TolC of Escherichia coli Functions as an Outer Membrane Channel
- 30 April 1993
- journal article
- Published by Elsevier BV in Zentralblatt für Bakteriologie
- Vol. 278 (2-3), 187-196
- https://doi.org/10.1016/s0934-8840(11)80836-4
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Functional complementation between bacterial MDR-like export systems: colicin V, alpha-hemolysin, and Erwinia proteaseJournal of Bacteriology, 1991
- Characterization, localization and transmembrane organization of the three proteins PrtD, PrtE and PrtF necessary for protease secretion by the Gram‐negative bacterium Erwinia chrysanthemiMolecular Microbiology, 1991
- The secretion genes of Pseudomonas aeruginosa alkaline protease are functionally related to those of Erwinia chrysanthemi proteases and Escherichia coliα‐haemolysinMolecular Microbiology, 1991
- Characterization of the nucleoside‐binding site inside the Tsx channel ofEscherichia coliouter membrane Reconstitution experiments with lipid bilayer membranesEuropean Journal of Biochemistry, 1988
- Structure and Function of Porins from Gram-Negative BacteriaAnnual Review of Microbiology, 1988
- Mechanism of sugar transport through the sugar-specific LamB channel ofEscherichia coli outer membraneThe Journal of Membrane Biology, 1987
- Role of porins in outer membrane permeabilityJournal of Bacteriology, 1987
- Mechanism of ion transport through the anion-selective channel of the Pseudomonas aeruginosa outer membrane.The Journal of general physiology, 1987
- Pore formation by LamB of Escherichia coli in lipid bilayer membranesJournal of Bacteriology, 1986
- Formation of large, ion-permeable membrane channels by the matrix protein (porin) of Escherichia coliBiochimica et Biophysica Acta (BBA) - Biomembranes, 1978