Both ATPase Domains of ClpA Are Critical for Processing of Stable Protein Structures
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference56 articles.
1. Protease Ti, a new ATP-dependent protease in Escherichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits.
2. The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component.
3. A multiple-component, ATP-dependent protease from Escherichia coli.
4. Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes
5. Asymmetric deceleration of ClpB or Hsp104 ATPase activity unleashes protein-remodeling activity
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