ArticleBiophysical journal2013
An imaging and systems modeling approach to fibril breakage enables prediction of amyloid behavior.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Spontaneous aging of mature amyloids alters structural stability, cytotoxicity, and susceptibility to biological clearance.Cell death discovery · 2026Article
- Fragmentation-Induced Disassembly and Reaggregation of α-Synuclein Amyloid Fibrils.ACS chemical neuroscience · 2026Article
- Inhibiting Disulfide Bonding in Truncated Tau297-391 Results in Enhanced Self-Assembly of Tau into Seed-Competent Assemblies.ACS chemical neuroscience · 2026Article
- Structural reconstruction of individual filaments in AβCommunications chemistry · 2025Article
- Comparative Analysis of the Relative Fragmentation Stabilities of Polymorphic Alpha-Synuclein Amyloid Fibrils.Biomolecules · 2022Article
- Amyloid particles facilitate surface-catalyzed cross-seeding by acting as promiscuous nanoparticles.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Insights into the dynamic trajectories of protein filament division revealed by numerical investigation into the mathematical model of pure fragmentation.PLoS computational biology · 2021Article
- Secondary Nucleation and the Conservation of Structural Characteristics of Amyloid Fibril Strains.Frontiers in molecular biosciences · 2021Review
- How and why to build a mathematical model: A case study using prion aggregation.The Journal of biological chemistry · 2020Review
- Polymer-Peptide Conjugates Convert Amyloid into Protein Nanobundles through Fragmentation and Lateral Association.ACS applied nano materials · 2020Article
- The role of annealing and fragmentation in human tau aggregation dynamics.The Journal of biological chemistry · 2019Article
- The structure of a βNature communications · 2018Article
- Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.ACS chemical neuroscience · 2018Article
- A Free Energy Barrier Caused by the Refolding of an Oligomeric Intermediate Controls the Lag Time of Amyloid Formation by hIAPP.Journal of the American Chemical Society · 2017Article
- The physical dimensions of amyloid aggregates control their infective potential as prion particles.eLife · 2017Article
- Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Chemical Society reviews · 2017Review
- The involvement of dityrosine crosslinking in α-synuclein assembly and deposition in Lewy Bodies in Parkinson's disease.Scientific reports · 2016Article
- α-Synuclein and huntingtin exon 1 amyloid fibrils bind laterally to the cellular membrane.Scientific reports · 2016Article
- Nanomechanics and intermolecular forces of amyloid revealed by four-dimensional electron microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Information content in data sets for a nucleated-polymerization model.Journal of biological dynamics · 2015Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Delineating the nanoscale properties and the dynamic assembly and disassembly behaviors of amyloid fibrils is key for technological applications that use the material properties of amyloid fibrils, as well as for developing treatments of amyloid-associated disease. However, quantitative mechanistic understanding of the complex processes involving these heterogeneous supramolecular systems presents challenges that have yet to be resolved. Here, we develop an approach that is capable of resolving the time dependence of fibril particle concentration, length distribution, and length and position dependence of fibril fragmentation rates using a generic mathematical framework combined with experimental data derived from atomic force microscopy analysis of fibril length distributions. By application to amyloid assembly of β2-microglobulin in vitro under constant mechanical stirring, we present a full description of the fibril fragmentation and growth behavior, and demonstrate the predictive power of the approach in terms of the samples' fibril dimensions, fibril load, and their efficiency to seed the growth of new amyloid fibrils. The approach developed offers opportunities to determine, quantify, and predict the course and the consequences of amyloid assembly.
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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.