The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
about
Click chemistry in peptide-based drug designAbasic phosphorothioate oligomers inhibit HIV-1 reverse transcription and block virus transmission across polarized ectocervical organ cultures.Covalent conjugation of a peptide triazole to HIV-1 gp120 enables intramolecular binding site occupancyLytic Inactivation of Human Immunodeficiency Virus by Dual Engagement of gp120 and gp41 Domains in the Virus Env Protein Trimer.Mechanism of multivalent nanoparticle encounter with HIV-1 for potency enhancement of peptide triazole virus inactivation.Antiviral breadth and combination potential of peptide triazole HIV-1 entry inhibitors.Peptide Triazole Inactivators of HIV-1 Utilize a Conserved Two-Cavity Binding Site at the Junction of the Inner and Outer Domains of Env gp120.Disulfide Sensitivity in the Env Protein Underlies Lytic Inactivation of HIV-1 by Peptide Triazole Thiols.HIV-1 Env gp120 structural determinants for peptide triazole dual receptor site antagonism.Peptide triazole inactivators of HIV-1: how do they work and what is their potential?Impact of HIV-1 Membrane Cholesterol on Cell-Independent Lytic Inactivation and Cellular Infectivity.A model of peptide triazole entry inhibitor binding to HIV-1 gp120 and the mechanism of bridging sheet disruptionNon-natural peptide triazole antagonists of HIV-1 envelope gp120.HIV envelope: challenges and opportunities for development of entry inhibitors.10 years of click chemistry: synthesis and applications of ferrocene-derived triazoles.Chemical optimization of macrocyclic HIV-1 inactivators for improving potency and increasing the structural diversity at the triazole ring.Recognition of HIV-inactivating peptide triazoles by the recombinant soluble Env trimer, BG505 SOSIP.664.Cell-free HIV-1 virucidal action by modified peptide triazole inhibitors of Env gp120.Interactions of peptide triazole thiols with Env gp120 induce irreversible breakdown and inactivation of HIV-1 virions.Restricted HIV-1 Env Glycan Engagement by Lectin-Reengineered DAVEI Protein Chimera is sufficient for Lytic Inactivation of the Virus.Synthesis and antioxidant evaluation of enantiomerically pure bis-(1,2,3-triazolylmethyl)amino esters from modified α-amino acids.
P2860
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P2860
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
description
2010 nî lūn-bûn
@nan
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@ast
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@en
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@nl
type
label
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@ast
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@en
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@nl
prefLabel
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@ast
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@en
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@nl
P2093
P2860
P356
P1433
P1476
The active core in a triazole peptide dual-site antagonist of HIV-1 gp120.
@en
P2093
Arne Schön
Ernesto Freire
Ferit Tuzer
Irwin Chaiken
Isaac Zentner
Judith Lalonde
Karyn McFadden
Mark Contarino
Muddegowda Umashankara
Srivats Rajagopal
P2860
P304
P356
10.1002/CMDC.201000222
P577
2010-11-01T00:00:00Z