Tryptophan 375 stabilizes the outer-domain core of gp120 for HIV vaccine immunogen design-Reference-Cited by-同舟云学术

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Tryptophan 375 stabilizes the outer-domain core of gp120 for HIV vaccine immunogen design

Published:2017-05 Issue:23 Volume:35 Page:3067-3075
ISSN:0264-410X
Container-title:Vaccine
language:en
Short-container-title:Vaccine

Author:

Hu Duoyi,Bowder Dane,Wei Wenzhong,Thompson Jesse,Wilson Mark A.,Xiang Shi-Hua

Funder

Bill and Melinda Gates Foundation

NCV Seed

ARD Strategic

Publisher

Elsevier BV

Subject

Infectious Diseases,Public Health, Environmental and Occupational Health,General Veterinary,General Immunology and Microbiology,Molecular Medicine

Reference35 articles.

1. Broad HIV-1 neutralization mediated by CD4-binding site antibodies;Li;Nat Med,2007

2. Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120;Chen;Science,2009

3. Rational design of envelope identifies broadly neutralizing human monoclonal antibodies to HIV-1;Wu;Science,2010

4. Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing;Wu;Science,2011

5. PGV04, an HIV-1 gp120 CD4 binding site antibody, is broad and potent in neutralization but does not induce conformational changes characteristic of CD4;Falkowska;J Virol,2012

Cited by 3 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. Identification of a Novel Antiviral Lectin Against Sars-Cov-2 Omicron Variant from Shiitake Mushroom-Derived Vesicle-Like Nanoparticles;2024

2. Design, display and immunogenicity of HIV1 gp120 fragment immunogens on virus-like particles;Vaccine;2018-10

3. Bacterially expressed HIV-1 gp120 outer-domain fragment immunogens with improved stability and affinity for CD4-binding site neutralizing antibodies;Journal of Biological Chemistry;2018-09

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