Evidence map›Paper›PMID 29192276›Full record

ArticleScientific reports2017

Protein-lysine methyltransferases G9a and GLP1 promote responses to DNA damage.

Vasudeva Ginjala, Lizahira Rodriguez-Colon, Bratati Ganguly, Prawallika Gangidi, Paul Gallina, Husam Al-Hraishawi, Atul Kulkarni, Jeremy Tang, Jinesh Gheeya, Srilatha Simhadri and 3 more

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

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

25 citing papers in PubMed, 35 citations in OpenAlex.

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  20. Screen identifies DYRK1B network as mediator of transcription repression on damaged chromatin.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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

13 authors at 2 institutions in 1 country.

Vasudeva GinjalaDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA. ginjalva@cinj.rutgers.edu.
Lizahira Rodriguez-ColonDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Bratati GangulyDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Prawallika GangidiCornell University, College of Engineering, Department of Biological Engineering, 111 Wing Drive, Ithaca, NY, 14853-5701, USA.
Paul GallinaDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Husam Al-HraishawiDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Atul KulkarniDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Jeremy TangDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Jinesh GheeyaDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Srilatha SimhadriDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Ming YaoDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Bing XiaDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA.
Shridar GanesanDepartment of Medicine, Rutgers Cancer Institute of New Jersey, Rutgers University, 195 Little Albany street, New Brunswick, New Jersey, 08903, USA. ganesash@cinj.rutgers.edu.
Rutgers, The State University of New Jersey · USCornell University · US

Funding

Role of PALB2 in the DNA Damage Response and Cancer SuppressionR01CA138804 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI XIA, BING · 2009 to 2024
$5.5M
Targeting Autophagy in Hereditary Breast CancerR01CA188096 · NCI · RBHS -CANCER INSTITUTE OF NEW JERSEY · PI WHITE, EILEEN P., XIA, BING · 2015 to 2019
$2.4M
53BP1-Mediated Regulation of DNA Repair and ChemoresistanceR01CA169182 · NCI · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI GANESAN, SHRIDAR · 2012 to 2016
$1.6M
NCI NIH HHS R01 CA138804NCI NIH HHS R01 CA169182NCI NIH HHS R01 CA188096
6 · The paper itself

Abstract

Upon induction of DNA breaks, ATM activation leads to a cascade of local chromatin modifications that promote efficient recruitment of DNA repair proteins. Errors in this DNA repair pathway lead to genomic instability and cancer predisposition. Here, we show that the protein lysine methyltransferase G9a (also known as EHMT2) and GLP1 (also known as EHMT1) are critical components of the DNA repair pathway. G9a and GLP1 rapidly localizes to DNA breaks, with GLP1 localization being dependent on G9a. ATM phosphorylation of G9a on serine 569 is required for its recruitment to DNA breaks. G9a catalytic activity is required for the early recruitment of DNA repair factors including 53BP and BRCA1 to DNA breaks. Inhibition of G9a catalytic activity disrupts DNA repair pathways and increases sensitivity to ionizing radiation. Thus, G9a is a potential therapeutic target in the DNA repair pathway.

Indexed as

DNA DamageAtaxia Telangiectasia Mutated ProteinsCell LineDNA RepairGlucagon-Like Peptide 1Histocompatibility AntigensHistone-Lysine N-MethyltransferaseHumansModels, BiologicalPhosphorylationProtein BindingProtein TransportTumor Suppressor p53-Binding Protein 1Ataxia Telangiectasia Mutated ProteinsATM protein, humanEHMT2 protein, humanGlucagon-Like Peptide 1Histocompatibility AntigensHistone-Lysine N-MethyltransferaseTumor Suppressor p53-Binding Protein 1

Identifiers

PMID29192276
PMCPMC5709370
OpenAlexW2770539701

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.