ReviewCellular and molecular life sciences : CMLS2010
Protein folding and aggregation in bacteria.
Review in Cellular and molecular life sciences : CMLS, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 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
40 citing papers in PubMed, 97 citations in OpenAlex.
- A signal peptide-guided approach towards in situ functionalization of bacterial nanocellulose in Komagataeibacter rhaeticus.Journal of biological engineering · 2026Article
- The biosynthesis and diversity of taxanes: From pathway elucidation to engineering and synthetic biology.Plant communications · 2025Review
- Comparative genomics of Shiga toxin-producingFrontiers in veterinary science · 2025Article
- CRISPR/Cas9-mediatedHorticulture research · 2025Article
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- Proteolytic stability and aggregation in a key metabolic enzyme of bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Pleiotropic cellular responses underlying antibiotic tolerance inFrontiers in microbiology · 2024Article
- Genome-wide analysis reveals Hsf1 maintains high transcript abundance of target genes controlled by strong constitutive promoter in Saccharomyces cerevisiae.Biotechnology for biofuels and bioproducts · 2023Article
- Review
- Increased Synthesis of a Magnesium Transporter MgtA During Recombinant Autotransporter Expression in Escherichia coli.Applied biochemistry and biotechnology · 2021Article
- Dual Inhibitors of Amyloid-β and Tau Aggregation with Amyloid-β Disaggregating Properties: ExtendedACS chemical neuroscience · 2021Article
- Cell-Free Expression of a Plant Membrane Protein BrPT2 From Boesenbergia Rotunda.Molecular biotechnology · 2021Article
- Protein Aggregation as a Bacterial Strategy to Survive Antibiotic Treatment.Frontiers in molecular biosciences · 2021Review
- Liquid-Liquid Phase Separation: Unraveling the Enigma of Biomolecular Condensates in Microbial Cells.Frontiers in microbiology · 2021Review
- Senescence in Bacteria and Its Underlying Mechanisms.Frontiers in cell and developmental biology · 2021Review
- Bacterial Protein Homeostasis Disruption as a Therapeutic Intervention.Frontiers in molecular biosciences · 2021Review
- Cell aging preserves cellular immortality in the presence of lethal levels of damage.PLoS biology · 2019Article
- Evolutionary evidence on suitability of SecD as a target for development of antibacterial agents against Staphylococcus aureus.Ecology and evolution · 2016Article
- Downsizing a pullulanase to a small molecule with improved soluble expression and secretion efficiency in Escherichia coli.Microbial cell factories · 2016Article
- Robustness of the Process of Nucleoid Exclusion of Protein Aggregates in Escherichia coli.Journal of bacteriology · 2016Article
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
Proteins might experience many conformational changes and interactions during their lifetimes, from their synthesis at ribosomes to their controlled degradation. Because, in most cases, only folded proteins are functional, protein folding in bacteria is tightly controlled genetically, transcriptionally, and at the protein sequence level. In addition, important cellular machinery assists the folding of polypeptides to avoid misfolding and ensure the attainment of functional structures. When these redundant protective strategies are overcome, misfolded polypeptides are recruited into insoluble inclusion bodies. The protein embedded in these intracellular deposits might display different conformations including functional and beta-sheet-rich structures. The latter assemblies are similar to the amyloid fibrils characteristic of several human neurodegenerative diseases. Interestingly, bacteria exploit the same structural principles for functional properties such as adhesion or cytotoxicity. Overall, this review illustrates how prokaryotic organisms might provide the bedrock on which to understand the complexity of protein folding and aggregation in the cell.
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.