Analysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids.
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Global changes in the RNA binding specificity of HIV-1 gag regulate virion genesisHIV type 1 Gag as a target for antiviral therapyStructural determinants and mechanism of HIV-1 genome packagingCoordination of Genomic RNA Packaging with Viral Assembly in HIV-1HIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchUnderstanding the process of envelope glycoprotein incorporation into virions in simian and feline immunodeficiency virusesThe matrix domain contributes to the nucleic acid chaperone activity of HIV-2 Gag.Nucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cellsTrio engagement via plasma membrane phospholipids and the myristoyl moiety governs HIV-1 matrix binding to bilayersThe Life-Cycle of the HIV-1 Gag-RNA ComplexHIV-1 Gag extension: conformational changes require simultaneous interaction with membrane and nucleic acidOpposing mechanisms involving RNA and lipids regulate HIV-1 Gag membrane binding through the highly basic region of the matrix domain.Mechanistic differences between nucleic acid chaperone activities of the Gag proteins of Rous sarcoma virus and human immunodeficiency virus type 1 are attributed to the MA domain.Definition of a high-affinity Gag recognition structure mediating packaging of a retroviral RNA genome.Retrovirus-specific differences in matrix and nucleocapsid protein-nucleic acid interactions: implications for genomic RNA packagingA large extension to HIV-1 Gag, like Pol, has negative impacts on virion assemblyMatrix domain modulates HIV-1 Gag's nucleic acid chaperone activity via inositol phosphate binding.Myristate exposure in the human immunodeficiency virus type 1 matrix protein is modulated by pH.Roles played by acidic lipids in HIV-1 Gag membrane bindingMolecular mechanism of arenavirus assembly and budding.Relationships between plasma membrane microdomains and HIV-1 assemblyAssembly and replication of HIV-1 in T cells with low levels of phosphatidylinositol-(4,5)-bisphosphate.Nucleic acid chaperone activity of retroviral Gag proteinsMembrane binding and subcellular localization of retroviral Gag proteins are differentially regulated by MA interactions with phosphatidylinositol-(4,5)-bisphosphate and RNA.Gag localization and virus-like particle release mediated by the matrix domain of human T-lymphotropic virus type 1 Gag are less dependent on phosphatidylinositol-(4,5)-bisphosphate than those mediated by the matrix domain of HIV-1 GagDiverse interactions of retroviral Gag proteins with RNAs.Molecular determinants that regulate plasma membrane association of HIV-1 GagHIV-1 matrix protein binding to RNA.Determinants of the HIV-1 core assembly pathway.Structural and molecular determinants of HIV-1 Gag binding to the plasma membrane.HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination.Solution properties of murine leukemia virus gag protein: differences from HIV-1 gag.HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors.Role 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 particlesPhosphatidylinositol-(4,5)-Bisphosphate Acyl Chains Differentiate Membrane Binding of HIV-1 Gag from That of the Phospholipase Cδ1 Pleckstrin Homology DomainBeyond plasma membrane targeting: role of the MA domain of Gag in retroviral genome encapsidation.Dynamic Association between HIV-1 Gag and Membrane Domains.New insights into HIV assembly and trafficking.HIV-1 Gag protein can sense the cholesterol and acyl chain environment in model membranes.
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Analysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 23 September 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Analysis of human immunodefici ...... o membranes and nucleic acids.
@en
Analysis of human immunodefici ...... o membranes and nucleic acids.
@nl
type
label
Analysis of human immunodefici ...... o membranes and nucleic acids.
@en
Analysis of human immunodefici ...... o membranes and nucleic acids.
@nl
prefLabel
Analysis of human immunodefici ...... o membranes and nucleic acids.
@en
Analysis of human immunodefici ...... o membranes and nucleic acids.
@nl
P2093
P2860
P356
P1433
P1476
Analysis of human immunodefici ...... o membranes and nucleic acids.
@en
P2093
Amelia Still
Ayna Alfadhli
Eric Barklis
P2860
P304
12196-12203
P356
10.1128/JVI.01197-09
P407
P577
2009-09-23T00:00:00Z