Evidence map›Paper›PMID 24717170›Full record

ArticleBiochemistry2014

Structure and mechanism of DNA polymerase β.

William A Beard, Samuel H Wilson

Abstract read
In one paragraph

Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed
–field-weighted citation impact
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

99 citing papers in PubMed.

  1. Engineering a Virus-Derived X Family DNA Polymerase FvPolX for de novo DNA Synthesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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39 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

2 authors.

William A BeardLaboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health , 111 T. W. Alexander Drive, P.O. Box 12233, MD F3-01, Research Triangle Park, North Carolina 27709, United States.
Samuel H Wilson

Funding

XRAY CRYSTALLOGRAPHIC STRUCTURE ANALYSIS: PROTEIN SORTINGP41RR001081 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COHEN, BRUCE E · 1985 to 2011
$17.6M
Mechanisms of Nucleic Acid Enzymes - Pol Beta, HIV-1 Reverse Transcriptase and Mammalian Base Repair EnzymesZIAES050158 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI WILSON, SAMUEL H · 2009 to 2022
$17.0M
Mechanistic Analysis of Pol Beta and Cancer-Associated MutantsU19CA105010 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 2004 to 2012
$9.8M
Molecular Mechanisms of Human DNA Polymerase Beta Catalysis, Fidelity and Selective InhibitionU19CA177547 · NCI · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 2013 to 2017
$5.5M
BIOLOGY OF MAMMALIAN BASE EXCISION REPAIRZ01ES050159 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI WILSON, SAMUEL H · 1997 to 2008
$4.5M
Nucleic Acid Enzymes--Pol Beta And Base Repair EnzymesZ01ES050158 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI WILSON, SAMUEL H · 1997 to 2008
$2.8M
Intramural NIH HHSNCI NIH HHS 1U19CA105010.NCI NIH HHS U19 CA177547NCRR NIH HHS P41 RR001081NIEHS NIH HHS Z01-ES050158NIEHS NIH HHS Z01-ES050159
6 · The paper itself

Abstract

DNA polymerase (pol) β is a small eukaryotic DNA polymerase composed of two domains. Each domain contributes an enzymatic activity (DNA synthesis and deoxyribose phosphate lyase) during the repair of simple base lesions. These domains are termed the polymerase and lyase domains, respectively. Pol β has been an excellent model enzyme for studying the nucleotidyl transferase reaction and substrate discrimination at a molecular level. In this review, recent crystallographic studies of pol β in various liganded and conformational states during the insertion of right and wrong nucleotides as well as during the bypass of damaged DNA (apurinic sites and 8-oxoguanine) are described. Structures of these catalytic intermediates provide unexpected insights into mechanisms by which DNA polymerases enhance genome stability. These structures also provide an improved framework that permits computational studies to facilitate the interpretation of detailed kinetic analyses of this model enzyme.

Indexed as

Crystallography, X-RayDeoxyribonucleotidesDNA-(Apurinic or Apyrimidinic Site) LyaseDNA Polymerase betaDNA RepairGuanineKineticsLigandsMagnesiumModels, ChemicalPhosphorus-Oxygen LyasesProtein Conformation8-hydroxyguanineDeoxyribonucleotidesDNA-(Apurinic or Apyrimidinic Site) LyaseDNA Polymerase betaGuanineLigandsMagnesiumPhosphorus-Oxygen Lyases

Identifiers

PMID24717170
PMCPMC4018062

What OpenQuestion holds

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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.