ReviewResearch in microbiology
Microbial manipulation of the amyloid fold.
Review in Research in microbiology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed, 65 citations in OpenAlex.
- Layer-By-Layer Functionalized Gauze With Designed α-Sheet Peptides Inhibits E. coli and S. aureus Biofilm Formation.Journal of biomedical materials research. Part A · 2025Article
- The role of shear rates on amyloid formation from biofilm peptide phenol-soluble modulins.Biophysical journal · 2024Article
- Importance of microbial amphiphiles: interaction potential of biosurfactants, amyloids, and other exo-polymeric-substances.World journal of microbiology & biotechnology · 2023Review
- Differential fibril morphologies and thermostability determine functional roles ofFrontiers in molecular biosciences · 2023Article
- The role of α-sheet structure in amyloidogenesis: characterization and implications.Open biology · 2022Review
- Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity.Applied and environmental microbiology · 2021Article
- Antimicrobial α-defensins as multi-target inhibitors against amyloid formation and microbial infection.Chemical science · 2021Article
- Gastrokine-1, an anti-amyloidogenic protein secreted by the stomach, regulates diet-induced obesity.Scientific reports · 2021Article
- Emerging Roles of Functional Bacterial Amyloids in Gene Regulation, Toxicity, and Immunomodulation.Microbiology and molecular biology reviews : MMBR · 2020Review
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- The Reversible Non-covalent Aggregation Into Fibers of PGLa and Magainin 2 Preserves Their Antimicrobial Activity and Synergism.Frontiers in cellular and infection microbiology · 2020Article
- Structural Insights into Curli CsgA Cross-β Fibril Architecture Inspire Repurposing of Anti-amyloid Compounds as Anti-biofilm Agents.PLoS pathogens · 2019Article
- Article
- Protein Engineering Reveals Mechanisms of Functional Amyloid Formation in Pseudomonas aeruginosa Biofilms.Journal of molecular biology · 2018Article
- De Novo Designed α-Sheet Peptides Inhibit Functional Amyloid Formation of Streptococcus mutans Biofilms.Journal of molecular biology · 2018Article
- Article
- Extreme amyloid polymorphism in Staphylococcus aureus virulent PSMα peptides.Nature communications · 2018Article
- The Extracellular Polymeric Substances of Legionella pneumophila Biofilms Contain Amyloid Structures.Current microbiology · 2018Article
- Maintaining a Healthy Proteome during Oxidative Stress.Molecular cell · 2018Review
- A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.Nature communications · 2017Article
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 at 1 institution in 1 country.
Funding
Abstract
Microbial biofilms are encased in a protein, DNA, and polysaccharide matrix that protects the community, promotes interactions with the environment, and helps cells adhere together. The protein component of these matrices is often a remarkably stable, β-sheet-rich polymer called amyloid. Amyloids form ordered, self-templating fibers that are highly aggregative, making them a valuable biofilm component. Some eukaryotic proteins inappropriately adopt the amyloid fold, and these misfolded protein aggregates disrupt normal cellular proteostasis, which can cause significant cytotoxicity. Indeed, until recently amyloids were considered solely the result of protein misfolding. However, research over the past decade has revealed how various organisms have capitalized on the amyloid fold by developing sophisticated biogenesis pathways that coordinate gene expression, protein folding, and secretion so that amyloid-related toxicities are minimized. How microbes manipulate amyloids, by augmenting their advantageous properties and by reducing their undesirable properties, will be the subject of this review.
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.