Rational Site-Directed Mutations of the LLP-1 and LLP-2 Lentivirus Lytic Peptide Domains in the Intracytoplasmic Tail of Human Immunodeficiency Virus Type 1 gp41 Indicate Common Functions in Cell-Cell Fusion but Distinct Roles in Virion Envelope Incorporation

Míreanna Comhchosúla

• Antibody Neutralization Escape Mediated by Point Mutations in the Intracytoplasmic Tail of Human Immunodeficiency Virus Type 1 gp41
  le: Kalia, Vandana, et al.
  Foilsithe: (2005)
• Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein
  le: Garry Robert F, et al.
  Foilsithe: (2007-11-01)
• Viroporin potential of the lentivirus lytic peptide (LLP) domains of the HIV-1 gp41 protein
  le: Costin, Joshua M, et al.
  Foilsithe: (2007)
• Differential Functional Phenotypes of Two Primary HIV-1 Strains Resulting from Homologous Point Mutations in the LLP Domains of the Envelope gp41 Intracytoplasmic Domain
  le: Newman, Jason T, et al.
  Foilsithe: (2007)
• Unique Functional Properties of Conserved Arginine Residues in the Lentivirus Lytic Peptide Domains of the C-terminal Tail of HIV-1 gp41
  le: Kuhlmann, Anne-Sophie, et al.
  Foilsithe: (2014)