The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
α‐Glucosidase inhibitors as potential broad based anti‐viral agents
Abstract
N‐Linked oligosaccharides play many roles in the fate and functions of glycoproteins. One function is to assist in the folding of proteins by mediating interactions of the lectin‐like chaperone proteins calnexin and calreticulin with nascent glycoproteins. These interactions can be prevented by inhibitors of the α‐glucosidases and this causes some proteins to be misfolded and retained within the endoplasmic reticulum. In human immunodeficiency virus (HIV) and hepatitis B virus (HBV) the misfolding of key viral envelope glycoproteins interferes with the viral life cycle. It has been demonstrated in an animal model of chronic HBV that glucosidase inhibitors can alter glycosylation and have anti‐viral activity. As the mechanism of action of α‐glucosidase inhibitors is the induction of misfolded or otherwise defective viral glycoproteins, such inhibitors may be useful therapeutics for many viruses, especially those which bud from the endoplasmic reticulum (where protein folding takes place). For example bovine viral diarrhea virus, a pestivirus akin to hepatitis C virus, is also extremely sensitive to glucosidase inhibition.
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Cites
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How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum.
Helenius, A. (1994) · Molecular Biology of the Cell · doi:10.1091/mbc.5.3.253 · Cited by 623
Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus
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Aminosugar derivatives as potential anti-human immunodeficiency virus agents.
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Self-citationSousa, M. C., Ferrero-Garcia, M. A., & Parodi, A. J. (1992) · Biochemistry · doi:10.1021/bi00116a015 · Cited by 319
Glycosylation inhibitors in biology and medicine
Jacob, G. S. (1995) · Current Opinion in Structural Biology · doi:10.1016/0959-440x(95)80051-4 · Cited by 278
Conformation-Independent Binding of Monoglucosylated Ribonuclease B to Calnexin
Zapun, A., Petrescu, S. M., Rudd, P. M., Dwek, R. A., Thomas, D. Y., & Bergeron, J. J. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81855-3 · Cited by 196
Self-citationSecretion of human hepatitis B virus is inhibited by the imino sugar N-butyldeoxynojirimycin.
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Cited by
Glycosylation and the Immune System
Rudd, P. M., Elliott, T., Cresswell, P., Wilson, I. A., & Dwek, R. A. (2001) · Science · doi:10.1126/science.291.5512.2370 · Cited by 1,588
Self-citationAsano, N., Nash, R. J., Molyneux, R. J., & Fleet, G. W. J. (2000) · Tetrahedron: Asymmetry · doi:10.1016/s0957-4166(00)00113-0 · Cited by 1,015
An overview on the role of bioactive α-glucosidase inhibitors in ameliorating diabetic complications
Hossain, U., Das, A. K., Ghosh, S., & Sil, P. C. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111738 · Cited by 438
Targeting glycosylation as a therapeutic approach
Dwek, R. A., Butters, T. D., Platt, F. M., & Zitzmann, N. (2002) · Nature Reviews Drug Discovery · doi:10.1038/nrd708 · Cited by 420
Self-citationSipkema, D., Franssen, M. C. R., Osinga, R., Tramper, J., & Wijffels, R. H. (2005) · Marine Biotechnology · doi:10.1007/s10126-004-0405-5 · Cited by 420
Metadata
- Authors
- Mehta, A., Zitzmann, N., Rudd, P. M., Block, T. M., & Dwek, R. A.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 1998-06-23
- Volume
- 430
- Issue
- 1-2
- Pages
- 17-22
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W1987287280
- Cited by
- 283
- References
- 21
- FWCI
- 2.81
- Type
- journal article
- Language
- en
- Open access
- closed
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- Mehta, A., Zitzmann, N., Rudd, P. M., Block, T. M., & Dwek, R. A. (1998). α‐Glucosidase inhibitors as potential broad based anti‐viral agents. FEBS Letters. https://doi.org/10.1016/s0014-5793(98)00525-0
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
