoic acid
additional information
-
inhibitor synthesis, overview
-
additional information
-
the enzyme is spontaneously inactivated by conformational changes
-
additional information
-
argatroban enhances fibrinolysis via a differential inhibition of thrombin-mediated activation of TAFI and factor XIII: Plasma is exposed to argatroban or heparin, with coagulation initiated with kaolin/tissue factor and fibrinolysis initiated with tissue plasminogen activator. Argatroban significantly decreases clot lysis time and increases the maximum rate of lysis compared with unexposed plasma, whereas heparin exposure only diminishs clot lysis time. Experiments with TAFI-deficient and factor XIII-deficient plasma demonstrate a sparing of thrombin-mediated factor XIII activation with concurrent inhibition of TAFI activation
-
additional information
inhibition of the carboxypeptidase U system because of hemolysis results in an increase of lysis in functional fibrinolysis assays
-
additional information
-
the enzyme is spontaneously inactivated by conformational changes
-
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glycoprotein
-
-
glycoprotein
-
the activation peptide contains four potential N-linked glycosylation sites at Asn22, Asn51, Asn63 and Asn96. The 36000 catalytic unit of 309 amino acids is not glycosylated. The glycosylation of the activation peptide may act to stabilize and increase the half-life of circulating TAFI
glycoprotein
5 N-glycosylation sites at Asn22, Asn51, Asn63, Asn86, and Asn219, detailed carbohydrate analysis, overview, no O-glycosylation
glycoprotein
-
different glycosylation patterns dependent on the enzyme source
glycoprotein
-
the enzyme contains 4 potential N-glycosylation sites at Asn22, Asn51, Asn63, and Asn96, carbohydrates account for 20% of total mass of TAFI and are responsable for stabilization
proteolytic modification
-
carboxypeptidase R is generated from pro-carboxypeptidase R by trypsin-like enzymes such as thrombin. Carboxypeptidase R regulates not only inflammatory peptides but also restricts fibrinolysis
proteolytic modification
-
carboxypeptidase R is generated from pro-carboxypeptidase R by trypsin-like enzymes such as thrombin. Carboxypeptidase R regulates not only inflammatory peptides but also restricts fibrinolysis
proteolytic modification
-
elastase can activate pro-carboxypeptidase R directly or indirectly through activation of some proteases
proteolytic modification
-
the proenzyme has a MW of 55000 Da (401 aa), the enzyme has a MW of 35999 Da (309 aa), activated at proteolytis at Arg92
proteolytic modification
-
the TAFI zymogen is activated to TAFIa by plasmin, thrombin, or the thrombin-thrombomodulin complex. Turnover-number for TAFI activation by solunin in presence of throbin is 0.74 per s, the Km-value is 0.00067 mM
proteolytic modification
-
the TAFI zymogen is activated to TAFIa by plasmin, thrombin, or the thrombin-thrombomodulin complex. Turnover-number for TAFI activation by solunin in presence of throbin is 1.06 per s, the Km-value is 0.00084 mM
proteolytic modification
-
the TAFI zymogen is activated to TAFIa by plasmin, thrombin, or the thrombin-thrombomodulin complex. Turnover-number for TAFI activation by solunin in presence of thrombin is 0.74 per s, the Km-value is 0.00082 mM
proteolytic modification
-
the TAFI zymogen is activated to TAFIa by plasmin, thrombin, or the thrombin-thrombomodulin complex. Turnover-number for TAFI activation by solunin in presence of thrombin is 0.85 per s, the Km-value is 0.00083 mM
proteolytic modification
-
activation of TAFI to TAFIa by cleavage through thrombin, activation reaction kinetics with wild-type isozymes and mutant enzymes at 37°C and pH 7.4
proteolytic modification
-
activation pathways overview, cleavage of the activation peptide from proCPU, in vitro catalyzed through thrombin, meizothrombin, plasmin, trypsin, or neutrophil elastase, only the thrombin cleaved enzyme is active, in vivo by the thrombin/thrombomodulin complex in a Ca2+-dependent manner, kinetics, overview, the plasminogen activation system, overview
proteolytic modification
-
Ca2+-dependent activation by thrombin at room temperature
proteolytic modification
-
Ca2+-dependent activation by thrombin/thrombumodulin or plasmin by cleavage of the activation peptide
proteolytic modification
Ca2+-dependent activation by thrombin/thrombumodulin or plasmin by cleavage of the activation peptide, in vitro activation by trypsin at 37°C and pH 7.5
proteolytic modification
-
ProCPU is activated by thrombin
proteolytic modification
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ProCPU is activated by thrombin or plasmin, the reaction is highly enhanced by thrombomodulin and glycosaminoglycans
proteolytic modification
-
the enzyme is activated by thrombin
proteolytic modification
-
the enzyme is synthesized as procarboxypeptidase B, activation through cleavage results in the active carboxypeptidase B and in the activation peptide of procarboxypeptidase B, enzyme activation is icreased in patients with acute pancreatitis, quantitative analysis of healthy persons' and patients' serum content of activation peptide, overview
proteolytic modification
-
the enzyme is synthesized as zymogen TAFI, activation by the thrombin/thrombomodulin or by plasmin to the active form TAFIa, cleavage patterns, overview
proteolytic modification
-
the enzyme is synthesized as zymogen, activation by the thrombin/thrombomodulin complex
proteolytic modification
-
the enzyme is synthesized as zymogen, activation by the thrombin/thrombomodulin complex or by plasmin
proteolytic modification
the enzyme is synthesized as zymogen, activation by thrombin and thrombomodulin at pH 8.5
proteolytic modification
-
the enzyme is synthesized as zymogen, activation of TAFI by thrombin to TAFIa, inactivation of TAFIa by cleavage through thrombin at Arg302
proteolytic modification
-
the inactive zymogen proCPU is Ca2+-dependently activated by thrombin/thrombumodulin or plasmin
proteolytic modification
-
the proenzyme is activated by many factors including thrombin, thrombomodulin, plasmmin, and trypsin
proteolytic modification
-
