Highly Dynamic Interactions Maintain Kinetic Stability of the ClpXP Protease During the ATP-Fueled Mechanical Cycle
Author:
Affiliation:
1. Department of Chemistry, Brown University, Providence, Rhode Island 02912, United States
Funder
NIH Office of the Director
Charles A. King Trust
National Institute of General Medical Sciences
Bank of America
Publisher
American Chemical Society (ACS)
Subject
Molecular Medicine,General Medicine,Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acschembio.6b00083
Reference38 articles.
1. ClpXP, an ATP-powered unfolding and protein-degradation machine
2. Enzymatic and Structural Similarities between theEscherichia coli ATP-dependent Proteases, ClpXP and ClpAP
3. Versatile Action of Escherichia coli ClpXP as Protease or Molecular Chaperone for Bacteriophage Mu Transposition
4. Energy-dependent degradation: Linkage between ClpX-catalyzed nucleotide hydrolysis and protein-substrate processing
5. Communication between ClpX and ClpP during substrate processing and degradation
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