Evidence map›Paper›PMID 20703100›Full record

ArticleCell cycle (Georgetown, Tex.)2010

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

Anyong Xie, Shobu Odate, Gurushankar Chandramouly, Ralph Scully

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.6field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Histone Phosphorylation in DNA Damage Response.International journal of molecular sciences · 2025
    Review
  3. Article
  4. Review
  5. Review
  6. Histone H2A variants: Diversifying chromatin to ensure genome integrity.Seminars in cell & developmental biology · 2023
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. Distinct roles foreLife · 2019
    Article
  12. Article
  13. Preserving genome integrity and function: the DNA damage response and histone modifications.Critical reviews in biochemistry and molecular biology · 2019
    Review
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Anyong XieDepartment of Medicine, Harvard Medical School, Beth Israel Deaconess Medical Center, Boston, MA, USA.
Shobu Odate
Gurushankar Chandramouly
Ralph Scully
Beth Israel Deaconess Medical Center · USHarvard University Press · USRussian State Agrarian Correspondence University · RU

Funding

ANALYSIS OF BRCA1 RECOMBINATION FUNCTIONSR01CA095175 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI SCULLY, RALPH · 2002 to 2021
$4.9M
The chromatin response in mammalian double strand break repairR01GM073894 · NIGMS · BETH ISRAEL DEACONESS MEDICAL CENTER · PI SCULLY, RALPH · 2005 to 2014
$2.5M
Targeting non-homologous end joining in cancer therapyRC1CA145867 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI SCULLY, RALPH · 2009 to 2010
$1.0M
NCI NIH HHS CA095175NCI NIH HHS R01 CA095175NCI NIH HHS RC1 CA145867NIGMS NIH HHS GM073894NIGMS NIH HHS R01 GM073894
6 · The paper itself

Abstract

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 immunoglobulin heavy chain loci in mammals. We showed previously that H2AX controls double strand break repair by homologous recombination (HR) between sister chromatids. The HR functions of H2AX are mediated by interaction of γ-H2AX with the chromatin-associated adaptor protein MDC1. H2AX is potentially subject to additional post-translational modifications associated with the DNA damage response and with other chromatin functions. To test this idea, we used mass spectroscopy to identify H2AX residues additional to serine 139 that are post-translationally modified following exposure of cells to ionizing radiation (IR) and identified several new IR-responsive residues of H2AX. We determined the impact of IR-responsive H2AX residues on cellular resistance to IR and on H2AX-dependent HR, and also analyzed the contribution to HR of other known or potential post-translationally modified residues of H2AX. The results suggest that the HR and IR-resistance functions of H2AX are controlled in large part by specific MDC1-interacting residues of H2AX, but that additional H2AX residues modulate these core functions of H2AX.

Indexed as

Radiation, IonizingRecombination, GeneticAdaptor Proteins, Signal TransducingAnimalsCell Cycle ProteinsDNA-Binding ProteinsDNA Breaks, Double-StrandedDNA RepairEmbryonic Stem CellsHistonesIntracellular Signaling Peptides and ProteinsMass SpectrometryMiceMutationProtein Processing, Post-TranslationalAdaptor Proteins, Signal TransducingCell Cycle ProteinsDNA-Binding Proteinsgamma-H2AX protein, mouseHistonesIntracellular Signaling Peptides and ProteinsMDC1 protein, mouseXLF protein, mouse

Identifiers

PMID20703100
PMCPMC2980696
OpenAlexW1964303708

What OpenQuestion holds

Textmetadata
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Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.