Evidence map›Paper›PMID 30894431›Full record

ArticlemSphere2019

Glu-108 in Saccharomyces cerevisiae Rad51 Is Critical for DNA Damage-Induced Nuclear Function.

Tanvi Suhane, Vijayalakshmi Bindumadhavan, Nupur Fangaria, Achuthsankar S Nair, Wahida Tabassum, Poorvaja Muley, Mrinal K Bhattacharyya, Sunanda Bhattacharyya

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

Article in mSphere, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.3field-weighted citation impact, top 42% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
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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

8 authors at 2 institutions in 1 country.

Tanvi SuhaneDepartment of Biotechnology and Bioinformatics, School of Life Sciences, University of Hyderabad, Hyderabad, India.
Vijayalakshmi BindumadhavanDepartment of Computational Biology and Bioinformatics, University of Kerala, Thiruvanthapuram, India.
Nupur FangariaDepartment of Biotechnology and Bioinformatics, School of Life Sciences, University of Hyderabad, Hyderabad, India.
Achuthsankar S NairDepartment of Computational Biology and Bioinformatics, University of Kerala, Thiruvanthapuram, India.
Wahida TabassumDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad, India.
Poorvaja MuleyDepartment of Biotechnology and Bioinformatics, School of Life Sciences, University of Hyderabad, Hyderabad, India.
Mrinal K BhattacharyyaDepartment of Biochemistry, School of Life Sciences, University of Hyderabad, Hyderabad, India.
Sunanda BhattacharyyaDepartment of Biotechnology and Bioinformatics, School of Life Sciences, University of Hyderabad, Hyderabad, India sdeb70@gmail.com.
University of Hyderabad · INUniversity of Kerala · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

DNA damage-induced Rad51 focus formation is the hallmark of homologous recombination-mediated DNA repair. Earlier, we reported that Rad51 physically interacts with Hsp90, and under the condition of Hsp90 inhibition, it undergoes proteasomal degradation. Here, we show that the dynamic interaction between Rad51 and Hsp90 is crucial for the DNA damage-induced nuclear function of Rad51. Guided by a bioinformatics study, we generated a single mutant of Rad51, which resides at the N-terminal domain, outside the ATPase core domain. The mutant with an E to L change at residue 108 (Rad51

Indexed as

DNA DamageDNA RepairAnimalsComputational BiologyDNA-Binding ProteinsDNA, FungalHSP90 Heat-Shock ProteinsHumansMethyl MethanesulfonateMiceMutationProtein BindingRad51 RecombinaseRad52 DNA Repair and Recombination ProteinSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsDNA-Binding ProteinsDNA, FungalHSP82 protein, S cerevisiaeHSP90 Heat-Shock ProteinsMethyl MethanesulfonateRAD51 protein, humanRad51 protein, mouseRAD51 protein, S cerevisiaeRad51 RecombinaseRad52 DNA Repair and Recombination ProteinRAD52 protein, humanSaccharomyces cerevisiae ProteinsDNA repairhomologous recombinationHsp90Hsp90-Rad51 interactionmolecular chaperoneRad51 recruitment to chromatin

Identifiers

PMID30894431
PMCPMC6429042
OpenAlexW2922629137

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.