Activation of gp120 of human immunodeficiency virus by their V3 loop-derived peptides
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference36 articles.
1. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens;Wyatt;Science,1998
2. Direct measurement of soluble CD4 binding to human immunodeficiency virus type 1 virions: gp120 dissociation and its implications for virus-cell binding and fusion reactions and their neutralization by soluble CD4;Moore;J. Virol.,1991
3. Enhancement of human immunodeficiency virus type 1 infection by antisera to peptides from the envelope glycoproteins gp120/gp41;Jiang;J. Exp. Med.,1991
4. Receptor-mediated activation of immunodeficiency viruses in viral fusion;Allan;Science,1991
5. Primary isolates of human immunodeficiency virus type1 are relatively resistant to neutralization by monoclonal antibodies to gp120, and their neutralization is not predicted by studies with monomeric gp120;Moore;J. Virol.,1995
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. Critical Amino Acids within the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein V4 N- and C-Terminals Contribute to Virus Entry;PLoS ONE;2014-01-21
2. Thrombin activates envelope glycoproteins of HIV type 1 and enhances fusion;Microbes and Infection;2004-04
3. The N-Terminal of the V3 Loop in HIV Type 1 gp120 Is Responsible for Its Conformation-Dependent Interaction with Cell Surface Molecules;AIDS Research and Human Retroviruses;2004-02
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