Evidence map›Paper›PMID 11743006›Full record

ArticleThe EMBO journal2001

Mutations in human DNA polymerase eta motif II alter bypass of DNA lesions.

E Glick, K L Vigna, L A Loeb

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

14 citing papers in PubMed, 55 citations in OpenAlex.

  1. Article
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  4. Structural basis of human DNA polymerase η-mediated chemoresistance to cisplatin.Proceedings of the National Academy of Sciences of the United States of America · 2012
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  11. Protein tolerance to random amino acid change.Proceedings of the National Academy of Sciences of the United States of America · 2004
    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.

E GlickThe Joseph Gottstein Memorial Cancer Research Laboratory, Department of Pathology, Box 357705, University of Washington, Seattle, WA 98195-357705, USA.
K L Vigna
L A Loeb
University of Washington · US

Funding

SPECIFICITY OF OXYGEN DNA DAMAGE AND MUTAGENESISP01AG001751 · NIA · UNIVERSITY OF WASHINGTON · PI RABINOVITCH, PETER S · 1985 to 2021
$29.6M
CREATING MUTANT ENZYMES FOR GENE THERAPY OF CANCERR01CA078885 · NCI · UNIVERSITY OF WASHINGTON · PI LOEB, LAWRENCE A · 1998 to 2007
$3.7M
NCI NIH HHS CA78885NCI NIH HHS R01 CA078885NIA NIH HHS AG01751NIA NIH HHS P01 AG001751
6 · The paper itself

Abstract

Human DNA polymerase eta (hPol eta) is one of the newly identified Y-family of DNA polymerases. These polymerases synthesize past template lesions that are postulated to block replication fork progression. hPol eta accurately bypasses UV-associated cis-syn cyclobutane thymine dimers in vitro and contributes to normal resistance to sunlight-induced skin cancer. We describe here mutational analysis of motif II, a highly conserved sequence, recently reported to reside in the fingers domain and to form part of the active site in Y-family DNA polymerases. We used a yeast-based complementation system to isolate biologically active mutants created by random sequence mutagenesis, synthesized the mutant proteins in vitro and assessed their ability to bypass thymine dimers. The mutability of motif II in 210 active mutants has parallels with natural evolution and identifies Tyr52 and Ala54 as prime candidates for involvement in catalytic activity or bypass. We describe the ability of hPol eta S62G, a mutant polymerase with enhanced activity, to bypass five other site-specific lesions. Our results may serve as a prototype for studying other members of the Y-family DNA polymerases.

Indexed as

DNA DamageMutationAmino Acid SequenceBase SequenceCloning, MolecularDimerizationDNA-Directed DNA PolymeraseDNA PrimersMolecular Sequence DataMutagenesis, Site-DirectedSequence Homology, Amino AcidThymineUltraviolet RaysY-Family DNA PolymerasesDNA-Directed DNA PolymeraseDNA PrimersRad30 proteinThymineY-Family DNA Polymerases

Identifiers

PMID11743006
PMCPMC125802
OpenAlexW2064430462

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.