ReviewMicrobial cell factories2010
Side effects of chaperone gene co-expression in recombinant protein production.
Review 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 40 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.
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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
40 citing papers in PubMed, 129 citations in OpenAlex.
- Outer membrane proteins mediate unconventional secretion of Pseudomonas peroxidase through crosstalk between the Sec pathway and outer membrane vesicles.PLoS genetics · 2026Article
- Multi-gene Co-expression systems inSynthetic and systems biotechnology · 2026Review
- Biocatalytic potential of Ensifer adhaerens S-5 D-Carbamoylase: Insights from in silico and in vitro analyses.Journal, genetic engineering & biotechnology · 2026Article
- A Novel Recombinant MAGE-B10-HSP110 Fusion Protein Enhances Innate and Adaptive Immune Responses in Mice: A Potential Vaccine Candidate for Canine Mammary Tumors.Animals : an open access journal from MDPI · 2026Article
- An effective strategy for soluble bovine enterokinase expression in Escherichia coli.Biotechnology letters · 2025Article
- Modulating bacterial function utilizing A knowledge base of transcriptional regulatory modules.Nucleic acids research · 2024Article
- Structural Analysis and Substrate Specificity of D-Carbamoylase fromBiotech (Basel (Switzerland)) · 2024Article
- Plant Heat Shock Proteins Are More Effective in Enhancing Recombinant Alcohol Dehydrogenase Activity than Bacterial OnesIranian journal of biotechnology · 2024Article
- Glycylglycine promotes the solubility and antigenic utility of recombinant HCV structural proteins in a point-of-care immunoassay for detection of active viremia.Microbial cell factories · 2024Article
- Effects of Signal Peptide and Chaperone Co-Expression on Heterologous Protein Production inMolecules (Basel, Switzerland) · 2023Article
- Optimisation of recombinant TNFα production inFrontiers in bioengineering and biotechnology · 2023Article
- Retro-protein XXA is a remarkable solubilizing fusion tag for inclusion bodies.Microbial cell factories · 2022Article
- Evaluation of factors influencing expression and extraction of recombinant bacteriophage endolysins in Escherichia coli.Microbial cell factories · 2022Article
- An operator-based expression toolkit forProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Efficient production of D-glucosamine by diacetylchitobiose deacetylase catalyzed deacetylation of N-acetyl-D-glucosamine.Biotechnology letters · 2022Article
- Chaperonin Abundance Enhances Bacterial Fitness.Frontiers in molecular biosciences · 2021Article
- Improvement of solubility and yield of recombinant protein expression inResearch in pharmaceutical sciences · 2019Article
- Characterization of Cauliflower OR Mutant Variants.Frontiers in plant science · 2019Article
- Cloning, Optimization of Periplasmic Expression and Purification of Recombinant Granulocyte Macrophage-Stimulating Factor inAdvanced biomedical research · 2019Article
- Thermostable exoshells fold and stabilize recombinant proteins.Nature communications · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insufficient availability of molecular chaperones is observed as a major bottleneck for proper protein folding in recombinant protein production. Therefore, co-production of selected sets of cell chaperones along with foreign polypeptides is a common approach to increase the yield of properly folded, recombinant proteins in bacterial cell factories. However, unbalanced amounts of folding modulators handling folding-reluctant protein species might instead trigger undesired proteolytic activities, detrimental regarding recombinant protein stability, quality and yield. This minireview summarizes the most recent observations of chaperone-linked negative side effects, mostly focusing on DnaK and GroEL sets, when using these proteins as folding assistant agents. These events are discussed in the context of the complexity of the cell quality network and the consequent intricacy of the physiological responses triggered by protein misfolding.
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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.