ReviewBiophysical reviews2019
Microbial functional amyloids serve diverse purposes for structure, adhesion and defence.
Review in Biophysical reviews, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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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.
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Who cites it
37 citing papers in PubMed, 76 citations in OpenAlex.
- Intrinsic Disorder as a New Frontier in Antimicrobial Resistance and Bacterial Fitness.MicrobiologyOpen · 2026Review
- Computational examination of magainin-I-KL mediated disruption of E. coli biofilms via CsgA amyloid interference.Archives of microbiology · 2026Article
- Encapsulated Control: Shaping Insulin Fibrillation through Polymer Confinement.Biomacromolecules · 2026Article
- AlphaFold modeling uncovers global structural features of class I and class II fungal hydrophobins.Protein science : a publication of the Protein Society · 2025Article
- Article
- Dietary Strategies to Mitigate Alzheimer's Disease: Insights into Antioxidant Vitamin Intake and Supplementation with Microbiota-Gut-Brain Axis Cross-Talk.Antioxidants (Basel, Switzerland) · 2024Review
- Biogenic amine tryptamine in human vaginal probiotic isolates mediates matrix inhibition and thwarts uropathogenic E. coli biofilm.Scientific reports · 2024Article
- Staphylococcus aureus functional amyloids catalyze degradation of β-lactam antibiotics.Nature communications · 2023Article
- Hierarchical organization and assembly of the archaeal cell sheath from an amyloid-like protein.Nature communications · 2023Article
- Metal Nanomaterials and Hydrolytic Enzyme-Based Formulations for Improved Antifungal Activity.International journal of molecular sciences · 2023Review
- CARD9 attenuates Aβ pathology and modifies microglial responses in an Alzheimer's disease mouse model.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- The Pga59 cell wall protein is an amyloid forming protein involved in adhesion and biofilm establishment in the pathogenic yeast Candida albicans.NPJ biofilms and microbiomes · 2023Article
- Clonal groups of extended-spectrum β-lactamase and biofilm producing uropathogenicPathogens and global health · 2022Article
- Comparative Study of the Solid-Liquid Interfacial Adsorption of Proteins in Their Native and Amyloid Forms.International journal of molecular sciences · 2022Article
- Amyloid Aggregates Are Localized to the Nonadherent Detached Fraction of Aging Streptococcus mutans Biofilms.Microbiology spectrum · 2022Article
- Designed peptides as nanomolar cross-amyloid inhibitors acting via supramolecular nanofiber co-assembly.Nature communications · 2022Article
- Bacterial biofilm functionalization through Bap amyloid engineering.NPJ biofilms and microbiomes · 2022Article
- The Cryo-EM structures of two amphibian antimicrobial cross-β amyloid fibrils.Nature communications · 2022Article
- Action Mechanisms of Effectors in Plant-Pathogen Interaction.International journal of molecular sciences · 2022Review
- Neurotoxic amyloidogenic peptides in the proteome of SARS-COV2: potential implications for neurological symptoms in COVID-19.Nature communications · 2022Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The functional amyloid state of proteins has in recent years garnered much attention for its role in serving crucial and diverse biological roles. Amyloid is a protein fold characterised by fibrillar morphology, binding of the amyloid-specific dyes Thioflavin T and Congo Red, insolubility and underlying cross-β structure. Amyloids were initially characterised as an aberrant protein fold associated with mammalian disease. However, in the last two decades, functional amyloids have been described in almost all biological systems, from viruses, to bacteria and archaea, to humans. Understanding the structure and role of these amyloids elucidates novel and potentially ancient mechanisms of protein function throughout nature. Many of these microbial functional amyloids are utilised by pathogens for invasion and maintenance of infection. As such, they offer novel avenues for therapies. This review examines the structure and mechanism of known microbial functional amyloids, with a particular focus on the pathogenicity conferred by the production of these structures and the strategies utilised by microbes to interfere with host amyloid structures. The biological importance of microbial amyloid assemblies is highlighted by their ubiquity and diverse functionality.
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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.