Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face - Wikidata - awgldk - TriplyDB

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

http://www.wikidata.org/entity/Q27664007

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A novel Toxoplasma gondii nuclear factor TgNF3 is a dynamic chromatin-associated component, modulator of nucleolar architecture and parasite virulence Crystal Structure and Function of Human Nucleoplasmin (Npm2): A Histone Chaperone in Oocytes and Embryos Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity Developmentally Regulated Post-translational Modification of Nucleoplasmin Controls Histone Sequestration and Deposition Protein arginine methyltransferase Prmt5-Mep50 methylates histones H2A and H4 and the histone chaperone nucleoplasmin in Xenopus laevis eggs The pentameric nucleoplasmin fold is present in Drosophila FKBP39 and a large number of chromatin-related proteins.A Quantitative Characterization of Nucleoplasmin/Histone Complexes Reveals Chaperone Versatility Histone chaperone networks shaping chromatin function.Organizing the genome with H2A histone variants.Nuclear reprogramming of sperm and somatic nuclei in eggs and oocytes Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Expression and purification of the full murine NPM2 and study of its interaction with protamines and histones.The intrinsically disordered distal face of nucleoplasmin recognizes distinct oligomerization states of histones.Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.Substrate specificity in the context of molecular chaperones.

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Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

http://www.wikidata.org/entity/Q27664007

description

2010 nî lūn-bûn

@nan

2010 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հոտեմբերին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

@ast

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

@en

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

@nl

type

label

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

@ast

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

@en

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

@nl

prefLabel

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

@ast

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

@en

Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face

@nl

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JBC.M110.150664

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Journal of Biological Chemistry

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Nucleoplasmin binds histone H2A-H2B dimers through its distal face

@en

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Adelina Prado

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

Isbaal Ramos

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

Juan Ausió

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

Laura Bretaña

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

Ron Finn

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

P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Histone chaperones and nucleosome assembly

The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly

The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding

Relationship between the structure of SET/TAF-I /INHAT and its histone chaperone activity

Crystal structure of human nucleophosmin-core reveals plasticity of the pentamer-pentamer interface

NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B

Activation of nucleoplasmin, an oligomeric histone chaperone, challenges its stability

Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

EMAN: semiautomated software for high-resolution single-particle reconstructions

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33771-33778

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scholarly article

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3896334

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10.1074/JBC.M110.150664

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44

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285

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José María Valpuesta

Jesus M Arizmendi

J Martín-Benito

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2010-08-09T00:00:00Z

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20696766

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2962476

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