Intramolecular Chaperone Activity of the Pro-region of Vibrio cholerae El Tor Cytolysin
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. Enterotoxicity of El Tor-like hemolysin of non-O1 Vibrio cholerae
2. Two-step processing for activation of the cytolysin/hemolysin of Vibrio cholerae O1 biotype El Tor: nucleotide sequence of the structural gene (hlyA) and characterization of the processed products
3. Pro-sequence of subtilisin can guide the refolding of denatured subtilisin in an intermolecular process
4. The αlytic protease pro-region does not require a physical linkage to activate the protease domain in vivo
5. Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity.
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1. Tyrosine in the hinge region of the pore‐forming motif regulates oligomeric β‐barrel pore formation by Vibrio cholerae cytolysin;Molecular Microbiology;2020-11-11
2. Spatiotemporal Regulation of Vibrio Exotoxins by HlyU and Other Transcriptional Regulators;Toxins;2020-08-22
3. Hemolysin of Vibrio Species;Microorganisms;2020-07-01
4. Vibrio choleraecytolysin: Multiple facets of the membrane interaction mechanism of aβ-barrel pore-forming toxin;IUBMB Life;2018-02-22
5. Vibrio cholerae hemolysin: The β-trefoil domain is required for folding to the native conformation;Biochemistry and Biophysics Reports;2016-12
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