Specificity and mechanism of the histone methyltransferase Pr-Set7.
about
PR-Set7 establishes a repressive trans-tail histone code that regulates differentiationThe structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylationBBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage responseModulation of p53 function by SET8-mediated methylation at lysine 382On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complexPHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53Dimerization of a viral SET protein endows its functionStructural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repairPR-Set7 and H4K20me1: at the crossroads of genome integrity, cell cycle, chromosome condensation, and transcriptionStructural and functional coordination of DNA and histone methylationStructural origins for the product specificity of SET domain protein methyltransferasesStructural Biology of Human H3K9 MethyltransferasesCrystal Structure of Cardiac-specific Histone Methyltransferase SmyD1 Reveals Unusual Active Site ArchitectureStructural 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 bindingSolution structure of the Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNAA novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferasesStructure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic MutationsMultivalent Interactions by the Set8 Histone Methyltransferase With Its Nucleosome SubstratePlasmodium falciparum PfSET7: enzymatic characterization and cellular localization of a novel protein methyltransferase in sporozoite, liver and erythrocytic stage parasitesThe epigenome: the next substrate for engineeringThe emerging role of lysine methyltransferase SETD8 in human diseasesUbiquitination of Lysine 867 of the Human SETDB1 Protein Upregulates Its Histone H3 Lysine 9 (H3K9) Methyltransferase ActivityThe diverse functions of histone lysine methylationCRL4(Cdt2) regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradationModulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectivesEpidermal stem cells are defined by global histone modifications that are altered by Myc-induced differentiation.Evolution of SET-domain protein families in the unicellular and multicellular Ascomycota fungi.Comparative analyses of SUV420H1 isoforms and SUV420H2 reveal differences in their cellular localization and effects on myogenic differentiation.Mixed lineage leukemia: a structure-function perspective of the MLL1 protein.The UBC9 E2 SUMO conjugating enzyme binds the PR-Set7 histone methyltransferase to facilitate target gene repression.Arabidopsis Histone Lysine Methyltransferases.QM/MM MD and free energy simulations of G9a-like protein (GLP) and its mutants: understanding the factors that determine the product specificityThe histone H4 lysine 20 monomethyl mark, set by PR-Set7 and stabilized by L(3)mbt, is necessary for proper interphase chromatin organization.SET8 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.Dynamics of histone lysine methylation: structures of methyl writers and erasersThe histone modifications governing TFF1 transcription mediated by estrogen receptor.Partitioning of the maize epigenome by the number of methyl groups on histone H3 lysines 9 and 27.Direct evidence for methyl group coordination by carbon-oxygen hydrogen bonds in the lysine methyltransferase SET7/9Biochemical reconstitution and phylogenetic comparison of human SET1 family core complexes involved in histone methylation
P2860
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P2860
Specificity and mechanism of the histone methyltransferase Pr-Set7.
description
2005 nî lūn-bûn
@nan
2005 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Specificity and mechanism of the histone methyltransferase Pr-Set7
@nl
Specificity and mechanism of the histone methyltransferase Pr-Set7.
@ast
Specificity and mechanism of the histone methyltransferase Pr-Set7.
@en
type
label
Specificity and mechanism of the histone methyltransferase Pr-Set7
@nl
Specificity and mechanism of the histone methyltransferase Pr-Set7.
@ast
Specificity and mechanism of the histone methyltransferase Pr-Set7.
@en
prefLabel
Specificity and mechanism of the histone methyltransferase Pr-Set7
@nl
Specificity and mechanism of the histone methyltransferase Pr-Set7.
@ast
Specificity and mechanism of the histone methyltransferase Pr-Set7.
@en
P2093
P2860
P3181
P356
P1433
P1476
Specificity and mechanism of the histone methyltransferase Pr-Set7.
@en
P2093
Frederick W Muskett
Jonathan R Wilson
Kavitha Sarma
Philip A Walker
Stephen R Martin
Steven J Gamblin
Thomas A Frenkiel
P2860
P304
P3181
P356
10.1101/GAD.1315905
P407
P577
2005-06-02T00:00:00Z