A Putative α-Helical Structure Which Overlaps the Capsid-p2 Boundary in the Human Immunodeficiency Virus Type 1 Gag Precursor Is Crucial for Viral Particle Assembly

Eitemau Tebyg

• Efficient Particle Production by Minimal Gag Constructs Which Retain the Carboxy-Terminal Domain of Human Immunodeficiency Virus Type 1 Capsid-p2 and a Late Assembly Domain
  gan: Accola, Molly A., et al.
  Cyhoeddwyd: (2000)
• Isolation of Human Immunodeficiency Virus Type 1 Cores: Retention of Vpr in the Absence of p6(gag)
  gan: Accola, Molly A., et al.
  Cyhoeddwyd: (2000)
• The C-Terminal Half of the Human Immunodeficiency Virus Type 1 Gag Precursor Is Sufficient for Efficient Particle Assembly
  gan: Borsetti, Alessandra, et al.
  Cyhoeddwyd: (1998)
• A Conserved Dileucine-Containing Motif in p6(gag) Governs the Particle Association of Vpx and Vpr of Simian Immunodeficiency Viruses SIV(mac) and SIV(agm)
  gan: Accola, Molly A., et al.
  Cyhoeddwyd: (1999)
• Characterization of a Putative α-Helix across the Capsid-SP1 Boundary That Is Critical for the Multimerization of Human Immunodeficiency Virus Type 1 Gag
  gan: Liang, Chen, et al.
  Cyhoeddwyd: (2002)