Multibranched peptide constructs derived from the V3 loop of envelope glycoprotein gp120 inhibit human immunodeficiency virus type 1 infection through interaction with CD4-Reference-Cited by-同舟云学术

Multibranched peptide constructs derived from the V3 loop of envelope glycoprotein gp120 inhibit human immunodeficiency virus type 1 infection through interaction with CD4

Published:1995-01 Issue:1 Volume:206 Page:457-464
ISSN:0042-6822
Container-title:Virology
language:en
Short-container-title:Virology

Author:

Benjouad Abdelaziz,Chapuis Françcoise,Fenouillet Emmanuel,Gluckman Jean-Claude

Publisher

Elsevier BV

Subject

Virology

Reference44 articles.

1. Mapping the CD4 binding site for human immunodeficiency virus by alanine-scanning mutagenesis;Ashkenazi,1990

2. Binding to CD4 of synthetic peptides patterned on the principal neutralizing domain of HIV-1 envelope protein;Autiero;Virology,1991

3. The V3 region of the envelope glycoprotein of human immunodeficiency virus type 1 binds sulfated polysaccharides and CD4-derived synthetic peptides;Batinic;J. Biol. Chem.,1992

4. Multi-branched peptide constructs (MBPC) of the V3 loop of envelope glycoprotein gp120 inhibit human immunodeficiency virus-induced syncytiumformation;Benjouad;Antiviral Chem. Chemother.,1994

5. Effect of sialic acid removal on the antibody response to the third variable domain of human immunodeficiency virus type-1 envelope glycoprotein;Benjouad;FEBS Letters,1994

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