Communication of ClpXP protease hypersensitivity to bacteriophage mu repressor isoforms 1 1Edited by M. Gottesman
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference39 articles.
1. Escherichia coli integration host factor stabilizes bacteriophage Mu repressor interactions with operator DNA in vitro;Alazard;Mol. Microbiol.,1992
2. Mutual stabilisation of bacteriophage Mu repressor and histone-like proteins in a nucleoprotein structure;Betermier;J. Mol. Biol.,1995
3. Site-specific recognition of the bacteriophage Mu ends by the Mu A protein;Craigie;Cell,1984
4. Stabilization of bacteriophage Mu repressor-operator complexes by the Escherichia coli integration host factor protein;Gama;Mol. Microbiol.,1992
5. Frameshift mutations in the bacteriophage Mu repressor gene can confer a trans-dominant virulent phenotype to the phage;Geuskens;J. Bacteriol.,1991
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2. FliT Selectively Enhances Proteolysis of FlhC Subunit in FlhD4C2 Complex by an ATP-dependent Protease, ClpXP;Journal of Biological Chemistry;2014-11
3. Potential Mechanisms for Linking Phage Mu Transposition with Cell Physiology;The Bacterial Chromosome;2014-04-30
4. Activation of a Dormant ClpX Recognition Motif of Bacteriophage Mu Repressor by Inducing High Local Flexibility;Journal of Biological Chemistry;2008-04
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