Electrostatic interactions between middle domain motif-1 and the AAA1 module of the bacterial ClpB chaperone are essential for protein disaggregation
Author:
Funder
MEXT | Japan Society for the Promotion of Science (JSPS)
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference38 articles.
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4. Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins;Glover;Cell,1998
5. Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones;Motohashi;Proc. Natl. Acad. Sci. U.S.A,1999
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