The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Protein N-Glycosylation in the Baculovirus-Insect Cell System
Open accessAbstract
One of the major advantages of the baculovirus-insect cell system is that it is a eukaryotic system that can provide posttranslational modifications, such as protein N-glycosylation. However, this is a vastly oversimplified view, which reflects a poor understanding of insect glycobiology. In general, insect protein glycosylation pathways are far simpler than the corresponding pathways of higher eukaryotes. Paradoxically, it is increasingly clear that various insects encode and can express more elaborate protein glycosylation functions in restricted fashion. Thus, the information gathered in a wide variety of studies on insect protein N-glycosylation during the past 25 years has provided what now appears to be a reasonably detailed, comprehensive, and accurate understanding of the protein N-glycosylation capabilities of the baculovirus-insect cell system. In this chapter, we discuss the models of insect protein N-glycosylation that have emerged from these studies and how this impacts the use of baculovirus-insect cell systems for recombinant glycoprotein production. We also discuss the use of these models as baselines for metabolic engineering efforts leading to the development of new baculovirus-insect cell systems with humanized protein N-glycosylation pathways, which can be used to produce more authentic recombinant N-glycoproteins for drug development and other biomedical applications.
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Cites
Molecular Analysis of Commensal Host-Microbial Relationships in the Intestine
Hooper, L. V., Wong, M. H., Thelin, A., Hansson, L., Falk, P. G., & Gordon, J. I. (2001) · Science · doi:10.1126/science.291.5505.881 · Cited by 2,202
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Solá, R. J., & Griebenow, K. (2010) · BioDrugs · doi:10.2165/11530550-000000000-00000 · Cited by 440
Enzymes in the Synthesis of Glycoconjugates
Schmaltz, R. M., Hanson, S. R., & Wong, C.-H. (2011) · Chemical Reviews · doi:10.1021/cr200113w · Cited by 283
Analysis of site-specific N-glycan remodeling in the endoplasmic reticulum and the Golgi
Hang, I., Lin, C.-W., Grant, O. C., Fleurkens, S., Villiger, T. K., Soos, M., Morbidelli, M., Woods, R. J., Gauss, R., & Aebi, M. (2015) · Glycobiology · doi:10.1093/glycob/cwv058 · Cited by 67
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Zhan, J., Lin, D., Watson, N., Esser, L., Tang, W. K., Zhang, A., Liu, X., Hassan, R., Gleinich, A., Shajahan, A., et al. (2023) · Cancer Research Communications · doi:10.1158/2767-9764.crc-22-0306 · Cited by 28
Metadata
- Authors
- Shi, X., & Jarvis, D.
- Venue
- Current Drug Targets
- Publisher
- Bentham Science Publishers Ltd.
- Published
- 2007-10-01
- Volume
- 8
- Issue
- 10
- Pages
- 1116-1125
- ISSN
- 1389-4501 (ISSN-L)
- OpenAlex
- W1992271352
- Cited by
- 197
- References
- 2
- FWCI
- 1.44
- Type
- journal article
- Language
- en
- Open access
- green
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