A mutation in the human immunodeficiency virus type 1 Gag protein destabilizes the interaction of the envelope protein subunits gp120 and gp41.
about
Uncovering viral protein-protein interactions and their role in arenavirus life cycleHIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchThe molecular basis of HIV entrySolution Structure of Calmodulin Bound to the Binding Domain of the HIV-1 Matrix ProteinFIV Gag: virus assembly and host-cell interactions.The roles of tetraspanins in HIV-1 replication.Binding of calmodulin to the HIV-1 matrix protein triggers myristate exposure.Assembly and replication of HIV-1 in T cells with low levels of phosphatidylinositol-(4,5)-bisphosphate.Human Ubc9 is involved in intracellular HIV-1 Env stability after trafficking out of the trans-Golgi network in a Gag dependent manner.Second-site compensatory mutations of HIV-1 capsid mutations.HIV-1 envelope glycoprotein biosynthesis, trafficking, and incorporation.HIV-1 matrix protein binding to RNA.The HIV matrix protein p17 promotes the activation of human hepatic stellate cells through interactions with CXCR2 and Syndecan-2.Multi-step inhibition explains HIV-1 protease inhibitor pharmacodynamics and resistance.NMR, biophysical, and biochemical studies reveal the minimal Calmodulin binding domain of the HIV-1 matrix proteinHuman immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamerRole of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.A highly conserved residue in the C-terminal helix of HIV-1 matrix is required for envelope incorporation into virus particlesAssociation of enhanced HIV-1 neutralization by a single Y681H substitution in gp41 with increased gp120-CD4 interaction and macrophage infectivity.Retroviral env glycoprotein trafficking and incorporation into virions.Mutations in envelope gp120 can impact proteolytic processing of the gp160 precursor and thereby affect neutralization sensitivity of human immunodeficiency virus type 1 pseudoviruses.Modulation of human immunodeficiency virus type 1 infectivity through incorporation of tetraspanin proteins.Functional diversity of HIV-1 envelope proteins expressed by contemporaneous plasma virusesAnalysis of small molecule ligands targeting the HIV-1 matrix protein-RNA binding site.Importance of the membrane-perturbing properties of the membrane-proximal external region of human immunodeficiency virus type 1 gp41 to viral fusionForced virus evolution reveals functional crosstalk between the disulfide bonded region and membrane proximal ectodomain region of HIV-1 gp41The frantic play of the concealed HIV envelope cytoplasmic tail.HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphateEvidence that productive human immunodeficiency virus type 1 assembly can occur in an intracellular compartment.Analysis of human immunodeficiency virus matrix domain replacements.Enhanced antibody-mediated neutralization of HIV-1 variants that are resistant to fusion inhibitors.Analysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids.Unique functional properties of conserved arginine residues in the lentivirus lytic peptide domains of the C-terminal tail of HIV-1 gp41.Enhanced central nervous system transduction with lentiviral vectors pseudotyped with RVG/HIV-1gp41 chimeric envelope glycoproteins.The roles of lipids and nucleic acids in HIV-1 assemblySecond-site suppressors of HIV-1 capsid mutations: restoration of intracellular activities without correction of intrinsic capsid stability defects.Formation of syncytia is repressed by tetraspanins in human immunodeficiency virus type 1-producing cells.Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion.Maturation-dependent human immunodeficiency virus type 1 particle fusion requires a carboxyl-terminal region of the gp41 cytoplasmic tail.TR1.3 viral pathogenesis and syncytium formation are linked to Env-Gag cooperation.
P2860
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P2860
A mutation in the human immunodeficiency virus type 1 Gag protein destabilizes the interaction of the envelope protein subunits gp120 and gp41.
description
2006 nî lūn-bûn
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2006 թուականի Մարտին հրատարակուած գիտական յօդուած
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2006 թվականի մարտին հրատարակված գիտական հոդված
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年论文
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name
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@ast
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@en
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@nl
type
label
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@ast
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@en
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@nl
prefLabel
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@ast
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@en
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@nl
P2093
P2860
P1433
P1476
A mutation in the human immuno ...... otein subunits gp120 and gp41.
@en
P2093
Christopher Aiken
Eric O Freed
Jiyang Jiang
Melody R Davis
P2860
P304
P356
10.1128/JVI.80.5.2405-2417.2006
P407
P577
2006-03-01T00:00:00Z