The C-terminal half of the colicin A pore-forming domain is active in vivo and in vitro
- 13 April 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 307 (5), 1293-1303
- https://doi.org/10.1006/jmbi.2001.4524
Abstract
No abstract availableKeywords
This publication has 26 references indexed in Scilit:
- Crystal structure of a colicin N fragment suggests a model for toxicityStructure, 1998
- A mechanism for toxin insertion into membranes is suggested by the crystal structure of the channel-forming domain of colicin E1Structure, 1997
- Crystal structure of colicin IaNature, 1997
- Refined structure of the pore-forming domain of colicin A at 2.4 Å resolutionJournal of Molecular Biology, 1992
- Structure of the membrane-pore-forming fragment of colicin ANature, 1989
- Functional domains of colicin AMolecular Microbiology, 1988
- Determination of the molecularity of the colicin E1 channel by stopped-flow ion flux kinetics.Proceedings of the National Academy of Sciences, 1986
- A very short peptide makes a voltage‐dependent ion channel: The critical length of the channel domain of colicin E1Proteins-Structure Function and Bioinformatics, 1986
- Colicins and other Bacteriocins with Established Modes of ActionAnnual Review of Microbiology, 1982
- Colicin K acts by forming voltage-dependent channels in phospholipid bilayer membranesNature, 1978