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Article

Heat shock protein 90 as a critical factor in maintaining glucocorticosteroid receptor in a nonfunctional state.

The Journal of biological chemistry - 25 Mar 1991

Cadepond F, Schweizer-Groyer G, Segard-Maurel I, Jibard N, Hollenberg S M, Giguère V, Evans R M, Baulieu E E

Abstract excerpt

Previous work demonstrated that the ligand binding domain (LBD) was required to determine the formation of the cytosolic, untransformed, inactive, 8 S, heterooligomeric form of the human glucocorticosteroid receptor (hGR) which includes the 90-kDa heat shock protein (hsp90) (Pratt, W.B., Jolly, D.J., Pratt, D.V., Hollenberg, S.M., Giguère, V., Cadepond, F.M., Schweizer-Groyer, G., Catelli, M.G., Evans, R.M., and...

Topics

Blotting, Western
Cells, Cultured
Electrophoresis, Polyacrylamide Gel
Heat-Shock Proteins
Humans
Mutation
Plasmids
Precipitin Tests
Receptors, Glucocorticoid
Steroids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Transcription, Genetic

Transfection

Source

Identifiers

PMID: 2005120

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2005120-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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