Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
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Predicting Bevirimat resistance of HIV-1 from genotypeHIV 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 targetDirect and dynamic detection of HIV-1 in living cellsProtease cleavage leads to formation of mature trimer interface in HIV-1 capsidFlexibility in HIV-1 Assembly Subunits: Solution Structure of the Monomeric C-Terminal Domain of the Capsid ProteinStructure of the Antiviral Assembly Inhibitor CAP-1 Complex with the HIV-1 CA ProteinResidues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid proteinX-ray structures of the hexameric building block of the HIV capsid.Structural Convergence between Cryo-EM and NMR Reveals Intersubunit Interactions Critical for HIV-1 Capsid FunctionProton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral ParticlesLimitations of Peptide Retro-inverso Isomerization in Molecular MimicryDisulfide bond stabilization of the hexameric capsomer of human immunodeficiency virusStructure of the HIV-1 Full-Length Capsid Protein in a Conformationally Trapped Unassembled State Induced by Small-Molecule BindingAtomic-level modelling of the HIV capsidA unique spumavirus Gag N-terminal domain with functional properties of orthoretroviral matrix and capsidA triclinic crystal structure of the carboxy-terminal domain of HIV-1 capsid protein with four molecules in the asymmetric unit reveals a novel packing interfaceDistinct Effects of Two HIV-1 Capsid Assembly Inhibitor Families That Bind the Same Site within the N-Terminal Domain of the Viral CA ProteinStructure and Dynamics of Full-Length HIV-1 Capsid Protein in SolutionMonitoring binding of HIV-1 capsid assembly inhibitors using (19)F ligand-and (15)N protein-based NMR and X-ray crystallography: early hit validation of a benzodiazepine seriesSTRUCTURAL VIROLOGY. Conformational plasticity of a native retroviral capsid revealed by x-ray crystallographyStructure of the Dimerization Interface in the Mature HIV-1 Capsid Protein Lattice from Solid State NMR of Tubular AssembliesRationally designed interfacial peptides are efficient in vitro inhibitors of HIV-1 capsid assembly with antiviral activityEfficient production of HIV-1 virus-like particles from a mammalian expression vector requires the N-terminal capsid domainStructure-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.STRUCTURAL VIROLOGY. X-ray crystal structures of native HIV-1 capsid protein reveal conformational variability.Viral DNA synthesis defects in assembly-competent Rous sarcoma virus CA mutants.MAS NMR of HIV-1 protein assemblies.Composite Sequence-Structure Stability Models as Screening Tools for Identifying Vulnerable Targets for HIV Drug and Vaccine Development.Solid-state NMR studies of HIV-1 capsid protein assemblies.Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments.A comparative analysis of the foamy and ortho virus capsid structures reveals an ancient domain duplication.Design of in vitro symmetric complexes and analysis by hybrid methods reveal mechanisms of HIV capsid assemblyThe structural biology of HIV assembly.Electron cryotomography of immature HIV-1 virions reveals the structure of the CA and SP1 Gag shells.CryoEM Structure Refinement by Integrating NMR Chemical Shifts with Molecular Dynamics Simulations.Helical structure determined by NMR of the HIV-1 (345-392)Gag sequence, surrounding p2: implications for particle assembly and RNA packaging
P2860
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P2860
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
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
name
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@ast
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@en
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@nl
type
label
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@ast
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@en
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@nl
prefLabel
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@ast
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@en
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@nl
P2093
P3181
P1476
Structures of the HIV-1 capsid protein dimerization domain at 2.6 A resolution
@en
P2093
P3181
P356
10.1107/S0907444998007689
P577
1999-01-01T00:00:00Z