ReviewFrontiers in microbiology2014
Inclusion bodies: not that bad….
Review in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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
42 citing papers in PubMed, 111 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
- Discovery and Preliminary Characterization of Lactose-Transforming Enzymes inInternational journal of molecular sciences · 2026Article
- Structural Stabilization of Clinically Oriented Oligomeric Proteins During their Transit through Synthetic Secretory Amyloids.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Online monitoring of protein refolding in inclusion body processing using intrinsic fluorescence.Analytical and bioanalytical chemistry · 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
- Therapeutic Potential of Engineered Virus-like Particles of Parvovirus B19.Pathogens (Basel, Switzerland) · 2023Review
- Refinement of the Fusion Tag PagP for Effective Formation of Inclusion Bodies in Escherichia coli.Microbiology spectrum · 2023Article
- Fundamental insights in early-stage inclusion body formation.Microbial biotechnology · 2023Article
- Cold-Active Lipases and Esterases: A Review on Recombinant Overexpression and Other Essential Issues.International journal of molecular sciences · 2022Review
- Plasmids for Controlled and Tunable High-Level Expression in E. coli.Applied and environmental microbiology · 2022Article
- Engineering sigma factors and chaperones for enhanced heterologous lipoxygenase production in Escherichia coli.Biotechnology for biofuels and bioproducts · 2022Article
- Article
- Regulation by Different Types of Chaperones of Amyloid Transformation of Proteins Involved in the Development of Neurodegenerative Diseases.International journal of molecular sciences · 2022Review
- Molecular cloning, heterologous expression, and in silico sequence analysis of Enterobacter GH19 class I chitinase (chiRAM gene).Molecular biology reports · 2022Article
- Is Protein Folding a Thermodynamically Unfavorable, Active, Energy-Dependent Process?International journal of molecular sciences · 2022Review
- Solubilization and Refolding of Inclusion Body Proteins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Intrinsically Disordered Proteins (IDP): Purification Under Denaturing Conditions.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Optimizing the Expression and Solubilization of an E. coli-Produced Leukemia Inhibitory Factor for Anti-LIF Antibody Production and Use Thereof for Contraception in Mice.Molecular biotechnology · 2021Article
- Study on the activity of recombinant mutant tissue-type plasminogen activator fused with the C-terminal fragment of hirudin.Journal of thrombosis and thrombolysis · 2021Article
- How Hierarchical Interactions Make Membraneless Organelles Tick Like Clockwork.Trends in biochemical sciences · 2021Review
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 at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The formation of inclusion bodies (IBs) constitute a frequent event during the production of heterologous proteins in bacterial hosts. Although the mechanisms leading to their formation are not completely understood, empirical data have been exploited trying to predict the aggregation propensity of specific proteins while a great number of strategies have been developed to avoid the generation of IBs. However, in many cases, the formation of such aggregates can be considered an advantage for basic research as for protein production. In this review, we focus on this positive side of IBs formation in bacteria. We present a compilation on recent advances on the understanding of IBs formation and their utilization as a model to understand protein aggregation and to explore strategies to control this process. We include recent information about their composition and structure, their use as an attractive approach to produce low cost proteins and other promising applications in Biomedicine.
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.