(Q28201846)

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Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress

scientific article (publication date: 21 December 2001)

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title

Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress (English)

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I M Ward

1

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J Chen

series ordinal

2

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language of work or name

English

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publication date

21 December 2001

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published in

Journal of Biological Chemistry

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volume

276

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page(s)

47759-62

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issue

51

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cites work

DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.C100569200

retrieved

21 January 2018

Megabase chromatin domains involved in DNA double-strand breaks in vivo

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reference URL

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21 January 2018

Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX

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21 January 2018

Recombinational DNA double-strand breaks in mice precede synapsis

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.C100569200

retrieved

21 January 2018

Initiation of DNA fragmentation during apoptosis induces phosphorylation of H2AX histone at serine 139

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reference URL

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21 January 2018

A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.C100569200

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21 January 2018

Tumor suppressor p53 binding protein 1 (53BP1) is involved in DNA damage-signaling pathways

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Crossref

reference URL

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21 January 2018

p53 binding protein 1 (53BP1) is an early participant in the cellular response to DNA double-strand breaks

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reference URL

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21 January 2018

A role for Saccharomyces cerevisiae histone H2A in DNA repair.

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21 January 2018

The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast

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reference URL

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21 January 2018

Targeted disruption of the cell-cycle checkpoint gene ATR leads to early embryonic lethality in mice

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reference URL

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21 January 2018

ATR disruption leads to chromosomal fragmentation and early embryonic lethality

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21 January 2018

Functional interactions between BRCA1 and the checkpoint kinase ATR during genotoxic stress

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21 January 2018

Association of BRCA1 with Rad51 in mitotic and meiotic cells

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21 January 2018

Roadblocks and detours during DNA replication: mechanisms of mutagenesis in mammalian cells

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21 January 2018

The DNA damage response: putting checkpoints in perspective

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reference URL

https://api.crossref.org/works/10.1074%2FJBC.C100569200

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21 January 2018

Overexpression of a kinase-inactive ATR protein causes sensitivity to DNA-damaging agents and defects in cell cycle checkpoints

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Crossref

reference URL

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21 January 2018

Physical interactions among human checkpoint control proteins HUS1p, RAD1p, and RAD9p, and implications for the regulation of cell cycle progression

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Crossref

reference URL

https://api.crossref.org/works/10.1074%2FJBC.C100569200

retrieved

21 January 2018

Identifiers

DOI

10.1074/JBC.C100569200

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stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1050255

OpenCitations bibliographic resource ID

1050255

1 reference

stated in

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1050255

(Q28201846)

Histone H2AX is phosphorylated in an ATR-dependent manner in response to replicational stress

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