Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase - Wikidata - awgldk - TriplyDB

Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

http://www.wikidata.org/entity/Q24529594

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Horizontal gene transfer of epigenetic machinery and evolution of parasitism in the malaria parasite Plasmodium falciparum and other apicomplexans Structural basis for the methylation site specificity of SET7/9 PR-Set7 establishes a repressive trans-tail histone code that regulates differentiation The structure of NSD1 reveals an autoregulatory mechanism underlying histone H3K36 methylation BBAP monoubiquitylates histone H4 at lysine 91 and selectively modulates the DNA damage response Modulation of p53 function by SET8-mediated methylation at lysine 382 On the mechanism of multiple lysine methylation by the human mixed lineage leukemia protein-1 (MLL1) core complex PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53 Crystal structure of the human histone methyltransferase ASH1L catalytic domain and its implications for the regulatory mechanism Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair PR-Set7 and H4K20me1: at the crossroads of genome integrity, cell cycle, chromosome condensation, and transcription Structural and functional coordination of DNA and histone methylation The Identification and Structure of an N-Terminal PR Domain Show that FOG1 Is a Member of the PRDM Family of Proteins Structural origins for the product specificity of SET domain protein methyltransferases Structural Biology of Human H3K9 Methyltransferases SET7/9 Catalytic Mutants Reveal the Role of Active Site Water Molecules in Lysine Multiple Methylation Crystal Structure of Cardiac-specific Histone Methyltransferase SmyD1 Reveals Unusual Active Site Architecture Structural 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 binding Crystal Structures of Histone and p53 Methyltransferase SmyD2 Reveal a Conformational Flexibility of the Autoinhibitory C-Terminal Domain Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3 Crystal Structure and Functional Analysis of JMJD5 Indicate an Alternate Specificity and Function Solution structure of the Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNA A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases Structure of the Catalytic Domain of EZH2 Reveals Conformational Plasticity in Cofactor and Substrate Binding Sites and Explains Oncogenic Mutations Crystal structures of the human histone H4K20 methyltransferases SUV420H1 and SUV420H2 Multivalent Interactions by the Set8 Histone Methyltransferase With Its Nucleosome Substrate The emerging role of lysine methyltransferase SETD8 in human diseases Discovery of a selective, substrate-competitive inhibitor of the lysine methyltransferase SETD8 Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives The 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 specificity The 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 erasers Polypeptide 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.

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

http://www.wikidata.org/entity/Q24529594

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2005 nî lūn-bûn

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2005 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2005年の論文

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Genes & Development

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Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferase

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Evys Collazo

http://www.w3.org/2001/XMLSchema#string

Jean-François Couture

http://www.w3.org/2001/XMLSchema#string

Joseph S Brunzelle

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Raymond C Trievel

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P2860

Structure and catalytic mechanism of the human histone methyltransferase SET7/9

Regulation of p53 activity through lysine methylation

A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin

In vitro and in vivo analyses of a Phe/Tyr switch controlling product specificity of histone lysine methyltransferases

Structure of the Neurospora SET domain protein DIM-5, a histone H3 lysine methyltransferase

Structural basis for the product specificity of histone lysine methyltransferases

Mitotic-specific methylation of histone H4 Lys 20 follows increased PR-Set7 expression and its localization to mitotic chromosomes.

Improved methods for building protein models in electron density maps and the location of errors in these models

Structure and catalytic mechanism of a SET domain protein methyltransferase

Crystal structure and functional analysis of the histone methyltransferase SET7/9

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1455-65

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scholarly article

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3094262

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10.1101/GAD.1318405

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12

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19

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15933070

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1151662

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