Myristate-protein interactions in poliovirus: interactions of VP4 threonine 28 contribute to the structural conformation of assembly intermediates and the stability of assembled virions.

Lignende værker

• Interaction of Poliovirus with Its Purified Receptor and Conformational Alteration in the Virion
  af: Arita, Minetaro, et al.
  Udgivet: (1998)
• Myristoylation is important at multiple stages in poliovirus assembly.
  af: Moscufo, N, et al.
  Udgivet: (1991)
• Lack of myristoylation of poliovirus capsid polypeptide VP0 prevents the formation of virions or results in the assembly of noninfectious virus particles.
  af: Marc, D, et al.
  Udgivet: (1990)
• Role and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 A resolution.
  af: Basavappa, R., et al.
  Udgivet: (1994)
• Identification of T-helper epitopes in the VP1 capsid protein of poliovirus.
  af: Kutubuddin, M, et al.
  Udgivet: (1992)