The Binding of a Glycoprotein 120 V3 Loop Peptide to HIV-1 Neutralizing Antibodies
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference68 articles.
1. Principal neutralizing domain of the human immunodeficiency virus type 1 envelope protein
2. Type-specific neutralization of the human immunodeficiency virus with antibodies to env-encoded synthetic peptides.
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4. CD4-induced interaction of primary HIV-1 gp120 glycoproteins with the chemokine receptor CCR-5
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1. Interaction of the HIV-1 gp120 Viral Protein V3 Loop with Bacterial Lipopolysaccharide;Journal of Biological Chemistry;2011-07
2. Computational Anti-AIDS Drug Design Based on the Analysis of the Specific Interactions Between Immunophilins and the HIV-1 gp120 V3 Loop. Application to the FK506-Binding Protein;Journal of Biomolecular Structure and Dynamics;2008-08
3. Structural Analysis of the HIV-1 gp120 V3 Loop: Application to the HIV-Haiti Isolates;Journal of Biomolecular Structure and Dynamics;2007-06
4. Design of immunogens that present the crown of the HIV-1 V3 loop in a conformation competent to generate 447-52D-like antibodies;Biochemical Journal;2006-10-13
5. Crystal Structures of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralizing Antibody 2219 in Complex with Three Different V3 Peptides Reveal a New Binding Mode for HIV-1 Cross-Reactivity;Journal of Virology;2006-06-15
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