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Article

Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth.

Eukaryotic cell - 1 Aug 2012

Pursell Natalie W, Mishra Parul, Bolon Daniel N A

Abstract excerpt

The Hsp90 chaperone is required for the maturation of signal transduction clients, including many kinases and nuclear steroid hormone receptors. The binding and hydrolysis of ATP by Hsp90 drive conformational rearrangements in three structure domains. Two intrinsically disordered regions of Hsp90 located between these domains and at the C terminus have traditionally been considered to impart flexibility. We...

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Share to Cell Enlargement
Share to HSP90 Heat-Shock Proteins
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Protein Processing, Post-Translational

Share to Receptors, Glucocorticoid

Share to Saccharomyces cerevisiae Proteins

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Share to src-Family Kinases

Source

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Identifiers

PMID: 22660624
DOI: 10.1128/EC.00099-12
PMCID: PMC3416057

Provenance

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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