Structural basis for the histone chaperone activity of Asf1 - Test2 - elhamkhani - TriplyDB

Structural basis for the histone chaperone activity of Asf1

Structural basis for the histone chaperone activity of Asf1

http://www.wikidata.org/entity/Q34312157

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Dimerization of the CENP-A assembly factor HJURP is required for centromeric nucleosome deposition Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP Structures of human nucleosomes containing major histone H3 variants The death-associated protein DAXX is a novel histone chaperone involved in the replication-independent deposition of H3.3 Centromere-specific assembly of CENP-a nucleosomes is mediated by HJURP.Structure-function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2 Histone H2A/H2B dimer exchange by ATP-dependent chromatin remodeling activities.Remodeling of chromatin structure in senescent cells and its potential impact on tumor suppression and aging Epigenetic Control of Cell Division and Cell Differentiation in the Root Apex Histone-modifying enzymes, histone modifications and histone chaperones in nucleosome assembly: Lessons learned from Rtt109 histone acetyltransferases Epigenetic inheritance: histone bookmarks across generations Histone transfer among chaperones Crystal structures of fission yeast histone chaperone Asf1 complexed with the Hip1 B-domain or the Cac2 C terminus Structural Basis for the Recognition of Histone H4 by the Histone-Chaperone RbAp46 The FACT Spt16 “peptidase” domain is a histone H3–H4 binding module NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75 Asf1-like structure of the conserved Yaf9 YEATS domain and role in H2A.Z deposition and acetylation Structural Analysis of Rtt106p Reveals a DNA Binding Role Required for Heterochromatin Silencing Structure, localization and histone binding properties of nuclear-associated nucleosome assembly protein from Plasmodium falciparum Structure of the histone chaperone CIA/ASF1-double bromodomain complex linking histone modifications and site-specific histone eviction Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face Structure and Biological Importance of the Spn1-Spt6 Interaction, and Its Regulatory Role in Nucleosome Binding Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3 Structure and Histone Binding Properties of the Vps75-Rtt109 Chaperone-Lysine Acetyltransferase Complex Structure and function of WD40 domain proteins Chromatin-modifying Complex Component Nurf55/p55 Associates with Histones H3 and H4 and Polycomb Repressive Complex 2 Subunit Su(z)12 through Partially Overlapping Binding Sites Novel Histone H3 Binding Protein ORF158L from the Singapore Grouper Iridovirus Structure of the variant histone H3.3–H4 heterodimer in complex with its chaperone DAXX Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing Surprising complexity of the Asf1 histone chaperone-Rad53 kinase interaction The conformational flexibility of the C-terminus of histone H4 promotes histone octamer and nucleosome stability and yeast viability Binding of the histone chaperone ASF1 to the CBP bromodomain promotes histone acetylation The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly Cooperation between the INO80 complex and histone chaperones determines adaptation of stress gene transcription in the yeast Saccharomyces cerevisiae.Asf1 facilitates dephosphorylation of Rad53 after DNA double-strand break repair.Histone levels are regulated by phosphorylation and ubiquitylation-dependent proteolysis A Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome assembly.

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P2860

Structural basis for the histone chaperone activity of Asf1

http://www.wikidata.org/entity/Q34312157

description

2006 nî lūn-bûn

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2006 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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Structural basis for the histone chaperone activity of Asf1

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Structural basis for the histone chaperone activity of Asf1

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Structural basis for the histone chaperone activity of Asf1

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Structural basis for the histone chaperone activity of Asf1

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Structural basis for the histone chaperone activity of Asf1

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Structural basis for the histone chaperone activity of Asf1

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Structural basis for the histone chaperone activity of Asf1

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Structural basis for the histone chaperone activity of Asf1

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Structural basis for the histone chaperone activity of Asf1

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Structural basis for the histone chaperone activity of Asf1

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Christine M English

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Joshua J Carson

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Melissa W Adkins

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P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

A human homologue of yeast anti-silencing factor has histone chaperone activity

Human Asf1 and CAF-1 interact and synergize in a repair-coupled nucleosome assembly pathway

Histone chaperones and nucleosome assembly

Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways dependent or independent of DNA synthesis

Nucleosome assembly by a complex of CAF-1 and acetylated histones H3/H4

The p150 and p60 subunits of chromatin assembly factor I: a molecular link between newly synthesized histones and DNA replication

Structural basis for the interaction of Asf1 with histone H3 and its functional implications

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

SuperPose: a simple server for sophisticated structural superposition

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