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Global regulation of H2A.Z localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity
scientific article published on 21 January 2011
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scholarly article
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PubMed
PubMed ID
21241891
retrieved
1 December 2016
title
Global regulation of H2A.Z localization by the INO80 chromatin-remodeling enzyme is essential for genome integrity
(English)
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stated in
PubMed
PubMed ID
21241891
retrieved
1 December 2016
main subject
Chromatin-remodeling ATPase INO80 YGL150C
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GOA release 2020-03-11
author
Oliver J Rando
object named as
Oliver J Rando
series ordinal
3
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author name string
Shinya Watanabe
series ordinal
2
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Manolis Papamichos-Chronakis
series ordinal
1
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Craig L Peterson
series ordinal
4
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language of work or name
English
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publication date
21 January 2011
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published in
Cell
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PubMed
PubMed ID
21241891
retrieved
1 December 2016
volume
144
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issue
2
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page(s)
200-13
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cites work
Roles of human INO80 chromatin remodeling enzyme in DNA replication and chromosome segregation suppress genome instability
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Asf1-like structure of the conserved Yaf9 YEATS domain and role in H2A.Z deposition and acetylation
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The euchromatic and heterochromatic landscapes are shaped by antagonizing effects of transcription on H2A.Z deposition
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Recombinational repair within heterochromatin requires ATP-dependent chromatin remodeling
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Cooperation between the INO80 complex and histone chaperones determines adaptation of stress gene transcription in the yeast Saccharomyces cerevisiae
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A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair
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Mec1/Tel1 phosphorylation of the INO80 chromatin remodeling complex influences DNA damage checkpoint responses
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Swc2 is a widely conserved H2AZ-binding module essential for ATP-dependent histone exchange
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Histone variant H2A.Z marks the 5' ends of both active and inactive genes in euchromatin
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A protein complex containing the conserved Swi2/Snf2-related ATPase Swr1p deposits histone variant H2A.Z into euchromatin
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A Snf2 family ATPase complex required for recruitment of the histone H2A variant Htz1.
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Persistent initiation of DNA replication and chromatin-bound MCM proteins during the cell cycle in cdc6 mutants
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H2A.Z overexpression promotes cellular proliferation of breast cancer cells
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Chromatin remodelling beyond transcription: the INO80 and SWR1 complexes.
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29 September 2017
The INO80 chromatin remodeling complex in transcription, replication and repair
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Interplay between Ino80 and Swr1 chromatin remodeling enzymes regulates cell cycle checkpoint adaptation in response to DNA damage.
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Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomyces cerevisiae
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Acetylation of H2AZ Lys 14 is associated with genome-wide gene activity in yeast
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H2A.Z alters the nucleosome surface to promote HP1alpha-mediated chromatin fiber folding
1 reference
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reference URL
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retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states
1 reference
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reference URL
https://pubmed.ncbi.nlm.nih.gov/21241891
retrieved
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based on heuristic
inferred from PubMed ID database lookup
Gene expression differences between the microsatellite instability (MIN) and chromosomal instability (CIN) phenotypes in colorectal cancer revealed by high-density cDNA array hybridization
1 reference
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PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21241891
retrieved
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based on heuristic
inferred from PubMed ID database lookup
Conserved Histone Variant H2A.Z Protects Euchromatin from the Ectopic Spread of Silent Heterochromatin
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/21241891
retrieved
12 December 2020
based on heuristic
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Identifiers
DOI
10.1016/J.CELL.2010.12.021
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1154865
OpenCitations bibliographic resource ID
1154865
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1154865
PMCID
3035940
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1154865
PubMed ID
21241891
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
1154865
ResearchGate publication ID
49762070
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