Evidence map›Paper›PMID 19783859›Full record

ArticleThe Journal of biological chemistry2009

Cellular redistribution of Rad51 in response to DNA damage: novel role for Rad51C.

Otto S Gildemeister, Jay M Sage, Kendall L Knight

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

58 citing papers in PubMed, 90 citations in OpenAlex.

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  10. Molecularly Defined Subsets of Ewing Sarcoma Tumors Differ in Their Responses to IGF1R and WEE1 Inhibition.Clinical cancer research : an official journal of the American Association for Cancer Research · 2023
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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

3 authors at 1 institution in 1 country.

Otto S GildemeisterDepartment of Biochemistry and Molecular Pharmacology, University of Massachusetts Medical School, Worcester, Massachusetts 01605, USA.
Jay M Sage
Kendall L Knight
University of Massachusetts Chan Medical School · US

Funding

FUNCTIONAL ORGANIZATION OF THE RECA PROTEINR01GM044772 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KNIGHT, KENDALL L. · 1991 to 2010
$2.2M
Role of Human Rad52 and Rad51- paralogs in DNA RepairR01GM065851 · NIGMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI KNIGHT, KENDALL L. · 2004 to 2007
$1.1M
NIGMS NIH HHS GM044772NIGMS NIH HHS GM065851NIGMS NIH HHS R01 GM044772NIGMS NIH HHS R01 GM065851
6 · The paper itself

Abstract

Exposure of cells to DNA-damaging agents results in a rapid increase in the formation of subnuclear complexes containing Rad51. To date, it has not been determined to what extent DNA damage-induced cytoplasmic to nuclear transport of Rad51 may contribute to this process. We have analyzed subcellular fractions of HeLa and HCT116 cells and found a significant increase in nuclear Rad51 levels following exposure to a modest dose of ionizing radiation (2 grays). We also observed a DNA damage-induced increase in nuclear Rad51 in the Brca2-defective cell line Capan-1. To address a possible Brca2-independent mechanism for Rad51 nuclear transport, we analyzed subcellular fractions for two other Rad51-interacting proteins, Rad51C and Xrcc3. Rad51C has a functional nuclear localization signal, and although we found that the subcellular distribution of Xrcc3 was not significantly affected by DNA damage, there was a damage-induced increase in nuclear Rad51C. Furthermore, RNA interference-mediated depletion of Rad51C in HeLa and Capan-1 cells resulted in lower steady-state levels of nuclear Rad51 as well as a diminished DNA damage-induced increase. Our results provide important insight into the cellular regulation of Rad51 nuclear entry and a role for Rad51C in this process.

Indexed as

DNA DamageActive Transport, Cell NucleusCell NucleusCytoplasmDNA-Binding ProteinsDNA, NeoplasmGenes, BRCA2HCT116 CellsHeLa CellsHumansImmunoblottingInfrared RaysNuclear Localization SignalsPancreatic NeoplasmsRad51 RecombinaseReverse Transcriptase Polymerase Chain ReactionDNA-Binding ProteinsDNA, NeoplasmNuclear Localization SignalsRAD51C protein, humanRad51 RecombinaseRNA, MessengerX-ray repair cross complementing protein 3

Identifiers

PMID19783859
PMCPMC2797266
OpenAlexW2064965689

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.