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Hsp90: from structure to phenotype

Nature Structural & Molecular Biology volume 11, pages 1152–1155 (2004)Cite this article

A recent international conference focused on Hsp90, a molecular chaperone that plays a critical role in a diverse array of cellular processes including the assembly and maturation of some important 'client' proteins, many of which are involved in signal transduction.

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Figure 1: Cytosolic Hsp90 and its homologs Grp94, TRAP and HTPG along with numerous cochaperones form the cellular assembly machine.

Notes

  1. *The EMBO workshop and second international conference on the Hsp90 Chaperone Machine was held in Gwatt, Switzerland, 25–29 September, 2004. For other information about the conference, see http://www.hsp90.org.

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Authors and Affiliations

  1. Chemistry Department, Cambridge University, Lensfield Road, Cambridge, CB2 1EW, UK

    Sophie E Jackson

  2. Bauer Center for Genomics Research, Harvard University, Cambridge, 02138, Massachusetts, USA

    Christine Queitsch

  3. Department of Biochemistry and Molecular Biology, Mayo Clinic, College of Medicine, 200 First Street SW, Rochester, 55905, Minnesota, USA

    David Toft

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  1. Sophie E Jackson
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  2. Christine Queitsch
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  3. David Toft
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Jackson, S., Queitsch, C. & Toft, D. Hsp90: from structure to phenotype. Nat Struct Mol Biol 11, 1152–1155 (2004). https://doi.org/10.1038/nsmb1204-1152

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