The DOI matches its Crossref record; 40 of the 41 references it cites were found in a registry or an index.
Applications of yeast in biotechnology: protein production and genetic analysis
Abstract
Improvements in yeast expression systems, coupled with the development of yeast surface display and refinements in two-hybrid methodology, are expanding the role of yeasts in the process of understanding and engineering eukaryotic proteins.
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“Numerous cases of superficial or mild systemic infections caused by Saccharomyces cerevisiae, a yeast”
In the citing paper
“From another point of view, yeasts isolates currently in use for industrial or biotechnological processes may be potentially pathogenic.20,26,34”
Citations
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Yeast surface display for screening combinatorial polypeptide libraries
Boder, E. T., & Wittrup, K. D. (1997) · Nature Biotechnology · doi:10.1038/nbt0697-553 · Cited by 1,774
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Self-citationExpression of thelacZgene from two methanol-regulated promoters inPichia pastoris
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Self-citation[25] Yeast surface display for directed evolution of protein expression, affinity, and stability
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Advances in the use of Pichia pastoris for high-level gene expression
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Research works printed but not linked: 1
- Lin Cereghino, 1999, Expression of heterologous proteins in the methylotrophic yeast Pichia pastoris, FEMS Microbiol Rev
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Bioprocess Engineering of Pichia pastoris, an Exciting Host Eukaryotic Cell Expression System
Valero, F. (2013) · InTech eBooks · doi:10.5772/56407 · Cited by 7
“(SIBIA, La Jolla, Ca, USA) used Pichia as a host system for heterologous protein expression [22-24].”
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Padan, E., Hunte, C., & Reiländer, H. (2003) · Elsevier eBooks · doi:10.1016/b978-012361776-7/50004-8 · Cited by 7
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“coli is an effective host for the mass production of recombinant protein, but for future applications of recombinant sporamin in agricultural, medical or health-care markets, and also for eukaryotespecific post-modification, Saccharomyces cerevisiae would be a preferred host [7,8].”
Backgroundvan Noort, D. (2016) · Wiley eBooks · doi:10.1002/9783527683369.ch3 · Cited by 7
Effects of methanol on expression of an anticoagulant hirudin in recombinant Hansenula polymorpha
Kim, M.-D., Kang, H.-A., Rhee, S. K., & Seo, J.-H. (2001) · Journal of Industrial Microbiology & Biotechnology · doi:10.1038/sj.jim.7000163 · Cited by 6
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Brunauer, G., Oliver Spadiut, A., Alfred, G., & Slouka, C. (2020) · Chemosensors · doi:10.3390/chemosensors8020027 · Cited by 5
DNA-ENCODED PEPTIDE LIBRARIES AND DRUG DISCOVERY
Sidhu, S. S., & Weiss, G. A. (2002) · Elsevier eBooks · doi:10.1016/b978-012072651-6/50014-0 · Cited by 5
Hu, Y., Bai, R., Dou, S., Wu, Z., Abdulkhani, A., Asadollahi, M. A., Abomohra, A., & Sun, F. F. (2022) · Systems Microbiology and Biomanufacturing · doi:10.1007/s43393-021-00071-7 · Cited by 5
“pastoris would be more amenable for the production of heterologous cellulases [16].”
BackgroundLe, H. H. M., Vang, D., Amer, N., Vue, T. Y., Yee, C., Kaou, H., Harrison, J. S., Xiao, N., Cereghino, J. L., Lin‐Cereghino, G. P., et al. (2020) · Protein Expression and Purification · doi:10.1016/j.pep.2020.105724 · Cited by 4
Quintero, J. S., Rojas, H. Y. T., González, J., Espejo-Mojica, A. J., Alméciga-Díaz, C. J., & Gutiérrez, M. F. (2023) · BMC Veterinary Research · doi:10.1186/s12917-023-03590-8 · Cited by 4
Brunauer, G. (2021) · Biomedical Journal of Scientific & Technical Research · doi:10.26717/bjstr.2021.35.005682 · Cited by 4
“The model organism for the application of AC measurements in the ß-dispersion range is yeast, it being a very important expression host for recombinant proteins [15-17] and of high interest because of its meaningfulness.”
