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.

مواد مشابهة

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