Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
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The matrix domain contributes to the nucleic acid chaperone activity of HIV-2 Gag.The Structure of Immature Virus-Like Rous Sarcoma Virus Gag Particles Reveals a Structural Role for the p10 Domain in Assembly.Quantitative Characterization of Configurational Space Sampled by HIV-1 Nucleocapsid Using Solution NMR, X-ray Scattering and Protein EngineeringStructural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic InstabilityHelical Conformation in the CA-SP1 Junction of the Immature HIV-1 Lattice Determined from Solid-State NMR of Virus-like Particles.Major Variations in HIV-1 Capsid Assembly Morphologies Involve Minor Variations in Molecular Structures of Structurally Ordered Protein Segments.In vitro assembly of the Rous Sarcoma Virus capsid protein into hexamer tubes at physiological temperature.Dynamic Nuclear Polarization Enhanced MAS NMR Spectroscopy for Structural Analysis of HIV-1 Protein Assemblies.Binding of Clinical Inhibitors to a Model Precursor of a Rationally Selected Multidrug Resistant HIV-1 Protease Is Significantly Weaker Than That to the Released Mature EnzymeTransient HIV-1 Gag-protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations.Mutations Proximal to Sites of Autoproteolysis and the α-Helix That Co-evolve under Drug Pressure Modulate the Autoprocessing and Vitality of HIV-1 Protease.A Direct Interaction with RNA Dramatically Enhances the Catalytic Activity of the HIV-1 Protease In VitroImmature HIV-1 lattice assembly dynamics are regulated by scaffolding from nucleic acid and the plasma membrane.Modeling the full length HIV-1 Gag polyprotein reveals the role of its p6 subunit in viral maturation and the effect of non-cleavage site mutations in protease drug resistance.1H, 13C and 15N backbone and partial side-chain resonance assignments of the C-terminal domain of HIV-1 Pr55Gag encompassed in NCp15.Binding kinetics and substrate selectivity in HIV-1 protease-Gag interactions probed at atomic resolution by chemical exchange NMR.
P2860
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P2860
Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.
description
2015 nî lūn-bûn
@nan
2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Conformation and dynamics of t ...... 1 studied by NMR spectroscopy.
@ast
Conformation and dynamics of t ...... 1 studied by NMR spectroscopy.
@en
type
label
Conformation and dynamics of t ...... 1 studied by NMR spectroscopy.
@ast
Conformation and dynamics of t ...... 1 studied by NMR spectroscopy.
@en
prefLabel
Conformation and dynamics of t ...... 1 studied by NMR spectroscopy.
@ast
Conformation and dynamics of t ...... 1 studied by NMR spectroscopy.
@en
P2860
P356
P1476
Conformation and dynamics of t ...... 1 studied by NMR spectroscopy
@en
P2093
Lalit Deshmukh
Rodolfo Ghirlando
P2860
P304
P356
10.1073/PNAS.1501985112
P407
P577
2015-02-23T00:00:00Z