ArticleCommunications chemistry2020
Quantification of amyloid fibril polymorphism by nano-morphometry reveals the individuality of filament assembly.
Article in Communications chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 50 citations in OpenAlex.
- Multipathway Aggregation Drives Concentration-Dependent Amyloid Polymorphism and Time-Dependent Morphological Evolution.The journal of physical chemistry letters · 2026Article
- An Optimized Protocol for High-Quality AFM Imaging of Amyloid Fibrils.Bio-protocol · 2025Article
- Structural reconstruction of individual filaments in AβCommunications chemistry · 2025Article
- Investigation of the Effect of NaCl Concentrations on the Formation of Amyloid Fibrils During the Cooking of Wheat Noodles.Foods (Basel, Switzerland) · 2025Article
- Shadowless amyloid imaging with quantitative birefringence contrast.Scientific reports · 2025Article
- A self-assembled protein β-helix as a self-contained biofunctional motif.Nature communications · 2025Article
- A Direct Relationship Between 'Blood Stasis' and Fibrinaloid Microclots in Chronic, Inflammatory, and Vascular Diseases, and Some Traditional Natural Products Approaches to Treatment.Pharmaceuticals (Basel, Switzerland) · 2025Review
- The p3 peptides (AβNature communications · 2025Article
- Article
- Proteomic Evidence for Amyloidogenic Cross-Seeding in Fibrinaloid Microclots.International journal of molecular sciences · 2024Article
- Data-mining unveils structure-property-activity correlation of viral infectivity enhancing self-assembling peptides.Nature communications · 2023Article
- Direct Observation of Competing Prion Protein Fibril Populations with Distinct Structures and Kinetics.ACS nano · 2023Article
- Role of conformational dynamics in pathogenic protein aggregation.Current opinion in chemical biology · 2023Review
- Heterotypic Amyloid β interactions facilitate amyloid assembly and modify amyloid structure.The EMBO journal · 2022Article
- Transferrin-Functionalized Liposomes for the Delivery of Gallic Acid: A Therapeutic Approach for Alzheimer's Disease.Pharmaceutics · 2022Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- Polymorphic Biological and Inorganic Functional Nanomaterials.Materials (Basel, Switzerland) · 2022Article
- Comparative Analysis of the Relative Fragmentation Stabilities of Polymorphic Alpha-Synuclein Amyloid Fibrils.Biomolecules · 2022Article
- Structural Identification of Individual Helical Amyloid Filaments by Integration of Cryo-Electron Microscopy-Derived Maps in Comparative Morphometric Atomic Force Microscopy Image Analysis.Journal of molecular biology · 2022Article
- General Principles Underpinning Amyloid Structure.Frontiers in neuroscience · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Amyloid fibrils are highly polymorphic structures formed by many different proteins. They provide biological function but also abnormally accumulate in numerous human diseases. The physicochemical principles of amyloid polymorphism are not understood due to lack of structural insights at the single-fibril level. To identify and classify different fibril polymorphs and to quantify the level of heterogeneity is essential to decipher the precise links between amyloid structures and their functional and disease associated properties such as toxicity, strains, propagation and spreading. Employing gentle, force-distance curve-based AFM, we produce detailed images, from which the 3D reconstruction of individual filaments in heterogeneous amyloid samples is achieved. Distinctive fibril polymorphs are then classified by hierarchical clustering, and sample heterogeneity is objectively quantified. These data demonstrate the polymorphic nature of fibril populations, provide important information regarding the energy landscape of amyloid self-assembly, and offer quantitative insights into the structural basis of polymorphism in amyloid populations.
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.