Structure and catalytic mechanism of a SET domain protein methyltransferase
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Structural basis for the methylation site specificity of SET7/9Specificity and mechanism of the histone methyltransferase Pr-Set7.Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet.On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complexStructural and functional analysis of SET8, a histone H4 Lys-20 methyltransferaseDimerization of a viral SET protein endows its functionIdentification of a novel gene, CIA6, required for normal pyrenoid formation in Chlamydomonas reinhardtiiStructural basis for the product specificity of histone lysine methyltransferasesCharacterization of the cofactor-binding site in the SPOUT-fold methyltransferases by computational docking of S-adenosylmethionine to three crystal structuresThe SET-domain protein superfamily: protein lysine methyltransferasesNatural history of S-adenosylmethionine-binding proteinsProtein and DNA modifications: evolutionary imprints of bacterial biochemical diversification and geochemistry on the provenance of eukaryotic epigeneticsThe functional diversity of protein lysine methylationCrystal Structure of a Putative Methyltransferase from Mycobacterium tuberculosis: Misannotation of a Genome Clarified by Protein Structural AnalysisStructural origins for the product specificity of SET domain protein methyltransferasesSET7/9 Catalytic Mutants Reveal the Role of Active Site Water Molecules in Lysine Multiple MethylationStructural and biochemical studies of human lysine methyltransferase Smyd3 reveal the important functional roles of its post-SET and TPR domains and the regulation of its activity by DNA bindingStructural basis of SETD6-mediated regulation of the NF-kB network via methyl-lysine signalingStructural and Functional Profiling of the Human Histone Methyltransferase SMYD3Catalytic and functional roles of conserved amino acids in the SET domain of the S. cerevisiae lysine methyltransferase Set1Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae.Identification of methylated proteins in the yeast small ribosomal subunit: a role for SPOUT methyltransferases in protein arginine methylation.Plasmodium falciparum PfSET7: enzymatic characterization and cellular localization of a novel protein methyltransferase in sporozoite, liver and erythrocytic stage parasitesRegulation of the brown and white fat gene programs through a PRDM16/CtBP transcriptional complexMany paths to methyltransfer: a chronicle of convergenceAssay development for histone methyltransferases.PR-domain-containing Mds1-Evi1 is critical for long-term hematopoietic stem cell function.In vivo residue-specific histone methylation dynamics.A chemiluminescence-based method for identification of histone lysine methyltransferase inhibitors.Development of homogeneous nonradioactive methyltransferase and demethylase assays targeting histone H3 lysine 4.Fluorescence-based methods for screening writers and readers of histone methyl marks.Arabidopsis Histone Lysine Methyltransferases.A full suite of histone and histone modifying genes are transcribed in the dinoflagellate LingulodiniumCharacterization of chloroplastic fructose 1,6-bisphosphate aldolases as lysine-methylated proteins in plantsORTH/VIM proteins that regulate DNA methylation are functional ubiquitin E3 ligases.Strategy for "detoxification" of a cancer-derived histone mutant based on mapping its interaction with the methyltransferase PRC2SET8 recognizes the sequence RHRK20VLRDN within the N terminus of histone H4 and mono-methylates lysine 20.Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases.Polypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase.SUVR2 is involved in transcriptional gene silencing by associating with SNF2-related chromatin-remodeling proteins in Arabidopsis.
P2860
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P2860
Structure and catalytic mechanism of a SET domain protein methyltransferase
description
2002 nî lūn-bûn
@nan
2002 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Structure and catalytic mechanism of a SET domain protein methyltransferase
@ast
Structure and catalytic mechanism of a SET domain protein methyltransferase
@en
Structure and catalytic mechanism of a SET domain protein methyltransferase
@nl
type
label
Structure and catalytic mechanism of a SET domain protein methyltransferase
@ast
Structure and catalytic mechanism of a SET domain protein methyltransferase
@en
Structure and catalytic mechanism of a SET domain protein methyltransferase
@nl
prefLabel
Structure and catalytic mechanism of a SET domain protein methyltransferase
@ast
Structure and catalytic mechanism of a SET domain protein methyltransferase
@en
Structure and catalytic mechanism of a SET domain protein methyltransferase
@nl
P2093
P1433
P1476
Structure and catalytic mechanism of a SET domain protein methyltransferase
@en
P2093
Bridgette M Beach
James H Hurley
Lynnette M A Dirk
Raymond C Trievel
Robert L Houtz
P304
P356
10.1016/S0092-8674(02)01000-0
P407
P577
2002-10-04T00:00:00Z