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Article

Interactions of Exo1p with components of MutLalpha in Saccharomyces cerevisiae.

Proceedings of the National Academy of Sciences of the United States of America - 14 Aug 2001

Tran P T, Simon J A, Liskay R M

Abstract excerpt

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...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 11481425
DOI: 10.1073/pnas.161175998
PMCID: PMC55526

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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