BackgroundProduction of selenomethionine labeled polyglycine hydrolases in Pichia pastoris
Naumann, T. A., Sollenberger, K. G., & Hao, G. (2022) · Protein Expression and Purification · doi:10.1016/j.pep.2022.106076 · Cited by 4
Kallas, Å. (2006) · KTH Publication Database DiVA (KTH Royal Institute of Technology) · Cited by 4
Müller, N. (2005) · Cited by 3
The evolution of type 1 diabetes mellitus care
Bulgakova, S. V., Dolgikh, Y. A., Sharonova, L. A., Kosareva, O. V., Treneva, E. V., Kurmaev, D. P., Lebedeva, E. A., & Galkin, R. A. (2023) · Endocrinology News Opinions Training · doi:10.33029/2304-9529-2023-12-3-46-53 · Cited by 2
Irshad, B., Lu, C., Nederstigt, A. E., Hu, P., Xue, L., Cereghino, J. L., Franz, A. H., Harrison, J. S., & Lin‐Cereghino, G. P. (2023) · Protein Expression and Purification · doi:10.1016/j.pep.2023.106355 · Cited by 2
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Verbovoy, A. F., Dolgikh, Y. A., Verbovaya, N. I., & Galkin, R. A. (2022) · Endocrinology News Opinions Training · doi:10.33029/2304-9529-2022-11-3-37-46 · Cited by 2
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HETEROLOGOUS EXPRESSION AND CHARACTERIZATION OF HUMAN ERYTHROPOIETIN IN PICHIA PASTORIS
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Mogmenga, I. (2019) · doi:10.21474/ijar01/8462 · Cited by 2
“For example, yeasts offer the ease of microbial growth and gene manipulation allowed to understand many eukaryote-specific post-translational modifications, such as proteolytic processing, folding, disulfide bridge formation, and glycosylation (Cereghino and Cregg, 1999; Jans et al., 2017).”
BackgroundExpression of a lipase in prokaryote and eukaryote host systems allowing engineering
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“TheADH1 promoterwas amplified from the vector pMA424 (Cereghino & Cregg, 1999) using the primers ADH1_F2 and ADH1_R2 (Table S1).”
MethodYeast Cell Factory for Production of Biomolecules
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Metadata
- Authors
- Cereghino, G. P. L., & Cregg, J. M.
- Corresponding author
- Cregg, James M
- Venue
- Current Opinion in Biotechnology
- Publisher
- Elsevier BV
- Published
- 1999-10
- Volume
- 10
- Issue
- 5
- Pages
- 422-427
- ISSN
- 0958-1669 (ISSN-L)
- OpenAlex
- W2124157676
- Cited by
- 176
- References
- 41
- Citations by year
- 2025: 3 · 2024: 1 · 2023: 7 · 2022: 3 · 2021: 5 · 2020: 8 · 2019: 3 · 2018: 6 · 2017: 5 · 2016: 8 · 2015: 3 · 2014: 9 · 2013: 9 · 2012: 10
- FWCI
- 0.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Biotechnology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (7r01dk043698-09)
- U.S. Public Health Service (ER20334)
- National Institute of Diabetes and Digestive and Kidney Diseases (DK-43698)
- National Institute of Environmental Health Sciences (ES05759, F32ES005759)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Immunology and Microbiology › Microbiology › Yeasts and Rust Fungi Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
- Keywords
- yeast, protein expression systems, yeast surface display, two-hybrid system, genetic analysis, recombinant protein expression
- MeSH terms
- Biotechnology, Pichia, Recombinant Proteins, Saccharomyces cerevisiae, Yeasts, Protein Engineering, Gene Expression Regulation, Fungal
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