the recombinant pre-enzyme and pre-enzyme chimera are activated by thrombin/thrombomodulin in presence of Ca2+ through cleavage at Arg92 releasing the activation peptide, cleavage of Arg302 leads to inactivation by disruption of the active site, cleavage pattern with wild-type and chimeric muatnt enzymes, overview, plasmin activates inactive TAFI and inactivates active TAFI, overview
proteolytic modification
-
proteolytic enzymes activate TAFI into TAFIa, by cleaving off the N-terminal activation peptide (amino acids 1-92), from the enzyme moiety. TAFIa is active both before and after removal of the activation peptide, and the half-life of TAFIa is identical in the two preparations
proteolytic modification
the inactive precursor procarboxypeptidase U is converted to its active form by thrombin, the thrombin-thrombomodulin complex or plasmin
proteolytic modification
the plasma zymogen pro-carboxypeptidase R is a plasma zymogen activated during coagulation
proteolytic modification
-
the enzyme is synthesized as zymogen TAFI, activation by the thrombin to the active form TAFIa
proteolytic modification
-
the enzyme is synthesized as zymogen, activation of TAFI by thrombin to TAFIa, inactivation of TAFIa by cleavage through thrombin at Arg302
proteolytic modification
-
carboxypeptidase R is generated from pro-carboxypeptidase R by trypsin-like enzymes such as thrombin. Carboxypeptidase R regulates not only inflammatory peptides but also restricts fibrinolysis
proteolytic modification
-
carboxypeptidase R is generated from pro-carboxypeptidase R by trypsin-like enzymes such as thrombin. Carboxypeptidase R regulates not only inflammatory peptides but also restricts fibrinolysis
proteolytic modification
-
procarboxypeptidase R is generated from pro-carboxypeptidase R, a plasma zymogen, by proteolytic enzymes such as thrombin, thrombin-thrombomodulin complex and plasmin
proteolytic modification
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the enzyme is activated by thrombin
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A505G
-
naturally occurring polymorphism
A93V
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mutant is comparably to wild-type activated by thrombin, mutant is slightly less activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.205, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000169, mutation shows no effect on the activation by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00043, Km (mM) (hippuryl-arginine, activated by plasmin): 0.00001, intrinsic stability of activated TAFI (half-life): 6.3 min
D87A
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activated with similar kinetics as wild-type enzyme by thrombin-thrombomodulin. Increase in activation by plasmin. Thermal inactivation at 37°C is similar to that of the wild-type enzyme
I182R
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site-directed mutagenesis, the mutant shows reduced activition by thrombin but similar fibrinogen and plasminogen binding capacitiy compared to the wild-type enzyme
I183E
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site-directed mutagenesis, the mutant shows reduced activition by thrombin but similar fibrinogen and plasminogen binding capacitiy compared to the wild-type enzyme
I325I
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a higher frequency of the most stable Ile325Ile proCPU is seen among carriers of FII G20210A mutation compared to the control group in comparison to Thr325Thr and Thr325Ile proCPU. In addition, proCPU as a risk factor for thrombosis is evaluated. In heterozygous carriers of FV Leiden or FII G20210A high levels of proCPU confers to an almost 4fold increased risk for spontaneous onset thrombosis. The more stable Ile325Ile proCPU seems to impose a higher risk for clinical manifestation of the thrombophilic condition
S305C/T329I
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generation of a stable activated thrombin activable fibrinolysis inhibitor variant by site-directed mutagenesis, the mutant's half-life is 11fold increased compared to the wild-type enzyme, the mutant also shows about 3fold higher fibrin clot lysis activityoverview
S90A
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activated with similar kinetics as wild-type enzyme by thrombin-thrombomodulin. Increase in activation by plasmin. Thermal inactivation at 37°C is similar to that of the wild-type enzyme
S90D/S94V/S90D
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mutant is not activated by thrombin or by thrombin in the presence of thrombomodulin, mutant is weakly activated by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00004, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000005, intrinsic stability of activated TAFI (half-life): 5.9 min
S94V
-
mutant is considerably more effectively activated by thrombin, mutant is also activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.328, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000232, mutation shows no effect on the activation by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.0003, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000006, intrinsic stability of activated TAFI (half-life): 6.1 min
T147A
-
naturally occurring polymorphism
T325I/T329I/H333Y/H335Q
-
inactive mutant has a 70fold increased half-life and a 3fold to 5fold increased antifibrinolytic function as compared to wild-type, mutant aggregates into large, insoluble complexes that can be removed by centrifugation
moe
-
construction of enzyme-deficient mice by gene disruption, which is not lethal and does not cause a pathogenic phenotype, the mice show delayed wound healing, overview
P91S
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mutant exhibits specific impairment of activation by thrombin or thrombin-TM, thrombin alone, and thrombin alone or plasmin, respectively
P91S
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mutant is not activated by thrombin or by thrombin in the presence of thrombomodulin, mutant is weakly activated by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00020, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000007, intrinsic stability of activated TAFI (half-life): 6.3 min
R302Q
-
