Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging
about
The prototype HIV-1 maturation inhibitor, bevirimat, binds to the CA-SP1 cleavage site in immature Gag particlesPredicting Bevirimat resistance of HIV-1 from genotypeThe host protein Staufen1 interacts with the Pr55Gag zinc fingers and regulates HIV-1 assembly via its N-terminusHIV type 1 Gag as a target for antiviral therapyImproved Bevirimat resistance prediction by combination of structural and sequence-based classifiersVirus maturation as a new HIV-1 therapeutic targetMagic angle spinning NMR of virusesProtease cleavage leads to formation of mature trimer interface in HIV-1 capsidCryo-electron microscopy of tubular arrays of HIV-1 Gag resolves structures essential for immature virus assemblyStructure of the immature HIV-1 capsid in intact virus particles at 8.8 Å resolutionCharacterization of a novel type of HIV-1 particle assembly inhibitor using a quantitative luciferase-Vpr packaging-based assayStructural and functional insights into the HIV-1 maturation inhibitor binding pocketMechanistic Studies and Modeling Reveal the Origin of Differential Inhibition of Gag Polymorphic Viruses by HIV-1 Maturation InhibitorsStructure-Activity Relationships of the Human Immunodeficiency Virus Type 1 Maturation Inhibitor PF-46396Helical Conformation in the CA-SP1 Junction of the Immature HIV-1 Lattice Determined from Solid-State NMR of Virus-like Particles.Crystal structure of an HIV assembly and maturation switch.Design of in vitro symmetric complexes and analysis by hybrid methods reveal mechanisms of HIV capsid assemblyThe structural biology of HIV assembly.Association of human immunodeficiency virus type 1 gag with membrane does not require highly basic sequences in the nucleocapsid: use of a novel Gag multimerization assayElectron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells.How HIV-1 Gag assembles in cells: Putting together pieces of the puzzle.Novel approaches to inhibiting HIV-1 replication.Investigation of the structure and dynamics of the capsid-spacer peptide 1-nucleocapsid fragment of the HIV-1 gag polyprotein by solution NMR spectroscopyThe capsid-spacer peptide 1 Gag processing intermediate is a dominant-negative inhibitor of HIV-1 maturation.Potential role for CA-SP in nucleating retroviral capsid maturation.NMR relaxation studies of an RNA-binding segment of the rous sarcoma virus gag polyprotein in free and bound states: a model for autoinhibition of assembly.On the role of the SP1 domain in HIV-1 particle assembly: a molecular switch?In vitro resistance to the human immunodeficiency virus type 1 maturation inhibitor PA-457 (Bevirimat).HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors.Conformation of the HIV-1 Gag protein in solution.Identification of an HIV-1 Mutation in Spacer Peptide 1 That Stabilizes the Immature CA-SP1 Lattice.Atomic Modeling of an Immature Retroviral Lattice Using Molecular Dynamics and Mutagenesis.Context surrounding processing sites is crucial in determining cleavage rate of a subset of processing sites in HIV-1 Gag and Gag-Pro-Pol polyprotein precursors by viral protease.Dimerization of the SP1 Region of HIV-1 Gag Induces a Helical Conformation and Association into Helical Bundles: Implications for Particle Assembly.Structure and assembly of immature HIVA two-pronged structural analysis of retroviral maturation indicates that core formation proceeds by a disassembly-reassembly pathway rather than a displacive transition.Magic angle spinning NMR reveals sequence-dependent structural plasticity, dynamics, and the spacer peptide 1 conformation in HIV-1 capsid protein assemblies.HIV-1 assembly, budding, and maturation.Functional and Structural Characterization of Novel Type of Linker Connecting Capsid and Nucleocapsid Protein Domains in Murine Leukemia Virus.Higher-order structure of the Rous sarcoma virus SP assembly domain.
P2860
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P2860
Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging
description
2005 nî lūn-bûn
@nan
2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Helical structure determined b ...... cle assembly and RNA packaging
@ast
Helical structure determined b ...... cle assembly and RNA packaging
@en
type
label
Helical structure determined b ...... cle assembly and RNA packaging
@ast
Helical structure determined b ...... cle assembly and RNA packaging
@en
prefLabel
Helical structure determined b ...... cle assembly and RNA packaging
@ast
Helical structure determined b ...... cle assembly and RNA packaging
@en
P2093
P2860
P356
P1433
P1476
Helical structure determined b ...... cle assembly and RNA packaging
@en
P2093
Bernard P Roques
Christine Lenoir
Serge Bouaziz
P2860
P304
P356
10.1110/PS.041087605
P577
2005-02-01T00:00:00Z