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

Antzeko izenburuak

• 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
  nork: Sackett, Kelly, et al.
  Argitaratua: (2013)
• Stabilities of the Soluble Ectodomain and Fusion Peptide Hairpins of the Influenza Virus Hemagglutinin Subunit II Protein Are Positively-Correlated with Membrane Fusion
  nork: Ranaweera, Ahinsa, et al.
  Argitaratua: (2018)
• Full-Length Trimeric Influenza Virus Hemagglutinin II Membrane Fusion Protein and Shorter Constructs Lacking the Fusion Peptide or Transmembrane Domain: Hyperthermostability of the Full-Length Protein and the Soluble Ectodomain and Fusion Peptide Make Significant Contributions to Fusion of Membrane Vesicles()
  nork: Ratnayake, Punsisi U., et al.
  Argitaratua: (2015)
• 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
  nork: Banerjee, Koyeli, et al.
  Argitaratua: (2014)
• 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
  nork: Sackett, Kelly, et al.
  Argitaratua: (2010)