Histone H3 lysine 56 acetylation and the response to DNA replication fork damage - Wikidata - awgldk - TriplyDB

Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Functions of Ubiquitin and SUMO in DNA Replication and Replication Stress Rescuing stalled or damaged replication forks Rtt109 prevents hyper-amplification of ribosomal RNA genes through histone modification in budding yeast.Asf1 facilitates dephosphorylation of Rad53 after DNA double-strand break repair.Histone H3K56 acetylation, Rad52, and non-DNA repair factors control double-strand break repair choice with the sister chromatid Damaged DNA-binding protein down-regulates epigenetic mark H3K56Ac through histone deacetylase 1 and 2.Hyper-Acetylation of Histone H3K56 Limits Break-Induced Replication by Inhibiting Extensive Repair Synthesis.Replisome function during replicative stress is modulated by histone h3 lysine 56 acetylation through Ctf4.Interplay between histone H3 lysine 56 deacetylation and chromatin modifiers in response to DNA damage.Mutations in Replicative Stress Response Pathways Are Associated with S Phase-specific Defects in Nucleotide Excision Repair Chromosome-wide histone deacetylation by sirtuins prevents hyperactivation of DNA damage-induced signaling upon replicative stress.Site-specific Acetylation of Histone H3 Decreases Polymerase β Activity on Nucleosome Core Particles in Vitro Cohesin and the nucleolus constrain the mobility of spontaneous repair foci.ADA3 regulates normal and tumor mammary epithelial cell proliferation through c-MYC.Regulation of Replication Fork Advance and Stability by Nucleosome Assembly.Monoubiquitylation of histone H2B contributes to the bypass of DNA damage during and after DNA replication Nucleosome assembly and genome integrity: The fork is the link.Epigenetic perspectives on cancer chemotherapy response.Chromatin modifications and DNA repair: beyond double-strand breaks.Histone modifications in DNA damage response.Regulation of the histone deacetylase Hst3 by cyclin-dependent kinases and the ubiquitin ligase SCFCdc4.Anaphase-promoting complex/cyclosome-mediated proteolysis of Ams2 in the G1 phase ensures the coupling of histone gene expression to DNA replication in fission yeast.Hst3p, a histone deacetylase, promotes maintenance of Saccharomyces cerevisiae chromosome III lacking efficient replication origins.Dissecting Nucleosome Function with a Comprehensive Histone H2A and H2B Mutant Library.FANCD2 binding identifies conserved fragile sites at large transcribed genes in avian cells.Rpb9-deficient cells are defective in DNA damage response and require histone H3 acetylation for survival.55th Annual Canadian Society for Molecular Biosciences Conference on Epigenetics and Genomic Stability. Whistler, British Columbia, Canada, 14–18 March 2012.An interplay between multiple sirtuins promotes completion of DNA replication in cells with short telomeres.Fission Yeast Sirtuin Hst4 Functions in Preserving Genomic Integrity by Regulating Replisome Component Mcl1.

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

http://www.wikidata.org/entity/Q24612284

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2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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type

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Molecular and Cellular Biology

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Histone H3 lysine 56 acetylation and the response to DNA replication fork damage

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Alain Verreault

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

Edlie St-Hilaire

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Eun-Hye Lee

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Gitte Schalck Kaiser

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Hugo Wurtele

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Julien Bacal

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Paul Maddox

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Translating the Histone Code

Methyl methanesulfonate (MMS) produces heat-labile DNA damage but no detectable in vivo DNA double-strand breaks.

Yeast Rtt109 promotes genome stability by acetylating histone H3 on lysine 56

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

CBP/p300-mediated acetylation of histone H3 on lysine 56

Reduction of nucleosome assembly during new DNA synthesis impairs both major pathways of double-strand break repair

Structure of the Rtt109-AcCoA/Vps75 Complex and Implications for Chaperone-Mediated Histone Acetylation

Rad52 forms DNA repair and recombination centers during S phase.

Genome-wide analysis of Rad52 foci reveals diverse mechanisms impacting recombination.

Ubc9- and mms21-mediated sumoylation counteracts recombinogenic events at damaged replication forks.

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154-72

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scholarly article

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1644529

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10.1128/MCB.05415-11

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1

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32

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Philippe Pasero

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2012-01-01T00:00:00Z

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22025679

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3255698

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