The molecular basis of HIV capsid assembly--five years of progress.
about
The prototype HIV-1 maturation inhibitor, bevirimat, binds to the CA-SP1 cleavage site in immature Gag particlesBluetongue virus RNA binding protein NS2 is a modulator of viral replication and assemblyDomain-swapped dimerization of the HIV-1 capsid C-terminal domainA triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interfaceStructure of the SCAN Domain of Human Paternally Expressed Gene 3 ProteinTy3 capsid mutations reveal early and late functions of the amino-terminal domainRationally designed interfacial peptides are efficient in vitro inhibitors of HIV-1 capsid assembly with antiviral activityCharacterization of a novel type of HIV-1 particle assembly inhibitor using a quantitative luciferase-Vpr packaging-based assayEfficient production of HIV-1 virus-like particles from a mammalian expression vector requires the N-terminal capsid domainThe structural biology of HIV assembly.Depletion of cellular cholesterol inhibits membrane binding and higher-order multimerization of human immunodeficiency virus type 1 Gag.Equine infectious anemia virus Gag p9 function in early steps of virus infection and provirus productionQuantitative 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.HIV-1 Gag: flipped out for PI(4,5)P(2).Antiviral activity of α-helical stapled peptides designed from the HIV-1 capsid dimerization domainSelective acquisition of host-derived ICAM-1 by HIV-1 is a matrix-dependent process.Coordinate linkage of HIV evolution reveals regions of immunological vulnerability.Molecular determinants that regulate plasma membrane association of HIV-1 GagIn vitro resistance to the human immunodeficiency virus type 1 maturation inhibitor PA-457 (Bevirimat).SOCS1 is an inducible host factor during HIV-1 infection and regulates the intracellular trafficking and stability of HIV-1 Gag.Interaction between the human immunodeficiency virus type 1 Gag matrix domain and phosphatidylinositol-(4,5)-bisphosphate is essential for efficient gag membrane binding.Ty3 nucleocapsid controls localization of particle assemblyParasitism and the retrotransposon life cycle in plants: a hitchhiker's guide to the genome.HIV-1 Assembly at the Plasma Membrane: Gag Trafficking and Localization.Methods to Study Determinants for Membrane Targeting of HIV-1 Gag In Vitro.The capsid protein of human immunodeficiency virus: intersubunit interactions during virus assembly.Retroviral matrix and lipids, the intimate interaction.Unraveling the dynamics of protein interactions with quantitative mass spectrometry.New developments in lentiviral vector design, production and purification.A temporospatial map that defines specific steps at which critical surfaces in the Gag MA and CA domains act during immature HIV-1 capsid assembly in cells.Requirement for an intact T-cell actin and tubulin cytoskeleton for efficient assembly and spread of human immunodeficiency virus type 1.TY3 GAG3 protein forms ordered particles in Escherichia coli.
P2860
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P2860
The molecular basis of HIV capsid assembly--five years of progress.
description
2004 nî lūn-bûn
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2004 թուականի Մարտին հրատարակուած գիտական յօդուած
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2004 թվականի մարտին հրատարակված գիտական հոդված
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2004年の論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年論文
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2004年论文
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name
The molecular basis of HIV capsid assembly--five years of progress.
@ast
The molecular basis of HIV capsid assembly--five years of progress.
@en
The molecular basis of HIV capsid assembly--five years of progress.
@nl
type
label
The molecular basis of HIV capsid assembly--five years of progress.
@ast
The molecular basis of HIV capsid assembly--five years of progress.
@en
The molecular basis of HIV capsid assembly--five years of progress.
@nl
prefLabel
The molecular basis of HIV capsid assembly--five years of progress.
@ast
The molecular basis of HIV capsid assembly--five years of progress.
@en
The molecular basis of HIV capsid assembly--five years of progress.
@nl
P356
P1476
The molecular basis of HIV capsid assembly--five years of progress.
@en
P304
P356
10.1002/RMV.418
P577
2004-03-01T00:00:00Z