Evidence map›Paper›PMID 22828282›Full record

ArticleFEBS letters2012

The C-terminal domain of human Rev1 contains independent binding sites for DNA polymerase η and Rev7 subunit of polymerase ζ.

Yulia Pustovalova, Irina Bezsonova, Dmitry M Korzhnev

Open access · greenAbstract read
In one paragraph

Article in FEBS letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

32 citing papers in PubMed, 52 citations in OpenAlex.

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  3. eLife · 2024
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  17. Review
  18. Rev7 dimerization is important for assembly and function of the Rev1/Polζ translesion synthesis complex.Proceedings of the National Academy of Sciences of the United States of America · 2018
    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

3 authors at 1 institution in 1 country.

Yulia PustovalovaDepartment of Molecular, Microbial and Structural Biology, University of Connecticut Health Center, Farmington, CT 06030, USA.
Irina Bezsonova
Dmitry M Korzhnev
UConn Health · US

Funding

New faculty recruitment in NMR structural biologyP30GM092369 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI WELLER, SANDRA K · 2009 to 2010
$765k
NIGMS NIH HHS P30 GM092369NIGMS NIH HHS P30GM092369
6 · The paper itself

Abstract

Human Rev1 is a translesion synthesis (TLS) DNA polymerase involved in bypass replication across sites of DNA damage and postreplicational gap-filling. Rev1 plays an essential structural role in TLS by providing a binding platform for other TLS polymerases that insert nucleotides across DNA lesions (polη, polι, polκ) and extend the distorted primer-terminus (polς). We use NMR spectroscopy to demonstrate that the Rev1 C-terminal domain utilizes independent interaction interfaces to simultaneously bind a fragment of the 'inserter' polη and Rev7 subunit of the 'extender' polς, thereby serving as a cassette that may accommodate several polymerases making them instantaneously available for TLS.

Indexed as

Binding SitesDNA-Binding ProteinsDNA DamageDNA-Directed DNA PolymeraseDNA ReplicationHumansIn Vitro TechniquesMad2 ProteinsModels, MolecularNuclear Magnetic Resonance, BiomolecularNuclear ProteinsNucleotidyltransferasesProtein Interaction Domains and MotifsProteinsProtein SubunitsRecombinant ProteinsDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA polymerase zetaMAD2L2 protein, humanMad2 ProteinsNuclear ProteinsNucleotidyltransferasesProteinsProtein SubunitsRad30 proteinRecombinant ProteinsREV1 protein, humanREV3L protein, humanY-Family DNA Polymerases

Identifiers

PMID22828282
PMCPMC3572780
OpenAlexW2064614219

What OpenQuestion holds

Textmetadata
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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.