ReviewInternational journal of molecular sciences2011
Active protein aggregates produced in Escherichia coli.
Review in International journal of molecular sciences, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed.
- Enhancing the E. coli Cell Density Expressing the Recombinant Cellulolytic Chimeric Enzyme from Acetivibrio thermocellus by Statistical Optimization of the Medium.Current microbiology · 2026Article
- The p40 fusion domain as a scaffold for producing functional inclusion bodies.Applied microbiology and biotechnology · 2026Article
- Catalytically active inclusion bodies of Bacillus clausii laccase protein recombinantly produced in E. coli for dye decolorization.Microbial cell factories · 2026Article
- Beyond Purification: Evolving Roles of Fusion Tags in Biotechnology.Current issues in molecular biology · 2025Review
- Fundamental insights in early-stage inclusion body formation.Microbial biotechnology · 2023Article
- Simultaneous Production of a Virus-Like Particle Linked to dsRNA to Enhance dsRNA Delivery for Yellow Head Virus Inhibition.Viruses · 2022Article
- Development of a plant-produced recombinant monoclonal antibody against Δ-9-tetrahydrocannabinol (Δ9-THC) for immunoassay application.Biotechnology reports (Amsterdam, Netherlands) · 2022Article
- Proteome-wide landscape of solubility limits in a bacterial cell.Scientific reports · 2022Article
- Production of recombinant human G-CSF from non-classical inclusion bodies in Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2021Article
- Gene cloning, expression, purification and characterization of a sn-1,3 extracellular lipase fromJournal of food science and technology · 2020Article
- Production of Active Recombinant Hyaluronidase Inclusion Bodies fromInternational journal of molecular sciences · 2020Article
- Targeting Antitumoral Proteins to Breast Cancer by Local Administration of Functional Inclusion Bodies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Article
- Transient Expression of Dengue Virus NS1 Antigen inFrontiers in plant science · 2019Article
- Expression of Rift Valley fever virus N-protein in Nicotiana benthamiana for use as a diagnostic antigen.BMC biotechnology · 2018Article
- Teaching an old pET new tricks: tuning of inclusion body formation and properties by a mixed feed system in E. coli.Applied microbiology and biotechnology · 2018Article
- Bioengineering toward direct production of immobilized enzymes: A paradigm shift in biocatalyst design.Bioengineered · 2018Review
- Enzyme Engineering for In Situ Immobilization.Molecules (Basel, Switzerland) · 2016Review
- Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process.Microbial cell factories · 2015Review
- Influence of pH control in the formation of inclusion bodies during production of recombinant sphingomyelinase-D in Escherichia coli.Microbial cell factories · 2014Article
- Polyhydroyxalkanoate synthase fusions as a strategy for oriented enzyme immobilisation.Molecules (Basel, Switzerland) · 2014Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Since recombinant proteins are widely used in industry and in research, the need for their low-cost production is increasing. Escherichia coli is one of the best known and most often used host organisms for economical protein production. However, upon over-expression, protein aggregates called inclusion bodies (IBs) are often formed. Until recently IBs formation represented a bottleneck in protein production as they were considered as deposits of inactive proteins. However, recent studies show that by choosing the appropriate host strain and designing an optimal production process, IBs composed from properly folded and biologically active recombinant proteins can be prepared. Such active protein particles can be further used for the isolation of pure proteins or as whole active protein particles in various biomedical and other applications. Therefore interest in understanding the mechanisms of their formation as well as their properties is increasing.
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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.