Unfolding of Vibrio cholerae Hemolysin Induces Oligomerization of the Toxin Monomer
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference27 articles.
1. Non-O1 Vibrio cholerae hemolysin: purification, partial characterization, and immunological relatedness to El Tor hemolysin
2. Molecular cloning of the hemolysin determinant from Vibrio cholerae El Tor
3. Oligomerization of Vibrio cholerae Cytolysin Yields a Pentameric Pore and Has a Dual Specificity for Cholesterol and Sphingolipids in the Target Membrane
4. Interaction of the Vibrio cholerae cytolysin (VCC) with cholesterol, some cholesterol esters, and cholesterol derivatives: a TEM study
5. β-Barrel Pore-Forming Toxins: Intriguing Dimorphic Proteins
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1. Elucidating liquid crystal-aqueous interface for the study of cholesterol-mediated action of a β-barrel pore forming toxin;Soft Matter;2022
2. Riverbed Sediments as Reservoirs of MultipleVibrio choleraeVirulence-Associated Genes: A Potential Trigger for Cholera Outbreaks in Developing Countries;Journal of Environmental and Public Health;2017
3. Vibrio cholerae hemolysin: The β-trefoil domain is required for folding to the native conformation;Biochemistry and Biophysics Reports;2016-12
4. Physicochemical constraints of elevated pH affect efficient membrane interaction and arrest an abortive membrane-bound oligomeric intermediate of the beta-barrel pore-forming toxin Vibrio cholerae cytolysin;Archives of Biochemistry and Biophysics;2015-10
5. Signaling beyond Punching Holes: Modulation of Cellular Responses by Vibrio cholerae Cytolysin;Toxins;2015-08-21
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