Results 181 to 190 of about 34,750 (223)
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HIV-1 gp120 Dimers Decrease the Overall Affinity of gp120 Preparations for CD4-Induced Ligands
Journal of Virological Methods, 2015For several years, tools to study the conformational changes of HIV-1 envelope glycoproteins have been developed in order to comprehend those changes and their role in the fusion process and immunogenicity of HIV-1. To facilitate these studies, expression of the HIV-1 gp120 envelope glycoprotein has been done in several over-expression settings ...
Andrés Finzi, Mathieu Coutu
exaly +3 more sources
Current Opinion in Immunology, 1991
The three-dimensional structure of the binding domain of the CD4 molecule has been determined and extensive mutational analyses of the respective binding sites on gp120 and CD4 have been completed. The consequences of gp120-CD4 binding with respect to secondary changes in the virion, or the cell, that may be required for infection or that may interfere
J S, McDougal +2 more
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The three-dimensional structure of the binding domain of the CD4 molecule has been determined and extensive mutational analyses of the respective binding sites on gp120 and CD4 have been completed. The consequences of gp120-CD4 binding with respect to secondary changes in the virion, or the cell, that may be required for infection or that may interfere
J S, McDougal +2 more
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Correlated mutations at gp120 positions 322 and 440: Implications for gp120 structure
Proteins: Structure, Function, and Bioinformatics, 2008AbstractAnalysis of V3 and C4 sequences of HIV‐1 reveals correlated mutations at gp120 positions 322 and 440, and a very strong preference for a positively charged residue at position 440 when position 322 is negatively charged. This observation suggests that these two residues are close to each other and interact electrostatically in R5 viruses.
Osnat, Rosen +2 more
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HIV-1 gp120 AND IMMUNE NETWORK
International Reviews of Immunology, 2004It has been demonstrated that the immunodominant V3 loop of HIV-1 gp120 and its flanking regions bear sequence and structural homology to the framework and complementarity-determining regions of human immunoglobulins. It has been proposed that the Ig-like domain of gp120 might encode idiotypes and in this way permit HIV-1 entry into the immune ...
Radmila, Metlas, Veljko, Veljkovic
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gp120 neurotoxicity in primary cortical cultures
Advances in Neuroimmunology, 1994The human immunodeficiency virus type 1 coat protein, gp120, kills neurons in a nitric oxide dependent manner in primary cortical cultures at low picomolar concentrations. gp120 neurotoxicity also requires calcium and glutamate and is blocked by glutamate receptor antagonists.
T M, Dawson, V L, Dawson
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Nitric Oxide Production and Apoptosis by GP120
Allergy and Asthma Proceedings, 2000Nitric oxide (NO) is increased by gp120 in astrocytes and in monocyte-derived macrophages. Of the gp120 fragments (F1: amino acid 254-274, F2: amino acid 315-329, F3: amino acid 421-438), F1 has been shown to increase NO in astrocytes and gp120 also primes CD4+ T cells for apoptosis.
A, Mansur +3 more
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Trends in Microbiology, 1998
When HIV-infected patients progress to AIDS, there is not only a drop in CD4 T-cell numbers but also an appreciable decline in CD8 T-cell populations. To determine if the depletion of CD8 T cells can be mediated directly by HIV, Herbein et al., 1998xApoptosis of CD8+ T cells is mediated by macrophages through interaction of HIV gp120 with chemokine ...
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When HIV-infected patients progress to AIDS, there is not only a drop in CD4 T-cell numbers but also an appreciable decline in CD8 T-cell populations. To determine if the depletion of CD8 T cells can be mediated directly by HIV, Herbein et al., 1998xApoptosis of CD8+ T cells is mediated by macrophages through interaction of HIV gp120 with chemokine ...
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Synergism Between HIV gp120 and gp120-Specific Antibody in Blocking Human T Cell Activation
Science, 1989The human immunodeficiency virus (HIV) binds to CD4-positive cells through interaction of its envelope glycoprotein (gp120) with the CD4 molecule. CD4 is a prominent immunoregulatory molecule, and chronic exposure to antibody against CD4 (anti-CD4) has been shown to cause immunodeficiency in mice. T cell-dependent in vitro immune responses
R S, Mittler, M K, Hoffmann
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Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997
A synthetic peptide resembling the C2 region of human immunodeficiency virus type 1 (HIV-1) gp120 (C2-Lai: amino acids (aa) 273-288), inhibited (C50 = 200 microM) gp120 calcium-dependent binding of N-acetyl-beta-D-glucosaminyl and mannosyl residues exposed on natural glycoprotein bovine fetuin whereas a peptide derived from an aa sequence downstream of
N, Seddiki +6 more
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A synthetic peptide resembling the C2 region of human immunodeficiency virus type 1 (HIV-1) gp120 (C2-Lai: amino acids (aa) 273-288), inhibited (C50 = 200 microM) gp120 calcium-dependent binding of N-acetyl-beta-D-glucosaminyl and mannosyl residues exposed on natural glycoprotein bovine fetuin whereas a peptide derived from an aa sequence downstream of
N, Seddiki +6 more
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Recognition of HIV glycoprotein gp120 by T cells. Role of monocyte CD4 in the presentation of gp120.
The Journal of Immunology, 1989Abstract The HIV envelope glycoprotein gp120 binds with high affinity to CD4 and is responsible for the tropism of HIV for CD4+ T cells and monocytes. Efforts to develop HIV vaccines have focused on gp120 and, therefore, a detailed molecular understanding of human immune responses to gp120 is essential. In this report, we have used human
R F, Siliciano +5 more
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