Myristoylation, a Protruding Loop, and Structural Plasticity Are Essential Features of a Nonenveloped Virus Fusion Peptide Motif
Open Access
- 1 December 2004
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 279 (49) , 51386-51394
- https://doi.org/10.1074/jbc.m406990200
Abstract
No abstract availableKeywords
This publication has 59 references indexed in Scilit:
- Hypothesis: spring-loaded boomerang mechanism of influenza hemagglutinin-mediated membrane fusionBiochimica et Biophysica Acta (BBA) - Biomembranes, 2003
- Fusion peptides and the mechanism of viral fusionBiochimica et Biophysica Acta (BBA) - Biomembranes, 2003
- Membrane FusionChemical Reviews, 2002
- Influenza fusion peptidesBiochemical Society Transactions, 2001
- Membrane Interactions of Mutated Forms of the Influenza Fusion PeptideBiochemistry, 2001
- Solid-State Nuclear Magnetic Resonance Evidence for an Extended β Strand Conformation of the Membrane-Bound HIV-1 Fusion PeptideBiochemistry, 2001
- Differential Roles of Two Conserved Glycine Residues in the Fusion Peptide of Semliki Forest VirusVirology, 2001
- Structure and Topology of the Influenza Virus Fusion Peptide in Lipid BilayersJournal of Biological Chemistry, 1995
- Orientation and structure of the NH2-terminal HIV-1 gp41 peptide in fused and aggregated liposomesBiochimica et Biophysica Acta (BBA) - Biomembranes, 1993
- Viral and Cellular Membrane Fusion ProteinsAnnual Review of Physiology, 1990