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Article

Intrinsic inhibition of the Hsp90 ATPase activity.

The Journal of biological chemistry - 21 Apr 2006

Richter Klaus, Moser Sandra, Hagn Franz, Friedrich Rainer, Hainzl Otmar, Heller Markus, Schlee Sandra, Kessler Horst, Reinstein Jochen, Buchner Johannes

Abstract excerpt

The molecular chaperone Hsp90 is required for the folding and activation of a large number of substrate proteins. These are involved in essential cellular processes ranging from signal transduction to viral replication. For the activation of its substrates, Hsp90 binds and hydrolyzes ATP, which is the key driving force for conformational conversions within the dimeric chaperone. Dimerization of Hsp90 is mediated...

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Identifiers

PMID: 16461354
DOI: 10.1074/jbc.M510142200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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