The DOI matches its Crossref record; 90 of the 90 references it cites were found in a registry or an index.
Production of Recombinant Proteins: Challenges and Solutions
Abstract
Efficient strategies for the production of recombinant proteins are gaining increasing importance, as more applications that require high amounts of high-quality proteins reach the market. Higher production efficiencies and, consequently, lower costs of the final product are needed for obtaining a commercially viable process. In this chapter, common problems in recombinant protein production are reviewed and strategies for their solution are discussed. Such strategies include molecular biology techniques, as well as manipulation of the culture environment. Finally, specific problems relevant to different hosts are discussed.
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Cites
Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., & Tuschl, T. (2001) · Nature · doi:10.1038/35078107 · Cited by 9,456
Heterologous protein expression in the methylotrophic yeast Pichia pastoris
Cereghino, J. (2000) · FEMS Microbiology Reviews · doi:10.1016/s0168-6445(99)00029-7 · Cited by 2,039
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,921
Recombinant protein expression in Escherichia coli
Baneyx, F. (1999) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(99)00003-8 · Cited by 1,481
Strategies for achieving high-level expression of genes in Escherichia coli
Makrides, S. C. (1996) · Microbiological Reviews · doi:10.1128/mmbr.60.3.512-538.1996 · Cited by 1,276
RNA interference by expression of short-interfering RNAs and hairpin RNAs in mammalian cells
Yu, J.-Y., DeRuiter, S. L., & Turner, D. L. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092143499 · Cited by 1,039
NAKAYAMA, K. (1997) · Biochemical Journal · doi:10.1042/bj3270625 · Cited by 789
Fire, A. (1999) · Trends in Genetics · doi:10.1016/s0168-9525(99)01818-1 · Cited by 625
Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris
Cereghino, G. P. L., Cereghino, J. L., Ilgen, C., & Cregg, J. M. (2002) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(02)00330-0 · Cited by 602
Davis, B. G. (2002) · Chemical Reviews · doi:10.1021/cr0004310 · Cited by 521
Cited by
Recombinant protein expression in Escherichia coli: advances and challenges
Rosano, G. L., & Ceccarelli, E. A. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00172 · Cited by 2,556
Costa, S., Almeida, A., Castro, A., & Domingues, L. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00063 · Cited by 450
Engineering of protein secretion in yeast: strategies and impact on protein production
Idiris, A., Tohda, H., Kumagai, H., & Takegawa, K. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2447-0 · Cited by 324
mRNA-based therapeutics: looking beyond COVID-19 vaccines
Parhiz, H., Atochina-Vasserman, E. N., & Weissman, D. (2024) · The Lancet · doi:10.1016/s0140-6736(23)02444-3 · Cited by 279
New baculovirus expression tools for recombinant protein complex production
Trowitzsch, S., Bieniossek, C., Nie, Y., Garzoni, F., & Berger, I. (2010) · Journal of Structural Biology · doi:10.1016/j.jsb.2010.02.010 · Cited by 224
Metadata
- Authors
- Palomares, L. A., Estrada-Mondaca, S., & Ramírez, O. T.
- Venue
- Recombinant Gene Expression
- Publisher
- Humana Press
- Published
- 2004-07-21
- Volume
- 267
- Pages
- 015-052
- OpenAlex
- W2422187119
- Cited by
- 256
- References
- 90
- FWCI
- 14.42
- Type
- book chapter
- Language
- en
- Open access
- closed
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- Palomares, L. A., Estrada-Mondaca, S., & Ramírez, O. T. (2004). Production of Recombinant Proteins: Challenges and Solutions. Recombinant Gene Expression. https://doi.org/10.1385/1-59259-774-2%3A015
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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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