specific activity with hippuryl-Arg is approximately half that of either recombinant wild-type enzyme or plasma derived enzymeR302Q-TAFIa is not proteolyzed by thrombin, even when 10times higher concentrations of thrombin/thrombomodulin are used
R302Q
-
mutant aggregates similarly to wild-type protein
R92K
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mutant exhibits specific impairment of activation by thrombin or thrombin-TM, thrombin alone, and thrombin alone or plasmin, respectively
R92K
-
mutant is not activated by thrombin, mutant is very efficiently activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.215, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000229, mutant is activated by plasmin with similar kinetics as wild-type, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00039, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000006, intrinsic stability of activated TAFI (half-life): 7.1 min
S90P
-
mutant exhibits specific impairment of activation by thrombin or thrombin-TM, thrombin alone, and thrombin alone or plasmin, respectively
S90P
-
mutant is not activated by thrombin, mutant is very efficiently activated by thrombin in the presence of thrombomodulin, kcat (1/sec) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.377, Km (mM) (p-anisylazoformyl-L-arginine, activated by thrombin in the presence of thrombomodulin): 0.000162, mutant is weakly activated by plasmin, kcat (1/sec) (hippuryl-arginine, activated by plasmin): 0.00008, Km (mM) (hippuryl-arginine, activated by plasmin): 0.000009, intrinsic stability of activated TAFI (half-life): 5.5 min
T325I
-
naturally occurring mutant showing a twofold increased stability compared to the wild-type enzyme
T325I
-
naturally occurring polymorphism
T325I
-
distribution of the Thr325Ile proCPU polymorphism in 193 patients with mucocutaneous bleeding of whom 116 are bleeders of unknown cause , and in 143 healthy, age and sex-matched controls is analyzed. ProCPU concentration is higher in women than in men, increases with age, and is significantly correlated with clot lysis time, platelet count, APTT, and PT. proCPU levels are unexpectedly higher in patients than in controls. The allele distribution of the Thr325Ile proCPU polymorphism is similar in both groups, with a low percentage of homozygous Ile/Ile
additional information
-
generation of a TAFI a form with a highly stable activity by replacing a region in TAFI with the corresponding region in pancreatic CPB (carboxypeptidase B). TAFI-CPB(293-333) can be activated by thrombin-thrombomodulin, but not as efficient as wild-type TAFI. After activation, this chimeric enzyme is unstable and hardly able to prolong clot lysis of TAFI-deficient plasma. Binding of the mutant enzyme to both plasminogen and fibrinogen is normal compared to wild-type TAFI. TAFI-CPB(293-401) can be activated by thrombin-thrombomodulin, although at a lower rate compared with wild-type TAFI. The activated mutant displays a markedly prolonged half-life of 1.5 h. The chimeric enzyme does not bind plasminogen and fibrinogen and can prolong the clot lysis time in TAFI-deficient plasma, although not as efficiently as wild-type TAFI
additional information
-
mutant with the fibrinogen Bbeta thrombin cleavage site Ala-Arg-Gly-His-Arg substituted into positions 91-95: activated with similar kinetics as wild-type enzyme by thrombin-thrombomodulin, activated by plasmin with the same kinetics as wild-type enzyme. Mutant enzyme with the protein C thrombin cleavage site Asp-Pro-Arg-Leu-Ile-Asp substituted into positions 90-95: no measurable activation by plasmin
additional information
-
construction of chimeric proteins composed by wild-type TAFI isozymes Thr147 and Thr325, and carboxypeptidase B, CPB, fragments comprising residues 288-395 and 288-327, the chimeric mutants show increase stability and 32-34fold increased half-lives compared to the wild-type TAFI
additional information
-
enzyme disorder phenotype, overview
additional information
immobilization of purified recombinnat Pro-CPU on Sepharose for specific antibody purification
additional information
-
immobilization of purified recombinnat Pro-CPU on Sepharose for specific antibody purification
additional information
-
the enzyme shows polymorphisms, e.g. at residue 325, genotypes, correlated diseases, overview
additional information
-
circulating TAFI levels and carotid intima-media thickness (CIMT) in polycystic ovary syndrome (PCOS) patients and control subjects are analysed. Plasma TAFI levels are similarly in polycystic ovary syndrome patients compared with healthy controls. No difference is observed in the combined IMT among the studied groups
additional information
-
coagulation and fibrinolytic parameters including TAFI and TFPI are assessed in patients with hypothyroidism: Factors V, VII, VIII activities, von Willebrand factor, protein C, protein S, thrombomodulin, TFPI, and TAFI are measured. Compared with the control subjects, factor VII activity, and thrombomodulin Ag and TAFI Ag levels are significantly increased in patients with hypothyroidism, whereas FV, FVIII, vWF, protein C and protein S activities, and TFPI Ag levels are significantly decreased
additional information
-
HT1080 cells mediate activation of TAFI in plasma in the presence of soluble-type thrombomodulin through cell-dependent prothrombin activation. HT1080 cells stably expressing thrombomodulin (TM-HT1080) mediate plasma TAFI activation without added soluble-type thrombomodulin, wild-type cells and Mock-transfected HT1080 cells (Mock) do not. Production of TAFIa suppresses cell-mediated plasminogen activation. Cell invasion by TMHT1080 is partially enhanced by addition of a TAFIa/CPB inhibitor
additional information
-
plasma TAFI and PAI-1 antigen levels are measured in pregnant women with gestational diabetes, pregnant women with normal glucose tolerance, and age-matched non-pregnant women with no history of gestational diabetes. Increased plasma TAFI antigen levels are found in pregnant women compared to non-pregnant controls. No statistically significant difference in TAFI antigen levels is observed between women with gestational diabetes and pregnant controls. Plasma PAI-1 antigen levels are higher in gestational diabetes than pregnant and non-pregnant controls
