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 Gag

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 Gag

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Q35076588

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Alterations in the MA and NC domains modulate phosphoinositide-dependent plasma membrane localization of the Rous sarcoma virus Gag protein Eukaryotic virulence determinants utilize phosphoinositides at the ER and host cell surface Trio engagement via plasma membrane phospholipids and the myristoyl moiety governs HIV-1 matrix binding to bilayers Membrane dynamics associated with viral infection How HIV finds the door Basic residues in the matrix domain and multimerization target murine leukemia virus Gag to the virological synapse.Human T-lymphotropic virus type 1-infected cells secrete exosomes that contain Tax protein.Retrovirus-specific differences in matrix and nucleocapsid protein-nucleic acid interactions: implications for genomic RNA packaging Identification of a small-molecule inhibitor of HIV-1 assembly that targets the phosphatidylinositol (4,5)-bisphosphate binding site of the HIV-1 matrix protein.Roles played by acidic lipids in HIV-1 Gag membrane binding Molecular mechanism of arenavirus assembly and budding.Membrane binding and subcellular localization of retroviral Gag proteins are differentially regulated by MA interactions with phosphatidylinositol-(4,5)-bisphosphate and RNA.Molecular determinants that regulate plasma membrane association of HIV-1 Gag Structural and molecular determinants of HIV-1 Gag binding to the plasma membrane.Molecular determinants of human T-lymphotropic virus type 1 transmission and spread.In situ quantification of protein binding to the plasma membrane.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 Domain Beyond plasma membrane targeting: role of the MA domain of Gag in retroviral genome encapsidation.Hydrodynamic and Membrane Binding Properties of Purified Rous Sarcoma Virus Gag Protein.Retroviral env glycoprotein trafficking and incorporation into virions.Equine Infectious Anemia Virus Gag Assembly and Export Are Directed by Matrix Protein through trans-Golgi Networks and Cellular Vesicles.Membrane Binding of the Rous Sarcoma Virus Gag Protein Is Cooperative and Dependent on the Spacer Peptide Assembly Domain.Evidence in support of RNA-mediated inhibition of phosphatidylserine-dependent HIV-1 Gag membrane binding in cells.Methods to Study Determinants for Membrane Targeting of HIV-1 Gag In Vitro.Interrelationship between cytoplasmic retroviral Gag concentration and Gag-membrane association.HIV-1 assembly, budding, and maturation.Membrane interaction of retroviral Gag proteins.The roles of lipids and nucleic acids in HIV-1 assembly New insights into retroviral Gag-Gag and Gag-membrane interactions.Role of Gag and lipids during HIV-1 assembly in CD4(+) T cells and macrophages.Rous sarcoma virus gag has no specific requirement for phosphatidylinositol-(4,5)-bisphosphate for plasma membrane association in vivo or for liposome interaction in vitro.Disparate Contributions of Human Retrovirus Capsid Subdomains to Gag-Gag Oligomerization, Virus Morphology, and Particle Biogenesis.Effect of multimerization on membrane association of Rous sarcoma virus and HIV-1 matrix domain proteins.Molecular Determinants Directing HIV-1 Gag Assembly to Virus-Containing Compartments in Primary Macrophages.Inhibition of HIV-1 Gag-membrane interactions by specific RNAs.Visualization of HIV-1 Gag Binding to Giant Unilamellar Vesicle (GUV) Membranes.Involvement of the Rac1-IRSp53-Wave2-Arp2/3 Signaling Pathway in HIV-1 Gag Particle Release in CD4 T Cells.Design and synthesis of lipid-coupled inositol 1,2,3,4,5,6-hexakisphosphate derivatives exhibiting high-affinity binding for the HIV-1 MA domain.Inositol phosphates compete with nucleic acids for binding to bovine leukemia virus matrix protein: implications for deltaretroviral assembly.

P2860

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P2860

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 Gag

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http://www.wikidata.org/entity/Q35076588

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2011 nî lūn-bûn

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2011 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2011 թվականի փետրվարին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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