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Hsp90: chaperoning signal transduction.
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Hsp90: a specialized but essential protein-folding tool.
J Cell Biol. 2001 Jul 23;154(2):267-73. doi: 10.1083/jcb.200104079.
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Folding of newly translated proteins in vivo: the role of molecular chaperones.
Annu Rev Biochem. 2001;70:603-47. doi: 10.1146/annurev.biochem.70.1.603.
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Mechanisms underlying ubiquitination.
Annu Rev Biochem. 2001;70:503-33. doi: 10.1146/annurev.biochem.70.1.503.
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Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin.
Mol Cell Biol. 2000 Dec;20(24):9262-70. doi: 10.1128/MCB.20.24.9262-9270.2000.
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Rpn9 is required for efficient assembly of the yeast 26S proteasome.
Mol Cell Biol. 1999 Oct;19(10):6575-84. doi: 10.1128/MCB.19.10.6575.
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Growth-dependent change of the 26S proteasome in budding yeast.
Biochem Biophys Res Commun. 1998 Oct 29;251(3):818-23. doi: 10.1006/bbrc.1998.9560.
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ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo.
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