additional information
-
proCPU levels in thrombophilia carriers and healthy subjects are assessed: Results show that patients with inherited thrombophilia have a tendency toward lower mean proCPU plasma levels compared to healthy controls. This difference is only significant in carriers of factor II G20210A
additional information
-
TAFI activity status and the effect of L-thyroxin hormone replacement treatment on fibrinolytic system in patients with Hashimotos thyroiditis is analysed: In the control group, TAFI activity levels are 9.6 microgram/ml. In patients with L-thyroxin before and after treatment there are high levels of TAFI activity value of 14.2 and 12.9 microgram/ml, respectively. In the patient group, after L-thyroxin treatment TAFI activity levels are decreased but they are not statistically significant. When compared to the control group, high levels of TAFI activity are observed in the patient group
additional information
-
the gastric intramucosal concentrations of TAFI are measured by enzyme immunoassay. This study comprises 65 patients with gastroduodenal disorders. The gastric levels of TAFI and plasminogen activator inhibitor-1 are significantly increased in patients with Helicobacter pylori compared to those without infection or cured Helicobacter pylori
additional information
-
the levels of TAFI antigen and also its relationship with other hemostasis markers in a group of patients affected with polycystic ovary syndrome (PCOS)-under Diane-35 (ethinyl estradiol/cyproterone acetate) treatment or not compared with a group of healthy controls is analysed. TAFI antigen levels of groups A and B are significantly higher than in controls, but no difference is observed between them. All of the other coagulation and fibrinolysis parameters are comparable between the three groups
additional information
-
variant mutants are constructed and expressed mutant variants that have key substitutions in the amino acids surrounding the scissile Arg92-Ala93 bond. Variants are identified that show patterns of resistance to specific activators. The variants that are tested also showed antifibrinolytic potentials that can be rationalized in terms of which enzymes are capable of activating them
additional information
-
enzyme-deficient mice phenotype, overview
additional information
the development of immune complex-mediated glomerulonephritis in wild-type and TAFI-deficient mice is compared. After six weeks of treatment with horse spleen apoferritin and lipoplysaccharide to induce glomerulonephritis, mice deficient in TAFI have significantly better renal function as shown by lower concentrations of albumin in urine and blood urea nitrogen compared to wild-type mice. The activity of plasmin and matrix metalloproteinases is significantly increased, and mesangial matrix expansion and the deposition of collagen and fibrin in kidney tissues are significantly decreased in TAFI-knockout mice as compared to their wild-type counterparts
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Bajazar, L.; Nesheim, M.; Morser, J.; Tracy, P.B.
Both cellular and soluble forms of thrombomodulin inhibit fibrinolysis by potentiating the activation of thrombin-activable fibrinolysis inhibitor
J. Biol. Chem.
273
2792-2798
1998
Homo sapiens
brenda
Boffa, M.B.; Wang, W.; Bajzar, l.; Nesheim, M.E.
Plasma and recombinant thrombin-activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respsct to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties
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273
2127-2135
1998
Homo sapiens
brenda
Kokame, K.; Zheng, X.; Sadler, J.E.
Activation of thrombin-activable fibrinolysis inhibitor requires epidermal growth factor-like domain 3 of thrombomodulin and is inhibited competitively by protein C
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1998
Homo sapiens
brenda
Cote, H.; Bajzar, L.; Stevens, W.K.; Samis, J.A.; Morser, J.; MacGillivray, R.T.A.; Nesheim, M.E.
Functional characterization of recombinant human meizothrombin and meizothrombin (desF1)
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1997
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Sakharov, D.V.; Plow, E.F.; Rijken, D.C.
On the mechanism of the antifibrinolytic activity of plasma carboxypeptidase B
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272
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1997
Homo sapiens
brenda
Nesheim, M.; Wang, W.; Boffa, M.; Nagashima, M.; Morser, J.; Bajzar, L.
Thrombin, thrombomodulin and TAFI in the molecular link between coagulation and fibrinolysis
Thromb. Haemost.
78
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1997
Homo sapiens
brenda
Von dem Borne, P.A.K.; Bajzar, L.; Meijers, J.C.M.; Nesheim, M.E.; Bouma, B.N.
Thrombin-mediated activation of factor XI results in a thrombin-activable fibrinolysis inhibitor-dependent inhibition of fibrinolysis
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99
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Homo sapiens
brenda
Broze, G.J.
Thrombin-dependent inhibition of fibrinolysis
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3
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1996
Homo sapiens
brenda
Bajzar, L.; Morser, J.; Nesheim, M.
TAFI, or plasma procarboxypeptidase B couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
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271
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1996
Homo sapiens
brenda
Broze, G.J.; Higuchi, D.A.
Coagulation-dependent inhibition of fibrinolysis: role of carboxypeptidase-U and the premature lysis of clots from hepatitis plasma
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1996
Homo sapiens
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Tan, A.K.; Eaton, D.L.
Activation and characterization of procarboxypeptidase B from human plasma
Biochemistry
34
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1995
Homo sapiens
brenda
Bajzar, L.; Manuel, R.; Nesheim, M.E.
Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
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270
14477-14484
1995
Homo sapiens
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Wang, W.; Hendricks, D.F.; Scharpe, S.S.
Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen
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269
15937-15944
1994
Homo sapiens
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Eaton, D.L.; Malloy, B.E.; Tsai, S.P.; Henzel, W.; Drayna, D.
Isolation, molecular cloning, and partial characterization of a novel carboxypeptidase B from human plasma
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1991
Homo sapiens
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Kawamura, T.; Okada, N.; Okada, H.
Elastase from activated human neutrophils activates procarboxypeptidase R
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2002
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Mao, S.S.; Colussi, D.; Bailey, C.M.; Bosserman, M.; Burlein, C.; Gardell, S.J.; Carroll, S.S.
Electrochemiluminescence assay for basic carboxypeptidases: inhibition of basic carboxypeptidases and activation of thrombin-activatable fibrinolysis inhibitor
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319
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2003
Chlorocebus aethiops, Canis lupus familiaris, Homo sapiens, Macaca mulatta, Rattus norvegicus
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Rational structure-based design of a novel carboxypeptidase R inhibitor
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Homo sapiens
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Marx, P.F.; Hackeng, T.M.; Dawson, P.E.; Griffin, J.H.; Meijers, J.C.; Bouma, B.N.
Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage
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Homo sapiens
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Schneider, M.; Nagashima, M.; Knappe, S.; Zhao, L.; Morser, J.; Nesheim, M.
Amino acid residues in the P6-P'3 region of thrombin-activable fibrinolysis inhibitor (TAFI) do not determine the thrombomodulin dependence of TAFI activation
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277
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2002
Homo sapiens
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Marx, P.F.; Havik, S.R.; Marquart, J.A.; Bouma, B.N.; Meijers, J.C.
Generation and characterization of a highly stable form of activated thrombin-activable fibrinolysis inhibitor
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279
6620-6628
2004
Homo sapiens
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Sato, T.; Miwa, T.; Akatsu, H.; Matsukawa, N.; Obata, K.; Okada, N.; Campbell, W.; Okada, H.
Pro-carboxypeptidase R is an acute phase protein in the mouse, whereas carboxypeptidase N is not
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165
1053-1058
2000
Mus musculus (Q9JHH6), Mus musculus
brenda
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Enhancement of fibrinolysis by EF6265 [(S)-7-amino-2-[[[(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxypho sphinoyl] methyl]heptanoic acid], a specific inhibitor of plasma carboxypeptidase B
J. Pharmacol. Exp. Ther.
309
607-615
2004
Homo sapiens, Rattus norvegicus
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Kato, T.; Akatsu, H.; Sato, T.; Matsuo, S.; Yamamoto, T.; Campbell, W.; Hotta, N.; Okada, N.; Okada, H.
Molecular cloning and partial characterization of rat procarboxypeptidase R and carboxypeptidase N
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44
719-728
2000
Rattus norvegicus
brenda
Campbell, W.D.; Lazoura, E.; Okada, N.; Okada, H.
Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
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46
131-134
2002
Homo sapiens
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Komura, H.; Shimomura, Y.; Yumoto, M.; Katsuya, H.; Okada, N.; Okada, H.
Heat stability of carboxypeptidase R of experimental animals
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46
217-223
2002
Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Rattus norvegicus
brenda
Bouma, B.N.; Marx, P.F.; Mosnier, L.O.; Meijers, J.C.
Thrombin-activatable fibrinolysis inhibitor (TAFI, plasma procarboxypeptidase B, procarboxypeptidase R, procarboxypeptidase U)
Thromb. Res.
101
329-354
2001
Papio sp., Canis lupus familiaris, Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Valnickova, Z.; Christensen, T.; Skottrup, P.; Th?gersen, I.B.; H?jrup, P.; Enghild, J.J.
Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation
Biochemistry
45
1525-1535
2006
Homo sapiens (Q96IY4), Homo sapiens
brenda
Polla, M.O.; Tottie, L.; Norden, C.; Linschoten, M.; Muesil, D.; Trumpp-Kallmeyer, S.; Aukrust, I.R.; Ringom, R.; Holm, K.H.; Neset, S.M.; Sandberg, M.; Thurmond, J.; Yu, P.; Hategan, G.; Anderson, H.
Design and synthesis of potent, orally active, inhibitors of carboxypeptidase U (TAFIa)
Bioorg. Med. Chem.
12
1151-1175
2004
Homo sapiens
brenda
Willemse, J.L.; Hendriks, D.F.
Measurement of procarboxypeptidase U (TAFI) in human plasma: a laboratory challenge
Clin. Chem.
52
30-36
2006
Homo sapiens
brenda
Stroemqvist, M.; Hansson, L.; Andersson, J.O.; Johansson, T.; Edlund, M.; Enoksson, M.; Goossens, F.; Scharpe, S.; Hendriks, D.
Properties of recombinant human plasma procarboxypeptidase U produced in mammalian and insect cells
Clin. Chim. Acta
347
49-59
2004
Homo sapiens (Q96IY4), Homo sapiens
brenda
Marx, P.F.
Thrombin-activatable fibrinolysis inhibitor
Curr. Med. Chem.
11
2335-2348
2004
Homo sapiens, Mus musculus
brenda
Ceresa, E.; Van de Borne, K.; Peeters, M.; Lijnen, H.R.; Declerck, P.J.; Gils, A.
Generation of a stable activated thrombin activable fibrinolysis inhibitor variant
J. Biol. Chem.
281
15878-15883
2006
Homo sapiens
brenda
Marx P. , M.P.; Meijers J. C. , M.J.
