ArticleJournal of biomolecular NMR1999
Production of large quantities of isotopically labeled protein in Pichia pastoris by fermentation.
Article in Journal of biomolecular NMR, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 110 citations in OpenAlex.
- A simple and effective method to remove pigments from heterologous secretory proteins expressed in Pichia pastoris.Advanced biotechnology · 2024Article
- Expression ofEPJ web of conferences · 2023Article
- Rapid screening method of Saccharomyces cerevisiae mutants using calcofluor white and aniline blue.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2021Article
- Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.The Journal of biological chemistry · 2019Review
- Isotopic Labeling of Eukaryotic Membrane Proteins for NMR Studies of Interactions and Dynamics.Methods in enzymology · 2019Article
- On the use of Pichia pastoris for isotopic labeling of human GPCRs for NMR studies.Journal of biomolecular NMR · 2018Review
- Solution NMR Spectroscopy in Target-Based Drug Discovery.Molecules (Basel, Switzerland) · 2017Review
- Current strategies for protein production and purification enabling membrane protein structural biology.Biochemistry and cell biology = Biochimie et biologie cellulaire · 2016Review
- Plasma membrane order and fluidity are diversely triggered by elicitors of plant defence.Journal of experimental botany · 2016Article
- Elicitin-Induced Distal Systemic Resistance in Plants is Mediated Through the Protein-Protein Interactions Influenced by Selected Lysine Residues.Frontiers in plant science · 2016Article
- Yeast-expressed human membrane protein aquaporin-1 yields excellent resolution of solid-state MAS NMR spectra.Journal of biomolecular NMR · 2013Article
- The role of ERp44 in maturation of serotonin transporter protein.The Journal of biological chemistry · 2012Article
- Physiological and proteomic approaches to evaluate the role of sterol binding in elicitin-induced resistance.Journal of experimental botany · 2012Article
- Article
- Thermodynamic compensation upon binding to exosite 1 and the active site of thrombin.Biochemistry · 2011Article
- Uniform isotope labeling of a eukaryotic seven-transmembrane helical protein in yeast enables high-resolution solid-state NMR studies in the lipid environment.Journal of biomolecular NMR · 2011Article
- Production of isotopically labeled heterologous proteins in non-E. coli prokaryotic and eukaryotic cells.Journal of biomolecular NMR · 2010Article
- Recent advances in segmental isotope labeling of proteins: NMR applications to large proteins and glycoproteins.Journal of biomolecular NMR · 2010Review
- Tuning microbial hosts for membrane protein production.Microbial cell factories · 2009Review
- Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Progress in nuclear magnetic resonance spectroscopy · 2009Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Heterologous expression in Pichia pastoris has many of the advantages of eukaryotic expression, proper folding and disulfide bond formation, glycosylation, and secretion. Contrary to other eukaryotic systems, protein production from P. pastoris occurs in simple minimal defined media making this system attractive for production of labeled proteins for NMR analysis. P. pastoris is therefore the expression system of choice for NMR of proteins that cannot be refolded from inclusion bodies or that require post-translational modifications for proper folding or function. The yield of expressed proteins from P. pastoris depends critically on growth conditions, and attainment of high cell densities by fermentation has been shown to improve protein yields by 10-100-fold. Unfortunately, the cost of the isotopically enriched fermentation media components, particularly 15NH4OH, is prohibitively high. We report fermentation methods that allow for both 15N-labeling from (15NH4)2SO4 and 13C-labeling from 13C-glucose or 13C-glycerol of proteins produced in Pichia pastoris. Expression of an 83 amino acid fragment of thrombomodulin with two N-linked glycosylation sites shows that fermentation is more cost effective than shake flask growth for isotopic enrichment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.