Suitable fusion of N-terminal heptad repeats to achieve covalently stabilized potent N-peptide inhibitors of HIV-1 infection-Reference-Cited by-同舟云学术

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Suitable fusion of N-terminal heptad repeats to achieve covalently stabilized potent N-peptide inhibitors of HIV-1 infection

Published:2020-02 Issue:4 Volume:28 Page:115214
ISSN:0968-0896
Container-title:Bioorganic & Medicinal Chemistry
language:en
Short-container-title:Bioorganic & Medicinal Chemistry

Author:

Lai Wenqing,Wang Chao,Yan Jun,Liu Huanliang,Zhang Wei,Lin Bencheng,Xi Zhuge

Funder

Chinese Academy of Sciences

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference30 articles.

1. Inhibition of HIV-1 by fusion inhibitors;Eggink;Curr Pharm Des,2010

2. Inhibition of HIV entry by targeting the envelope transmembrane subunit gp41;Yi;Curr HIV Res,2016

3. HIV-1 gp41-targeting fusion inhibitory peptides enhance the gp120-targeting protein-mediated inactivation of HIV-1 virions;Qi;Emerg Microbes Infect,2017

4. Biological and structural characterization of rotamers of C-C chemokine receptor type 5 (CCR5) inhibitor GSK214096;Kazmierski;ACS Med Chem Lett,2014

5. HIV-1 gp41 residues modulate CD4-induced conformational changes in the envelope glycoprotein and evolution of a relaxed conformation of gp120;Keller;J Virol,2018

Cited by 1 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Isopeptide Bond Bundling Superhelix for Designing Antivirals against Enveloped Viruses with Class I Fusion Proteins: A Review;Current Pharmaceutical Biotechnology;2023-11

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