Fusion Peptides Derived from the HIV Type 1 Glycoprotein 41 Associate within Phospholipid Membranes and Inhibit Cell-Cell Fusion
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference68 articles.
1. Folding and Assembly of Viral Membrane Proteins
2. Protein-Mediated Membrane Fusion
3. Hydrophobie Binding of the Ectodomain of Influenza Hemagglutinin to Membranes Occurs through the “Fusion Peptide”
4. Membrane Fusion
5. Lipid interactions of the hemagglutinin HA2 NH2-terminal segment during influenza virus-induced membrane fusion.
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1. A large HIV gp41 construct with trimer-of-hairpins structure exhibits V2E mutation-dominant attenuation of vesicle fusion and helicity very similar to V2E attenuation of HIV fusion and infection and supports: (1) hairpin stabilization of membrane apposition with larger distance for V2E; and (2) V2E dominance by an antiparallel β sheet with interleaved fusion peptide strands from two gp41 trimers;Biophysical Chemistry;2023-02
2. Structural and Mechanistic Evidence for Calcium Interacting Sites in the HIV Transmembrane Protein gp41 Involved in Membrane Fusion;Biochemistry;2022-08-22
3. Regulation of epitope exposure in the gp41 membrane-proximal external region through interactions at the apex of HIV-1 Env;PLOS Pathogens;2022-05-18
4. Investigation of Human Endogenous Retrovirus-K (ERVK) Expression and Function in Normal Placentation and Preterm Pregnancy;2021-11-22
5. Membranotropic peptides mediating viral entry;Peptide Science;2018-02-13
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