ReviewMolecular and cellular biochemistry2008
Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies.
Review in Molecular and cellular biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 157 papers.
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Who cites it
157 citing papers in PubMed.
- The establishment of a universal blocking ELISA for echinococcosis using immunoglobulin against a new conserved linear B-cell epitope.Microbiology spectrum · 2026Article
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- Optimized Expression and Purification of Outer Membrane Protein 25 (Omp25) of Brucella melitensis.Current protocols · 2026Article
- Potential of inclusion bodies for disease control in aquaculture and livestock.Veterinary and animal science · 2026Review
- Improvement of soluble expression of anti-PD-1/CTLA-4 diabody in the cytoplasm of Escherichia coli.Molecular biology reports · 2026Article
- Versatile vector tools for efficient protein screening across multiple expression systems.FEBS open bio · 2026Article
- Plant-produced encapsulin displays non-typhoidal Salmonella enterica antigens and assembles into mosaic nanoparticles.The FEBS journal · 2026Article
- Soluble Expression of Recombinant Human Mitsugumin 53 in Escherichia coli NiCo21(DE3).The protein journal · 2026Article
- Precise, minimally evolved adenine base editors generated through mutation reversion analysis.Nature biotechnology · 2026Article
- Recombinant Proteins: A Molecular Tool to Understand Marine Adhesion and to Advance Biomaterials.Advanced healthcare materials · 2026Review
- Advanced adhesion and targeting strategies to prolong gut residence time and improve eLBP efficacy in colonic diseases.Advanced drug delivery reviews · 2025Review
- Beyond Purification: Evolving Roles of Fusion Tags in Biotechnology.Current issues in molecular biology · 2025Review
- Identification of histidine decarboxylase and its multi-enzyme cascade system for cost-efficient biosynthesis of carcinine.3 Biotech · 2025Article
- Recombinant Production of a TRAF-Domain Lectin from Cauliflower: A Soluble Expression Strategy for Functional Protein Recovery inInternational journal of molecular sciences · 2025Article
- Recombinant Cell-Permeable PuromycinJournal of microbiology and biotechnology · 2025Article
- Scientific and technological challenges of recombinant egg protein production.BMC biotechnology · 2025Review
- Development of an indirect enzyme-linked immunosorbent assay based on nucleocapsid protein for the detection of swine acute diarrhea syndrome coronavirus antibody.Virology journal · 2025Article
- Harnessing Transient Expression Systems with Plant Viral Vectors for the Production of Biopharmaceuticals inInternational journal of molecular sciences · 2025Review
- Site-Specific Functionalization of Recombinant Spider Silk Using Enzymatic Sortase Coupling.ACS omega · 2025Article
- Functional expression and secretion of basic fibroblast growth factor inFrontiers in bioengineering and biotechnology · 2025Article
97 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Among the various expression systems employed for the over-production of proteins, bacteria still remains the favorite choice of a Protein Biochemist. However, even today, due to the lack of post-translational modification machinery in bacteria, recombinant eukaryotic protein production poses an immense challenge, which invariably leads to the production of biologically in-active protein in this host. A number of techniques are cited in the literature, which describe the conversion of inactive protein, expressed as an insoluble fraction, into a soluble and active form. Overall, we have divided these methods into three major groups: Group-I, where the factors influencing the formation of insoluble fraction are modified through a stringent control of the cellular milieu, thereby leading to the expression of recombinant protein as soluble moiety; Group-II, where protein is refolded from the inclusion bodies and thereby target protein modification is avoided; Group-III, where the target protein is engineered to achieve soluble expression through fusion protein technology. Even within the same family of proteins (e.g., tyrosine kinases), optimization of standard operating protocol (SOP) may still be required for each protein's over-production at a pilot-scale in Escherichia coli. However, once standardized, this procedure can be made amenable to the industrial production for that particular protein with minimum alterations.
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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.