Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers Containing the Fusion Peptide and Transmembrane Domains
Author:
Affiliation:
1. Department of Chemistry, Michigan State University, East Lansing, Michigan 48824, United States
Funder
National Institute of Allergy and Infectious Diseases
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00753
Reference84 articles.
1. HIV Entry and Envelope Glycoprotein-mediated Fusion
2. A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity.
3. The Tale of the Long Tail: the Cytoplasmic Domain of HIV-1 gp41
4. Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer
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5. 2H nuclear magnetic resonance spectroscopy supports larger amplitude fast motion and interference with lipid chain ordering for membrane that contains β sheet human immunodeficiency virus gp41 fusion peptide or helical hairpin influenza virus hemagglutinin fusion peptide at fusogenic pH;Biochimica et Biophysica Acta (BBA) - Biomembranes;2020-10
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