Evidence map›Paper›PMID 11481425›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Interactions of Exo1p with components of MutLalpha in Saccharomyces cerevisiae.

P T Tran, J A Simon, R M Liskay

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
7.6field-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

59 citing papers in PubMed, 124 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. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Dynamic human MutSα-MutLα complexes compact mismatched DNA.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. DNA duplex recognition activates Exo1 nuclease activity.The Journal of biological chemistry · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
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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

3 authors at 1 institution in 1 country.

P T TranDepartment of Molecular and Medical Genetics, Oregon Health Sciences University, Portland 97201, USA.
J A Simon
R M Liskay
Oregon Health & Science University · US

Funding

TRAINING PROGRAM IN MOLECULAR HEMATOLOGYT32HL007781 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI BAGBY, GROVER CARLTON · 1993 to 2012
$5.1M
HOMOLOGOUS RECOMBINATION IN MAMMALIAN CELLSR01GM045413 · NIGMS · YALE UNIVERSITY · PI LISKAY, ROBERT MICHAEL · 1991 to 2006
$2.0M
NHLBI NIH HHS 5-T32-HL07781NHLBI NIH HHS T32 HL007781NIGMS NIH HHS GM45413NIGMS NIH HHS R01 GM045413
6 · The paper itself

Abstract

Previously, we reported evidence suggesting that Saccharomyces cerevisiae MutLalpha, composed of Mlh1p and Pms1p, was a functional member of the gyrase b/Hsp90/MutL (GHL) dimeric ATPase superfamily characterized by highly conserved ATPase domains. Similar to other GHL ATPases, these putative ATPase domains of MutLalpha may be important for the recruitment and/or activation of downstream effectors. One downstream effector candidate is Exo1p, a 5'-3' double stranded DNA exonuclease that has previously been implicated in DNA mismatch repair (MMR). Here we report yeast two-hybrid results suggesting that Exo1p can interact physically with MutLalpha through the Mlh1p subunit. We also report epistasis analysis involving MutLalpha ATPase mutations combined with exo1Delta. One interpretation of our genetic results is that MutLalpha ATPase domains function to direct Exo1p and other functionally redundant exonucleases during MMR. Finally, our results show that much of the increase in spontaneous mutation observed in an exo1Delta strain is REV3-dependent, in turn suggesting that Exo1p is also involved in one or more MMR-independent mutation avoidance pathways.

Indexed as

Amino Acid Transport SystemsSaccharomyces cerevisiae ProteinsAdaptor Proteins, Signal TransducingBase Pair MismatchCarrier ProteinsDNA, FungalDNA RepairEpistasis, GeneticExodeoxyribonucleasesFungal ProteinsMacromolecular SubstancesMembrane Transport ProteinsMutationMutL Protein Homolog 1MutL ProteinsPeptide FragmentsAdaptor Proteins, Signal TransducingAmino Acid Transport SystemsCAN1 protein, Candida albicansCarrier ProteinsDNA, Fungalexodeoxyribonuclease IExodeoxyribonucleasesFungal ProteinsMacromolecular SubstancesMembrane Transport ProteinsMLH1 protein, S cerevisiaeMutL Protein Homolog 1MutL ProteinsPeptide FragmentsPMS1 protein, S cerevisiaeSaccharomyces cerevisiae Proteins

Identifiers

PMID11481425
PMCPMC55526
OpenAlexW2140384792

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.