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Article

Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.

The Journal of biological chemistry - 18 Nov 2005

Bösl Benjamin, Grimminger Valerie, Walter Stefan

Abstract excerpt

The Hsp104 protein from Saccharomyces cerevisiae is a member of the Hsp100/Clp family of molecular chaperones. It mediates the solubilization of aggregated proteins in an ATP-dependent process assisted by the Hsp70/40 system. Although the principal function of Hsp104 is well established, the mechanistic details of this catalyzed disaggregation are poorly understood. In this work, we have investigated the...

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PMID: 16135516
DOI: 10.1074/jbc.M506149200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides.PMID 16135516Read ↗

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