Structure and in vivo function of Hsp90
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference50 articles.
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2. Identification and structural characterisation of the ATP/ADP binding site in the Hsp90 molecular chaperone;Prodromou;Cell,1997
3. The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation;Grenert;J Biol Chem,1997
4. ATP binding and hydrolysis are essential to the function of the Hsp90 molecular chaperone in vivo;Panaretou;EMBO J,1998
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