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

Podobné jednotky

• 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
  Autor: Sackett, Kelly, a další
  Vydáno: (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
  Autor: Ratnayake, Punsisi U., a další
  Vydáno: (2014)
• HIV-1 gp41 Transmembrane Domain Interacts with the Fusion Peptide: Implication in Lipid Mixing and Inhibition of Virus-Cell Fusion
  Autor: Reuven, Eliran Moshe, a další
  Vydáno: (2012)
• HIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion
  Autor: Sackett, Kelly, a další
  Vydáno: (2011)
• Viral envelope protein folding and membrane hemifusion are enhanced by the conserved loop region of HIV-1 gp41
  Autor: Ashkenazi, Avraham, a další
  Vydáno: (2011)