ReviewBiomolecules2014
Refolding techniques for recovering biologically active recombinant proteins from inclusion bodies.
Review in Biomolecules, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
91 citing papers in PubMed.
- Ferritin Complex Vaccine against Influenza A Using Screened Immunogenic Sequences from Fv-Antibody Library.ACS pharmacology & translational science · 2026Article
- Design and functional characterization of recombinant chimeras as vaccine candidates against Lawsonia intracellularis.Biotechnology letters · 2026Article
- Refolding Protocol of the Cysteine-Rich Domain of Frizzled8 from Inclusion Bodies.International journal of molecular sciences · 2026Article
- Review
- Scalable production of monovalent streptavidin with high yield and purity.Scientific reports · 2026Article
- Cloning and Heterologous Expression of Laccase from Beauveria pseudobassiana PHF4 in E. coli and its Application in the Degradation of Catechol.Current microbiology · 2026Article
- Genetically engineered lipases: advances in expression and upscaling for industrial applications.Archives of microbiology · 2026Review
- On-Column Dual-Gradient Refolding for Efficient Recovery of Insoluble Affinity-Tagged Recombinant Proteins.Bio-protocol · 2026Article
- Site-Specific PEGylation at Residue 86 Improves Pharmacokinetic Properties of Interferon α-2b.Iranian journal of biotechnology · 2026Article
- Immunogenic insights and experimental validation of a multiepitope vaccine construct againstFrontiers in immunology · 2026Article
- Optimization of Recombinant Human Interferon-Gamma Expression and Purification inBiologics : targets & therapy · 2026Article
- The recombinant protein of scorpion venom phospholipase A2 exhibits potential anti-leishmanial activity.Scientific reports · 2025Article
- Recovering ImmunogenicVaccines · 2025Article
- Recombinant Production of Ib-AMPProtein and peptide letters · 2025Article
- Expression and purification of recombinant tilapia lake virus segment 4 protein and its in-vitro biological activity for potential use in vaccine development.Scientific reports · 2024Article
- Class IIb Microcin MccM Interferes with Oxidative Phosphorylation inACS chemical biology · 2024Article
- Online monitoring of protein refolding in inclusion body processing using intrinsic fluorescence.Analytical and bioanalytical chemistry · 2024Article
- Design andInternational journal of molecular sciences · 2024Article
- Recognition ofBiology · 2024Article
- Comparing the Soluble Form of Recombinant Human Insulin-like Growth Factor-1 (rhIGF-1) inProtein and peptide letters · 2024Article
31 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biologically active proteins are useful for studying the biological functions of genes and for the development of therapeutic drugs and biomaterials in a biotechnology industry. Overexpression of recombinant proteins in bacteria, such as Escherichia coli, often results in the formation of inclusion bodies, which are protein aggregates with non-native conformations. As inclusion bodies contain relatively pure and intact proteins, protein refolding is an important process to obtain active recombinant proteins from inclusion bodies. However, conventional refolding methods, such as dialysis and dilution, are time consuming and, often, recovered yields of active proteins are low, and a trial-and-error process is required to achieve success. Recently, several approaches have been reported to refold these aggregated proteins into an active form. The strategies largely aim at reducing protein aggregation during the refolding procedure. This review focuses on protein refolding techniques using chemical additives and laminar flow in microfluidic chips for the efficient recovery of active proteins from inclusion bodies.
Indexed as
Identifiers
What OpenQuestion holds
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.