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Article

The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride.

The Journal of biological chemistry - 8 Mar 2013

Zeymer Cathleen, Werbeck Nicolas D, Schlichting Ilme, Reinstein Jochen

Abstract excerpt

The Hsp100 chaperones ClpB and Hsp104 utilize the energy from ATP hydrolysis to reactivate aggregated proteins in concert with the DnaK/Hsp70 chaperone system, thereby playing an important role in protein quality control. They belong to the family of AAA+ proteins (ATPases associated with various cellular activities), possess two nucleotide binding domains per monomer (NBD1 and NBD2), and oligomerize into...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 23341453
DOI: 10.1074/jbc.M112.432583
PMCID: PMC3591616

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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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The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride.PMID 23341453Read ↗

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