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    Chaperone function of Hsp90-associated proteins (1996)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1996-12-06
    Description: The Hsp90 heat shock protein of eukaryotic cells regulates the activity of proteins involved in signal transduction pathways and may direct intracellular protein folding in general. Hsp90 performs at least part of its function in a complex with a specific set of partner proteins that include members of the prolyl isomerase family. The properties of the major components of the Hsp90 complex were examined through the use of in vitro protein folding assays. Two of the components, FKBP52 and p23, functioned as mechanistically distinct molecular chaperones. These results suggest the existence of a super-chaperone complex in the cytosol of eukaryotic cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bose, S -- Weikl, T -- Bugl, H -- Buchner, J -- New York, N.Y. -- Science. 1996 Dec 6;274(5293):1715-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Biophysik und Physikalische Biochemie, Universitat Regensburg, 93040 Regensburg, Germany. johannes.buchner@biologie.uni-regensburg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8939863" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Isomerases/antagonists & inhibitors/metabolism ; Carrier Proteins/antagonists & inhibitors/metabolism/pharmacology/*physiology ; Citrate (si)-Synthase/*chemistry ; DNA-Binding Proteins/metabolism/pharmacology/*physiology ; Drosophila Proteins ; Enzyme Inhibitors/pharmacology ; HSP90 Heat-Shock Proteins/metabolism/*physiology ; Heat-Shock Proteins/metabolism/pharmacology/*physiology ; Intramolecular Oxidoreductases ; Janus Kinases ; Molecular Chaperones/metabolism/pharmacology/*physiology ; Peptidylprolyl Isomerase ; Phosphoproteins/metabolism/pharmacology/*physiology ; Polyenes/pharmacology ; Protein Denaturation ; *Protein Folding ; Protein-Tyrosine Kinases/metabolism/pharmacology ; Recombinant Proteins/metabolism ; Sirolimus ; Tacrolimus Binding Proteins ; Temperature ; Transcription Factors
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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