Vibrio cholerae cytolysin: assembly and membrane insertion of the oligomeric pore are tightly linked and are not detectably restricted by membrane fluidity
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Biochemistry,Biophysics
Reference41 articles.
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1. Single-particle cryo-EM reveals conformational variability of the oligomeric VCC β-barrel pore in a lipid bilayer;Journal of Cell Biology;2021-10-07
2. Taking Toll on Membranes: Curious Cases of Bacterial β-Barrel Pore-Forming Toxins;Biochemistry;2019-10-14
3. Revisiting the role of cholesterol in regulating the pore-formation mechanism of Vibrio cholerae cytolysin, a membrane-damaging β-barrel pore-forming toxin;Biochemical Journal;2018-10-10
4. Vibrio choleraecytolysin: Multiple facets of the membrane interaction mechanism of aβ-barrel pore-forming toxin;IUBMB Life;2018-02-22
5. The Relationship between Glycan Binding and Direct Membrane Interactions in Vibrio cholerae Cytolysin, a Channel-forming Toxin;Journal of Biological Chemistry;2015-11
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