Structural Chemistry of Human SET Domain Protein Methyltransferases.
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Sinefungin derivatives as inhibitors and structure probes of protein lysine methyltransferase SETD2Histone lysine-specific methyltransferases and demethylases in carcinogenesis: new targets for cancer therapy and preventionCurrent chemical biology approaches to interrogate protein methyltransferasesStructure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic MutationsCatalytic and functional roles of conserved amino acids in the SET domain of the S. cerevisiae lysine methyltransferase Set1Methanol may function as a cross-kingdom signalEndogenous methanol regulates mammalian gene activityAn alternative mechanism for the methylation of phosphoethanolamine catalyzed by Plasmodium falciparum phosphoethanolamine methyltransferase.Structural diversity of the epigenetics pocketome.Dietary methanol regulates human gene activity(R)-PFI-2 is a potent and selective inhibitor of SETD7 methyltransferase activity in cells.Selective inhibition of Ezh2 by a small molecule inhibitor blocks tumor cells proliferationGlobal chromatin profiling reveals NSD2 mutations in pediatric acute lymphoblastic leukemia.Structural and functional studies of S-adenosyl-L-methionine binding proteins: a ligand-centric approachA chemical proteomics approach for global analysis of lysine monomethylome profiling.Structural insights into binding of small molecule inhibitors to Enhancer of Zeste Homolog 2.A continuous kinetic assay for protein and DNA methyltransferase enzymatic activities.Bromo-deaza-SAH: a potent and selective DOT1L inhibitor.S-adenosyl-methionine-dependent methyltransferases: highly versatile enzymes in biocatalysis, biosynthesis and other biotechnological applications.A journey toward Bioorthogonal Profiling of Protein Methylation inside living cells.Lysine-specific modifications of p53: a matter of life and death?The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic integrity.Inhibitors of Protein Methyltransferases and Demethylases.Orchestration of H3K27 methylation: mechanisms and therapeutic implication.The promise of epigenomic therapeutics in pancreatic cancerpUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine Methyltransferase 6 via a Domain That Is Crucial for mRNA Export and Efficient Viral ReplicationPR Domain-containing Protein 7 (PRDM7) Is a Histone 3 Lysine 4 Trimethyltransferase.A high throughput scintillation proximity imaging assay for protein methyltransferases.Structure-Based Design of a Covalent Inhibitor of the SET Domain-Containing Protein 8 (SETD8) Lysine Methyltransferase.Lysine Possesses the Optimal Chain Length for Histone Lysine Methyltransferase Catalysis.Investigating d-lysine stereochemistry for epigenetic methylation, demethylation and recognition.In silico probing and biological evaluation of SETDB1/ESET-targeted novel compounds that reduce tri-methylated histone H3K9 (H3K9me3) level.Targeting of epigenetic regulators in neuroblastoma.
P2860
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P2860
Structural Chemistry of Human SET Domain Protein Methyltransferases.
description
article científic
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article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
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artikull shkencor
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artículo científico
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name
Structural Chemistry of Human SET Domain Protein Methyltransferases.
@en
Structural Chemistry of Human SET Domain Protein Methyltransferases.
@nl
type
label
Structural Chemistry of Human SET Domain Protein Methyltransferases.
@en
Structural Chemistry of Human SET Domain Protein Methyltransferases.
@nl
prefLabel
Structural Chemistry of Human SET Domain Protein Methyltransferases.
@en
Structural Chemistry of Human SET Domain Protein Methyltransferases.
@nl
P2860
P1476
Structural Chemistry of Human SET Domain Protein Methyltransferases.
@en
P2093
Matthieu Schapira
P2860
P356
10.2174/1875397301005010085
P433
P577
2011-08-22T00:00:00Z