ArticleMicrobial cell factories2012
Packaging protein drugs as bacterial inclusion bodies for therapeutic applications.
Article in Microbial cell factories, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed.
- Sequence-Encoded Aggregation of AA10 LPMO Domains as a Basis for Inclusion Body Design.International journal of molecular sciences · 2026Article
- Immobilized inclusion bodies of recombinant cold-adaptive lipase from Antarctic Pseudomonas sp. as catalysts.Applied microbiology and biotechnology · 2025Article
- An end-to-end approach for single-cell infrared absorption spectroscopy of bacterial inclusion bodies: from AFM-IR measurement to data interpretation of large sample sets.Journal of nanobiotechnology · 2024Article
- The pre-induction temperature affects recombinant HuGM-CSF aggregation in thermoinducible Escherichia coli.Applied microbiology and biotechnology · 2022Article
- The Poly-Histidine Tag H6 Mediates Structural and Functional Properties of Disintegrating, Protein-Releasing Inclusion Bodies.Pharmaceutics · 2022Article
- The Biological Potential Hidden in Inclusion Bodies.Pharmaceutics · 2020Article
- Structure-Function Relationship of Inclusion Bodies of a Multimeric Protein.Frontiers in microbiology · 2020Article
- Targeting Antitumoral Proteins to Breast Cancer by Local Administration of Functional Inclusion Bodies.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2019Article
- Trends in recombinant protein use in animal production.Microbial cell factories · 2017Review
- Bacterial mimetics of endocrine secretory granules as immobilized in vivo depots for functional protein drugs.Scientific reports · 2016Article
- Feeding transgenic plants that express a tolerogenic fusion protein effectively protects against arthritis.Plant biotechnology journal · 2016Article
- Overview of the purification of recombinant proteins.Current protocols in protein science · 2015Review
- Protein recovery from inclusion bodies of Escherichia coli using mild solubilization process.Microbial cell factories · 2015Review
- Inclusion bodies: not that bad….Frontiers in microbiology · 2014Review
- Recombinant polypeptide production in E. coli: towards a rational approach to improve the yields of functional proteins.Microbial cell factories · 2013Review
- Active inclusion bodies of acid phosphatase PhoC: aggregation induced by GFP fusion and activities modulated by linker flexibility.Microbial cell factories · 2013Article
- Why and how protein aggregation has to be studied in vivo.Microbial cell factories · 2013Article
- Bacterial inclusion bodies as potential synthetic devices for pathogen recognition and a therapeutic substance release.Microbial cell factories · 2013Article
- Modeling amyloids in bacteria.Microbial cell factories · 2012Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A growing number of insights on the biology of bacterial inclusion bodies (IBs) have revealed intriguing utilities of these protein particles. Since they combine mechanical stability and protein functionality, IBs have been already exploited in biocatalysis and explored for bottom-up topographical modification in tissue engineering. Being fully biocompatible and with tuneable bio-physical properties, IBs are currently emerging as agents for protein delivery into mammalian cells in protein-replacement cell therapies. So far, IBs formed by chaperones (heat shock protein 70, Hsp70), enzymes (catalase and dihydrofolate reductase), grow factors (leukemia inhibitory factor, LIF) and structural proteins (the cytoskeleton keratin 14) have been shown to rescue exposed cells from a spectrum of stresses and restore cell functions in absence of cytotoxicity. The natural penetrability of IBs into mammalian cells (reaching both cytoplasm and nucleus) empowers them as an unexpected platform for the controlled delivery of essentially any therapeutic polypeptide. Production of protein drugs by biopharma has been traditionally challenged by IB formation. However, a time might have arrived in which recombinant bacteria are to be engineered for the controlled packaging of therapeutic proteins as nanoparticulate materials (nanopills), for their extra- or intra-cellular release in medicine and cosmetics.
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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.