Evidence map›Paper›PMID 9012806›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1997

Activities of human recombination protein Rad51.

R C Gupta, L R Bazemore, E I Golub, C M Radding

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
9.8field-weighted citation impact, top 1% 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

92 citing papers in PubMed, 255 citations in OpenAlex.

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  11. Diverse role of survival motor neuron protein.Biochimica et biophysica acta. Gene regulatory mechanisms · 2017
    Review
  12. Article
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  15. Article
  16. Review
  17. Article
  18. DNA strand exchange and RecA homologs in meiosis.Cold Spring Harbor perspectives in biology · 2014
    Review
  19. Article
  20. Article

32 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

R C GuptaDepartment of Genetics, Yale University School of Medicine, New Haven, CT 06510, USA.
L R Bazemore
E I Golub
C M Radding
Yale University · US

Funding

RECOMBINATION IN VITRO--ENZYMOLOGY AND INTERMEDIATESR37GM033504 · NIGMS · YALE UNIVERSITY · PI RADDING, CHARLES M. · 1994 to 2003
$2.1M
DNA REPAIR, RECOMBINATION, AND MUTAGENESISP01CA039238 · NCI · YALE UNIVERSITY · PI SUMMERS, WILLIAM C · 1986 to 1995
–
NCI NIH HHS 5PO1 CA39238-09NIGMS NIH HHS 5R37 GM33504-13
6 · The paper itself

Abstract

Homologous pairing and strand exchange, which are catalyzed by Escherichia coli RecA protein, are central to homologous recombination. Homologs of this protein are found in eukaryotes; however, little has been reported on the recombinase activities of the mammalian homologs, including the human protein, denoted HsRad51. For the studies described here, we purified HsRad51 form E. coli. Although the activities of HsRad51 and RecA were qualitatively similar in the presence of ATP, there were also striking differences. The stoichiometry of binding to DNA and the rate of renaturation of complementary strands were similar for the two proteins, but rates of ATP hydrolysis, homologous pairing, and subsequent strand exchange promoted by HsRad51 were less than 1/10 those of RecA. In addition, HsRad51 bound gamma-thio-ATP and formed stable presynaptic complexes that promoted renaturation as rapidly as RecA, but the recombinant human protein catalyzed neither strand exchange nor homologous pairing of a single strand with duplex DNA in the presence of the ATP analog. By contrast, RecA promoted both of the latter reactions in control experiments. These observations suggest that among RecA-like proteins, HsRad51 may be a variant in which homologous pairing and strand exchange are more closely linked to the hydrolysis of ATP.

Indexed as

Recombination, GeneticAdenosine TriphosphateBase SequenceDeoxyribonuclease IDNA-Binding ProteinsEnergy TransferHumansMolecular Sequence DataNucleic Acid RenaturationOligonucleotidesProtein BindingRad51 RecombinaseSpectrometry, FluorescenceAdenosine TriphosphateDeoxyribonuclease IDNA-Binding ProteinsOligonucleotidesRAD51 protein, humanRad51 Recombinase

Identifiers

PMID9012806
PMCPMC19535
OpenAlexW2081581449

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.