Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase - Wikidata - wikimedia - TriplyDB

Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase

Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase

http://www.wikidata.org/entity/Q37208358

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A novel disrupter of telomere silencing 1-like (DOT1L) interaction is required for signal transducer and activator of transcription 1 (STAT1)-activated gene expression Specificity and mechanism of the histone methyltransferase Pr-Set7.Implication of posttranslational histone modifications in nucleotide excision repair Structural and functional coordination of DNA and histone methylation Protein and DNA modifications: evolutionary imprints of bacterial biochemical diversification and geochemistry on the provenance of eukaryotic epigenetics 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 Interplay of chromatin modifiers on a short basic patch of histone H4 tail defines the boundary of telomeric heterochromatin Multiple Motif Scanning to identify methyltransferases from the yeast proteome.A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathway Identification of lysine 37 of histone H2B as a novel site of methylation The role of multiple marks in epigenetic silencing and the emergence of a stable bivalent chromatin state A barcode screen for epigenetic regulators reveals a role for the NuB4/HAT-B histone acetyltransferase complex in histone turnover Bioinformatic Identification of Novel Methyltransferases The tale beyond the tail: histone core domain modifications and the regulation of chromatin structure Histone H3 lysine 79 methyltransferase Dot1 is required for immortalization by MLL oncogenes.Dynamics of histone lysine methylation: structures of methyl writers and erasers Histone methyltransferase DOT1L drives recovery of gene expression after a genotoxic attack.Deficiency of H3K79 histone methyltransferase Dot1-like protein (DOT1L) inhibits cell proliferation Structural and sequence motifs of protein (histone) methylation enzymes.Cross-talking histones: implications for the regulation of gene expression and DNA repair.The histone methyltransferase DOT1L: regulatory functions and a cancer therapy target.Structural basis for substrate recognition by the human N-terminal methyltransferase 1 Functional analyses of Trichoderma reesei LAE1 reveal conserved and contrasting roles of this regulator.Structural dynamics of protein lysine methylation and demethylation.A prototypic lysine methyltransferase 4 from archaea with degenerate sequence specificity methylates chromatin proteins Sul7d and Cren7 in different patterns.Chemical mechanisms of histone lysine and arginine modifications Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation Nutritional control of epigenetic processes in yeast and human cells Controlling histone methylation via trans-histone pathways.Epigenome manipulation as a pathway to new natural product scaffolds and their congeners.The histone methyltransferase Dot1/DOT1L as a critical regulator of the cell cycle.A modified epigenetics toolbox to study histone modifications on the nucleosome core.The diverse functions of Dot1 and H3K79 methylation.On your histone mark, SET, methylate!Small molecule epigenetic inhibitors targeted to histone lysine methyltransferases and demethylases.The upstreams and downstreams of H3K79 methylation by DOT1L.Writing, erasing and reading histone lysine methylations.Proteasome inhibition protects HT22 neuronal cells from oxidative glutamate toxicity.Dot1 binding induces chromatin rearrangements by histone methylation-dependent and -independent mechanisms.

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Structure of the conserved core of the yeast Dot1p, a nucleosomal histone H3 lysine 79 methyltransferase

http://www.wikidata.org/entity/Q37208358

description

article científic

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article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 29 July 2004

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Structure of the conserved cor ...... H3 lysine 79 methyltransferase

@en

Structure of the conserved cor ...... 3 lysine 79 methyltransferase.

@nl

type

label

Structure of the conserved cor ...... H3 lysine 79 methyltransferase

@en

Structure of the conserved cor ...... 3 lysine 79 methyltransferase.

@nl

prefLabel

Structure of the conserved cor ...... H3 lysine 79 methyltransferase

@en

Structure of the conserved cor ...... 3 lysine 79 methyltransferase.

@nl

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Journal of Biological Chemistry

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Structure of the conserved cor ...... H3 lysine 79 methyltransferase

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Ken Sawada

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

Robert E Collins

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

Xiaodong Cheng

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

Xing Zhang

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

Zhe Yang

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

P2860

Translating the Histone Code

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

Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9-AdoMet.

Set2 is a nucleosomal histone H3-selective methyltransferase that mediates transcriptional repression.

Structure of human DNMT2, an enigmatic DNA methyltransferase homolog that displays denaturant-resistant binding to DNA

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

Structural basis for the product specificity of histone lysine methyltransferases

Histone sumoylation is associated with transcriptional repression

Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein association

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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43296-43306

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scholarly article

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10.1074/JBC.M405902200

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41

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279

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