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a [histone H3]-N6,N6-dimethyl-L-lysine4 + O2 + 2 H2O
a [histone H3]-L-lysine4 + 2 formaldehyde + 2 H2O2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6,N6-dimethyl-L-lysine 4 + acceptor + H2O
[histone H3]-N6-methyl-L-lysine 4 + formaldehyde + reduced acceptor
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[histone H3]-N6,N6-dimethyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 9 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 acceptor + 2 H2O
[histone H3]-L-lysine4 + 2 formaldehyde + 2 reduced acceptor
overall reaction
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[histone H3]-N6,N6-methyl-L-lysine 4 + acceptor + H2O
[histone H3]-L-lysine 4 + formaldehyde + reduced acceptor
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
[histone H3]-N6-methyl-L-lysine 9 + 2-oxoglutarate + O2
[histone H3]-L-lysine 9 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
additional information
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6,N6-dimethyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 N6-methyl-L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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histone H3 N6-methyl-L-lysine4 + 2-oxoglutarate + O2
histone H3 L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-N6-methyl-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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dimethyl-H3K4 is an activation markers for gene expression
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
dimethyl-H3K4 is an activation markers for gene expression
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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lack of H3K4diMe is possibly due to complex epigenetic regulation involving Ash2 and LSD1
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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[histone H3]-N6,N6-dimethyl-L-lysine4 + 2 2-oxoglutarate + 2 O2
[histone H3]-L-lysine4 + 2 succinate + 2 formaldehyde + 2 CO2
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demethylation of H3K4 is critical for establishing the DNA methylation imprints during oogenesis
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6,N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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demethylation of H3K4 is critical for establishing the DNA methylation imprints during oogenesis
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine 4 + 2-oxoglutarate + O2
[histone H3]-L-lysine 4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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[histone H3]-N6-methyl-L-lysine4 + 2-oxoglutarate + O2
[histone H3]-L-lysine4 + succinate + formaldehyde + CO2
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additional information
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LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview
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additional information
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functional interplay between histone demethylase and histone deacetylase
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additional information
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LSD1 forms a complex with CoREST and histone deacetylase 1. LSD1 mediates the transrepressive function of TLX, an orphan nuclear receptor, also called NR2E1, that regulates the expression of target genes by functioning as a constitutive transrepressor, through direct interaction via its SWIRM and amine oxidase domains. Physiological significance of TLX in the cytodifferentiation of neural cells in the brain
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additional information
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LSD1 forms a stable complex with Rb, but with E2F1, cell cycle regulatory proteins. LSD1 binds to Epstein-Barr virus C promoter Cp in a cell cycle-dependent manner, as do the the cell cycle regulatory proteins E2F1 and Rb. Rb and LSD1 binding to Cp increase after the S phase, corresponding to a decrease in histone H3 K4 methylation and Cp transcription, overview
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additional information
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LSD1 interacts with CoREST, a co-repressor protein that binds REST and recruits other histone-modifying enzymes such as histone deacetylases 1 ? 2. The function of the LSD1CoRESThistone deacetylase subcomplex in transcriptional repression events is not limited to REST-regulated neuronal genes, but can be extended to other contexts such as hematopoietic differentiation and the telomerase reverse transcriptase genes
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additional information
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LSD1 interacts with several interaction partners and transcription factors for performing its role in gene regulation, overview. LSD1 forms a complex with CoREST, structure with bound histone H3 peptide substrate, overview. LSD1 tightly associates with the CoREST C-terminal SANT domain. This intermolecular association is mediated by the LSD1 tower domain, whose alpha-helices are embraced by a helical segment of CoREST, generating an intermolecular helical coil. The histone H3 N-terminal peptide binds deeply in the LSD1 amine oxidase domain in proximity to the flavin cofactor
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additional information
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LSD1 removes the methyl groups from lysines 4 and 9 of histone 3 with the generation of formaldehyde from the methyl group
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additional information
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LSD1 directly binds to the promoter of P21 where it catalyzes H3K4me2 demethylation. FEZF1-AS1, a 2564 bp RNA overexpressed in gastric cancer, epigenetically represses the expression of P21 via binding with LSD1
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additional information
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lysine-specific demethylase 1(LSD1) demethylates mono- and dimethylated residues of lysine-4 on histone H3 (H3K4me1 and H3K4me2) and lysine-9 on histone H3 (H3K9me1 and H3K9me2)
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additional information
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amine oxidase flavin-containing domain 1, AOF1, also called lysine demethylase 1B , KDM1B, is a protein related to the lysine demethylase KDM1or LSD1, it functions as a H3K4 demethylase and is required for de novo DNA methylation of some imprinted genes in oocytes
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additional information
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p53 directly interacts with LSD1 to alter chromatin structure and confer developmental repression of the tumor marker alpha-fetoprotein, AFP, p53 and LSD1 cooccupy a p53 response element, concomitant with dimethylated histone H3 lysine 4 demethylation and postnatal repression of AFP transcription, overview
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additional information
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the enzyme is organized in histone demethylase complexes containing LSD1, RE1 silencing transcription factor corepressor, CoREST, histone deacetylase 1, HDAC1, and histone deacetylase 2 in erythroleukemia and T cell leukemia cells. the Complex interacts with TAL, a critical transcription factor required for hematopoiesis, overview. The enzymatic domain of LSD1 plays an important role in repressing the TAL1-directed transcription, overview. TAL1-associated LSD1 and HDM activity are dynamically regulated during hematopoiesis
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additional information
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LSD1 demethylates mono- and dimethylated H3K4 and H3K9, but does not alter trimethylated H3K4 and H3K9
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additional information
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LSD1 demethylates mono- and dimethylated H3K4 and H3K9, but does not alter trimethylated H3K4 and H3K9
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