Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency.
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Inhibition of the Hantavirus Fusion Process by Predicted Domain III and Stem Peptides from Glycoprotein GcMeasles Virus Fusion Protein: Structure, Function and InhibitionHedgehog Cholesterolysis: Specialized Gatekeeper to Oncogenic SignalingProtease-resistant peptide design-empowering nature's fragile warriors against HIVRational improvement of gp41-targeting HIV-1 fusion inhibitors: an innovatively designed Ile-Asp-Leu tail with alternative conformations.The M-T Hook Structure Is Critical for Design of HIV-1 Fusion InhibitorsStructure-based discovery of Middle East respiratory syndrome coronavirus fusion inhibitorAsymmetric deactivation of HIV-1 gp41 following fusion inhibitor bindingHIV-1 fusion inhibitor peptides enfuvirtide and T-1249 interact with erythrocyte and lymphocyte membranesConjugation of cholesterol to HIV-1 fusion inhibitor C34 increases peptide-membrane interactions potentiating its actionA general strategy to endow natural fusion-protein-derived peptides with potent antiviral activityFatal measles virus infection prevented by brain-penetrant fusion inhibitors.The Membrane-Proximal Region of C-C Chemokine Receptor Type 5 Participates in the Infection of HIV-1.Developing a Bayesian adaptive design for a phase I clinical trial: a case study for a novel HIV treatment.Inhibition of Nipah virus infection in vivo: targeting an early stage of paramyxovirus fusion activation during viral entryEarly and late HIV-1 membrane fusion events are impaired by sphinganine lipidated peptides that target the fusion site.Viral entry inhibitors targeted to the membrane site of action.Discovery of entry inhibitors for HIV-1 via a new de novo protein design framework.Biophysical property and broad anti-HIV activity of albuvirtide, a 3-maleimimidopropionic acid-modified peptide fusion inhibitor.Internalization of p53(14-29) peptide amphiphiles and subsequent endosomal disruption results in SJSA-1 cell death.Inhibition of HIV Entry by Targeting the Envelope Transmembrane Subunit gp41.Enhanced potency of bivalent small molecule gp41 inhibitors.Circulating clinical strains of human parainfluenza virus reveal viral entry requirements for in vivo infection.Dramatic potentiation of the antiviral activity of HIV antibodies by cholesterol conjugation.Inhibition of Ebola virus entry by a C-peptide targeted to endosomes.Biochemistry and biophysics of HIV-1 gp41 - membrane interactions and implications for HIV-1 envelope protein mediated viral-cell fusion and fusion inhibitor designCapturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide, a new antiviral strategy for influenza virus.Targeting HIV-1 gp41-induced fusion and pathogenesis for anti-viral therapyIn vitro activities of candidate microbicides against cell-associated HIVSmall lipidated anti-obesity compounds derived from neuromedin U.Preclinical evaluation of the HIV-1 fusion inhibitor L'644 as a potential candidate microbicideSwapped-domain constructs of the glycoprotein-41 ectodomain are potent inhibitors of HIV infectionThe Cholestanol-Conjugated Sulfated Oligosaccharide PG545 Disrupts the Lipid Envelope of Herpes Simplex Virus Particles.A cholesterol tag at the N terminus of the relatively broad-spectrum fusion inhibitory peptide targets an earlier stage of fusion glycoprotein activation and increases the peptide's antiviral potency in vivo.Conformational properties of peptides corresponding to the ebolavirus GP2 membrane-proximal external region in the presence of micelle-forming surfactants and lipids.C-peptide inhibitors of Ebola virus glycoprotein-mediated cell entry: effects of conjugation to cholesterol and side chain-side chain crosslinkingPeptides in the treatment of AIDS.Improvement of HIV fusion inhibitor C34 efficacy by membrane anchoring and enhanced exposure.Broad spectrum antiviral activity for paramyxoviruses is modulated by biophysical properties of fusion inhibitory peptides.Insights into the mechanism of HIV-1 envelope induced membrane fusion as revealed by its inhibitory peptides.
P2860
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P2860
Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 18 March 2009
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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Addition of a cholesterol grou ...... creases its antiviral potency.
@en
Addition of a cholesterol grou ...... creases its antiviral potency.
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label
Addition of a cholesterol grou ...... creases its antiviral potency.
@en
Addition of a cholesterol grou ...... creases its antiviral potency.
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Addition of a cholesterol grou ...... creases its antiviral potency.
@en
Addition of a cholesterol grou ...... creases its antiviral potency.
@nl
P2093
P2860
P356
P1476
Addition of a cholesterol grou ...... creases its antiviral potency.
@en
P2093
Antonello Pessi
Elisabetta Bianchi
Fabio Bonelli
John P Moore
Maria Veneziano
Michael D Miller
Neal A Ladwa
Paolo Ingallinella
Renee Hrin
Thomas J Ketas
P2860
P304
P356
10.1073/PNAS.0901007106
P407
P577
2009-03-18T00:00:00Z