Bose, Suchira and Weikl, Tina and Bügl, Hans and Buchner, Johannes (1996) Chaperone function of Hsp90-associated proteins. SCIENCE, 274 (5293). pp. 1715-1717. ISSN 0036-8075, 1095-9203
Full text not available from this repository.Abstract
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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | HEAT-SHOCK PROTEINS; ENDOPLASMIC-RETICULUM; MOLECULAR CHAPERONES; HSP90; RECEPTOR |
| Subjects: | 500 Science > 540 Chemistry & allied sciences 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 25 May 2023 10:50 |
| Last Modified: | 25 May 2023 10:50 |
| URI: | https://pred.uni-regensburg.de/id/eprint/51284 |
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