Evidence map›Paper›PMID 21496642›Full record

ArticleCell2011

Structures of human exonuclease 1 DNA complexes suggest a unified mechanism for nuclease family.

Jillian Orans, Elizabeth A McSweeney, Ravi R Iyer, Michael A Hast, Homme W Hellinga, Paul Modrich, Lorena S Beese

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 121 papers.

0numbers the graph read from it
0cells of the map it votes in
121citing papers in PubMed
6.9field-weighted citation impact, top 2% 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

121 citing papers in PubMed, 161 citations in OpenAlex.

  1. Review
  2. DNA polymerase I: structure, activity, and function in bacterial DNA replication and repair.Critical reviews in biochemistry and molecular biology · 2026
    Review
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61 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 1 country.

Jillian OransDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Elizabeth A McSweeney
Ravi R Iyer
Michael A Hast
Homme W Hellinga
Paul Modrich
Lorena S Beese
Duke Medical Center · USDuke University Hospital · USHoward Hughes Medical Institute · US

Funding

Transcription-Coupled & Replication-Associated Excision RepairP01CA092584 · NCI · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI John A. Tainer · 2001 to 2026
$89.6M
Enzymology Of Eukaryotic Mismatch RepairR01GM045190 · NIGMS · DUKE UNIVERSITY · PI MODRICH, PAUL LAWRENCE · 1991 to 2018
$6.8M
Structural biology of human DNA mismatch repair machineryR01GM091487 · NIGMS · DUKE UNIVERSITY · PI BEESE, LORENA S. · 2009 to 2010
$647k
Howard Hughes Medical InstituteNCI NIH HHS P01 CA092584NIGMS NIH HHS R01 GM045190NIGMS NIH HHS R01 GM091487NIGMS NIH HHS R01 GM45190
6 · The paper itself

Abstract

Human exonuclease 1 (hExo1) plays important roles in DNA repair and recombination processes that maintain genomic integrity. It is a member of the 5' structure-specific nuclease family of exonucleases and endonucleases that includes FEN-1, XPG, and GEN1. We present structures of hExo1 in complex with a DNA substrate, followed by mutagenesis studies, and propose a common mechanism by which this nuclease family recognizes and processes diverse DNA structures. hExo1 induces a sharp bend in the DNA at nicks or gaps. Frayed 5' ends of nicked duplexes resemble flap junctions, unifying the mechanisms of endo- and exonucleolytic processing. Conformational control of a mobile region in the catalytic site suggests a mechanism for allosteric regulation by binding to protein partners. The relative arrangement of substrate binding sites in these enzymes provides an elegant solution to a complex geometrical puzzle of substrate recognition and processing.

Indexed as

Amino Acid SequenceDNADNA Repair EnzymesEndonucleasesExodeoxyribonucleasesFlap EndonucleasesHumansModels, MolecularMolecular Sequence DataSequence AlignmentDNADNA Repair EnzymesEndonucleasesEXO1 protein, humanExodeoxyribonucleasesFEN1 protein, humanFlap Endonucleases

Identifiers

PMID21496642
PMCPMC3093132
OpenAlexW2142587778

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.