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Article

Processing of proteins by the molecular chaperone Hsp104.

Journal of molecular biology - 20 Jul 2007

Schaupp Andreas, Marcinowski Moritz, Grimminger Valerie, Bösl Benjamin, Walter Stefan

Abstract excerpt

The molecular chaperone Hsp104 is an AAA+ ATPase (ATPase associated with a variety of cellular activities) from yeast that catalyzes protein disaggregation. Using mutagenesis, we impaired nucleotide binding or hydrolysis in the two nucleotide-binding domains (NBD) of Hsp104 and analyzed the consequences for chaperone function by monitoring ATP hydrolysis, polypeptide binding, polypeptide processing, and...

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Identifiers

PMID: 17543332
DOI: 10.1016/j.jmb.2007.04.070

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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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