The hyperglycosylation of HIV envelope: An opportunity to alter virus infectivity?
- 1 December 1996
- journal article
- research article
- Published by Springer Nature in Perspectives in Drug Discovery and Design
- Vol. 5 (1) , 203-212
- https://doi.org/10.1007/bf02174015
Abstract
No abstract availableKeywords
This publication has 55 references indexed in Scilit:
- Glycosylation and stability of mature HIV envelope glycoprotein conformation under various conditionsFEBS Letters, 1996
- Identification of three N-linked glycans in the V4–V5 region of HIV-1 gp 120, dispensable for CD4-binding and fusion activity of gp 120Archiv für die gesamte Virusforschung, 1994
- Deletion of a single N-linked glycosylation site from the transmembrane envelope protein of human immunodeficiency virus type 1 stops cleavage and transport of gp160 preventing env-mediated fusionJournal of General Virology, 1994
- An O-linked carbohydrate neutralization epitope of HIV-1 gp 120 is expressed by HIV-1env gene recombinant vaccinia virusArchiv für die gesamte Virusforschung, 1992
- Mutation of conserved N-glycosylation sites around the CD4-binding site of human immunodeficiency virus type 1 GP120 affects viral infectivityVirus Research, 1990
- Expression of HIV-1 gp120 and Human Soluble CD4 by Recombinant Baculoviruses and their Interaction In VitroAIDS Research and Human Retroviruses, 1990
- A General Model for the Transmembrane Proteins of HIV and Other RetrovirusesAIDS Research and Human Retroviruses, 1989
- Role of N-linked glycans in the interaction between the envelope glycoprotein of human immunodeficiency virus and its CD4 cellular receptor. Structural enzymatic analysis.The Journal of Experimental Medicine, 1989
- INHIBITORS OF THE BIOSYNTHESIS AND PROCESSING OF N-LINKED OLIGOSACCHARIDE CHAINSAnnual Review of Biochemistry, 1987
- Spatial conformation of glycans and glycoproteinsBiology of the Cell, 1984