Studies of the protein encoded by the lon mutation, capR9, in Escherichia coli. A labile form of the ATP-dependent protease La that inhibits the wild type protease.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
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1. A 5+1 assemble-to-activate mechanism of the Lon proteolytic machine;Nature Communications;2023-11-13
2. Structure of the catalytic domain of the human mitochondrial Lon protease: Proposed relation of oligomer formation and activity;Protein Science;2010-03-10
3. Oligomeric Structure of the ATP-dependent Protease La (Lon) of Escherichia coli;Molecules and Cells;2006-02
4. Functional Domains of Brevibacillus thermoruber Lon Protease for Oligomerization and DNA Binding;Journal of Biological Chemistry;2004-08
5. [25] ATP-dependent protease La (Lon) from Escherichia coli;Methods in Enzymology;1994
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