Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides
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HIV-1 envelope glycoprotein structureStructural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis.Mutations that destabilize the gp41 core are determinants for stabilizing the simian immunodeficiency virus-CPmac envelope glycoprotein complexThe 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 CP621-652The HIVToolbox 2 web system integrates sequence, structure, function and mutation analysisEvidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusionHIV-1 gp41 and gp160 are hyperthermostable proteins in a mesophilic environment. Characterization of gp41 mutants.Design and characterization of swapped-domain constructs of HIV-1 glycoprotein-41 as receptors for drug discovery.Identification of the HIV-1 gp41 core-binding motif--HXXNPF.Identification of the HIV-1 gp41 core-binding motif in the scaffolding domain of caveolin-1.The mechanism by which molecules containing the HIV gp41 core-binding motif HXXNPF inhibit HIV-1 envelope glycoprotein-mediated syncytium formation.A novel fluorescence intensity screening assay identifies new low-molecular-weight inhibitors of the gp41 coiled-coil domain of human immunodeficiency virus type 1Phage display of functional, full-length human and viral membrane proteins.Structure-based design, synthesis and biological evaluation of new N-carboxyphenylpyrrole derivatives as HIV fusion inhibitors targeting gp41.Glycine Substitution at Helix-to-Coil Transitions Facilitates the Structural Determination of a Stabilized Subtype C HIV Envelope GlycoproteinNovel recombinant engineered gp41 N-terminal heptad repeat trimers and their potential as anti-HIV-1 therapeutics or microbicidesDesigning human m1 muscarinic receptor-targeted hydrophobic eigenmode matched peptides as functional modulatorsBiophysical property and broad anti-HIV activity of albuvirtide, a 3-maleimimidopropionic acid-modified peptide fusion inhibitor.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.Clustering patterns of cytotoxic T-lymphocyte epitopes in human immunodeficiency virus type 1 (HIV-1) proteins reveal imprints of immune evasion on HIV-1 global variation.The conserved residue Arg46 in the N-terminal heptad repeat domain of HIV-1 gp41 is critical for viral fusion and entryPotent strategy to inhibit HIV-1 by binding both gp120 and gp41.Folded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external regionHIV-1 envelope accessible surface and polarity: clade, blood, and brain.In vitro evolution of ligands to the membrane protein caveolinCo-expression of foreign proteins tethered to HIV-1 envelope glycoprotein on the cell surface by introducing an intervening second membrane-spanning domain.Selection with a peptide fusion inhibitor corresponding to the first heptad repeat of HIV-1 gp41 identifies two genetic pathways conferring cross-resistance to peptide fusion inhibitors corresponding to the first and second heptad repeats (HR1 and HTrimeric, coiled-coil extension on peptide fusion inhibitor of HIV-1 influences selection of resistance pathwaysSwapped-domain constructs of the glycoprotein-41 ectodomain are potent inhibitors of HIV infectionProgress in identifying peptides and small-molecule inhibitors targeted to gp41 of HIV-1.Potent HIV fusion inhibitors against Enfuvirtide-resistant HIV-1 strainsRole of human immunodeficiency virus type 1 envelope structure in the induction of broadly neutralizing antibodies.Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA.Computer-Aided Approaches for Targeting HIVgp41.Identification of a critical motif for the human immunodeficiency virus type 1 (HIV-1) gp41 core structure: implications for designing novel anti-HIV fusion inhibitors.The six-helix bundle of human immunodeficiency virus Env controls pore formation and enlargement and is initiated at residues proximal to the hairpin turnConserved 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.The fusion activity of HIV-1 gp41 depends on interhelical interactions.HIV gp41 six-helix bundle constructs induce rapid vesicle fusion at pH 3.5 and little fusion at pH 7.0: understanding pH dependence of protein aggregation, membrane binding, and electrostatics, and implications for HIV-host cell fusion.
P2860
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P2860
Helical interactions in the HIV-1 gp41 core reveal structural basis for the inhibitory activity of gp41 peptides
description
2000 nî lūn-bûn
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2000 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի փետրվարին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
@yue
2000年論文
@zh-hant
2000年論文
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2000年論文
@zh-mo
2000年論文
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2000年论文
@wuu
name
Helical interactions in the HI ...... tory activity of gp41 peptides
@ast
Helical interactions in the HI ...... tory activity of gp41 peptides
@en
Helical interactions in the HI ...... tory activity of gp41 peptides
@nl
type
label
Helical interactions in the HI ...... tory activity of gp41 peptides
@ast
Helical interactions in the HI ...... tory activity of gp41 peptides
@en
Helical interactions in the HI ...... tory activity of gp41 peptides
@nl
prefLabel
Helical interactions in the HI ...... tory activity of gp41 peptides
@ast
Helical interactions in the HI ...... tory activity of gp41 peptides
@en
Helical interactions in the HI ...... tory activity of gp41 peptides
@nl
P2093
P356
P1433
P1476
Helical interactions in the HI ...... tory activity of gp41 peptides
@en
P2093
P304
P356
10.1021/BI9921687
P407
P577
2000-02-22T00:00:00Z