Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity.
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Potent D-peptide inhibitors of HIV-1 entryComplexes of neutralizing and non-neutralizing affinity matured Fabs with a mimetic of the internal trimeric coiled-coil of HIV-1 gp41Design of an engineered N-terminal HIV-1 gp41 trimer with enhanced stability and potencyStructural Basis of HIV-1 Neutralization by Affinity Matured Fabs Directed against the Internal Trimeric Coiled-Coil of gp41Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide regionAsymmetric deactivation of HIV-1 gp41 following fusion inhibitor bindingAntibody elicited against the gp41 N-heptad repeat (NHR) coiled-coil can neutralize HIV-1 with modest potency but non-neutralizing antibodies also bind to NHR mimetics.A monoclonal Fab derived from a human nonimmune phage library reveals a new epitope on gp41 and neutralizes diverse human immunodeficiency virus type 1 strains.Sequestering of the prehairpin intermediate of gp41 by peptide N36Mut(e,g) potentiates the human immunodeficiency virus type 1 neutralizing activity of monoclonal antibodies directed against the N-terminal helical repeat of gp41Stable extended human immunodeficiency virus type 1 gp41 coiled coil as an effective target in an assay for high-affinity fusion inhibitors.Affinity maturation by targeted diversification of the CDR-H2 loop of a monoclonal Fab derived from a synthetic naïve human antibody library and directed against the internal trimeric coiled-coil of gp41 yields a set of Fabs with improved HIV-1 neutCovalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection.Binding of HIV-1 gp41-directed neutralizing and non-neutralizing fragment antibody binding domain (Fab) and single chain variable fragment (ScFv) antibodies to the ectodomain of gp41 in the pre-hairpin and six-helix bundle conformationsNovel recombinant engineered gp41 N-terminal heptad repeat trimers and their potential as anti-HIV-1 therapeutics or microbicidesThe prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions.Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation.Phages and HIV-1: from display to interplay.Resistance to N-peptide fusion inhibitors correlates with thermodynamic stability of the gp41 six-helix bundle but not HIV entry kinetics.Identification and characterization of a broadly cross-reactive HIV-1 human monoclonal antibody that binds to both gp120 and gp41.Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus.Single-chain protein mimetics of the N-terminal heptad-repeat region of gp41 with potential as anti-HIV-1 drugs.Targeting therapeutics to an exposed and conserved binding element of the HIV-1 fusion protein.Synergistic inhibition of HIV-1 envelope-mediated membrane fusion by inhibitors targeting the N and C-terminal heptad repeats of gp41.Swapped-domain constructs of the glycoprotein-41 ectodomain are potent inhibitors of HIV infectionReceptor Activation of HIV-1 Env Leads to Asymmetric Exposure of the gp41 Trimer.Progress in identifying peptides and small-molecule inhibitors targeted to gp41 of HIV-1.The potent human immunodeficiency virus type 1 (HIV-1) entry inhibitor HR212 blocks formation of the envelope glycoprotein gp41 six-helix bundle.Cross-reactive human immunodeficiency virus type 1-neutralizing human monoclonal antibody that recognizes a novel conformational epitope on gp41 and lacks reactivity against self-antigens.Interactions of HIV-1 inhibitory peptide T20 with the gp41 N-HR coiled coilNew carbohydrate specificity and HIV-1 fusion blocking activity of the cyanobacterial protein MVL: NMR, ITC and sedimentation equilibrium studies.Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency.Insight into the mechanisms of aminoglycoside derivatives interaction with HIV-1 entry steps and viral gene transcription.Peptides in the treatment of AIDS.HIV envelope: challenges and opportunities for development of entry inhibitors.Escape from human immunodeficiency virus type 1 (HIV-1) entry inhibitors.Covalent trimers of the internal N-terminal trimeric coiled-coil of gp41 and antibodies directed against them are potent inhibitors of HIV envelope-mediated cell fusion.Complex interplay of kinetic factors governs the synergistic properties of HIV-1 entry inhibitors."Fusion and binding inhibition" key target for HIV-1 treatment and pre-exposure prophylaxis: targets, drug delivery and nanotechnology approaches.Antiviral properties of two trimeric recombinant gp41 proteins.The C34 Peptide Fusion Inhibitor Binds to the Six-Helix Bundle Core Domain of HIV-1 gp41 by Displacement of the C-Terminal Helical Repeat Region.
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Design and properties of N(CCG)-gp41, a chimeric gp41 molecule with nanomolar HIV fusion inhibitory activity.
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh
2001年學術文章
@zh-hant
name
Design and properties of N(CCG ...... IV fusion inhibitory activity.
@en
type
label
Design and properties of N(CCG ...... IV fusion inhibitory activity.
@en
prefLabel
Design and properties of N(CCG ...... IV fusion inhibitory activity.
@en
P2093
P2860
P356
P1476
Design and properties of N(CCG ...... IV fusion inhibitory activity.
@en
P2093
P2860
P304
29485-29489
P356
10.1074/JBC.C100317200
P407
P577
2001-06-19T00:00:00Z