Critical role of Arg59 in the high-affinity gp120-binding region of CD4 for human immunodeficiency virus type 1 infection
Author:
Publisher
Elsevier BV
Subject
Virology
Reference27 articles.
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2. Human immunodeficiency virus type 1 envelope glycoprotein molecules containing membrane fusion-impairing mutations in the V3 region efficiently undergo soluble CD4-stimulated gp120 release;Berger;J. Virol.,1992
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4. Identification of a major co-receptor for primary isolates of HIV-1;Deng;Nature,1996
5. Engineering a CD4 mimetic inhibiting the binding of the human immunodeficiency virus-1 (HIV-1) envelope glycoprotein gp120 to human lymphocyte CD4 by the transfer of a CD4 functional site to a small neutral scaffold;Drakopoulou;Lett. Pept. Sci.,1998
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2. The Griffithsin Dimer Is Required for High-Potency Inhibition of HIV-1: Evidence for Manipulation of the Structure of gp120 as Part of the Griffithsin Dimer Mechanism;Antimicrobial Agents and Chemotherapy;2013-06-10
3. RISUG®: A potential candidate for the entry inhibitor group of antiretroviral drugs;Medical Hypotheses;2009-08
4. Small-Molecule CD4 Mimics Interact with a Highly Conserved Pocket on HIV-1 gp120;Structure;2008-11
5. Genetic subspecies diversity of the chimpanzee CD4 virus-receptor gene;Genomics;2008-11
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