The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
Inhibition of formation of complex oligosaccharides by the glucosidase inhibitor bromoconduritol
Open accessAbstract
The alpha-glucosidase inhibitor bromoconduritol (6-bromo-3,4,5-trihydroxycyclohex-1-ene) inhibits trimming of the innermost glucose residue from the Glc3Man9GlcNAc2 precursor of high-mannose and complex oligosaccharides. This inhibition occurs both in intact cells and with a microsomal enzyme preparation. The formation of lipid-linked oligosaccharides was increased in glucosidase-inhibited cells. Inhibition of transfer of high-mannose oligosaccharides to protein was not observed. In bromoconduritol-treated virus-infected cells, trimming of mannose can occur despite incomplete removal of glucose. The glucosylated high-mannose oligosaccharides GlcMan9GlcNAc, GlcMan8GlcNAc, and GlcMan7GlcNAc were released from viral glycoproteins after digestion with Pronase and endo-beta-N-acetylglucosaminidase H. The formation of complex oligosaccharides was concomitantly inhibited. The release of infectious fowl plague virus particles (an influenza virus) was inhibited from bromoconduritol-treated infected chicken-embryo cells.
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“Finally, Bromoconduritol (6-bromo-3,4,5-trihydroxycyclohex-1-ene) inhibits the removal of the innermost α1,3-linked glucose residue from Glc2Man9GlcNAc2, leading to the accumulation of unprocessed high-mannose N-glycans in treated cells [378].”
From GANAB and N-Glycans Substrates Are Relevant in Human Physiology, Polycystic Pathology and Multiple Sclerosis: A Review (2022) · cites this paper as [378]
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Cites
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The role of lipid intermediates in the glycosylation of proteins in the eucaryotic cell
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Swainsonine: an inhibitor of glycoprotein processing.
Elbein, A. D., Solf, R., Dorling, P. R., & Vosbeck, K. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.12.7393 · Cited by 255
Schwarz, R. Τ., Rohrschneider, J. M., & Schmidt, M. F. G. (1976) · Journal of Virology · doi:10.1128/jvi.19.3.782-791.1976 · Cited by 253
Self-citationBeyer, T. A., Sadler, J. E., Rearick, J. I., Paulson, J. C., & Hill, R. L. (1981) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122976.ch2 · Cited by 227
Schwarz, R. Τ., & DATEMA, R. (1982) · Advances in carbohydrate chemistry and biochemistry · doi:10.1016/s0065-2318(08)60111-0 · Cited by 177
Self-citationPHYSICAL AND BIOLOGICAL PROPERTIES OF INFLUENZA VIRUS COMPONENTS OBTAINED AFTER ETHER TREATMENT
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Self-citationProcessing of carbohydrate units of glycoproteins. Characterization of a thyroid glucosidase.
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Cited by
Pelletier, M. F., Marcil, A., Sevigny, G., Jakob, C. A., Tessier, D. C., Chevet, E., Menard, R., Bergeron, J. J. M., & Thomas, D. Y. (2000) · Glycobiology · doi:10.1093/glycob/10.8.815 · Cited by 123
Parodi, A. J., Mendelzon, D. H., Lederkremer, G. Z., & Martin-Barrientos, J. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)82148-6 · Cited by 88
De Masi, R., & Orlando, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137373 · Cited by 20
“Finally, Bromoconduritol (6-bromo-3,4,5-trihydroxycyclohex-1-ene) inhibits the removal of the innermost α1,3-linked glucose residue from Glc2Man9GlcNAc2, leading to the accumulation of unprocessed high-mannose N-glycans in treated cells [378].”
Background
Metadata
- Authors
- Datema, R., Romero, P. A., Legler, G., & Schwarz, R. T.
- ORCID
- Romero, P A
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1982-11
- Volume
- 79
- Issue
- 22
- Pages
- 6787-6791
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC347218
- OpenAlex
- W2039308658
- Cited by
- 84
- References
- 17
- Citations by year
- 2024: 1 · 2023: 1 · 2022: 2 · 2021: 1 · 2019: 1 · 2015: 1 · 2014: 1 · 2013: 2
- FWCI
- 3.91
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glycosylation and Glycoproteins Research
- Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- α-glucosidase inhibition, high-mannose oligosaccharides, N-glycosylation, lipid-linked oligosaccharides, viral glycoproteins, influenza virus, fowl plague virus, chicken embryo cells
- MeSH terms
- Animals, Carbohydrate Conformation, Cell Transformation, Viral, Cells, Cultured, Chick Embryo, Glucosidases, Glycoproteins, Inositol, Kinetics, Oligosaccharides, Orthomyxoviridae, Influenza A virus, Cyclohexenes, Glycoside Hydrolase Inhibitors
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