NMR and CD studies on the conformation of a synthetic peptide containing epitopes of the human immunodeficiency virus 1 transmembrane protein gp41
- 1 March 1996
- journal article
- Published by Wiley in Biopolymers
- Vol. 38 (3) , 423-435
- https://doi.org/10.1002/(sici)1097-0282(199603)38:3<423::aid-bip13>3.0.co;2-d
Abstract
No abstract availableKeywords
This publication has 31 references indexed in Scilit:
- Identification of Human Immunodeficiency Virus Type 1 Glycoprotein gp120/gp41 Interacting Sites by the Idiotypic Mimicry of Two Monoclonal AntibodiesAIDS Research and Human Retroviruses, 1993
- A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition.Proceedings of the National Academy of Sciences, 1992
- HIV-1 gp41 contains two sites for interaction with several proteins on the helper T-lymphoid cell line, H9AIDS, 1992
- Human immunodeficiency virus type 1 activates the classical pathway of complement by direct C1 binding through specific sites in the transmembrane glycoprotein gp41.The Journal of Experimental Medicine, 1991
- Characterization of a putative cellular receptor for HIV-1 transmembrane glycoprotein using synthetic peptidesAIDS, 1990
- Oligomeric structure of the human immunodeficiency virus type 1 envelope glycoprotein.Proceedings of the National Academy of Sciences, 1990
- Internalization of the human immunodeficiency virus does not require the cytoplasmic domain of CD4Nature, 1988
- Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virusCell, 1988
- Functional Regions of the Envelope Glycoprotein of Human Immunodeficiency Virus Type 1Science, 1987
- Delineation of a region of the human immunodeficiency virus type 1 gp120 glycoprotein critical for interaction with the CD4 receptorCell, 1987