Evidence map›Paper›PMID 28439008›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Interaction of proliferating cell nuclear antigen with PMS2 is required for MutLα activation and function in mismatch repair.

Jochen Genschel, Lyudmila Y Kadyrova, Ravi R Iyer, Basanta K Dahal, Farid A Kadyrov, Paul Modrich

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.9field-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

49 citing papers in PubMed, 61 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Mechanism of MutLβ-dependent DNA expansions.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  5. Article
  6. Review
  7. Review
  8. 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
  9. Review
  10. Article
  11. Article
  12. Therapeutic targeting of mismatch repair-deficient cancers.Nature reviews. Clinical oncology · 2025
    Review
  13. Article
  14. Article
  15. The mismatch repair factor Mlh1-Pms1 uses ATP to compact and remodel DNA.bioRxiv : the preprint server for biology · 2025
    Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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

6 authors at 3 institutions in 1 country.

Jochen GenschelDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710.
Lyudmila Y KadyrovaDepartment of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901.
Ravi R IyerDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710.
Basanta K DahalDepartment of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901.
Farid A KadyrovDepartment of Biochemistry and Molecular Biology, Southern Illinois University School of Medicine, Carbondale, IL 62901.
Paul ModrichDepartment of Biochemistry, Duke University Medical Center, Durham, NC 27710; modrich@biochem.duke.edu.
Southern Illinois University School of Medicine · USDuke Medical Center · USHoward Hughes Medical Institute · US

Funding

Enzymology Of Eukaryotic Mismatch RepairR01GM045190 · NIGMS · DUKE UNIVERSITY · PI MODRICH, PAUL LAWRENCE · 1991 to 2018
$6.8M
DNA mismatch repair in the nucleosomal environmentR01GM095758 · NIGMS · SOUTHERN ILLINOIS UNIVERSITY CARBONDALE · PI KADYROV, FARID · 2013 to 2017
$1.2M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM045190NIGMS NIH HHS R01 GM095758
6 · The paper itself

Abstract

Eukaryotic MutLα (mammalian MLH1-PMS2 heterodimer; MLH1-PMS1 in yeast) functions in early steps of mismatch repair as a latent endonuclease that requires a mismatch, MutSα/β, and DNA-loaded proliferating cell nuclear antigen (PCNA) for activation. We show here that human PCNA and MutLα interact specifically but weakly in solution to form a complex of approximately 1:1 stoichiometry that depends on PCNA interaction with the C-terminal endonuclease domain of the MutLα PMS2 subunit. Amino acid substitution mutations within a PMS2 C-terminal

Indexed as

DNA Mismatch RepairMismatch Repair Endonuclease PMS2MutL ProteinsProliferating Cell Nuclear AntigenSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAmino Acid MotifsHumansMismatch Repair Endonuclease PMS2MutLalpha protein, humanMutL ProteinsPMS2 protein, humanProliferating Cell Nuclear AntigenSaccharomyces cerevisiae ProteinsDNA repairendonucleasemismatch repairMutLalphaproliferating cell nuclear antigen

Identifiers

PMID28439008
PMCPMC5441711
OpenAlexW2607625935

What OpenQuestion holds

Textmetadata
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.