FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs
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The CENP-T/-W complex is a binding partner of the histone chaperone FACT.Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1FACT is a sensor of DNA torsional stress in eukaryotic cells.Epigenome Maintenance in Response to DNA DamageIntegrated molecular mechanism directing nucleosome reorganization by human FACTStructural basis for histone H2B deubiquitination by the SAGA DUB module.A basic domain in the histone H2B N-terminal tail is important for nucleosome assembly by FACT.The Chd1 chromatin remodeler shifts hexasomes unidirectionally.Histone chaperone networks shaping chromatin function.Chromatin remodeller Fun30Fft3 induces nucleosome disassembly to facilitate RNA polymerase II elongation.Structure of the human histone chaperone FACT Spt16 N-terminal domain.The FACT Complex Promotes Avian Leukosis Virus DNA Integration.Recognition of ubiquitinated nucleosomes.Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.Solution structure of the isolated histone H2A-H2B heterodimer.Large-scale ATP-independent nucleosome unfolding by a histone chaperone.Dual function of Swc5 in SWR remodeling ATPase activation and histone H2A eviction.Stabilization of Nucleosomes by Histone Tails and by FACT Revealed by spFRET Microscopy.Dynamic intramolecular regulation of the histone chaperone nucleoplasmin controls histone binding and release.It's fun to transcribe with Fun30: A model for nucleosome dynamics during RNA polymerase II-mediated elongation.TRAIN (Transcription of Repeats Activates INterferon) in response to chromatin destabilization induced by small molecules in mammalian cells.Charged residues on the side of the nucleosome contribute to normal Spt16-gene interactions in budding yeast.Residues in the Nucleosome Acidic Patch Regulate Histone Occupancy and Are Important for FACT Binding in Saccharomyces cerevisiae.C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4.Acetylation-Dependent Recruitment of the FACT Complex and Its Role in Regulating Pol II Occupancy Genome-Wide in Saccharomyces cerevisiae.Replication-Coupled Nucleosome Assembly in the Passage of Epigenetic Information and Cell Identity.Histone chaperones FACT and Spt6 prevent histone variants from turning into histone deviants.Structure-specific recognition protein-1 (SSRP1) is an elongated homodimer that binds histones.DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surfaceMechanism of FACT removal from transcribed genes by anticancer drugs curaxins
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P2860
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs
@ast
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs
@en
type
label
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs
@ast
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs
@en
prefLabel
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs
@ast
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs
@en
P2093
P2860
P1433
P1476
FACT Disrupts Nucleosome Structure by Binding H2A-H2B with Conserved Peptide Motifs
@en
P2093
Christopher P Hill
David J Kemble
Frank G Whitby
Laura L McCullough
P2860
P304
P356
10.1016/J.MOLCEL.2015.09.008
P50
P577
2015-10-06T00:00:00Z