ArticleJournal of molecular biology2010
Role of small oligomers on the amyloidogenic aggregation free-energy landscape.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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Who cites it
11 citing papers in PubMed.
- Potent inhibitors of toxic alpha-synuclein identified via cellular time-resolved FRET biosensors.NPJ Parkinson's disease · 2021Article
- Early aggregation preceding the nucleation of insulin amyloid fibrils as monitored by small angle X-ray scattering.Scientific reports · 2015Article
- Amyloid misfolding, aggregation, and the early onset of protein deposition diseases: insights from AFM experiments and computational analyses.AIMS molecular science · 2015Article
- Stepwise organization of the β-structure identifies key regions essential for the propagation and cytotoxicity of insulin amyloid fibrils.The Journal of biological chemistry · 2014Article
- Effect of metals on kinetic pathways of amyloid-β aggregation.Biomolecules · 2014Review
- The role of initial oligomers in amyloid fibril formation by human stefin B.International journal of molecular sciences · 2013Article
- Molecular mechanism of misfolding and aggregation of Aβ(13-23).The journal of physical chemistry. B · 2013Article
- Cu(2+) affects amyloid-β (1-42) aggregation by increasing peptide-peptide binding forces.PloS one · 2013Article
- Early amyloidogenic oligomerization studied through fluorescence lifetime correlation spectroscopy.International journal of molecular sciences · 2012Article
- Single-molecule atomic force microscopy force spectroscopy study of Aβ-40 interactions.Biochemistry · 2011Article
- Review
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Authors and funding
3 authors.
Funding
Abstract
We combine atomic-force-microscopy particle-size-distribution measurements with earlier measurements on 1-anilino-8-naphthalene sulfonate, thioflavin T, and dynamic light scattering to develop a quantitative kinetic model for the aggregation of beta-lactoglobulin into amyloid. We directly compare our simulations to the population distributions provided by dynamic light scattering and atomic force microscopy. We combine species in the simulation according to structural type for comparison with fluorescence fingerprint results. The kinetic model of amyloidogenesis leads to an aggregation free-energy landscape. We define the roles of and propose a classification scheme for different oligomeric species based on their location in the aggregation free-energy landscape. We relate the different types of oligomers to the amyloid cascade hypothesis and the toxic oligomer hypothesis for amyloid-related diseases. We discuss existing kinetic mechanisms in terms of the different types of oligomers. We provide a possible resolution to the toxic oligomer-amyloid coincidence.
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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.