Human immunodeficiency virus type 1 protease triggers a myristoyl switch that modulates membrane binding of Pr55(gag) and p17MA.
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Predicting N-terminal myristoylation sites in plant proteinsStructure of equine infectious anemia virus matrix protein.Entropic switch regulates myristate exposure in the HIV-1 matrix proteinStructure of the Myristylated Human Immunodeficiency Virus Type 2 Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Membrane TargetingThe Structure of Myristoylated Mason-Pfizer Monkey Virus Matrix Protein and the Role of Phosphatidylinositol-(4,5)-Bisphosphate in Its Membrane BindingTrio engagement via plasma membrane phospholipids and the myristoyl moiety governs HIV-1 matrix binding to bilayersBiophysical characterization and crystal structure of the Feline Immunodeficiency Virus p15 matrix proteinDepletion of cellular cholesterol inhibits membrane binding and higher-order multimerization of human immunodeficiency virus type 1 Gag.How HIV-1 Gag assembles in cells: Putting together pieces of the puzzle.Single vector system for efficient N-myristoylation of recombinant proteins in E. coli.Biochemical characterization of rous sarcoma virus MA protein interaction with membranes.Relationship between human immunodeficiency virus type 1 Gag multimerization and membrane binding.Kinetic analysis of human immunodeficiency virus type 1 assembly reveals the presence of sequential intermediates.Localization of human immunodeficiency virus type 1 Gag and Env at the plasma membrane by confocal imaging.Positive and negative aspects of the human immunodeficiency virus protease: development of inhibitors versus its role in AIDS pathogenesisNuclear entry and CRM1-dependent nuclear export of the Rous sarcoma virus Gag polyprotein.Specificity of plasma membrane targeting by the rous sarcoma virus gag protein.Roles played by acidic lipids in HIV-1 Gag membrane bindingQuantitative 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.Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly.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 GagMolecular determinants that regulate plasma membrane association of HIV-1 GagDeterminants 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.Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamerA myristoyl switch regulates membrane binding of HIV-1 Gag.Role of the HIV-1 Matrix Protein in Gag Intracellular Trafficking and Targeting to the Plasma Membrane for Virus Assembly.Electrostatic interactions drive membrane association of the human immunodeficiency virus type 1 Gag MA domainInteraction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding.Discovery of a small-molecule antiviral targeting the HIV-1 matrix protein.Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity.HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphateAnalysis of human immunodeficiency virus matrix domain replacements.Total chemical synthesis of N-myristoylated HIV-1 matrix protein p17: structural and mechanistic implications of p17 myristoylation.Analysis of human immunodeficiency virus type 1 matrix binding to membranes and nucleic acids.The signal peptide of the Junín arenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex.Retroviral matrix and lipids, the intimate interaction.Subcellular Localization of HIV-1 gag-pol mRNAs Regulates Sites of Virion Assembly.
P2860
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P2860
Human immunodeficiency virus type 1 protease triggers a myristoyl switch that modulates membrane binding of Pr55(gag) and p17MA.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Human immunodeficiency virus t ...... lates membrane binding of Pr55
@nl
Human immunodeficiency virus t ...... inding of Pr55(gag) and p17MA.
@en
type
label
Human immunodeficiency virus t ...... lates membrane binding of Pr55
@nl
Human immunodeficiency virus t ...... inding of Pr55(gag) and p17MA.
@en
prefLabel
Human immunodeficiency virus t ...... lates membrane binding of Pr55
@nl
Human immunodeficiency virus t ...... inding of Pr55(gag) and p17MA.
@en
P2860
P1433
P1476
Human immunodeficiency virus t ...... inding of Pr55(gag) and p17MA.
@en
P2093
L Hermida-Matsumoto
P2860
P304
P407
P577
1999-03-01T00:00:00Z