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Article

Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.

Proceedings of the National Academy of Sciences of the United States of America - 14 Sept 2010

Ratzke C, Mickler M, Hellenkamp B, Buchner J, Hugel T

Abstract excerpt

The molecular chaperone heat shock protein 90 (Hsp90) is an important and abundant protein in eukaryotic cells, essential for the activation of a large set of signal transduction and regulatory proteins. During the functional cycle, the Hsp90 dimer performs large conformational rearrangements. Th...

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PMID: 20736353
DOI: 10.1073/pnas.1000916107
PMCID: PMC2941327

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20736353-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

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