Propensity for a leucine zipper-like domain of human immunodeficiency virus type 1 gp41 to form oligomers correlates with a role in virus-induced fusion rather than assembly of the glycoprotein complex.

Lignende værker

• Biophysical characterization of recombinant proteins expressing the leucine zipper-like domain of the human immunodeficiency virus type 1 transmembrane protein gp41.
  af: Shugars, D C, et al.
  Udgivet: (1996)
• Peptides corresponding to a predictive alpha-helical domain of human immunodeficiency virus type 1 gp41 are potent inhibitors of virus infection.
  af: Wild, C T, et al.
  Udgivet: (1994)
• A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition.
  af: Wild, C, et al.
  Udgivet: (1992)
• Human immunodeficiency virus type 1 envelope glycoprotein oligomerization requires the gp41 amphipathic alpha-helical/leucine zipper-like sequence.
  af: Poumbourios, P, et al.
  Udgivet: (1997)
• Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivity.
  af: Dubay, J W, et al.
  Udgivet: (1992)