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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.

References

  1. Wegele, H., Muller, L. & Buchner, J. Rev. Physiol. Biochem. Pharmacol. 151, 1–44 (2004).

    Article  CAS  Google Scholar 

  2. Picard, D. Cell. Mol. Life Sci. 59, 1640–1648 (2002).

    Article  CAS  Google Scholar 

  3. Workman, P. Cancer Lett. 206, 149–157 (2004).

    Article  CAS  Google Scholar 

  4. Pearl, L.H. & Prodromou, C. Adv. Prot. Chem. 59, 157–186 (2002).

    CAS  Google Scholar 

  5. Harris, S.F., Shiau, A.K. & Agard, D.A. Struct. Fold. Des. 12, 1087–1097 (2004).

    Article  CAS  Google Scholar 

  6. Meyer, P. et al. EMBO J. 23, 511–519 (2004).

    Article  CAS  Google Scholar 

  7. Wegele, H., Haslbeck, M., Reinstein, J. & Buchner, J. J. Biol. Chem. 278, 25970–25976 (2003).

    Article  CAS  Google Scholar 

  8. McLaughlin, S.M., Ventouras, L.-A., Lobbezoo, B.G. & Jackson, S.E. J. Mol. Biol. 344, 813–826 (2004).

    Article  CAS  Google Scholar 

  9. Immormino, R.M. et al. J. Biol. Chem. 279, 46162–46171 (2004).

    Article  CAS  Google Scholar 

  10. Kamal, A. et al. Nature 425, 407–410 (2003).

    Article  CAS  Google Scholar 

  11. Caplan, A.J. Cell Stress Chaperones 8, 105–107 (2003).

    Article  Google Scholar 

  12. Freeman, B.C. & Yamamoto, K.R. Science 296, 2232–2235 (2002).

    Article  CAS  Google Scholar 

  13. Tanioka, T., Nakatani, Y., Wemmyo, N., Murakami, M. & Kudo, I. J. Biol. Chem. 275, 32775–32782 (2000).

    Article  CAS  Google Scholar 

  14. Smith, D.F. Cell Stress Chaperones 9, 109–121 (2004).

    Article  CAS  Google Scholar 

  15. Takahashi, A., Casais, C., Ichimura, K. & Shirasu, K. Proc. Natl. Acad. Sci. USA 100, 11777–11782 (2003).

    Article  CAS  Google Scholar 

  16. Hubert, D.A. et al. EMBO J. 22, 5679–5689 (2003).

    Article  CAS  Google Scholar 

  17. Shen, Q.H. et al. Plant Cell 15, 732–744 (2003).

    Article  CAS  Google Scholar 

  18. Stahl, E.A., Dwyer, G., Mauricio, R., Kreitman, M. & Bergelson, J. Nature 400, 667–671 (1999).

    Article  CAS  Google Scholar 

  19. Bergelson, J., Kreitman, M., Stahl, E.A. & Tian, D. Science 292, 2281–2285 (2001).

    Article  CAS  Google Scholar 

  20. Queitsch, C., Sangster, T.A. & Lindquist, S. Nature 417, 618–624 (2002).

    Article  CAS  Google Scholar 

  21. Rutherford, S.L. & Lindquist, S. Nature 396, 336–342 (1998).

    Article  CAS  Google Scholar 

  22. Schulze-Lefert, P. Curr. Biol. 14, R22–R24 (2004).

    Article  CAS  Google Scholar 

  23. Wiesgigl, M. & Clos, J. Mol. Biol. Cell 12, 3307–3316 (2001).

    Article  CAS  Google Scholar 

  24. Hossain, M.M. & Nakamoto, H. Curr. Microbiol. 46, 70–76 (2003).

    Article  CAS  Google Scholar 

  25. Hossain, M.M. & Nakamoto, H. Curr. Microbiol. 44, 291–296 (2002).

    Article  CAS  Google Scholar 

  26. Tanaka, N. & Nakamoto, H. FEBS Lett. 458, 117–123 (1999).

    Article  CAS  Google Scholar 

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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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