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Article

H2AX post-translational modifications in the ionizing radiation response and homologous recombination.

Cell cycle (Georgetown, Tex.) - 1 Sept 2010

Xie Anyong, Odate Shobu, Chandramouly Gurushankar, Scully Ralph

Abstract excerpt

Histone H2AX phosphorylation on a C-terminal serine residue to form "γ-H2AX" is a critical early event in the chromatin response to chromosomal DNA double strand breaks in eukaryotes. In mammalian cells, γ-H2AX is formed when H2AX is phosphorylated on serine 139 by ATM or by other DNA damage response kinases. H2AX prevents genomic instability and tumorigenesis, and supports class-switch recombination at...

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Topics

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Share to Adaptor Proteins, Signal Transducing
Share to DNA Breaks, Double-Stranded

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Share to Intracellular Signaling Peptides and Proteins

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Share to Protein Processing, Post-Translational

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Source

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Identifiers

PMID: 20703100
DOI: 10.4161/cc.9.17.12884
PMCID: PMC2980696

Genes

H2AX
MDC1
ATM

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

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H2AX post-translational modifications in the ionizing radiation response and homologous recombination.PMID 20703100Read ↗

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Activation of DNA damage response signaling in mammalian cells by ionizing radiationSemantic proximity Read ↗

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Factors to Consider for the Correct Use of γH2AX in the Evaluation of DNA Double-Strand Breaks Damage Caused by Ionizing RadiationSemantic proximity Read ↗

Critical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair.Semantic proximity Read ↗

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