The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
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HIV-1 envelope glycoprotein structureRational improvement of gp41-targeting HIV-1 fusion inhibitors: an innovatively designed Ile-Asp-Leu tail with alternative conformations.Molecular dynamics studies of the inhibitor C34 binding to the wild-type and mutant HIV-1 gp41: inhibitory and drug resistant mechanismImproved Pharmacological and Structural Properties of HIV Fusion Inhibitor AP3 over Enfuvirtide: Highlighting Advantages of Artificial Peptide StrategyTwo M-T hook residues greatly improve the antiviral activity and resistance profile of the HIV-1 fusion inhibitor SC29EK.Mechanism of HIV-1 Resistance to Short-Peptide Fusion Inhibitors Targeting the Gp41 PocketGenetic Pathway of HIV-1 Resistance to Novel Fusion Inhibitors Targeting the Gp41 Pocket.A Helical Short-Peptide Fusion Inhibitor with Highly Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus.Escape from human immunodeficiency virus type 1 (HIV-1) entry inhibitors.Peptide fusion inhibitors targeting the HIV-1 gp41: a patent review (2009 - 2014).Enfuvirtide (T20)-Based Lipopeptide Is a Potent HIV-1 Cell Fusion Inhibitor: Implications for Viral Entry and Inhibition.A Lipopeptide HIV-1/2 Fusion Inhibitor with Highly Potent In Vitro, Ex Vivo, and In Vivo Antiviral Activity.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.Glycosyl Phosphatidylinositol-Anchored C34 Peptide Derived From Human Immunodeficiency Virus Type 1 Gp41 Is a Potent Entry Inhibitor.The M-T hook structure increases the potency of HIV-1 fusion inhibitor sifuvirtide and overcomes drug resistance.Efficient Fusion at Neutral pH by Human Immunodeficiency Virus gp41 Trimers containing the Fusion Peptide and Transmembrane Domain.Mechanism of HIV-1 Resistance to an Electronically Constrained α-Helical Peptide Membrane Fusion Inhibitor.Structural Insights into the Mechanisms of Action of Short-Peptide HIV-1 Fusion Inhibitors Targeting the Gp41 Pocket.Structural and Functional Characterization of Membrane Fusion Inhibitors with Extremely Potent Activity against Human Immunodeficiency Virus Type 1 (HIV-1), HIV-2, and Simian Immunodeficiency Virus
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P2860
The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
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2012 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
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2012 թվականի հոտեմբերին հրատարակված գիտական հոդված
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年論文
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2012年论文
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The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
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The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
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The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
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The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
@ast
The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
@en
The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
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The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
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The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
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The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
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P2093
P2860
P3181
P356
P1476
The M-T Hook Structure Is Critical for Design of HIV-1 Fusion Inhibitors
@en
P2093
Huihui Chong
Jianping Sun
Meitian Wang
Meng Zhang
Sandro Waltersperger
Zonglin Qiu
P2860
P304
P3181
P356
10.1074/JBC.M112.390393
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P50
P577
2012-10-05T00:00:00Z