Examination of the nucleotide‐linked assembly mechanism of E . coli ClpA
Author:
Affiliation:
1. Chemistry Department University of Alabama at Birmingham Birmingham Alabama 35205
Funder
National Science Foundation
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/pro.3638
Reference32 articles.
1. A molecular chaperone, ClpA, functions like DnaK and DnaJ.
2. Protein quality control: triage by chaperones and proteases.
3. Self-compartmentalized bacterial proteases and pathogenesis
4. Design Principles of a Universal Protein Degradation Machine
5. Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines
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2. Examination of the Role of Mg2+ in the Mechanism of Nucleotide Binding to the Monomeric YME1L AAA+ Domain;Biochemistry;2020-11-06
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