Secretion and properties of the large and small lobes of the channel-forming toxin aerolysin
Author:
Publisher
Wiley
Subject
Molecular Biology,Microbiology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1046/j.1365-2958.1998.01068.x/fullpdf
Reference39 articles.
1. The primary structure of Clostridium septicum alpha-toxin exhibits similarity with that of Aeromonas hydrophila aerolysin;Ballard;Infect Immun,1995
2. The disulfide bond in the Aeromonas hydrophila lipase/acyltransferase stabilizes the structure, but is not required for secretion or activity;Brumlik;J Bacteriol,1997
3. Purification of cloned proaerolysin released by a low protease mutant of Aeromonas salmonicida;Buckley;Biochem Cell Biol,1990
4. Protonation of His-132 promotes oligomerization of the channel-forming toxin aerolysin;Buckley;Biochemistry,1995
5. The erythrocyte receptor for the channel-forming toxin aerolysin is a novel glycosylphosphatidylinositol anchored protein;Cowell;Mol Microbiol,1997
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1. The Pore-Forming α-Toxin from Clostridium septicum Activates the MAPK Pathway in a Ras-c-Raf-Dependent and Independent Manner;Toxins;2015-02-10
2. Aerolysin and Related Aeromonas Toxins;The Comprehensive Sourcebook of Bacterial Protein Toxins;2015
3. Site-Specific Chemoenzymatic Labeling of Aerolysin Enables the Identification of New Aerolysin Receptors;PLoS ONE;2014-10-02
4. Clostridium septicum alpha-toxin forms pores and induces rapid cell necrosis;Toxicon;2010-01
5. Glycosylphosphatidylinositols are potential targets for the development of novel inhibitors for aerolysin-type of pore-forming bacterial toxins;Medicinal Research Reviews;2009-06-25
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