Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure. - Wikidata - awgldk - TriplyDB

Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.

Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.

http://www.wikidata.org/entity/Q37734360

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An Overview of Chromatin-Regulating Proteins in Cells Post-translational modifications of histones that influence nucleosome dynamics Chemical and biological tools for the preparation of modified histone proteins Histones: at the crossroads of peptide and protein chemistry.Histone core phosphorylation regulates DNA accessibility.Hybrid phase ligation for efficient synthesis of histone proteins.Aurora-A mediated histone H3 phosphorylation of threonine 118 controls condensin I and cohesin occupancy in mitosis.Studying protein-DNA interactions using atomic force microscopy.Quantitative analysis of single-molecule force spectroscopy on folded chromatin fibers.Excess free histone H3 localizes to centrosomes for proteasome-mediated degradation during mitosis in metazoans Modulation of nucleosomal DNA accessibility via charge-altering post-translational modifications in histone core.

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Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.

http://www.wikidata.org/entity/Q37734360

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 21 February 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.

@en

Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.

@nl

type

label

Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.

@en

Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.

@nl

prefLabel

Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.

@en

Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure.

@nl

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P1433

Nucleic Acids Research

P1476

Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure

@en

P2093

Alex M Mooney

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

John van Noort

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

Jonathan W Picking

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

Justin A North

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

Marek Šimon

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

Matthew A Shoffner

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Michael G Poirier

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Michelle B Ferdinand

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

P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Regulation of transcription through acetylation of H3K122 on the lateral surface of the histone octamer

JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin

Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions

The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure

Comprehensive structural analysis of mutant nucleosomes containing lysine to glutamine (KQ) substitutions in the H3 and H4 histone-fold domains

Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

Chromatin modifications and their function

Chromatin remodeling by nucleosome disassembly in vitro.

Identification of combinatorial patterns of post-translational modifications on individual histones in the mouse brain

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4922-4933

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scholarly article

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10.1093/NAR/GKU150

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8

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42

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Jennifer J Ottesen

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2014-02-21T00:00:00Z

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260374825

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24561803

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phosphorylation

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4005658

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