Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding.
about
Molecular Studies of HTLV-1 Replication: An UpdateNew insights into HTLV-1 particle structure, assembly, and Gag-Gag interactions in living cellsWrapping up the bad news: HIV assembly and releaseNucleocapsid promotes localization of HIV-1 gag to uropods that participate in virological synapses between T cellsThree-Dimensional Reconstruction of Three-Way FRET Microscopy Improves Imaging of Multiple Protein-Protein InteractionsN-way FRET microscopy of multiple protein-protein interactions in live cellsAnalysis of the initiating events in HIV-1 particle assembly and genome packagingA large extension to HIV-1 Gag, like Pol, has negative impacts on virion assemblyMyristate exposure in the human immunodeficiency virus type 1 matrix protein is modulated by pH.Uniform total internal reflection fluorescence illumination enables live cell fluorescence resonance energy transfer microscopy.Relationships between plasma membrane microdomains and HIV-1 assemblyBasic residues in the nucleocapsid domain of Gag are critical for late events of HIV-1 budding.FLIM FRET technology for drug discovery: automated multiwell-plate high-content analysis, multiplexed readouts and application in situ.Membrane 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 GagIn vitro analysis of human immunodeficiency virus particle dissociation: gag proteolytic processing influences dissociation kinetics.Gag induces the coalescence of clustered lipid rafts and tetraspanin-enriched microdomains at HIV-1 assembly sites on the plasma membrane.HIV-1 matrix domain removal ameliorates virus assembly and processing defects incurred by positive nucleocapsid charge elimination.Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.Phosphatidylinositol-(4,5)-Bisphosphate Acyl Chains Differentiate Membrane Binding of HIV-1 Gag from That of the Phospholipase Cδ1 Pleckstrin Homology DomainBudding of retroviruses utilizing divergent L domains requires nucleocapsid.Dynamic Association between HIV-1 Gag and Membrane Domains.Human endogenous retrovirus K Gag coassembles with HIV-1 Gag and reduces the release efficiency and infectivity of HIV-1.Functional redundancy in HIV-1 viral particle assembly.Efavirenz enhances HIV-1 gag processing at the plasma membrane through Gag-Pol dimerizationRoles played by capsid-dependent induction of membrane curvature and Gag-ESCRT interactions in tetherin recruitment to HIV-1 assembly sites.Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodelingHIV-1 assembly in macrophagesProperties and functions of the nucleocapsid protein in virus assembly.Quantitative live-cell imaging of human immunodeficiency virus (HIV-1) assembly.Membrane interaction of retroviral Gag proteins.New insights into retroviral Gag-Gag and Gag-membrane interactions.The HIV-1 nucleocapsid protein recruits negatively charged lipids to ensure its optimal binding to lipid membranesPolymorphic Nature of Human T-Cell Leukemia Virus Type 1 Particle Cores as Revealed through Characterization of a Chronically Infected Cell Line.HIV-1 Gag associates with specific uropod-directed microdomains in a manner dependent on its MA highly basic region.Molecular Determinants Directing HIV-1 Gag Assembly to Virus-Containing Compartments in Primary Macrophages.Basic motifs target PSGL-1, CD43, and CD44 to plasma membrane sites where HIV-1 assembles.Mathematical modeling and quantitative analysis of HIV-1 Gag trafficking and polymerization.FRET analysis of HIV-1 Gag and GagPol interactions.Secondary lymphoid organ fibroblastic reticular cells mediate trans-infection of HIV-1 via CD44-hyaluronan interactions.
P2860
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P2860
Quantitative fluorescence resonance energy transfer microscopy analysis of the human immunodeficiency virus type 1 Gag-Gag interaction: relative contributions of the CA and NC domains and membrane binding.
description
2009 nî lūn-bûn
@nan
2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Quantitative fluorescence reso ...... domains and membrane binding.
@ast
Quantitative fluorescence reso ...... domains and membrane binding.
@en
Quantitative fluorescence reso ...... domains and membrane binding.
@nl
type
label
Quantitative fluorescence reso ...... domains and membrane binding.
@ast
Quantitative fluorescence reso ...... domains and membrane binding.
@en
Quantitative fluorescence reso ...... domains and membrane binding.
@nl
prefLabel
Quantitative fluorescence reso ...... domains and membrane binding.
@ast
Quantitative fluorescence reso ...... domains and membrane binding.
@en
Quantitative fluorescence reso ...... domains and membrane binding.
@nl
P2860
P356
P1433
P1476
Quantitative fluorescence reso ...... domains and membrane binding.
@en
P2093
Adam Hoppe
P2860
P304
P356
10.1128/JVI.02545-08
P407
P577
2009-04-29T00:00:00Z