ArticleThe journal of physical chemistry. B2012
Dissecting the kinetic process of amyloid fiber formation through asymptotic analysis.
Article in The journal of physical chemistry. B, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 20 citations in OpenAlex.
- Gallium nanoparticles as novel inhibitors of Aβ40 aggregation.Materials advances · 2021Article
- Measurement of Tau Filament Fragmentation Provides Insights into Prion-like Spreading.ACS chemical neuroscience · 2018Article
- Growth-incompetent monomers of human calcitonin lead to a noncanonical direct relationship between peptide concentration and aggregation lag time.The Journal of biological chemistry · 2017Article
- Nanoscale Control of Amyloid Self-Assembly Using Protein Phase Transfer by Host-Guest Chemistry.Scientific reports · 2017Article
- Probing the sources of the apparent irreproducibility of amyloid formation: drastic changes in kinetics and a switch in mechanism due to micellelike oligomer formation at critical concentrations of IAPP.The journal of physical chemistry. B · 2015Article
- Statistical mechanical treatments of protein amyloid formation.International journal of molecular sciences · 2013Review
- A necessary condition for coexistence of autocatalytic replicators in a prebiotic environment.Life (Basel, Switzerland) · 2013Article
- Simple moment-closure model for the self-assembly of breakable amyloid filaments.Biophysical journal · 2013Article
- A variational model for oligomer-formation process of GNNQQNY peptide from yeast prion protein Sup35.Biophysical journal · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Amyloids are insoluble fibrous protein aggregates which, when abnormally accumulated in the body, can result in amyloidosis and various neurodegenerative diseases. In this work, we describe a new approach to the asymptotic solution of the master equation of amyloid fiber aggregations. It is found that four distinct and successive stages (lag phase, exponential growth phase, breaking phase, and static phase) dominate the fiber formation process. On the basis of the distinctive power-law dependence of the half-time and apparent growth rate of the fiber formation on the initial protein concentration, we propose a novel classification for amyloid proteins theoretically.
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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.