3.10 Chaperones and Protein Folding
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Elsevier
Reference178 articles.
1. Hsp70 chaperones: Cellular functions and molecular mechanism;Mayer;Cell Mol. Life Sci.,2005
2. Pharmacological targeting of the Hsp70 chaperone;Patury;Curr. Top. Med. Chem.,2009
3. The Escherichia coli DnaK chaperone, the 70 kDa heat shock protein eukaryotic equivalent, changes conformation upon ATP hydrolysis, thus triggering its dissociation from a bound target protein;Liberek;J. Biol. Chem.,1991
4. ATP-induced protein Hsp70 complex dissociation requires K+ but not ATP hydrolysis;Palleros;Nature,1993
5. Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding;Ha;Biochemistry,1995
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