Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex. - Test2 - elhamkhani - TriplyDB

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

http://www.wikidata.org/entity/Q27939462

about

Subunit composition and substrate specificity of a MOF-containing histone acetyltransferase distinct from the male-specific lethal (MSL) complex The human monocytic leukemia zinc finger histone acetyltransferase domain contains DNA-binding activity implicated in chromatin targeting Catalysis and substrate selection by histone/protein lysine acetyltransferases Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75 Effects of histone acetylation and CpG methylation on the structure of nucleosomes.Combinatorial depletion analysis to assemble the network architecture of the SAGA and ADA chromatin remodeling complexes.Multivalent engagement of chromatin modifications by linked binding modules Catalytic-site mutations in the MYST family histone Acetyltransferase Esa1 Effects of histone acetylation by Piccolo NuA4 on the structure of a nucleosome and the interactions between two nucleosomes.Structural and mechanistic insights into regulation of HBO1 histone acetyltransferase activity by BRPF2 Acetylation of core histones in response to HDAC inhibitors is diminished in mitotic HeLa cells.Catalytic activation of histone acetyltransferase Rtt109 by a histone chaperone.Processing mechanism and substrate selectivity of the core NuA4 histone acetyltransferase complex.Structure and nucleosome interaction of the yeast NuA4 and Piccolo-NuA4 histone acetyltransferase complexes.Eaf1p Is Required for Recruitment of NuA4 in Targeting TFIID to the Promoters of the Ribosomal Protein Genes for Transcriptional Initiation In Vivo.Piccolo NuA4-catalyzed acetylation of nucleosomal histones: critical roles of an Esa1 Tudor/chromo barrel loop and an Epl1 enhancer of polycomb A (EPcA) basic region Site specificity analysis of Piccolo NuA4-mediated acetylation for different histone complexes.Measuring specificity in multi-substrate/product systems as a tool to investigate selectivity in vivo.MYSTs mark chromatin for chromosomal functions.Properties of Nat4, an N(alpha)-acetyltransferase of Saccharomyces cerevisiae that modifies N termini of histones H2A and H4 Histone acetylation: truth of consequences?Synthetic chromatin approaches to probe the writing and erasing of histone modifications.Histone target selection within chromatin: an exemplary case of teamwork.Site-specific binding affinities within the H2B tail domain indicate specific effects of lysine acetylation.Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure.Probing the reaction coordinate of the p300/CBP histone acetyltransferase with bisubstrate analogs.Critical genomic regulation mediated by Enhancer of Polycomb.

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P2860

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

http://www.wikidata.org/entity/Q27939462

description

2007 nî lūn-bûn

@nan

2007 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2007年の論文

@ja

2007年論文

@yue

2007年論文

@zh-hant

2007年論文

@zh-hk

2007年論文

@zh-mo

2007年論文

@zh-tw

2007年论文

@wuu

name

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

@ast

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

@en

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

@nl

type

label

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

@ast

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

@en

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

@nl

prefLabel

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

@ast

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

@en

Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex.

@nl

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Nucleosome recognition by the Piccolo NuA4 histone acetyltransferase complex

@en

P2093

Jeffrey C Hansen

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

John M Denu

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

Song Tan

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

Steven J McBryant

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

William Selleck

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

P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans

The histone H4 acetyltransferase MOF uses a C2HC zinc finger for substrate recognition.

NuA4, an essential transcription adaptor/histone H4 acetyltransferase complex containing Esa1p and the ATM-related cofactor Tra1p

ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide

Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain

Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases

The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate

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2091-2099

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scholarly article

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10.1021/BI602366N

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8

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46

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Christopher E. Berndsen

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2007-02-03T00:00:00Z

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6529348

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1994252

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