Mechanism of action of carboxypeptidase U: staying above the threshold
J. Thromb. Haemost.
2
414-415
2004
Homo sapiens
brenda
Guimaraes, A.H.; Bertina, R.M.; Rijken, D.C.
A new functional assay of thrombin activatable fibrinolysis inhibitor
J. Thromb. Haemost.
3
1284-1292
2005
Homo sapiens
brenda
Marx, P.F.; Havik, S.R.; Bouma, B.N.; Meijers, J.C.
Role of isoleucine residues 182 and 183 in thrombin-activatable fibrinolysis inhibitor
J. Thromb. Haemost.
3
1293-1300
2005
Homo sapiens
brenda
Willemse, J.L.; Leurs, J.R.; Hendriks, D.F.
Fast kinetic assay for the determination of procarboxypeptidase U in human plasma
J. Thromb. Haemost.
3
2353-2355
2005
Homo sapiens
brenda
Matthews, K.W.; Mueller-Ortiz, S.L.; Wetsel, R.A.
Carboxypeptidase N: a pleiotropic regulator of inflammation
Mol. Immunol.
40
785-793
2004
Homo sapiens
brenda
Borgstroem, A.; Regner, S.
Active carboxypeptidase B is present in free form in serum from patients with acute pancreatitis
Pancreatology
5
530-536
2005
Homo sapiens
brenda
Bouma, B.N.; Mosnier, L.O.
Thrombin activatable fibrinolysis inhibitor (TAFI) at the interface between coagulation and fibrinolysis
Pathophysiol. Haemost. Thromb.
33
375-381
2005
Homo sapiens, Mus musculus
brenda
Bouma, B.N.; Meijers, J.C.
New insights into factors affecting clot stability: A role for thrombin activatable fibrinolysis inhibitor (TAFI; plasma procarboxypeptidase B, plasma procarboxypeptidase U, procarboxypeptidase R)
Semin. Hematol.
41 Suppl 1
13-19
2004
Homo sapiens
brenda
Mousa, H.A.; Downey, C.; Alfirevic, Z.; Toh, C.H.
Thrombin activatable fibrinolysis inhibitor and its fibrinolytic effect in normal pregnancy
Thromb. Haemost.
92
1025-1031
2004
Homo sapiens
brenda
Frere, C.; Morange, P.E.; Saut, N.; Tregouet, D.A.; Grosley, M.; Beltran, J.; Juhan-Vague, I.; Alessi, M.C.
Quantification of thrombin activatable fibrinolysis inhibitor (TAFI) gene polymorphism effects on plasma levels of TAFI measured with assays insensitive to isoform-dependent artefact
Thromb. Haemost.
94
373-379
2005
Homo sapiens
brenda
Leurs, J.; Hendriks, D.
Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease
Thromb. Haemost.
94
471-487
2005
Homo sapiens
brenda
Donmez, A.; Aksu, K.; Celik, H.A.; Keser, G.; Cagirgan, S.; Omay, S.B.; Inal, V.; Aydin, H.H.; Tombuloglu, M.; Doganavsargil, E.
Thrombin activatable fibrinolysis inhibitor in Behcets disease
Thromb. Res.
115
287-292
2005
Homo sapiens
brenda
Do, Y.H.; Gifford-Moore, D.S.; Beight, D.W.; Rathnachalam, R.; Klimkowski, V.J.; Warshawsky, A.M.; Lu, D.
Inhibition of thrombin activatable fibrinolysis inhibitor by cysteine derivatives
Thromb. Res.
116
265-271
2005
Homo sapiens
brenda
Bjoerkman, J.A.; Abrahamsson, T.I.; Nerme, V.K.; Mattsson, C.J.
Inhibition of carboxypeptidase U (TAFIa) activity improves rt-PA induced thrombolysis in a dog model of coronary artery thrombosis
Thromb. Res.
116
519-524
2005
Canis lupus familiaris
brenda
Uszynski, W.; Uszynski, M.; Zekanowska, E.
Thrombin activatable fibrinolysis inhibitor (TAFI) in human amniotic fluid. A preliminary study
Thromb. Res.
119
241-245
2006
Homo sapiens
brenda
Higuchi, T.; Nakamura, T.; Kakutani, H.; Ishii, H.
Thrombomodulin suppresses invasiveness of HT1080 tumor cells by reducing plasminogen activation on the cell surface through activation of thrombin-activatable fibrinolysis inhibitor
Biol. Pharm. Bull.
32
179-185
2009
Homo sapiens
brenda
Nielsen, V.G.
Clot life span model analysis of clot growth and fibrinolysis in normal subjects: role of thrombin activatable fibrinolysis inhibitor
Blood Coagul. Fibrinolysis
19
283-287
2008
Homo sapiens
brenda
Kilicarslan, A.; Yavuz, B.; Guven, G.S.; Atalar, E.; Sahiner, L.; Beyazit, Y.; Kekilli, M.; Ozer, N.; Oz, G.; Haznedaroglu, I.C.; Sozen, T.
Fenofibrate improves endothelial function and decreases thrombin-activatable fibrinolysis inhibitor concentration in metabolic syndrome
Blood Coagul. Fibrinolysis
19
310-314
2008
Homo sapiens
brenda
Nielsen, V.G.; Kirklin, J.K.
Argatroban enhances fibrinolysis by differential inhibition of thrombin-mediated activation of thrombin activatable fibrinolysis inhibitor and factor XIII
Blood Coagul. Fibrinolysis
19
793-800
2008
Homo sapiens
brenda
Matus, V.; Willemse, J.; Quiroga, T.; Goycoolea, M.; Aranda, E.; Panes, O.; Pereira, J.; Hendriks, D.; Mezzano, D.
