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Article

A cyclophilin function in Hsp90-dependent signal transduction.

Science (New York, N.Y.) - 6 Dec 1996

Duina A A, Chang H C, Marsh J A, Lindquist S, Gaber R F

Abstract excerpt

Cpr6 and Cpr7, the Saccharomyces cerevisiae homologs of cyclophilin-40 (CyP-40), were shown to form complexes with Hsp90, a protein chaperone that functions in several signal transduction pathways. Deletion of CPR7 caused severe growth defects when combined with mutations that decrease the amount...

Topics

Amino Acid Isomerases
Carrier Proteins
Peptidyl-Prolyl Isomerase F
Cyclophilins
Fungal Proteins
HSP90 Heat-Shock Proteins
Heat-Shock Proteins
Molecular Chaperones
Mutation
Oncogene Protein pp60(v-src)
Peptidylprolyl Isomerase
Proto-Oncogene Proteins pp60(c-src)

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Receptors, Glucocorticoid

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Signal Transduction

Source

Identifiers

PMID: 8939862
DOI: 10.1126/science.274.5293.1713

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8939862-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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A cyclophilin function in Hsp90-dependent signal transduction.PMID 8939862Read ↗

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