Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
about
A small-molecule dengue virus entry inhibitorThe C terminus of the B5 receptor for herpes simplex virus contains a functional region important for infection.Potent D-peptide inhibitors of HIV-1 entryProtease-resistant peptide design-empowering nature's fragile warriors against HIVComplexes of neutralizing and non-neutralizing affinity matured Fabs with a mimetic of the internal trimeric coiled-coil of HIV-1 gp41Molecular dissection of the Semliki Forest virus homotrimer reveals two functionally distinct regions of the fusion protein.Functions of the Stem Region of the Semliki Forest Virus Fusion Protein during Virus Fusion and AssemblyThe Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core ComplexA computational approach identifies two regions of Hepatitis C Virus E1 protein as interacting domains involved in viral fusion processStructure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformationMolecular basis of coiled-coil formationDesign of an engineered N-terminal HIV-1 gp41 trimer with enhanced stability and potencyDesign of a Potent D-Peptide HIV-1 Entry Inhibitor with a Strong Barrier to ResistanceStructural Basis of HIV-1 Neutralization by Affinity Matured Fabs Directed against the Internal Trimeric Coiled-Coil of gp41Versatile C(3)-symmetric scaffolds and their use for covalent stabilization of the foldon trimerAsymmetric deactivation of HIV-1 gp41 following fusion inhibitor bindingMembrane-anchored HIV-1 N-heptad repeat peptides are highly potent cell fusion inhibitors via an altered mode of actionViral envelope protein folding and membrane hemifusion are enhanced by the conserved loop region of HIV-1 gp41.Antibody 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.Phage display of random peptide libraries: applications, limits, and potential.Crystal structures of Nipah and Hendra virus fusion core proteins.Phage display of functional, full-length human and viral membrane proteins.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 gp41Affinity 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 neutAffinity maturation and characterization of a human monoclonal antibody against HIV-1 gp41Human immunodeficiency virus (HIV) gp41 escape mutants: cross-resistance to peptide inhibitors of HIV fusion and altered receptor activation of gp120.Origins of resistance to the HIVgp41 viral entry inhibitor T20.Inhibiting HIV fusion with a beta-peptide foldamer.Differences in serum IgA responses to HIV-1 gp41 in elite controllers compared to viral suppressors on highly active antiretroviral therapyVaccination with peptide mimetics of the gp41 prehairpin fusion intermediate yields neutralizing antisera against HIV-1 isolates.Covalent stabilization of coiled coils of the HIV gp41 N region yields extremely potent and broad inhibitors of viral infection.A low-molecular-weight entry inhibitor of both CCR5- and CXCR4-tropic strains of human immunodeficiency virus type 1 targets a novel site on gp41A conserved trimerization motif controls the topology of short coiled coils.Novel recombinant engineered gp41 N-terminal heptad repeat trimers and their potential as anti-HIV-1 therapeutics or microbicidesA human monoclonal antibody neutralizes diverse HIV-1 isolates by binding a critical gp41 epitopeSequential involvement of Cdk1, mTOR and p53 in apoptosis induced by the HIV-1 envelope.The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions.Phages and HIV-1: from display to interplay.Virus-cell and cell-cell fusion mediated by the HIV-1 envelope glycoprotein is inhibited by short gp41 N-terminal membrane-anchored peptides lacking the critical pocket domain.Resistance to N-peptide fusion inhibitors correlates with thermodynamic stability of the gp41 six-helix bundle but not HIV entry kinetics.
P2860
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P2860
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
description
2001 nî lūn-bûn
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2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@ast
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@en
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@nl
type
label
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@ast
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@en
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@nl
prefLabel
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@ast
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@en
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@nl
P2860
P3181
P356
P1476
Design of potent inhibitors of HIV-1 entry from the gp41 N-peptide region
@en
P2093
P2860
P304
P3181
P356
10.1073/PNAS.201392898
P407
P577
2001-09-25T00:00:00Z