Pardaxin, a hydrophobic toxin of the Red Sea flatfish, disassembles the intact membrane of vesicular stomatitis virus.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference15 articles.
1. Viral Membranes: Model Systems for Studying Biological Membrane
2. Association of vesicular stomatitis virus glycoprotein with virion membrane: characterization of the lipophilic tail fragment
3. Localization of Membrane-Associated Proteins in Vesicular Stomatitis Virus by Use of Hydrophobic Membrane Probes and Cross-Linking Reagents
4. Spatial relationships of the proteins of vesicular stomatitis virus: induction of reversible oligomers by cleavable protein cross-linkers and oxidation
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1. The mechanisms by which pardaxin, a natural cationic antimicrobial peptide, targets the endoplasmic reticulum and induces c-FOS;Biomaterials;2014-04
2. Proteomic and functional analysis of zebrafish after administration of antimicrobial peptide epinecidin-1;Fish & Shellfish Immunology;2013-02
3. Pardaxin, an Antimicrobial Peptide, Triggers Caspase-Dependent and ROS-Mediated Apoptosis in HT-1080 Cells;Marine Drugs;2011-10-19
4. Gene Expression and Localization of the Epinecidin-1 Antimicrobial Peptide in the Grouper (Epinephelus coioides), and Its Role in Protecting Fish Against Pathogenic Infection;DNA and Cell Biology;2007-06
5. Antimicrobial Peptides;Nutraceutical Proteins and Peptides in Health and Disease;2005-09-29
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