Structural plasticity of the feline leukaemia virus fusion peptide: a circular dichroism study
- 3 April 1998
- journal article
- Published by Wiley in FEBS Letters
- Vol. 425 (3) , 415-418
- https://doi.org/10.1016/s0014-5793(98)00274-9
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- Effect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayersBiophysical Journal, 1996
- Membrane FusionScience, 1992
- Are fusion peptides really “sided” insertional helices?Cell, 1992
- A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusionNature, 1992
- Orientation into the lipid bilayer of an asymmetric amphipathic helical peptide located at the N-terminus of viral fusion proteinsBiochimica et Biophysica Acta (BBA) - Biomembranes, 1990
- Viral and Cellular Membrane Fusion ProteinsAnnual Review of Physiology, 1990
- Membrane fusion of enveloped viruses: Especially a matter of proteinsJournal of Bioenergetics and Biomembranes, 1990
- Identification of the Fusion Peptide of Primate Immunodeficiency VirusesScience, 1989
- Hydrophobie Binding of the Ectodomain of Influenza Hemagglutinin to Membranes Occurs through the “Fusion Peptide”Journal of Biological Chemistry, 1989
- Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus.The Journal of cell biology, 1986