Analysis of the C-Terminal Membrane Anchor Domains of Hepatitis C Virus Glycoproteins E1 and E2: toward a Topological Model
Author:
Affiliation:
1. Centre de Biophysique Moléculaire Numérique, Faculté Universitaire des Sciences Agronomiques de Gembloux, B-5030 Gembloux
2. Innogenetics, B-9052 Ghent, Belgium
Abstract
Publisher
American Society for Microbiology
Subject
Virology,Insect Science,Immunology,Microbiology
Link
https://journals.asm.org/doi/pdf/10.1128/JVI.76.4.1944-1958.2002
Reference62 articles.
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2. Alter, M. J., S. C. Hadler, F. N. Judson, A. Mares, W. J. Alexander, P. Y. Hu, J. K. Miller, L. A. Moyer, H. A. Fields, and D. W. Bradley. 1990. Risk factors for acute non-A, non-B hepatitis in the United States and association with hepatitis C virus infection. JAMA 264 : 2231-2235.
3. Arunkumar, A. I., T. K. Kumar, G. Jayaraman, D. Samuel, and C. Yu. 1996. Induction of helical conformation in all beta-sheet proteins by trifluoroethanol. J. Biomol. Struct. Dyn. 14 : 381-385.
4. Bonifacino, J. S., P. Cosson, N. Shah, and R. D. Klausner. 1991. Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum. EMBO J. 10 : 2783-2793.
5. Brasseur, R. 1990. TAMMO: theoretical analysis of membrane molecular organization, p. 203-219. In R. Brasseur (ed.), Molecular description of biological membrane components by computer-aided conformational analysis. CRC Press, Boca Raton, Fla.
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