ReviewInternational journal of biological macromolecules2017
An overview on molecular chaperones enhancing solubility of expressed recombinant proteins with correct folding.
Review in International journal of biological macromolecules, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 51 citations in OpenAlex.
- Recombinant expression of natural Arabidopsis PRLIP1 variants reveals temperature-dependent differences in fluorescence and functional protein recovery in Escherichia coli.World journal of microbiology & biotechnology · 2026Article
- Enhancing soluble expression and purification of a bispecific scFv antibody inResearch in pharmaceutical sciences · 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
- Understanding the strengths and limitations of recombinant protein studies.Frontiers in molecular biosciences · 2026Review
- Production Technologies for Recombinant Antibodies: Insights into Eukaryotic, Prokaryotic, and Transgenic Expression Systems.Biochemical genetics · 2025Review
- The function of chaperones in the radioresistance of glioblastoma: a new insight into the current knowledge.Brain tumor pathology · 2025Review
- High-Throughput Pipeline for Protein Expression and Solubility Profiling Using Synthetically Generated Plasmids.Current protocols · 2025Article
- SAS: Split antibiotic selection for identifying chaperones that improve protein solubility.Heliyon · 2024Article
- Improvement of Carotenoids' Production by Increasing the Activity of Beta-Carotene Ketolase with Different Strategies.Microorganisms · 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
- A Light-Driven In Vitro Enzymatic Biosystem for the Synthesis of α-Farnesene from Methanol.Biodesign research · 2024Article
- Stabilization challenges and aggregation in protein-based therapeutics in the pharmaceutical industry.RSC advances · 2023Review
- Modes of therapeutic delivery in synthetic microbiology.Trends in microbiology · 2023Review
- Directed Evolution of Soluble α-1,2-Fucosyltransferase Using Kanamycin Resistance Protein as a Phenotypic Reporter for Efficient Production of 2'-Fucosyllactose.Journal of microbiology and biotechnology · 2022Article
- Simultaneous Production of a Virus-Like Particle Linked to dsRNA to Enhance dsRNA Delivery for Yellow Head Virus Inhibition.Viruses · 2022Article
- Engineering sigma factors and chaperones for enhanced heterologous lipoxygenase production in Escherichia coli.Biotechnology for biofuels and bioproducts · 2022Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- In silico screening and heterologous expression of soluble dimethyl sulfide monooxygenases of microbial origin in Escherichia coli.Applied microbiology and biotechnology · 2022Article
- Recombinant antibodies aggregation and overcoming strategies in CHO cells.Applied microbiology and biotechnology · 2022Review
- Halogenation in Fungi: What Do We Know and What Remains to Be Discovered?Molecules (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The majority of research topics declared that most of the recombinant proteins have been expressed by Escherichia coli in basic investigations. But the majority of high expressed proteins formed as inactive recombinant proteins that are called inclusion body. To overcome this problem, several methods have been used including suitable promoter, environmental factors, ladder tag to secretion of proteins into the periplasm, gene protein optimization, chemical chaperones and molecular chaperones sets. Co-expression of the interest protein with molecular chaperones is one of the common methods The chaperones are a group of proteins, which are involved in making correct folding of recombinant proteins. Chaperones are divided two groups including; cytoplasmic and periplasmic chaperones. Moreover, periplasmic chaperones and proteases can be manipulated to increase the yields of secreted proteins. In this article, we attempted to review cytoplasmic chaperones such as Hsp families and periplasmic chaperones including; generic chaperones, specialized chaperones, PPIases, and proteins involved in disulfide bond formation.
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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.