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The large conformational changes of Hsp90 are only weakly coupled to ATP hydrolysis
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Structural basis of J cochaperone binding and regulation of Hsp70
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The glucocorticoid responses are shaped by molecular chaperones
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Structural analysis of E-coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements
Andrew K. Shiau et al.
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Structural basis of interdomain communication in the Hsc70 chaperone
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JOURNAL OF MOLECULAR BIOLOGY (2005)
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CELLULAR AND MOLECULAR LIFE SCIENCES (2005)
Multiple domains of the co-chaperone Hop are important for Hsp70 binding
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The assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex
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JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition
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Ligand discrimination by TPR domains -: Relevance and selectivity of EEVD-recognition in Hsp70•Hop•Hsp90 complexes
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JOURNAL OF BIOLOGICAL CHEMISTRY (2002)
Size-distribution analysis of proteins by analytical ultracentrifugation: Strategies and application to model systems
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Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1
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HYDROMIC: prediction of hydrodynamic properties of rigid macromolecular structures obtained from electron microscopy images
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EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS (2001)
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Evidence for iterative ratcheting of receptor-bound hsp70 between its ATP and ADP conformations during assembly of glucocorticoid receptor•hsp90 heterocomplexes
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