Cyanovirin-N, a Potent Human Immunodeficiency Virus-Inactivating Protein, Blocks both CD4-Dependent and CD4-Independent Binding of Soluble gp120 (sgp120) to Target Cells, Inhibits sCD4-Induced Binding of sgp120 to Cell-Associated CXCR4, and Dissociates Bound sgp120 from Target Cells

Παρόμοια τεκμήρια

• Cyanovirin-N Binds to gp120 To Interfere with CD4-Dependent Human Immunodeficiency Virus Type 1 Virion Binding, Fusion, and Infectivity but Does Not Affect the CD4 Binding Site on gp120 or Soluble CD4-Induced Conformational Changes in gp120
  ανά: Esser, Mark T., κ.ά.
  Έκδοση: (1999)
• AFM Force measurements of the gp120-sCD4 and gp120 or CD4 antigen-antibody interactions
  ανά: Chen, Yong, κ.ά.
  Έκδοση: (2011)
• CCR5/CD4/CXCR4 oligomerization prevents HIV-1 gp120(IIIB) binding to the cell surface
  ανά: Martínez-Muñoz, Laura, κ.ά.
  Έκδοση: (2014)
• Virions of primary human immunodeficiency virus type 1 isolates resistant to soluble CD4 (sCD4) neutralization differ in sCD4 binding and glycoprotein gp120 retention from sCD4-sensitive isolates.
  ανά: Moore, J P, κ.ά.
  Έκδοση: (1992)
• Dissociation of the CD4 and CXCR4 Binding Properties of Human Immunodeficiency Virus Type 1 gp120 by Deletion of the First Putative Alpha-Helical Conserved Structure
  ανά: Missé, Dorothée, κ.ά.
  Έκδοση: (1998)