ReviewCell biochemistry and biophysics2021
A Review: Molecular Chaperone-mediated Folding, Unfolding and Disaggregation of Expressed Recombinant Proteins.
Review in Cell biochemistry and biophysics, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed.
- Structural interplay of the redox co-chaperone CnoX to GroEL/ES chaperonin.Life science alliance · 2026Article
- Multi-gene Co-expression systems inSynthetic and systems biotechnology · 2026Review
- Enhancing soluble expression and purification of a bispecific scFv antibody inResearch in pharmaceutical sciences · 2026Article
- Adverse effects of thermal pollution on rainbow trout (Oncorhynchus mykiss): unveiling the roles of heat shock proteins and acute-phase proteinsMette.Veterinary research communications · 2026Review
- Antimicrobial peptide resistance in Salmonella AMR: the role of surface binding and lipopolysaccharide remodelling: one health implications.World journal of microbiology & biotechnology · 2026Review
- EngineeringInternational journal of molecular sciences · 2025Review
- Recombinant DNA the Bio-Revolution, Between Promise, Hurdles, and Achievements.International journal of molecular sciences · 2025Article
- Endoplasmic reticulum homeostasis in plant-pathogen interactions: new scenarios for an old story.Journal of experimental botany · 2025Review
- Identification of cellular signatures associated with chinese hamster ovary cell adaptation for secretion of antibodies.Computational and structural biotechnology journal · 2025Article
- Purification of SlREC2 from wild-type tomato leaflets using immunoaffinity chromatography and immunoprecipitation.Frontiers in plant science · 2025Article
- Comprehensive Overview of Bottom-Up Proteomics Using Mass Spectrometry.ACS measurement science au · 2024Review
- Powdery mildew effectors AVRMolecular plant pathology · 2024Article
- Advances in protein subunit vaccines against H1N1/09 influenza.Frontiers in immunology · 2024Review
- Genetically modified chickens as bioreactors for protein-based drugs.Frontiers in genome editing · 2024Review
- Stabilization challenges and aggregation in protein-based therapeutics in the pharmaceutical industry.RSC advances · 2023Review
- Article
- Engineering and Expression Strategies for Optimization of L-Asparaginase Development and Production.International journal of molecular sciences · 2023Review
- Hydroxylases involved in terpenoid biosynthesis: a review.Bioresources and bioprocessing · 2023Review
- Critical Beginnings: Selective Tuning of Solubility and Structural Accuracy of Newly Synthesized Proteins by the Hsp70 Chaperone System.The journal of physical chemistry. B · 2023Article
- Distribution and solvent exposure of Hsp70 chaperone binding sites across the Escherichia coli proteome.Proteins · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The advancements in biotechnology over time have led to an increase in the demand of pure, soluble and functionally active proteins. Recombinant protein production has thus been employed to obtain high expression of purified proteins in bulk. E. coli is considered as the most desirable host for recombinant protein production due to its inexpensive and fast cultivation, simple nutritional requirements and known genetics. Despite all these benefits, recombinant protein production often comes with drawbacks, such as, the most common being the formation of inclusion bodies due to improper protein folding. Consequently, this can lead to the loss of the structure-function relationship of a protein. Apart from various strategies, one major strategy to resolve this issue is the use of molecular chaperones that act as folding modulators for proteins. Molecular chaperones assist newly synthesized, aggregated or misfolded proteins to fold into their native conformations. Chaperones have been widely used to improve the expression of various proteins which are otherwise difficult to produce in E. coli. Here, we discuss the structure, function, and role of major E. coli molecular chaperones in recombinant technology such as trigger factor, GroEL, DnaK and ClpB.
Indexed as
Identifiers
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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.