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()

Ítems similars

• Hydrogen-deuterium exchange supports independent membrane-interfacial fusion peptide and transmembrane domains in subunit 2 of influenza virus hemagglutinin protein, a structured and aqueous-protected connection between the fusion peptide and soluble ectodomain, and the importance of membrane apposition by the trimer-of-hairpins structure
  per: Ranaweera, Ahinsa, et al.
  Publicat: (2019)
• Stabilities of the Soluble Ectodomain and Fusion Peptide Hairpins of the Influenza Virus Hemagglutinin Subunit II Protein Are Positively-Correlated with Membrane Fusion
  per: Ranaweera, Ahinsa, et al.
  Publicat: (2018)
• 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
  per: Ratnayake, Punsisi U., et al.
  Publicat: (2014)
• 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
  per: Banerjee, Koyeli, et al.
  Publicat: (2014)
• Isotopically Labeled Expression in E. coli, Purification, and Refolding of the Full Ectodomain of the Influenza Virus Membrane Fusion Protein
  per: Curtis-Fisk, Jaime, et al.
  Publicat: (2008)