Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
about
Horizontal gene transfer of epigenetic machinery and evolution of parasitism in the malaria parasite Plasmodium falciparum and other apicomplexansStructural basis for the methylation site specificity of SET7/9PR-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 p53Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanismStructural 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 methylationThe Identification and Structure of an N-Terminal PR Domain Show that FOG1 Is a Member of the PRDM Family of ProteinsStructural origins for the product specificity of SET domain protein methyltransferasesStructural Biology of Human H3K9 MethyltransferasesSET7/9 Catalytic Mutants Reveal the Role of Active Site Water Molecules in Lysine Multiple MethylationCrystal 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 bindingCrystal Structures of Histone and p53 Methyltransferase SmyD2 Reveal a Conformational Flexibility of the Autoinhibitory C-Terminal DomainStructural and Functional Profiling of the Human Histone Methyltransferase SMYD3Crystal Structure and Functional Analysis of JMJD5 Indicate an Alternate Specificity and FunctionSolution 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 MutationsCrystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2Multivalent Interactions by the Set8 Histone Methyltransferase With Its Nucleosome SubstrateThe emerging role of lysine methyltransferase SETD8 in human diseasesDiscovery of a selective, substrate-competitive inhibitor of the lysine methyltransferase SETD8Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectivesThe UBC9 E2 SUMO conjugating enzyme binds the PR-Set7 histone methyltransferase to facilitate target gene repression.Fluorescence-based methods for screening writers and readers of histone methyl marks.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.Catalytic roles for carbon-oxygen hydrogen bonding in SET domain lysine methyltransferases.Histone H4 Lys 20 monomethylation by histone methylase SET8 mediates Wnt target gene activation.Dynamics of histone lysine methylation: structures of methyl writers and erasersPolypeptide substrate specificity of PsLSMT. A set domain protein methyltransferase.The 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.
P2860
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P2860
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
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
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@ast
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@en
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@en-gb
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@nl
type
label
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@ast
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@en
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@en-gb
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@nl
prefLabel
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@ast
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@en
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@en-gb
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@nl
P2093
P2860
P3181
P356
P1433
P1476
Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase
@en
P2093
Evys Collazo
Jean-François Couture
Joseph S Brunzelle
Raymond C Trievel
P2860
P304
P3181
P356
10.1101/GAD.1318405
P407
P577
2005-06-15T00:00:00Z