Differential contributions of histone H3 and H4 residues to heterochromatin structure. - Wikidata - awgldk - TriplyDB

Differential contributions of histone H3 and H4 residues to heterochromatin structure.

Differential contributions of histone H3 and H4 residues to heterochromatin structure.

http://www.wikidata.org/entity/Q35065523

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The molecular topography of silenced chromatin in Saccharomyces cerevisiae Structural Basis of Silencing: Sir3 BAH Domain in Complex with a Nucleosome at 3.0 A Resolution Chemical and biological tools for the preparation of modified histone proteins Epigenetics in Saccharomyces cerevisiae.Contributions of histone H3 nucleosome core surface mutations to chromatin structures, silencing and DNA repair.Heritable capture of heterochromatin dynamics in Saccharomyces cerevisiae.Proliferating cell nuclear antigen (PCNA) contributes to the high-order structure and stability of heterochromatin in Saccharomyces cerevisiae.

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Differential contributions of histone H3 and H4 residues to heterochromatin structure.

http://www.wikidata.org/entity/Q35065523

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Differential contributions of histone H3 and H4 residues to heterochromatin structure.

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Differential contributions of histone H3 and H4 residues to heterochromatin structure.

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type

label

Differential contributions of histone H3 and H4 residues to heterochromatin structure.

@ast

Differential contributions of histone H3 and H4 residues to heterochromatin structure.

@en

prefLabel

Differential contributions of histone H3 and H4 residues to heterochromatin structure.

@ast

Differential contributions of histone H3 and H4 residues to heterochromatin structure.

@en

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GENETICS.111.127886

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Differential contributions of histone H3 and H4 residues to heterochromatin structure.

@en

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Jef D Boeke

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

Lars Olsen

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

Qun Yu

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

Xin Bi

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

Xinmin Zhang

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

P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Human histone gene organization: nonregular arrangement within a large cluster

Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions

Long-range nucleosome ordering is associated with gene silencing in Drosophila melanogaster pericentric heterochromatin

Histone H4 lysine 91 acetylation a core domain modification associated with chromatin assembly

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

Saccharomyces cerevisiae linker histone Hho1p functionally interacts with core histone H4 and negatively regulates the establishment of transcriptionally silent chromatin

Acetylation in histone H3 globular domain regulates gene expression in yeast.

Type B histone acetyltransferase Hat1p participates in telomeric silencing

The human and mouse replication-dependent histone genes

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291-308

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scholarly article

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10.1534/GENETICS.111.127886

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2

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