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

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

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

http://www.wikidata.org/entity/Q27651273

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ANP32E is a histone chaperone that removes H2A.Z from chromatin Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP Nucleoplasmin Binds Histone H2A-H2B Dimers through Its Distal Face Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3 Neisseria conserved hypothetical protein DMP12 is a DNA mimic that binds to histone-like HU protein The Catalytic Subunit of the SWR1 Remodeler Is a Histone Chaperone for the H2A.Z-H2B Dimer Anp32e, a higher eukaryotic histone chaperone directs preferential recognition for H2A.Z Structural basis of histone H2A-H2B recognition by the essential chaperone FACT Protein design by fusion: implications for protein structure prediction and evolution Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1 Molecular basis and specificity of H2A.Z-H2B recognition and deposition by the histone chaperone YL1 Mutations in non-acid patch residues disrupt H2A.Z's association with chromatin through multiple mechanisms.NMR Backbone Assignment of Large Proteins by Using (13) Cα -Only Triple-Resonance Experiments.Histone chaperones link histone nuclear import and chromatin assembly Histone H2A.Z acid patch residues required for deposition and function Nap1 and Chz1 have separate Htz1 nuclear import and assembly functions.Probing the (H3-H4)2 histone tetramer structure using pulsed EPR spectroscopy combined with site-directed spin labelling.Histone chaperone Chz1p regulates H2B ubiquitination and subtelomeric anti-silencing.Electrostatic forces govern the binding mechanism of intrinsically disordered histone chaperones.Global analysis for functional residues of histone variant Htz1 using the comprehensive point mutant library.Distinct roles for histone chaperones in the deposition of Htz1 in chromatin Large multimeric assemblies of nucleosome assembly protein and histones revealed by small-angle X-ray scattering and electron microscopy Importance of electrostatic interactions in the association of intrinsically disordered histone chaperone Chz1 and histone H2A.Z-H2B.Chaperone Nap1 shields histone surfaces used in a nucleosome and can put H2A-H2B in an unconventional tetrameric form.Targeting of the SUN protein Mps3 to the inner nuclear membrane by the histone variant H2A.Z.Histone chaperone-mediated nucleosome assembly process Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR.Histone chaperones, histone acetylation, and the fluidity of the chromogenome Towards a mechanism for histone chaperones.H2A histone-fold and DNA elements in nucleosome activate SWR1-mediated H2A.Z replacement in budding yeast.DNA repair factor APLF is a histone chaperone.The right place at the right time: chaperoning core histone variants Ascending the nucleosome face: recognition and function of structured domains in the histone H2A-H2B dimer.Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly.Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy.Histone chaperone networks shaping chromatin function.Chaperoning histones during DNA replication and repair.DAXX co-folds with H3.3/H4 using high local stability conferred by the H3.3 variant recognition residues.The histone shuffle: histone chaperones in an energetic dance.Conservation of the three-dimensional structure in non-homologous or unrelated proteins.

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

http://www.wikidata.org/entity/Q27651273

description

2008 nî lūn-bûn

@nan

2008 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի օգոստոսին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

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

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

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

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type

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

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

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

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

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

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

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Nature Structural & Molecular Biology

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

@en

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Carl Wu

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

D Flemming Hansen

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

Daron I Freedberg

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

Hanqiao Feng

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

Hidenori Kato

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

Yawen Bai

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

Zheng Zhou

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

P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Crystal structure of a nucleosome core particle containing the variant histone H2A.Z

Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4

Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange.

ATP-driven exchange of histone H2AZ variant catalyzed by SWR1 chromatin remodeling complex.

Chz1, a nuclear chaperone for histone H2AZ.

Structural basis for the histone chaperone activity of Asf1

Histone chaperones: an escort network regulating histone traffic.

The nucleosomal surface as a docking station for Kaposi's sarcoma herpesvirus LANA.

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1624254

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10.1038/NSMB.1465

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8

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15

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1038333625

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18641662

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molecular chaperones

structural biology

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2574748

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