The Measles Virus Hemagglutinin β-Propeller Head β4-β5 Hydrophobic Groove Governs Functional Interactions with Nectin-4 and CD46 but Not Those with the Signaling Lymphocytic Activation Molecule

Lignende værker

• Hydrophobic and Charged Residues in the Central Segment of the Measles Virus Hemagglutinin Stalk Mediate Transmission of the Fusion-Triggering Signal
  af: Apte-Sengupta, Swapna, et al.
  Udgivet: (2013)
• Different Roles of the Three Loops Forming the Adhesive Interface of Nectin-4 in Measles Virus Binding and Cell Entry, Nectin-4 Homodimerization, and Heterodimerization with Nectin-1
  af: Mateo, Mathieu, et al.
  Udgivet: (2014)
• The Measles Virus Hemagglutinin Stalk: Structures and Functions of the Central Fusion Activation and Membrane-Proximal Segments
  af: Navaratnarajah, Chanakha K., et al.
  Udgivet: (2014)
• Adherens junction protein nectin-4 (PVRL4) is the epithelial receptor for measles virus
  af: Mühlebach, Michael D., et al.
  Udgivet: (2011)
• A Structurally Unresolved Head Segment of Defined Length Favors Proper Measles Virus Hemagglutinin Tetramerization and Efficient Membrane Fusion Triggering
  af: Navaratnarajah, Chanakha K., et al.
  Udgivet: (2015)