ArticleMicrobial cell factories2010
Towards universal systems for recombinant gene expression.
Article in Microbial cell factories, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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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Who cites it
27 citing papers in PubMed, 75 citations in OpenAlex.
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- DMSO-tolerant ornithine decarboxylase (ODC) tandem assay optimised for high-throughput screening.Journal of enzyme inhibition and medicinal chemistry · 2023Article
- Chaperone assisted recombinant expression of a mycobacterial aminoacylase in Vibrio natriegens and Escherichia coli capable of N-lauroyl-L-amino acid synthesis.Microbial cell factories · 2023Article
- Cocktail Anti-Tick Vaccines: The Unforeseen Constraints and Approaches toward Enhanced Efficacies.Vaccines · 2020Review
- Continuous Cultivation as a Tool Toward the Rational Bioprocess Development WithFrontiers in bioengineering and biotechnology · 2020Review
- The impact of respiration and oxidative stress response on recombinant α-amylase production byMetabolic engineering communications · 2016Article
- Generation of monoclonal antibodies against native viral proteins using antigen-expressing mammalian cells for mouse immunization.BMC biotechnology · 2016Article
- Recent advances in the production of recombinant subunit vaccines in Pichia pastoris.Bioengineered · 2016Review
- A portable expression resource for engineering cross-species genetic circuits and pathways.Nature communications · 2015Article
- Role of N-linked glycosylation in the secretion and enzymatic properties of Rhizopus chinensis lipase expressed in Pichia pastoris.Microbial cell factories · 2015Article
- Yeast surface display is a novel tool for the rapid immunological characterization of plant-derived food allergens.Immunologic research · 2015Article
- Evaluation of the Leptospira interrogans Outer Membrane Protein OmpL37 as a Vaccine Candidate.PloS one · 2015Article
- Playing catch-up with Escherichia coli: using yeast to increase success rates in recombinant protein production experiments.Frontiers in microbiology · 2014Article
- Bacterial cell factories for recombinant protein production; expanding the catalogue.Microbial cell factories · 2013Article
- Expression of recombinant Atlantic salmon serum C-type lectin in Drosophila melanogaster Schneider 2 cells.Cytotechnology · 2013Article
- Expression of Neospora caninum NcSRS2 surface protein in Pichia pastoris and its application for serodiagnosis of Neospora infection.Pathogens and global health · 2013Article
- Cloning, production, and functional expression of the bacteriocin enterocin A, produced by Enterococcus faecium T136, by the yeasts Pichia pastoris, Kluyveromyces lactis, Hansenula polymorpha, and Arxula adeninivorans.Applied and environmental microbiology · 2012Article
- Beyond de-foaming: the effects of antifoams on bioprocess productivity.Computational and structural biotechnology journal · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recombinant gene expression is among the most important techniques used both in molecular and medical research and in industrial settings. Today, two recombinant expression systems are particularly well represented in the literature reporting on recombinant expression of specific genes. According to searches in the PubMed citation database, during the last 15 years 80% of all recombinant genes reported on in the literature were expressed in either the enterobacterium Escherichia coli or the methylotropic yeast Pichia pastoris. Nevertheless, some eukaryotic proteins are misfolded or inadequately posttranslationally modified in these expression systems. This situation demands identification of other recombinant expression systems that enable the proper expression of the remaining eukaryotic genes. As of now, a single universal system allowing expression of all target genes is still a distant goal. In this light, thorough experimental screening for systems that can yield satisfying quantity and quality of target protein is required. In recent years, a number of new expression systems have been described and used for protein production. Two systems, namely Drosophila melanogaster S2 insect cells and human embryonic kidney 293 (HEK293) cells stably expressing the EBNA-1 gene, show exceptional promise. The time has come to identify a few well-performing systems that will allow us to express, purify, and characterize entire eukaryotic genomes.
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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.