ArticleThe Journal of biological chemistry2012
A generic crystallization-like model that describes the kinetics of amyloid fibril formation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- YB-1 AP-CSD Forms Cross-β Amyloid Fibrils Without Secondary-Structure Conversion In Vitro.International journal of molecular sciences · 2026Article
- The intrinsically disordered region of the human parathyroid hormone controls functional amyloid properties.The Journal of biological chemistry · 2026Article
- The Catalyzing Effect of Aggregates on the Fibrillation Pathway of Human Insulin: A Spectroscopic Investigation During the Lag Phase.International journal of molecular sciences · 2025Article
- Protein-RNA condensation kinetics via filamentous nanoclusters.Protein science : a publication of the Protein Society · 2025Article
- Experimental kinetic mechanism of P53 condensation-amyloid aggregation.Biophysical journal · 2025Article
- Challenges and Advances in the Encapsulation of Bioactive Ingredients Using Whey Proteins.Foods (Basel, Switzerland) · 2025Review
- NAGPKin: Nucleation-and-growth parameters from the kinetics of protein phase separation.Molecular biology of the cell · 2024Article
- α-Synuclein liquid condensates fuel fibrillar α-synuclein growth.Science advances · 2023Article
- Quantification of Surface Tension Effects and Nucleation-and-Growth Rates during Self-Assembly of Biological Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Molecular Mechanisms of Inhibition of Protein Amyloid Fibril Formation: Evidence and Perspectives Based on Kinetic Models.International journal of molecular sciences · 2022Review
- Chicago sky blue 6B inhibits α-synuclein aggregation and propagation.Molecular brain · 2022Article
- Dissection of the amyloid formation pathway in AL amyloidosis.Nature communications · 2021Article
- A generic approach to decipher the mechanistic pathway of heterogeneous protein aggregation kinetics.Chemical science · 2021Article
- Fibril Surface-Dependent Amyloid Precursors Revealed by Coarse-Grained Molecular Dynamics Simulation.Frontiers in molecular biosciences · 2021Article
- Bleomycin modulates amyloid aggregation in β-amyloid and hIAPP.RSC advances · 2020Article
- MIRRAGGE - Minimum Information Required for Reproducible AGGregation Experiments.Frontiers in molecular neuroscience · 2020Review
- Life in Phases: Intra- and Inter- Molecular Phase Transitions in Protein Solutions.Biomolecules · 2019Review
- How Fluorescent Tags Modify Oligomer Size Distributions of the Alzheimer Peptide.Biophysical journal · 2019Article
- Probing the Occurrence of Soluble Oligomers through Amyloid Aggregation Scaling Laws.Biomolecules · 2018Article
- Enhancement of therapeutic potential of a naturally occurring human antibody targeting a phosphorylated SerActa neuropathologica communications · 2018Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Associated with neurodegenerative disorders such as Alzheimer, Parkinson, or prion diseases, the conversion of soluble proteins into amyloid fibrils remains poorly understood. Extensive "in vitro" measurements of protein aggregation kinetics have been reported, but no consensus mechanism has emerged until now. This contribution aims at overcoming this gap by proposing a theoretically consistent crystallization-like model (CLM) that is able to describe the classic types of amyloid fibrillization kinetics identified in our literature survey. Amyloid conversion represented as a function of time is shown to follow different curve shapes, ranging from sigmoidal to hyperbolic, according to the relative importance of the nucleation and growth steps. Using the CLM, apparently unrelated data are deconvoluted into generic mechanistic information integrating the combined influence of seeding, nucleation, growth, and fibril breakage events. It is notable that this complex assembly of interdependent events is ultimately reduced to a mathematically simple model, whose two parameters can be determined by little more than visual inspection. The good fitting results obtained for all cases confirm the CLM as a good approximation to the generalized underlying principle governing amyloid fibrillization. A perspective is presented on possible applications of the CLM during the development of new targets for amyloid disease therapeutics.
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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.