RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones. - Test2 - elhamkhani - TriplyDB

RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

http://www.wikidata.org/entity/Q33953340

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Minor groove binder distamycin remodels chromatin but inhibits transcription reSETting chromatin during transcription elongation Mechanism of transcription through a nucleosome by RNA polymerase II Post-translational modifications of histones that influence nucleosome dynamics Molecular traffic jams on DNA A PWWP domain-containing protein targets the NuA3 acetyltransferase complex via histone H3 lysine 36 trimethylation to coordinate transcriptional elongation at coding regions.Control of chromatin structure by spt6: different consequences in coding and regulatory regions.Altered chromatin architecture underlies progressive impairment of the heat shock response in mouse models of Huntington disease.Recent advances in single molecule studies of nucleosomes Patterns and mechanisms of ancestral histone protein inheritance in budding yeast.Identification of histone mutants that are defective for transcription-coupled nucleosome occupancy The 3-base periodicity and codon usage of coding sequences are correlated with gene expression at the level of transcription elongation.RNA polymerase mapping during stress responses reveals widespread nonproductive transcription in yeast.Structural Analysis of the Key Intermediate Formed during Transcription through a Nucleosome Heavy transcription of yeast genes correlates with differential loss of histone H2B relative to H4 and queued RNA polymerases Dynamics of nucleosome assembly and effects of DNA methylation.A genetic screen and transcript profiling reveal a shared regulatory program for Drosophila linker histone H1 and chromatin remodeler CHD1.Heat shock reduces stalled RNA polymerase II and nucleosome turnover genome-wide Transcription factories in the context of the nuclear and genome organization.Direct regulation of nucleosome density by the conserved AAA-ATPase Yta7 Chromatin and transcription in yeast The elongation rate of RNA polymerase determines the fate of transcribed nucleosomes.Histone Chaperones Spt6 and FACT: Similarities and Differences in Modes of Action at Transcribed Genes SAYP and Brahma are important for 'repressive' and 'transient' Pol II pausing.Structural analysis of nucleosomal barrier to transcription Histone chaperone FACT action during transcription through chromatin by RNA polymerase II Spt6 prevents transcription-coupled loss of posttranslationally modified histone H3.Experimental analysis of hFACT action during Pol II transcription in vitro.WHSC1 links transcription elongation to HIRA-mediated histone H3.3 deposition Nucleosome fragility is associated with future transcriptional response to developmental cues and stress in C. elegans.Analysis of the mechanism of nucleosome survival during transcription.Molecular mechanisms of transcription through single-molecule experiments.Structure and function of active chromatin and DNase I hypersensitive sites.Nucleosome positioning in Saccharomyces cerevisiae.Single-molecule studies of RNAPII elongation.The heat shock response: A case study of chromatin dynamics in gene regulation.Nucleosome-specific, time-dependent changes in histone modifications during activation of the early growth response 1 (Egr1) gene.The mechanism of nucleosome traversal by RNA polymerase II: roles for template uncoiling and transcript elongation factors.Regulation of chaperone binding and nucleosome dynamics by key residues within the globular domain of histone H3.Nucleosomal Barrier to Transcription: Structural Determinants and Changes in Chromatin Structure.

P2860

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P2860

RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

http://www.wikidata.org/entity/Q33953340

description

2010 nî lūn-bûn

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2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

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RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

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type

label

RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

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RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

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prefLabel

RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

@ast

RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

@en

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PNAS.1001148107

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Proceedings of the National Academy of Sciences of the United States of America

P1476

RNA polymerase complexes cooperate to relieve the nucleosomal barrier and evict histones.

@en

P2093

Fu-Kai Hsieh

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

Olga I Kulaeva

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Vasily M Studitsky

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P2860

Crystal structure of the nucleosome core particle at 2.8 A resolution

Histone crosstalk between H3S10ph and H4K16ac generates a histone code that mediates transcription elongation

Transcriptional activation domains of human heat shock factor 1 recruit human SWI/SNF

RNA polymerase stalling at developmental control genes in the Drosophila melanogaster embryo

Transcription through chromatin by RNA polymerase II: histone displacement and exchange

Histone H3 methylation by Set2 directs deacetylation of coding regions by Rpd3S to suppress spurious intragenic transcription.

Genome-wide replication-independent histone H3 exchange occurs predominantly at promoters and implicates H3 K56 acetylation and Asf1.

FACT facilitates transcription-dependent nucleosome alteration

Genome-wide mapping of HATs and HDACs reveals distinct functions in active and inactive genes

Chromatin- and transcription-related factors repress transcription from within coding regions throughout the Saccharomyces cerevisiae genome

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11325-11330

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25

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107

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20534568

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2895129

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