Evidence map›Paper›PMID 24829455›Full record

ArticleNucleic acids research2014

Hydrolytic function of Exo1 in mammalian mismatch repair.

Hongbing Shao, Celia Baitinger, Erik J Soderblom, Vickers Burdett, Paul Modrich

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

17 citing papers in PubMed, 27 citations in OpenAlex.

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  10. Single-molecule imaging reveals the mechanism of Exo1 regulation by single-stranded DNA binding proteins.Proceedings of the National Academy of Sciences of the United States of America · 2016
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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

5 authors at 2 institutions in 1 country.

Hongbing ShaoDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Celia BaitingerDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA.
Erik J SoderblomProteomics Core Facility, Duke University Medical Center, Durham, NC 27710, USA.
Vickers BurdettDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Paul ModrichDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA Howard Hughes Medical Institute, Duke University Medical Center, Durham, NC 27710, USA modrich@biochem.duke.edu.
Duke University Hospital · USHoward Hughes Medical Institute · US

Funding

Women's Cancer Research ProgramP30CA014236 · NCI · DUKE UNIVERSITY · PI DONNA NIEDZWIECKI · 1985 to 2026
$174.8M
Enzymology Of Eukaryotic Mismatch RepairR01GM045190 · NIGMS · DUKE UNIVERSITY · PI MODRICH, PAUL LAWRENCE · 1991 to 2018
$6.8M
Howard Hughes Medical InstituteNCI NIH HHS P30 CA014236NIGMS NIH HHS GM45190NIGMS NIH HHS R01 GM045190
6 · The paper itself

Abstract

Genetic and biochemical studies have previously implicated exonuclease 1 (Exo1) in yeast and mammalian mismatch repair, with results suggesting that function of the protein in the reaction depends on both its hydrolytic activity and its ability to interact with other components of the repair system. However, recent analysis of an Exo1-E109K knockin mouse has concluded that Exo1 function in mammalian mismatch repair is restricted to a structural role, a conclusion based on a prior report that N-terminal His-tagged Exo1-E109K is hydrolytically defective. Because Glu-109 is distant from the nuclease hydrolytic center, we have compared the activity of untagged full-length Exo1-E109K with that of wild type Exo1 and the hydrolytically defective active site mutant Exo1-D173A. We show that the activity of Exo1-E109K is comparable to that of wild type enzyme in a conventional exonuclease assay and that in contrast to a D173A active site mutant, Exo1-E109K is fully functional in mismatch-provoked excision and repair. We conclude that the catalytic function of Exo1 is required for its participation in mismatch repair. We also consider the other phenotypes of the Exo1-E109K mouse in the context of Exo1 hydrolytic function.

Indexed as

DNA Mismatch RepairAnimalsExodeoxyribonucleasesHydrolysisMiceMutationexodeoxyribonuclease IExodeoxyribonucleases

Identifiers

PMID24829455
PMCPMC4066806
OpenAlexW1985420529

What OpenQuestion holds

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LicenceCC BY
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.