Evidence map›Paper›PMID 30344095›Full record

ArticleMolecular cell2018

The Histone Chaperone FACT Coordinates H2A.X-Dependent Signaling and Repair of DNA Damage.

Sandra Piquet, Florent Le Parc, Siau-Kun Bai, Odile Chevallier, Salomé Adam, Sophie E Polo

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.9field-weighted citation impact, top 5% 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

60 citing papers in PubMed, 101 citations in OpenAlex.

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  5. Beyond Chaperoning: The Multifaceted Role of FACT in Chromatin Transactions.International journal of molecular sciences · 2025
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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

6 authors at 3 institutions in 1 country.

Sandra PiquetEpigenome Integrity Group, Epigenetics & Cell Fate Centre, UMR7216 CNRS, Paris Diderot University, Sorbonne Paris Cité, 75013 Paris, France.
Florent Le ParcEpigenome Integrity Group, Epigenetics & Cell Fate Centre, UMR7216 CNRS, Paris Diderot University, Sorbonne Paris Cité, 75013 Paris, France.
Siau-Kun BaiEpigenome Integrity Group, Epigenetics & Cell Fate Centre, UMR7216 CNRS, Paris Diderot University, Sorbonne Paris Cité, 75013 Paris, France.
Odile ChevallierEpigenome Integrity Group, Epigenetics & Cell Fate Centre, UMR7216 CNRS, Paris Diderot University, Sorbonne Paris Cité, 75013 Paris, France.
Salomé AdamEpigenome Integrity Group, Epigenetics & Cell Fate Centre, UMR7216 CNRS, Paris Diderot University, Sorbonne Paris Cité, 75013 Paris, France.
Sophie E PoloEpigenome Integrity Group, Epigenetics & Cell Fate Centre, UMR7216 CNRS, Paris Diderot University, Sorbonne Paris Cité, 75013 Paris, France. Electronic address: sophie.polo@univ-paris-diderot.fr.
Université Paris Cité · FREpigénétique et Destin Cellulaire · FRSorbonne Paris Cité · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Safeguarding cell function and identity following a genotoxic stress challenge entails a tight coordination of DNA damage signaling and repair with chromatin maintenance. How this coordination is achieved and with what impact on chromatin integrity remains elusive. Here, we address these questions by investigating the mechanisms governing the distribution in mammalian chromatin of the histone variant H2A.X, a central player in damage signaling. We reveal that H2A.X is deposited de novo at sites of DNA damage in a repair-coupled manner, whereas the H2A.Z variant is evicted, thus reshaping the chromatin landscape at repair sites. Our mechanistic studies further identify the histone chaperone FACT (facilitates chromatin transcription) as responsible for the deposition of newly synthesized H2A.X. Functionally, we demonstrate that FACT potentiates H2A.X-dependent signaling of DNA damage. We propose that new H2A.X deposition in chromatin reflects DNA damage experience and may help tailor DNA damage signaling to repair progression.

Indexed as

DNA RepairAlpha-AmanitinAnimalsAtaxia Telangiectasia Mutated ProteinsCell Line, TumorChromatin Assembly and DisassemblyDNADNA-Binding ProteinsDNA DamageEpithelial CellsGene Expression RegulationHigh Mobility Group ProteinsHistonesHumansMiceMorpholines2-morpholin-4-yl-6-thianthren-1-yl-pyran-4-one4-(4-(3-methylmorpholin-4-yl)-6-(1-(methylsulfonyl)cyclopropyl)pyrimidin-2-yl)-1H-indoleAlpha-AmanitinAtaxia Telangiectasia Mutated ProteinsATM protein, humanATR protein, humanDNADNA-Binding ProteinsH2AX protein, humanHigh Mobility Group Proteinshistone H2A.F-ZHistonesMorpholinesNucleosomesPoisonsPyrimidinesPyronesSSRP1 protein, humanTranscriptional Elongation FactorsANP32EchromatinDNA damage signalingDNA repairFACTH2A.XH2A.Zhistone chaperoneshistone variantsUV damage

Identifiers

PMID30344095
PMCPMC6292839
OpenAlexW2897716354

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.