The DOI matches its Crossref record; 65 of the 65 references it cites were found in a registry or an index.
Glycoprotein biosynthesis in yeast
Abstract
Many proteins in the yeast Saccharomyces cerevisiae are modified by the attachment of N‐linked saccharides to asparagine, of O ‐linked mannose glycans to serine or threonine, and of glycosylphosphoinositol membrane anchors. The biosynthetic events leading to these modifications are coupled to the secretory pathway. Early stages of N ‐linked glycosylation and the formation of glycosylphosphoinositol anchors have been conserved through evolution of eukaryotes. Studies of yeast offer a variety of genetic and molecular biological approaches, which have led to the isolation of different glycosylation mutants and of genes for enzymes involved in glycosylation. Yeast mutants are useful to identify biosynthetic intermediates, to establish whether a given enzyme is essential for viability, and to determine how cellular functions are affected when glycosylation is perturbed. Yeast glycosylation mutants and genes can be used to identify their counterparts in other eukaryotes.—Herscovics, A.; Orlean, P. Glycoprotein biosynthesis in yeast. FASEB J. 7 : 540‐550; 1993.
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Citations
Cites
Guide to Yeast Genetics and Molecular Biology
Kurtzman, C. P., Guthrie, C., & Fink, G. R. (1993) · Mycologia · doi:10.2307/3760517 · Cited by 2,363
Chien, C. T., Bartel, P. L., Sternglanz, R., & Fields, S. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.21.9578 · Cited by 1,492
Chitinase is required for cell separation during growth of Saccharomyces cerevisiae.
Kuranda, M. J., & Robbins, P. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55057-2 · Cited by 591
PROTEIN GLYCOSYLATION IN YEAST
Kukuruzinska, M. A., Bergh, M. L. E., & Jackson, B. J. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.004411 · Cited by 445
Antebi, A., & Fink, G. R. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.6.633 · Cited by 443
Glycosylation and processing of prepro-α-factor through the yeast secretory pathway
Julius, D., Schekman, R., & Thorner, J. (1984) · Cell · doi:10.1016/0092-8674(84)90224-1 · Cited by 410
Protein glycosylation in yeast
Tanner, W., & Lehle, L. (1987) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(87)90006-2 · Cited by 336
Kelleher, D. J., Kreibich, G., & Gilmore, R. (1992) · Cell · doi:10.1016/0092-8674(92)90118-v · Cited by 285
Saunier, B., Kilker, R. D., Tkacz, J. S., Quaroni, A., & Herscovics, A. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45358-1 · Cited by 283
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Cited by
Concepts and Principles of O-Linked Glycosylation
Steen, P. V. D., Rudd, P. M., Dwek, R. A., & Opdenakker, G. (1998) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409239891204198 · Cited by 760
Daly, R., & Hearn, M. T. W. (2005) · Journal of Molecular Recognition · doi:10.1002/jmr.687 · Cited by 746
Getting the glycosylation right: Implications for the biotechnology industry
Jenkins, N., Parekh, R. B., & James, D. C. (1996) · Nature Biotechnology · doi:10.1038/nbt0896-975 · Cited by 458
Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast.
Knop, M., Finger, A., Braun, T., Hellmuth, K., & Wolf, D. H. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00411.x · Cited by 388
Jakob, C. A., Burda, P., Roth, J., & Aebi, M. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.142.5.1223 · Cited by 338
Metadata
- Authors
- Herscovics, A., & Orlean, P.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1993-04
- Volume
- 7
- Issue
- 6
- Pages
- 540-550
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2119388326
- Cited by
- 517
- References
- 65
- FWCI
- 11.49
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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