Structural requirements for and consequences of an antiviral porphyrin binding to the V3 loop of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp120-Reference-Cited by-同舟云学术

Structural requirements for and consequences of an antiviral porphyrin binding to the V3 loop of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp120

Published:1995-11 Issue:6 Volume:8 Page:345-357
ISSN:0952-3499
Container-title:Journal of Molecular Recognition
language:en
Short-container-title:J. Mol. Recognit.

Author:

Neurath A. Robert,Strick Nathan,Debnath Asim K.

Publisher

Wiley

Subject

Molecular Biology,Structural Biology

Reference76 articles.

1. Two groups of rhinoviruses revealed by a panel of antiviral compounds present sequence divergence and differential pathogenicity

2. Target cell-specific determinants of membrane fusion within the human immunodeficiency virus type 1 gp120 third variable region and gp41 amino terminus

3. Equilibrium and kinetic studies of the aggregation of porphyrins in aqueous solution

4. Binding of Human Immunodeficiency Virus Type I (HIV-1) Gp120 to Galactosylceramide (GalCer): Relationship to the V3 Loop

5. Rat monoclonal antibodies to nonoverlapping epitopes of human immunodeficiency virus type 1 gp120 block CD4 binding in Vitro

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