Procarboxypeptidase U (TAFI) and the Thr325Ile proCPU polymorphism in patients with hereditary mucocutaneous hemorrhages
Clin. Chim. Acta
401
158-161
2009
Homo sapiens
brenda
Koldas, M.; Gummus, M.; Seker, M.; Seval, H.; Hulya, K.; Dane, F.; Kural, A.; Gumus, A.; Salepci, T.; Turhal, N.S.
Thrombin-activatable fibrinolysis inhibitor levels in patients with non-small-cell lung cancer
Clin. Lung Cancer
9
112-115
2008
Homo sapiens (Q8IWV7), Homo sapiens
brenda
Brouns, R.; Heylen, E.; Sheorajpanday, R.; Willemse, J.L.; Kunnen, J.; De Surgeloose, D.; Hendriks, D.F.; De Deyn, P.P.
Carboxypeptidase U (TAFIa) decreases the efficacy of thrombolytic therapy in ischemic stroke patients
Clin. Neurol. Neurosurg.
111
165-170
2009
Homo sapiens
brenda
Muto, Y.; Suzuki, K.; Iida, H.; Sakakibara, S.; Kato, E.; Itoh, F.; Kakui, N.; Ishii, H.
EF6265, a novel thrombin-activatable fibrinolysis inhibitor-a inhibitor, protects against sepsis-induced organ dysfunction in rats
Crit. Care Med.
37
1744-1749
2009
Rattus norvegicus
brenda
Akinci, B.; Demir, T.; Saygili, S.; Yener, S.; Alacacioglu, I.; Saygili, F.; Bayraktar, F.; Yesil, S.
Gestational diabetes has no additional effect on plasma thrombin-activatable fibrinolysis inhibitor antigen levels beyond pregnancy
Diabetes Res. Clin. Pract.
81
93-96
2008
Homo sapiens
brenda
Erem, C.; Ucuncu, O.; Yilmaz, M.; Kocak, M.; Nuhoglu, I.; Ersoz, H.O.
Increased thrombin-activatable fibrinolysis inhibitor and decreased tissue factor pathway inhibitor in patients with hypothyroidism
Endocrine
35
75-80
2009
Homo sapiens
brenda
Koutroubakis, I.E.; Sfiridaki, A.; Tsiolakidou, G.; Coucoutsi, C.; Theodoropoulou, A.; Kouroumalis, E.A.
Plasma thrombin-activatable fibrinolysis inhibitor and plasminogen activator inhibitor-1 levels in inflammatory bowel disease
Eur. J. Gastroenterol. Hepatol.
20
912-916
2008
Homo sapiens
brenda
Erdogan, M.; Karadeniz, M.; Alper, G.E.; Tamsel, S.; Uluer, H.; Caglayan, O.; Saygili, F.; Yilmaz, C.
Thrombin-activatable fibrinolysis inhibitor and cardiovascular risk factors in polycystic ovary syndrome
Exp. Clin. Endocrinol. Diabetes
116
143-147
2008
Homo sapiens
brenda
Karakurt, F.; Gumus, I.I.; Bavbek, N.; Kargili, A.; Koca, C.; Selcoki, Y.; Ozbek, M.; Kosar, A.; Akcay, A.
Increased thrombin-activatable fibrinolysis inhibitor antigen levels as a clue for prothrombotic state in polycystic ovary syndrome
Gynecol. Endocrinol.
24
491-497
2008
Homo sapiens
brenda
Ikeda, A.; Gabazza, E.C.; Morser, J.; Imoto, I.; Kuroda, M.; DAlessandro-Gabazza, C.N.; Hara, K.; Ruiz, D.B.; Bernabe, P.G.; Katsurahara, M.; Toda, M.; Kobayashi, Y.; Yano, Y.; Sumida, Y.; Suzuki, K.; Taguchi, O.; Takei, Y.
Presence of thrombin-activatable fibrinolysis inhibitor in Helicobacter pylori-associated gastroduodenal disease
Helicobacter
14
147-155
2009
Homo sapiens
brenda
Cetinkalp, S.; Tobu, M.; Karadeniz, M.; Buyukkececi, F.; Yilmaz, C.
The effect of hormone replacement treatment on thrombin-activatable fibrinolysis inhibitor activity levels in patients with Hashimoto thyroiditis
Intern. Med.
48
281-285
2009
Homo sapiens
brenda
Willemse, J.L.; Brouns, R.; Heylen, E.; De Deyn, P.P.; Hendriks, D.F.
Carboxypeptidase U (TAFIa) activity is induced in vivo in ischemic stroke patients receiving thrombolytic therapy
J. Thromb. Haemost.
6
200-202
2008
Homo sapiens
brenda
Marx, P.F.; Plug, T.; Havik, S.R.; Moergelin, M.; Meijers, J.C.
The activation peptide of thrombin-activatable fibrinolysis inhibitor: a role in activity and stability of the enzyme?
J. Thromb. Haemost.
7
445-452
2009
Homo sapiens
brenda
Foley, J.H.; Nesheim, M.E.
Soluble thrombomodulin partially corrects the premature lysis defect in FVIII-deficient plasma by stimulating the activation of thrombin activatable fibrinolysis inhibitor
J. Thromb. Haemost.
7
453-459
2009
Homo sapiens
brenda
Miah, M.F.; Boffa, M.B.
