Versatile Action of Escherichia coli ClpXP as Protease or Molecular Chaperone for Bacteriophage Mu Transposition
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference46 articles.
1. Protease Ti, a new ATP-dependent protease in Escherichia coli, contains protein-activated ATPase and proteolytic functions in distinct subunits.
2. ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities.
3. Isolation and characterization of ClpX, a new ATP-dependent specificity component of the Clp protease of Escherichia coli.
4. A molecular chaperone, ClpA, functions like DnaK and DnaJ.
5. The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone.
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1. Resisting the Heat: Bacterial Disaggregases Rescue Cells From Devastating Protein Aggregation;Frontiers in Molecular Biosciences;2021-05-04
2. A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery;eLife;2020-01-09
3. A processive rotary mechanism couples substrate unfolding and proteolysis in the ClpXP degradation machinery;2019-09-24
4. Highly Dynamic Interactions Maintain Kinetic Stability of the ClpXP Protease During the ATP-Fueled Mechanical Cycle;ACS Chemical Biology;2016-03-30
5. Deciphering the Roles of Multicomponent Recognition Signals by the AAA + Unfoldase ClpX;Journal of Molecular Biology;2015-09
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