Structure-function studies of the self-assembly domain of the human immunodeficiency virus type 1 transmembrane protein gp41.
about
Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis.The M-T Hook Structure Is Critical for Design of HIV-1 Fusion InhibitorsDiscovery of Critical Residues for Viral Entry and Inhibition through Structural Insight of HIV-1 Fusion Inhibitor CP621-652Comparison of predicted scaffold-compatible sequence variation in the triple-hairpin structure of human imunodeficiency virus type 1 gp41 with patient data.Protein intrinsic disorder toolbox for comparative analysis of viral proteins.Role of the simian virus 5 fusion protein N-terminal coiled-coil domain in folding and promotion of membrane fusion.Human immunodeficiency virus (HIV) gp41 escape mutants: cross-resistance to peptide inhibitors of HIV fusion and altered receptor activation of gp120.A conserved trimerization motif controls the topology of short coiled coils.Genetic evidence that interhelical packing interactions in the gp41 core are critical for transition of the human immunodeficiency virus type 1 envelope glycoprotein to the fusion-active state.Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1.The conserved residue Arg46 in the N-terminal heptad repeat domain of HIV-1 gp41 is critical for viral fusion and entryHIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formationCharacterization of HIV-1 envelope gp41 genetic diversity and functional domains following perinatal transmission.Significant differences in cell-cell fusion and viral entry between strains revealed by scanning mutagenesis of the C-heptad repeat of HIV gp41Regulation of human immunodeficiency virus type 1 Env-mediated membrane fusion by viral protease activity.Role of hydrophobic residues in the central ectodomain of gp41 in maintaining the association between human immunodeficiency virus type 1 envelope glycoprotein subunits gp120 and gp41.Conserved salt bridge between the N- and C-terminal heptad repeat regions of the human immunodeficiency virus type 1 gp41 core structure is critical for virus entry and inhibition.High throughput screening for cyanovirin-N mimetics binding to HIV-1 gp41.In silico vaccine design based on molecular simulations of rhinovirus chimeras presenting HIV-1 gp41 epitopes.Conserved residue Lys574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry.
P2860
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P2860
Structure-function studies of the self-assembly domain of the human immunodeficiency virus type 1 transmembrane protein gp41.
description
2000 nî lūn-bûn
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2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
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2000 թվականի հունիսին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
Structure-function studies of ...... 1 transmembrane protein gp41.
@ast
Structure-function studies of ...... 1 transmembrane protein gp41.
@en
type
label
Structure-function studies of ...... 1 transmembrane protein gp41.
@ast
Structure-function studies of ...... 1 transmembrane protein gp41.
@en
prefLabel
Structure-function studies of ...... 1 transmembrane protein gp41.
@ast
Structure-function studies of ...... 1 transmembrane protein gp41.
@en
P2860
P1433
P1476
Structure-function studies of ...... e 1 transmembrane protein gp41
@en
P2860
P304
P356
10.1128/JVI.74.11.5368-5372.2000
P577
2000-06-01T00:00:00Z