ReviewInterface focus2017
The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.
Review in Interface focus, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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
8 citing papers in PubMed, 29 citations in OpenAlex.
- Origin of life: β-sheet amyloid conformers as the primordial functional polymers on the early Earth and their role in the emergence of complex dynamic networks.FEBS letters · 2025Review
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Solvent induced amyloid polymorphism and the uncovering of the elusive class 3 amyloid topology.Communications biology · 2024Article
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- Data-mining unveils structure-property-activity correlation of viral infectivity enhancing self-assembling peptides.Nature communications · 2023Article
- The Way forward for the Origin of Life: Prions and Prion-Like Molecules First Hypothesis.Life (Basel, Switzerland) · 2021Article
- A theoretical study of polymorphism in VQIVYK fibrils.Biophysical journal · 2021Article
- Multistep Changes in Amyloid Structure Induced by Cross-Seeding on a Rugged Energy Landscape.Biophysical journal · 2021Article
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 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Amyloidogenic peptides are well known for their involvement in diseases such as type 2 diabetes and Alzheimer's disease. However, more recently, amyloid fibrils have been shown to provide scaffolding and protection as functional materials in a range of organisms from bacteria to humans. These roles highlight the incredible tensile strength of the cross-β amyloid architecture. Many amino acid sequences are able to self-assemble to form amyloid with a cross-β core. Here we describe our recent advances in understanding how sequence contributes to amyloidogenicity and structure. For example, we describe penta- and hexapeptides that assemble to form different morphologies; a 12mer peptide that forms fibrous crystals; and an eight-residue peptide originating from α-synuclein that has the ability to form nanotubes. This work provides a wide range of peptides that may be exploited as fibrous bionanomaterials. These fibrils provide a scaffold upon which functional groups may be added, or templated assembly may be performed.
Indexed as
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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.