Evidence map›Paper›PMID 30061603›Full record

ArticleNature structural & molecular biology2018

Identification of Exo1-Msh2 interaction motifs in DNA mismatch repair and new Msh2-binding partners.

Eva M Goellner, Christopher D Putnam, William J Graham, Christine M Rahal, Bin-Zhong Li, Richard D Kolodner

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

36 citing papers in PubMed, 44 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. DNA mismatch repair mediated by Mlh1-Pms1 endonuclease-catalyzed mispair excision.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Therapeutic targeting of mismatch repair-deficient cancers.Nature reviews. Clinical oncology · 2025
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. The unstructured linker of Mlh1 contains a motif required for endonuclease function which is mutated in cancers.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. A RareGenes · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Eva M GoellnerLudwig Institute for Cancer Research San Diego, University of California School of Medicine, San Diego, La Jolla, CA, USA.
Christopher D PutnamLudwig Institute for Cancer Research San Diego, University of California School of Medicine, San Diego, La Jolla, CA, USA.
William J GrahamLudwig Institute for Cancer Research San Diego, University of California School of Medicine, San Diego, La Jolla, CA, USA.
Christine M RahalLudwig Institute for Cancer Research San Diego, University of California School of Medicine, San Diego, La Jolla, CA, USA.
Bin-Zhong LiLudwig Institute for Cancer Research San Diego, University of California School of Medicine, San Diego, La Jolla, CA, USA.
Richard D KolodnerLudwig Institute for Cancer Research San Diego, University of California School of Medicine, San Diego, La Jolla, CA, USA. rkolodner@ucsd.edu.ORCID http://orcid.org/0000-0002-4806-8384
Ludwig Cancer Research · USUniversity of California San Diego · USUniversity of Kentucky · US

Funding

ENZYMOLOGY OF MISMATCH REPAIR IN YEASTR01GM050006 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Richard D Kolodner · 1994 to 2026
$10.5M
Mechanisms of mismatch repair mediated cell death after alkylating agent exposureK99ES026653 · NIEHS · LUDWIG INSTITUTE FOR CANCER RES LTD · PI GOELLNER, EVA MARIE · 2016 to 2017
$133k
The role of S. cerevisiae Mlh1-Pms1 during MMR strand discriminationF32CA210407 · NCI · LUDWIG INSTITUTE FOR CANCER RES LTD · PI GRAHAM, WILLIAM J. · 2016 to 2018
$122k
NCI NIH HHS F32 CA210407NIEHS NIH HHS K99 ES026653NIGMS NIH HHS R01 GM050006
6 · The paper itself

Abstract

Eukaryotic DNA mismatch repair (MMR) involves both exonuclease 1 (Exo1)-dependent and Exo1-independent pathways. We found that the unstructured C-terminal domain of Saccharomyces cerevisiae Exo1 contains two MutS homolog 2 (Msh2)-interacting peptide (SHIP) boxes downstream from the MutL homolog 1 (Mlh1)-interacting peptide (MIP) box. These three sites were redundant in Exo1-dependent MMR in vivo and could be replaced by a fusion protein between an N-terminal fragment of Exo1 and Msh6. The SHIP-Msh2 interactions were eliminated by the msh2

Indexed as

DNA Mismatch RepairProtein Interaction Domains and MotifsAmino Acid SequenceConserved SequenceDNA Repair EnzymesExodeoxyribonucleasesHumansMutS Homolog 2 ProteinSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidDNA Repair EnzymesEXO1 protein, humanExodeoxyribonucleasesMSH2 protein, humanMutS Homolog 2 ProteinSaccharomyces cerevisiae Proteins

Identifiers

PMID30061603
PMCPMC6837739
OpenAlexW2883274990

What OpenQuestion holds

Textmetadata
LicenceTDM
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.