Visualization and functional analysis of the oligomeric states of Escherichia coli heat shock protein 70 (Hsp70/DnaK)
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Biochemistry
Link
http://link.springer.com/content/pdf/10.1007/s12192-011-0307-1.pdf
Reference64 articles.
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2. Benaroudj N, Batelier G, Triniolles F, Ladjimi MM (1995) Self-association of the molecular chaperone HSC70. Biochemistry 34:15282–15290
3. Benaroudj N, Triniolles F, Ladjimi MM (1996) Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70. J Biol Chem 271:18471–18476
4. Benaroudj N, Fouchaq B, Ladjimi MM (1997) The COOH-terminal peptide binding domain is essential for self-association of the molecular chaperone HSC70. J Biol Chem 272:8744–8751
5. Bertelsen EB, Chang L, Gestwicki JE, Zuiderweg ER (2009) Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate. Proc Natl Acad Sci U S A 106:8471–8476
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