Functional analysis of mutant variants of thrombin-activatable fibrinolysis inhibitor resistant to activation by thrombin or plasmin
J. Thromb. Haemost.
7
665-672
2009
Homo sapiens
brenda
Sanglas, L.; Valnickova, Z.; Arolas, J.L.; Pallares, I.; Guevara, T.; Sola, M.; Kristensen, T.; Enghild, J.J.; Aviles, F.X.; Gomis-Rueth, F.X.
Structure of activated thrombin-activatable fibrinolysis inhibitor, a molecular link between coagulation and fibrinolysis
Mol. Cell
31
598-606
2008
Homo sapiens, Bos taurus (Q2KIG3), Bos taurus
brenda
Soni, H.; Sharma, A.; Bhatt, S.; Jain, M.R.; Patel, P.R.
Antithrombotic effects due to pharmacological modulation of thrombin-activatable fibrinolysis inhibitor in rats
Pharmacology
82
304-309
2008
Rattus norvegicus (Q9EQV9)
brenda
Folkeringa, N.; Coppens, M.; Veeger, N.J.; Bom, V.J.; Middeldorp, S.; Hamulyak, K.; Prins, M.H.; Bueller, H.R.; van der Meer, J.
Absolute risk of venous and arterial thromboembolism in thrombophilic families is not increased by high thrombin-activatable fibrinolysis inhibitor (TAFI) levels
Thromb. Haemost.
100
38-44
2008
Homo sapiens
brenda
Bruno, N.E.; Yano, Y.; Takei, Y.; Qin, L.; Suzuki, T.; Morser, J.; D'Alessandro-Gabazza, C.N.; Mizoguchi, A.; Suzuki, K.; Taguchi, O.; Gabazza, E.C.; Sumida, Y.
Immune complex-mediated glomerulonephritis is ameliorated by thrombin-activatable fibrinolysis inhibitor deficiency
Thromb. Haemost.
100
90-100
2008
Mus musculus (Q9JHH6)
brenda
Heylen, E.; Miljic, P.; Willemse, J.; Djordjevic, V.; Radojkovic, D.; Colovic, M.; Elezovic, I.; Hendriks, D.
Procarboxypeptidase U (TAFI) contributes to the risk of thrombosis in patients with hereditary thrombophilia
Thromb. Res.
124
427-432
2009
Homo sapiens
brenda
Heylen, E.; Van Goethem, S.; Willemse, J.; Olsson, T.; Augustyns, K.; Hendriks, D.
Development of a sensitive and selective assay for the determination of procarboxypeptidase U (thrombin-activatable fibrinolysis inhibitor) in plasma
Anal. Biochem.
396
152-154
2010
Homo sapiens
brenda
Heylen, E.; Van Goethem, S.; Augustyns, K.; Hendriks, D.
Measurement of carboxypeptidase U (active thrombin-activatable fibrinolysis inhibitor) in plasma: Challenges overcome by a novel selective assay
Anal. Biochem.
403
114-116
2010
Homo sapiens
brenda
Fernandez, D.; Pallares, I.; Vendrell, J.; Aviles, F.X.
Progress in metallocarboxypeptidases and their small molecular weight inhibitors
Biochimie
93
1484-1500
2010
Homo sapiens
brenda
Willemse, J.L.; Heylen, E.; Nesheim, M.E.; Hendriks, D.F.
Carboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy?
J. Thromb. Haemost.
7
1962-1971
2009
Homo sapiens
brenda
Brouns, R.; Heylen, E.; Willemse, J.L.; Sheorajpanday, R.; De Surgeloose, D.; Verkerk, R.; De Deyn, P.P.; Hendriks, D.F.
The decrease in procarboxypeptidase U (TAFI) concentration in acute ischemic stroke correlates with stroke severity, evolution and outcome
J. Thromb. Haemost.
8
75-80
2010
Homo sapiens
brenda
Leenaerts, D.; Bosmans, J.M.; van der Veken, P.; Sim, Y.; Lambeir, A.M.; Hendriks, D.
Plasma levels of carboxypeptidase U (CPU, CPB2 or TAFIa) are elevated in patients with acute myocardial infarction
J. Thromb. Haemost.
13
2227-2232
2015
Homo sapiens (Q96IY4), Homo sapiens
brenda
Leenaerts, D.; Loyau, S.; Mertens, J.C.; Boisseau, W.; Michel, J.B.; Lambeir, A.M.; Jandrot-Perrus, M.; Hendriks, D.
Carboxypeptidase U (CPU, carboxypeptidase B2, activated thrombin-activatable fibrinolysis inhibitor) inhibition stimulates the fibrinolytic rate in different invitro models
J. Thromb. Haemost.
16
2057-2069
2018
Homo sapiens (Q96IY4)
brenda
Mertens, J.; Claesen, K.; Leenaerts, D.; Sim, Y.; Lambeir, A.; Hendriks, D.
Inhibition of the procarboxypeptidase U (proCPU, TAFI, proCPB2) system due to hemolysis
J. Thromb. Haemost.
17
878-884
2019
Homo sapiens (Q96IY4)
brenda
Leenaerts, D.; Aernouts, J.; Van Der Veken, P.; Sim, Y.; Lambeir, A.M.; Hendriks, D.
Plasma carboxypeptidase U (CPU, CPB2, TAFIa) generation during in vitro clot lysis and its interplay between coagulation and fibrinolysis
Thromb. Haemost.
117
1498-1508
2017
Homo sapiens (Q96IY4)
brenda