ReviewJournal of internal medicine2016
Amyloid formation: functional friend or fearful foe?
Review in Journal of internal medicine, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 35 citations in OpenAlex.
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- Unravelling the antimicrobial activity of peptide hydrogel systems: current and future perspectives.Soft matter · 2021Review
- Prion-Like Proteins in Phase Separation and Their Link to Disease.Biomolecules · 2021Review
- Article
- The broad-spectrum antibiofilm activity of amyloid-forming hexapeptides.Microbial biotechnology · 2021Article
- Supramolecular Bait to Trigger Non-Equilibrium Co-Assembly and Clearance of Aβ42.Angewandte Chemie (International ed. in English) · 2021Article
- Supramolecular Peptide Assemblies as Antimicrobial Scaffolds.Molecules (Basel, Switzerland) · 2020Review
- On the Role of Platelet-Generated Amyloid Beta Peptides in Certain Amyloidosis Health Complications.Frontiers in immunology · 2020Review
- Calcium signalling in mammalian cell lines expressing wild type and mutant human α1-Antitrypsin.Scientific reports · 2019Article
- IL-1β PromotesFrontiers in immunology · 2019Article
- Cooperative Induction of Ordered Peptide and Fatty Acid Aggregates.Biophysical journal · 2018Article
- Semen inhibits Zika virus infection of cells and tissues from the anogenital region.Nature communications · 2018Article
- Amyloid assembly and disassembly.Journal of cell science · 2018Review
- Can an Infection Hypothesis Explain the Beta Amyloid Hypothesis of Alzheimer's Disease?Frontiers in aging neuroscience · 2018Review
- Article
- Lipopolysaccharide (LPS) Accumulates in Neocortical Neurons of Alzheimer's Disease (AD) Brain and Impairs Transcription in Human Neuronal-Glial Primary Co-cultures.Frontiers in aging neuroscience · 2017Article
- Microbiome-Derived Lipopolysaccharide Enriched in the Perinuclear Region of Alzheimer's Disease Brain.Frontiers in immunology · 2017Article
- The amyloid interactome: Exploring protein aggregation.PloS one · 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
5 authors at 4 institutions in 3 countries.
Funding
Abstract
Amyloid formation has been most studied in the context of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease, as well as in amyloidosis. However, it is becoming increasingly clear that amyloid is also present in the healthy setting; for example nontoxic amyloid formation is important for melanin synthesis and in innate immunity. Furthermore, bacteria have mechanisms to produce functional amyloid structures with important roles in bacterial physiology and interaction with host cells. Here, we will discuss some novel aspects of fibril-forming proteins in humans and bacteria. First, the amyloid-forming properties of the antimicrobial peptide human defensin 6 (HD6) will be considered. Intriguingly, unlike other antimicrobial peptides, HD6 does not kill bacteria. However, recent data show that HD6 can form amyloid structures at the gut mucosa with strong affinity for bacterial surfaces. These so-called nanonets block bacterial invasion by entangling the bacteria in net-like structures. Next, the role of functional amyloid fibrils in human semen will be discussed. These fibrils were discovered through their property to enhance HIV infection but they may also have other yet unknown functions. Finally, the role of amyloid formation in bacteria will be reviewed. The recent finding that bacteria can make amyloid in a controlled fashion without toxic effects is of particular interest and may have implications for human disease. The role of amyloid in health and disease is beginning to be unravelled, and here, we will review some of the most recent findings in this exciting area.
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.