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Cited by 178

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Molecular Mechanism of Inhibition of the Human Protein Complex Hsp90–Cdc37, a Kinome Chaperone–Cochaperone, by Triterpene Celastrol

Sreeramulu, Sridhar, Gande, Santosh Lakshmi, Göbel, Michael, Schwalbe, Harald·2009·Angewandte Chemie International Edition

Abstract

The correct target: The cell division cycle protein 37 (Cdc37) and the heat shock protein (Hsp90) are molecular chaperones crucial for the folding and stabilization of protein kinases including the oncogenic kinases. NMR studies show that celastrol, a recently identified triterpene targeting Hsp90, in fact binds to Cdc37 and disrupts the Cdc37–Hsp90 complex. Celastrol inactivates Cdc37 through a thiol-mediated mechanism.

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Crossref · 10.1002/anie.200900929

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Metadata

Authors
Sreeramulu, S., Gande, S. L., Göbel, M., & Schwalbe, H.
Venue
Angewandte Chemie International Edition
Publisher
Wiley
Published
2009-07-22
Volume
48
Issue
32
Pages
5853-5855
ISSN
  • 1433-7851 (ISSN-L)
  • 1521-3773
OpenAlex
W2148065722
Cited by
178
References
1
FWCI
5.04
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Molecular Mechanism of Inhibition of the Human Protein Complex Hsp90–Cdc37, a Kinome Chaperone–Cochaperone, by Triterpene Celastrol. https://app.cochat.ai/papers/10.1002/anie.200900929
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Sreeramulu, S., Gande, S. L., Göbel, M., & Schwalbe, H. (2009). Molecular Mechanism of Inhibition of the Human Protein Complex Hsp90–Cdc37, a Kinome Chaperone–Cochaperone, by Triterpene Celastrol. Angewandte Chemie International Edition. https://doi.org/10.1002/anie.200900929

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