The N-Terminal of the V3 Loop in HIV Type 1 gp120 Is Responsible for Its Conformation-Dependent Interaction with Cell Surface Molecules-Reference-Cited by-同舟云学术

The N-Terminal of the V3 Loop in HIV Type 1 gp120 Is Responsible for Its Conformation-Dependent Interaction with Cell Surface Molecules

Published:2004-02 Issue:2 Volume:20 Page:213-218
ISSN:0889-2229
Container-title:AIDS Research and Human Retroviruses
language:en
Short-container-title:AIDS Research and Human Retroviruses

Author:

Ling Hong¹,Usami Osamu,Xiao Peng,Gu Hong-Xi,Hattori Toshio

Affiliation:

1. Division of Allergy and Infectious Diseases, Department of Internal Medicine, Graduate School of Medicine, Tohoku University, Aoba-ku, Sendai 980-8574, Japan

Publisher

Mary Ann Liebert Inc

Subject

Infectious Diseases,Virology,Immunology

Link

http://www.liebertpub.com/doi/pdf/10.1089/088922204773004932

Reference25 articles.

1. HIV-1 attachment: another look

2. CHEMOKINE RECEPTORS AS HIV-1 CORECEPTORS: Roles in Viral Entry, Tropism, and Disease

3. Characterization of V3 Loop-Binding Protein(s) of Molt-4 and U937 Cells

4. Applications of biotinylated V3 loop peptides of human immunodeficiency virus type 1 to flow cytometric analyses and affinity chromatographic techniques

5. T-cell Membrane-Associated Serine Protease, Tryptase TL2, Binds Human Immunodeficiency Virus Type 1 gp120 and Cleaves the Third-Variable-Domain Loop of gp120. Neutralizing Antibodies of Human Immunodeficiency Virus Type 1 Inhibit Cleavage of gp120

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