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Cited by 188

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

Sti1 Is a Non-competitive Inhibitor of the Hsp90 ATPase

Open access
Richter, Klaus, Muschler, Paul, Hainzl, Otmar, Reinstein, Jochen, Buchner, Johannes·2003·Journal of Biological Chemistry

Abstract

The molecular chaperone Hsp90 is known to be involved in the activation of key regulatory proteins such as kinases, steroid hormone receptors, and transcription factors in an ATP-dependent manner. During the chaperone cycle, Hsp90 has been found associated with the partner protein Hop/Sti1, which seems to be required for the progression of the cycle. However, little is known about its specific function. Here we have investigated the interaction of Sti1 from Saccharomyces cerevisiae with Hsp90 and its influence on the ATPase activity. We show that the inhibitory mechanism of Sti1 on the ATPase activity of Hsp90 is non-competitive. Sti1 binds to the N- and C-terminal part of Hsp90 and prevents the N-terminal dimerization reaction that is required for efficient ATP hydrolysis. The first 24 amino acids of Hsp90, a region shown previously to be important for the association of the N-terminal domains and stimulation of ATP hydrolysis, seems to be important for this interaction.

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Metadata

Authors
Richter, K., Muschler, P., Hainzl, O., Reinstein, J., & Buchner, J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2003-03
Volume
278
Issue
12
Pages
10328-10333
ISSN
0021-9258 (ISSN-L)
OpenAlex
W1982177408
Cited by
188
References
2
FWCI
3.32
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Sti1 Is a Non-competitive Inhibitor of the Hsp90 ATPase. https://app.cochat.ai/papers/10.1074/jbc.m213094200
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Richter, K., Muschler, P., Hainzl, O., Reinstein, J., & Buchner, J. (2003). Sti1 Is a Non-competitive Inhibitor of the Hsp90 ATPase. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m213094200

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