Evidence map›Paper›PMID 29036368›Full record

ArticleNucleic acids research2017

Proteomic identification of histone post-translational modifications and proteins enriched at a DNA double-strand break.

Pingping Wang, Stephanie Byrum, Faith C Fowler, Sangita Pal, Alan J Tackett, Jessica K Tyler

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

7 citing papers in PubMed, 14 citations in OpenAlex.

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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 4 institutions in 1 country.

Pingping WangWeill Cornell Medicine, Department of Pathology and Laboratory Medicine, New York, NY 10065, USA.
Stephanie ByrumUniversity of Arkansas for Medical Sciences, Department of Biochemistry and Molecular Biology, Little Rock, AR 72205, USA.
Faith C FowlerWeill Cornell Medicine, Department of Pathology and Laboratory Medicine, New York, NY 10065, USA.
Sangita PalWeill Cornell Medicine, Department of Pathology and Laboratory Medicine, New York, NY 10065, USA.
Alan J TackettUniversity of Arkansas for Medical Sciences, Department of Biochemistry and Molecular Biology, Little Rock, AR 72205, USA.
Jessica K TylerWeill Cornell Medicine, Department of Pathology and Laboratory Medicine, New York, NY 10065, USA.
University of Arkansas for Medical Sciences · USWeill Cornell Medicine · USCornell University · USThe University of Texas MD Anderson Cancer Center · US

Funding

Translational Regulation in Normal Erythropoiesis and Diamond Blackfan AnemiaP20GM121293 · NIGMS · ARKANSAS CHILDREN'S HOSPITAL RES INST · PI Alan Tackett, Sean D. Taverna · 2017 to 2026
$27.6M
Chromatin's Role in Repair of Radiation-induced Damage.R01CA095641 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI TYLER, JESSICA K · 2002 to 2023
$5.2M
Chromatin Assembly, Structure and FunctionR01GM064475 · NIGMS · WEILL MEDICAL COLL OF CORNELL UNIV · PI TYLER, JESSICA K · 2002 to 2019
$4.4M
NCI NIH HHS R01 CA095641NIGMS NIH HHS P20 GM121293NIGMS NIH HHS R01 GM064475
6 · The paper itself

Abstract

Here, we use ChAP-MS (chromatin affinity purification with mass spectrometry), for the affinity purification of a sequence-specific single-copy endogenous chromosomal locus containing a DNA double-strand break (DSB). We found multiple new histone post-translational modifications enriched on chromatin bearing a DSB from budding yeast. One of these, methylation of histone H3 on lysine 125, has not previously been reported. Among over 100 novel proteins enriched at a DSB were the phosphatase Sit4, the RNA pol II degradation factor Def1, the mRNA export protein Yra1 and the HECT E3 ligase Tom1. Each of these proteins was required for resistance to radiomimetics, and many were required for resistance to heat, which we show here to cause a defect in DSB repair in yeast. Yra1 and Def1 were required for DSB repair per se, while Sit4 was required for rapid inactivation of the DNA damage checkpoint after DSB repair. Thus, our unbiased proteomics approach has led to the unexpected discovery of novel roles for these and other proteins in the DNA damage response.

Indexed as

DNA Breaks, Double-StrandedProtein Processing, Post-TranslationalChromosomal Proteins, Non-HistoneDNA RepairHistonesLysineMass SpectrometryMethylationNuclear ProteinsProtein Phosphatase 2ProteomeProteomicsRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein LigasesChromosomal Proteins, Non-HistoneDEF1 protein, S cerevisiaeHistonesLysineNuclear ProteinsProtein Phosphatase 2ProteomeRNA-Binding ProteinsSaccharomyces cerevisiae ProteinsSIT4 protein, S cerevisiaeTOM1 protein, S cerevisiaeUbiquitin-Protein LigasesYRA1 protein, S cerevisiae

Identifiers

PMID29036368
PMCPMC5737490
OpenAlexW2760534580

What OpenQuestion holds

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LicenceCC BY-NC
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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.