Hairpin Folding of HIV gp41 Abrogates Lipid Mixing Function at Physiologic pH and Inhibits Lipid Mixing by Exposed gp41 Constructs

Eitemau Tebyg

• Comparative analysis of membrane-associated fusion peptide secondary structure and lipid mixing function of HIV gp41 constructs which model the early pre-Hairpin intermediate and final Hairpin conformations
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  Cyhoeddwyd: (2010)
• pH-Dependent Vesicle Fusion Induced by the Ectodomain of the Human Immunodeficiency Virus Membrane Fusion Protein gp41: Two Kinetically Distinct Processes and Fully-Membrane-Associated gp41 with Predominant β Sheet Fusion Peptide Conformation
  gan: Ratnayake, Punsisi U., et al.
  Cyhoeddwyd: (2014)
• HIV-1 gp41 Transmembrane Domain Interacts with the Fusion Peptide: Implication in Lipid Mixing and Inhibition of Virus-Cell Fusion
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  Cyhoeddwyd: (2012)
• Viral envelope protein folding and membrane hemifusion are enhanced by the conserved loop region of HIV-1 gp41
  gan: Ashkenazi, Avraham, et al.
  Cyhoeddwyd: (2011)
• Folded Monomers and Hexamers of the Ectodomain of the HIV gp41 Membrane Fusion Protein: Potential Roles in Fusion and Synergy Between the Fusion Peptide, Hairpin, and Membrane-Proximal External Region
  gan: Banerjee, Koyeli, et al.
  Cyhoeddwyd: (2014)