Virus-like particles highly expressing DC-SIGN concentrate trimeric HIV-envelope proteins with noncovalently linked immunoreactive gp120 and gp41

Ngā tūemi rite

• Variable-Loop-Deleted Variants of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Can Be Stabilized by an Intermolecular Disulfide Bond between the gp120 and gp41 Subunits
  mā: Sanders, Rogier W., me ētahi atu.
  I whakaputaina: (2000)
• A Recombinant Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Complex Stabilized by an Intermolecular Disulfide Bond between the gp120 and gp41 Subunits Is an Antigenic Mimic of the Trimeric Virion-Associated Structure
  mā: Binley, James M., me ētahi atu.
  I whakaputaina: (2000)
• Stabilization of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers by Disulfide Bonds Introduced into the gp41 Glycoprotein Ectodomain
  mā: Farzan, Michael, me ētahi atu.
  I whakaputaina: (1998)
• Cooperative subunit interactions within the oligomeric envelope glycoprotein of HIV-1: Functional complementation of specific defects in gp120 and gp41
  mā: Salzwedel, Karl, me ētahi atu.
  I whakaputaina: (2000)
• Functional Analysis of the Disulfide-Bonded Loop/Chain Reversal Region of Human Immunodeficiency Virus Type 1 gp41 Reveals a Critical Role in gp120-gp41 Association
  mā: Maerz, Anne L., me ētahi atu.
  I whakaputaina: (2001)