Evidence map›Paper›PMID 30237169›Full record

ArticleThe Journal of biological chemistry2018

The properties of Msh2-Msh6 ATP binding mutants suggest a signal amplification mechanism in DNA mismatch repair.

William J Graham, Christopher D Putnam, Richard D Kolodner

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

21 citing papers in PubMed, 28 citations in OpenAlex.

  1. Review
  2. 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
  3. Article
  4. Article
  5. Article
  6. Article
  7. 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
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Coordinated roles of SLX4 and MutSβ in DNA repair and the maintenance of genome stability.Critical reviews in biochemistry and molecular biology · 2021
    Review
  15. Article
  16. Role of mismatch repair in aging.International journal of biological sciences · 2021
    Review
  17. DNA Mismatch Repair and its Role in Huntington's Disease.Journal of Huntington's disease · 2021
    Review
  18. Review
  19. MutS sliding clamps on an uncertain track to DNA mismatch repair.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. Recurrent mismatch binding by MutS mobile clamps on DNA localizes repair complexes nearby.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
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 2 institutions in 2 countries.

William J GrahamFrom the Ludwig Institute for Cancer Research San Diego.
Christopher D PutnamFrom the Ludwig Institute for Cancer Research San Diego,; Departments of Medicine and.
Richard D KolodnerFrom the Ludwig Institute for Cancer Research San Diego,; Cellular and Molecular Medicine,; Moores-UCSD Cancer Center, and; Institute of Genomic Medicine, University of California School of Medicine, San Diego, La Jolla, California 92093-0669. Electronic address: rkolodner@ucsd.edu.
Ludwig Cancer Research · BEUniversity of California San Diego · US

Funding

ENZYMOLOGY OF MISMATCH REPAIR IN YEASTR01GM050006 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI Richard D Kolodner · 1994 to 2026
$10.5M
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 CA210407NIGMS NIH HHS R01 GM050006
6 · The paper itself

Abstract

DNA mismatch repair (MMR) corrects mispaired DNA bases and small insertion/deletion loops generated by DNA replication errors. After binding a mispair, the eukaryotic mispair recognition complex Msh2-Msh6 binds ATP in both of its nucleotide-binding sites, which induces a conformational change resulting in the formation of an Msh2-Msh6 sliding clamp that releases from the mispair and slides freely along the DNA. However, the roles that Msh2-Msh6 sliding clamps play in MMR remain poorly understood. Here, using

Indexed as

DNA Mismatch RepairAdenosine TriphosphateCrystallography, X-RayDNA-Binding ProteinsMutL Protein Homolog 1MutS Homolog 2 ProteinProtein BindingSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAdenosine TriphosphateDNA-Binding ProteinsMLH1 protein, S cerevisiaeMSH2 protein, S cerevisiaeMSH6 protein, S cerevisiaeMutL Protein Homolog 1MutS Homolog 2 ProteinSaccharomyces cerevisiae ProteinsDNA binding proteinDNA endonucleaseDNA mismatch repairDNA repairDNA replicationexonuclease 1Mlh1-Pms1Msh2-Msh6mutagenesisMutSS. cerevisiae

Identifiers

PMID30237169
PMCPMC6254361
OpenAlexW2892024408

What OpenQuestion holds

Textmetadata
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.