Evidence map›Paper›PMID 34570618›Full record

ArticleMolecular and cellular biology2021

DNA Damage-Induced Phosphorylation of Histone H2A at Serine 15 Is Linked to DNA End Resection.

Salar Ahmad, Valérie Côté, Jacques Côté

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular and cellular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.2field-weighted citation impact, top 50% 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

4 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Histone Phosphorylation in DNA Damage Response.International journal of molecular sciences · 2025
    Review
  3. Article
  4. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Salar AhmadSt-Patrick Research Group in Basic Oncology, Centre Hospitalier Universitaire de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, Quebec, Canada.
Valérie CôtéSt-Patrick Research Group in Basic Oncology, Centre Hospitalier Universitaire de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, Quebec, Canada.
Jacques CôtéSt-Patrick Research Group in Basic Oncology, Centre Hospitalier Universitaire de Québec-Université Laval Research Center, Laval University Cancer Research Center, Quebec City, Quebec, Canada.ORCID 0000-0001-6751-555X
Centre hospitalier universitaire de Québec · CA

Funding

CIHR FDN-143314CIHR FDN-314413
6 · The paper itself

Abstract

The repair of DNA double-strand breaks (DSBs) occurs in chromatin, and several histone posttranslational modifications have been implicated in the process. Modifications of the histone H2A N-terminal tail have also been linked to DNA damage response, through acetylation or ubiquitination of lysine residues that regulate repair pathway choice. Here, we characterize a new DNA damage-induced phosphorylation on chromatin, at serine 15 of H2A in yeast. We show that this SQ motif functions independently of the classical S129 C-terminal site (γ-H2A) and that mutant-mimicking constitutive phosphorylation increases cell sensitivity to DNA damage. H2AS129ph is induced by Tel1

Indexed as

Adaptor Proteins, Signal TransducingCell Cycle ProteinsChromatinDNA Breaks, Double-StrandedDNA DamageGene Expression Regulation, FungalHistonesIntracellular Signaling Peptides and ProteinsMethyl MethanesulfonatePhosphorylationProtein Serine-Threonine KinasesReplication Protein ASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingCell Cycle ProteinsChromatinHistonesIntracellular Signaling Peptides and ProteinsLCD1 protein, S cerevisiaeMEC1 protein, S cerevisiaeMethyl MethanesulfonateProtein Serine-Threonine Kinasesrad9 proteinReplication Protein ARFA1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsDNA damagedouble strand breakH2Ahistone phosphorylationRad9resection

Identifiers

PMID34570618
PMCPMC8608016
OpenAlexW3203975814

What OpenQuestion holds

Textmetadata
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.