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PP4 is a gamma H2AX phosphatase required for recovery from the DNA damage checkpoint
scientific journal article
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scholarly article
1 reference
stated in
PubMed
PubMed publication ID
18758438
retrieved
4 January 2017
title
PP4 is a gamma H2AX phosphatase required for recovery from the DNA damage checkpoint
(English)
1 reference
stated in
PubMed
PubMed publication ID
18758438
retrieved
4 January 2017
author
Daniel Durocher
series ordinal
4
0 references
Anne-Claude Gingras
series ordinal
3
0 references
Shinichiro Nakada
object named as
Shinichiro Nakada
series ordinal
1
0 references
Ginny I. Chen
series ordinal
2
object named as
Ginny I. Chen
1 reference
stated in
PubMed
PubMed publication ID
18758438
retrieved
4 January 2017
publication date
1 October 2008
1 reference
stated in
PubMed
PubMed publication ID
18758438
retrieved
4 January 2017
published in
EMBO Reports
1 reference
stated in
PubMed
PubMed publication ID
18758438
retrieved
4 January 2017
volume
9
1 reference
stated in
PubMed
PubMed publication ID
18758438
retrieved
4 January 2017
issue
10
1 reference
stated in
PubMed
PubMed publication ID
18758438
retrieved
4 January 2017
page(s)
1019–1026
1 reference
stated in
PubMed
PubMed publication ID
18758438
retrieved
4 January 2017
cites work
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PubMed Central
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20 March 2017
MDC1 directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks
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PubMed Central
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A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity
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PubMed Central
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20 March 2017
Chromatin association of human origin recognition complex, cdc6, and minichromosome maintenance proteins during the cell cycle: assembly of prereplication complexes in late mitosis
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20 March 2017
PPX, a novel protein serine/threonine phosphatase localized to centrosomes
1 reference
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PubMed Central
reference URL
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20 March 2017
Megabase chromatin domains involved in DNA double-strand breaks in vivo
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Systematic identification of protein complexes in Saccharomyces cerevisiae by mass spectrometry
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20 March 2017
A phosphatase complex that dephosphorylates gammaH2AX regulates DNA damage checkpoint recovery
1 reference
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PubMed Central
reference URL
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20 March 2017
DNA Double-stranded Breaks Induce Histone H2AX Phosphorylation on Serine 139
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PubMed Central
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20 March 2017
The DNA damage response: ten years after
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PubMed Central
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A public domain image-analysis program for the single-cell gel-electrophoresis (comet) assay
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20 March 2017
Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks
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PubMed Central
reference URL
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FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16.
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Chromatin disassembly and reassembly during DNA repair.
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29 September 2017
gamma-H2AX dephosphorylation by protein phosphatase 2A facilitates DNA double-strand break repair
1 reference
stated in
PubMed Central
reference URL
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29 September 2017
Autophosphorylation of ataxia-telangiectasia mutated is regulated by protein phosphatase 2A.
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PubMed Central
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29 September 2017
ATM and DNA-PK function redundantly to phosphorylate H2AX after exposure to ionizing radiation
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PubMed Central
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29 September 2017
The formation and activity of PP2A holoenzymes do not depend on the isoform of the catalytic subunit
1 reference
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PubMed Central
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29 September 2017
Protein serine/threonine phosphatases; an expanding family
1 reference
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PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2527856
retrieved
29 September 2017
Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth and bud morphogenesis
1 reference
stated in
PubMed Central
reference URL
https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2527856
retrieved
29 September 2017
The protein phosphatases involved in cellular regulation. 2. Purification, subunit structure and properties of protein phosphatases-2A0, 2A1, and 2A2 from rabbit skeletal muscle
1 reference
stated in
PubMed
reference URL
https://pubmed.ncbi.nlm.nih.gov/18758438
retrieved
12 December 2020
based on heuristic
inferred from PubMed ID database lookup
Saccharomyces cerevisiae Elongator mutations confer resistance to the Kluyveromyces lactis zymocin
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1038%2FEMBOR.2008.162
retrieved
7 January 2021
based on heuristic
inferred from DOI database lookup
Identifiers
DOI
10.1038/EMBOR.2008.162
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3251065
OpenCitations bibliographic resource ID
3251065
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3251065
PMC publication ID
2527856
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3251065
PubMed publication ID
18758438
1 reference
stated in
Consolidated OpenCitations Corpus – April 2017
OpenCitations bibliographic resource ID
3251065
ResearchGate publication ID
232761527
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