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Cited by 371

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Chaperone Function of Hsp90-Associated Proteins

Bose, Suchira, Weikl, Tina, Bügl, Hans, Buchner, Johannes·1996·Science

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.

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Crossref · 10.1126/science.274.5293.1715

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Metadata

Authors
Bose, S., Weikl, T., Bügl, H., & Buchner, J.
Venue
Science
Published
1996-12-06
Volume
274
Issue
5293
Pages
1715-1717
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2079336387
Cited by
371
References
2
FWCI
8.91
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Chaperone Function of Hsp90-Associated Proteins. https://app.cochat.ai/papers/10.1126/science.274.5293.1715
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Bose, S., Weikl, T., Bügl, H., & Buchner, J. (1996). Chaperone Function of Hsp90-Associated Proteins. Science. https://doi.org/10.1126/science.274.5293.1715

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.