A salt bridge between an N-terminal coiled coil of gp41 and an antiviral agent targeted to the gp41 core is important for anti-HIV-1 activity
about
Pharmacological inhibition of feline immunodeficiency virus (FIV)Binding of a potent small-molecule inhibitor of six-helix bundle formation requires interactions with both heptad-repeats of the RSV fusion proteinThe adaptor protein CIN85 assembles intracellular signaling clusters for B cell activationN-substituted pyrrole derivatives as novel human immunodeficiency virus type 1 entry inhibitors that interfere with the gp41 six-helix bundle formation and block virus fusion.A novel fluorescence intensity screening assay identifies new low-molecular-weight inhibitors of the gp41 coiled-coil domain of human immunodeficiency virus type 1ADS-J1 inhibits HIV-1 entry by interacting with gp120 and does not block fusion-active gp41 core formation.Covalent fusion inhibitors targeting HIV-1 gp41 deep pocket.NMR-assisted computational studies of peptidomimetic inhibitors bound in the hydrophobic pocket of HIV-1 glycoprotein 41.Footprint-based identification of viral entry inhibitors targeting HIVgp41.Filling the hole: evidence of a small molecule binding to the fusion core pocket in human respiratory syncytial virus.Progress in identifying peptides and small-molecule inhibitors targeted to gp41 of HIV-1.Rationally designed anti-HIV peptides containing multifunctional domains as molecule probes for studying the mechanisms of action of the first and second generation HIV fusion inhibitors.Design, synthesis, and biological evaluation of N-carboxyphenylpyrrole derivatives as potent HIV fusion inhibitors targeting gp41Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.Targeting a binding pocket within the trimer-of-hairpins: small-molecule inhibition of viral fusion.Small molecule HIV entry inhibitors: Part II. Attachment and fusion inhibitors: 2004-2010.Structure-activity relationship studies of indole-based compounds as small molecule HIV-1 fusion inhibitors targeting glycoprotein 41.Development of indole compounds as small molecule fusion inhibitors targeting HIV-1 glycoprotein-41.ADS-J1 inhibits human immunodeficiency virus type 1 entry by interacting with the gp41 pocket region and blocking fusion-active gp41 core formation.The role of amphiphilicity and negative charge in glycoprotein 41 interactions in the hydrophobic pocket.Design of highly potent HIV fusion inhibitors based on artificial peptide sequences.Conserved residue Lys574 in the cavity of HIV-1 Gp41 coiled-coil domain is critical for six-helix bundle stability and virus entry.Precisely Designed Isopeptide Bridge-Crosslinking Endows Artificial Hydrolases with High Stability and Catalytic Activity under Extreme Denaturing Conditions.
P2860
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P2860
A salt bridge between an N-terminal coiled coil of gp41 and an antiviral agent targeted to the gp41 core is important for anti-HIV-1 activity
description
2000 nî lūn-bûn
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2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
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2000 թվականի ապրիլին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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name
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@ast
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@en
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@nl
type
label
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@ast
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@en
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@nl
prefLabel
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@ast
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@en
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@nl
P356
P1476
A salt bridge between an N-ter ...... ortant for anti-HIV-1 activity
@en
P2093
P356
10.1006/BBRC.2000.2411
P407
P577
2000-04-02T00:00:00Z