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Article

Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70.

Molecular endocrinology (Baltimore, Md.) - 1 Jun 1996

Chen S, Prapapanich V, Rimerman R A, Honoré B, Smith D F

Abstract excerpt

Previous studies on the assembly of progesterone receptor (PR) complexes in vitro have suggested that PR assembly is a dynamic, ordered process involving at least eight nonreceptor proteins. One of these proteins, p60, appears transiently during assembly and is not a component of functionally mature PR complexes. In the present study we observe that a monoclonal antibody specific for p60 can, on the one hand,...

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PMID: 8776728
DOI: 10.1210/mend.10.6.8776728

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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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Interactions of p60, a mediator of progesterone receptor assembly, with heat shock proteins hsp90 and hsp70.PMID 8776728Read ↗

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The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes.Semantic proximity Read ↗

GCUNC-45 Is a Novel Regulator for the Progesterone Receptor/hsp90 Chaperoning PathwaySemantic proximity Read ↗

Interaction of heat shock protein 90 and the co-chaperone Cpr6 with Ura2, a bifunctional enzyme required for pyrimidine biosynthesis.Semantic proximity Read ↗

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