Human cyclophilin 40 is a heat shock protein that exhibits altered intracellular localization following heat shock

The unactivated steroid receptors are chaperoned into a conformation that is optimal for binding hormone by a number of heat shock proteins, including Hsp90, Hsp70, Hsp40, and the immunophilin, FKBP52 (Hsp56). Together with its partner cochaperones, cyclophilin 40 (CyP40) and FKBP51, FKBP52 belongs...

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Veröffentlicht in:	Cell stress & chaperones 2001-01, Vol.6 (1), p.59-70
Hauptverfasser:	J. Mark, Peter, K. Ward, Bryan, Kumar, Premlata, Lahooti, Hooshang, F. Minchin, Rodney, Ratajczak, Thomas
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibodies Arsenites - toxicity Breast Neoplasms Carrier Proteins - analysis Carrier Proteins - genetics Carrier Proteins - metabolism Cell lines Cell nucleolus Cell Nucleolus - chemistry Cell Nucleolus - metabolism Cellular immunity Cultured cells Cyclophilins Dactinomycin - pharmacology Female Gene Expression - drug effects Gene Expression - physiology Heat shock proteins Heat shock response Heat-Shock Proteins - analysis Heat-Shock Proteins - genetics Heat-Shock Proteins - metabolism Heat-Shock Response - physiology Hot Temperature Humans Immunohistochemistry Messenger RNA Nucleic Acid Synthesis Inhibitors - pharmacology Original Original s Peptidyl-Prolyl Isomerase F Peptidylprolyl Isomerase - analysis Peptidylprolyl Isomerase - genetics Peptidylprolyl Isomerase - metabolism RNA, Messenger - analysis Shock heating Sodium Compounds - toxicity Steroid receptors Tacrolimus Binding Proteins - analysis Tacrolimus Binding Proteins - genetics Tacrolimus Binding Proteins - metabolism Tumor Cells, Cultured
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