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

Παρόμοια τεκμήρια

• Solid-state NMR spectroscopy of the HIV gp41 membrane fusion protein supports intermolecular antiparallel β sheet fusion peptide structure in the final six-helix bundle state
  ανά: Sackett, Kelly, κ.ά.
  Έκδοση: (2013)
• Hairpin Folding of HIV gp41 Abrogates Lipid Mixing Function at Physiologic pH and Inhibits Lipid Mixing by Exposed gp41 Constructs
  ανά: Sackett, Kelly, κ.ά.
  Έκδοση: (2009)
• 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
  ανά: Ratnayake, Punsisi U., κ.ά.
  Έκδοση: (2014)
• Evidence That the Transition of HIV-1 Gp41 into a Six-Helix Bundle, Not the Bundle Configuration, Induces Membrane Fusion
  ανά: Melikyan, Grigory B., κ.ά.
  Έκδοση: (2000)
• Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domains
  ανά: Liang, S., κ.ά.
  Έκδοση: (2018)