The Sixth International Conference on Hsp90 in 2012 revealed new functions of this key molecular chaperone. Attendees of the meeting at Les Diablerets, Switzerland, addressed new discoveries about Hsp90 and its cochaperones.
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References
Li, J., Soroka, J. & Buchner, J. Biochim. Biophys. Acta 1823, 624–635 (2012).
Schmid, A.B. et al. EMBO J. 31, 1506–1517 (2012).
Lee, C.T., Graf, C., Mayer, F.J., Richter, S.M. & Mayer, M.P. EMBO J. 31, 1518–1528 (2012).
Xu, W. et al. Mol. Cell 47, 434–443 (2012).
Ratzke, C., Nguyen, M.N., Mayer, M.P. & Hugel, T. J. Mol. Biol. 423, 462–471 (2012).
Vaughan, C.K. et al. Mol. Cell 23, 697–707 (2006).
Echeverría, P.C., Bernthaler, A., Dupuis, P., Mayer, B. & Picard, D. PLoS ONE 6, e26044 (2011).
Wu, Z., Moghaddas Gholami, A. & Kuster, B. Mol. Cell. Proteomics 11, M111 016675 (2012).
Moulick, K. et al. Nat. Chem. Biol. 7, 818–826 (2011).
Taipale, M. et al. Cell 150, 987–1001 (2012).
Sawarkar, R., Sievers, C. & Paro, R. Cell 149, 807–818 (2012).
De Raedt, T. et al. Cancer Cell 20, 400–413 (2011).
Morales, M.A. et al. Proc. Natl. Acad. Sci. USA 107, 8381–8386 (2010).
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The authors declare that Memorial Sloan-Kettering Cancer Center owns the intellectual rights to PU-H71. Samus Therapeutics, of which G.C. has partial ownership, has licensed PU-H71.
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Chiosis, G., Dickey, C. & Johnson, J. A global view of Hsp90 functions. Nat Struct Mol Biol 20, 1–4 (2013). https://doi.org/10.1038/nsmb.2481
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DOI: https://doi.org/10.1038/nsmb.2481
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