ArticleThe Journal of biological chemistry2015
Supersaturation-limited and Unlimited Phase Transitions Compete to Produce the Pathway Complexity in Amyloid Fibrillation.
Article in The Journal of biological chemistry, 2015. 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, 65 citations in OpenAlex.
- Multipathway Aggregation Drives Concentration-Dependent Amyloid Polymorphism and Time-Dependent Morphological Evolution.The journal of physical chemistry letters · 2026Article
- Quantitative Analysis of Amyloid Fibril Nucleation by Linking Folding and Nucleation Pathways Using a Robust Ultrasonic Assay.ACS omega · 2026Article
- Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy.Protein science : a publication of the Protein Society · 2025Article
- Global analysis of kinetics reveals the role of secondary nucleation in recombinant spider silk self-assembly.Protein science : a publication of the Protein Society · 2023Article
- Multivariate effects of pH, salt, and ZnCommunications chemistry · 2022Article
- Influence of Centrifugation and Shaking on the Self-Assembly of Lysozyme Fibrils.Biomolecules · 2022Article
- Macromolecular crowding and supersaturation protect hemodialysis patients from the onset of dialysis-related amyloidosis.Nature communications · 2022Article
- Supersaturation-Dependent Formation of Amyloid Fibrils.Molecules (Basel, Switzerland) · 2022Review
- Molecular mechanisms of amyloid formation in living systems.Chemical science · 2022Review
- The pre-induction temperature affects recombinant HuGM-CSF aggregation in thermoinducible Escherichia coli.Applied microbiology and biotechnology · 2022Article
- Relevance of Amorphous and Amyloid-Like Aggregates of the p53 Core Domain to Loss of its DNA-Binding Activity.Frontiers in molecular biosciences · 2022Article
- Polyphenol-solubility alters amyloid fibril formation of α-synuclein.Protein science : a publication of the Protein Society · 2021Article
- Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis.Chemical reviews · 2021Review
- Structure-Function Relationship of Inclusion Bodies of a Multimeric Protein.Frontiers in microbiology · 2020Article
- Heating during agitation of βThe Journal of biological chemistry · 2019Article
- Polyphosphates diminish solubility of a globular protein and thereby promote amyloid aggregation.The Journal of biological chemistry · 2019Article
- Mechanism of Fibril and Soluble Oligomer Formation in Amyloid Beta and Hen Egg White Lysozyme Proteins.The journal of physical chemistry. B · 2019Article
- Possible mechanisms of polyphosphate-induced amyloid fibril formation of βProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Early stage prion assembly involves two subpopulations with different quaternary structures and a secondary templating pathway.Communications biology · 2019Article
- Aggregation-phase diagrams of βThe Journal of biological chemistry · 2018Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although amyloid fibrils and amorphous aggregates are two types of aggregates formed by denatured proteins, their relationship currently remains unclear. We used β2-microglobulin (β2m), a protein responsible for dialysis-related amyloidosis, to clarify the mechanism by which proteins form either amyloid fibrils or amorphous aggregates. When ultrasonication was used to accelerate the spontaneous fibrillation of β2m at pH 2.0, the effects observed depended on ultrasonic power; although stronger ultrasonic power effectively accelerated fibrillation, excessively strong ultrasonic power decreased the amount of fibrils formed, as monitored by thioflavin T fluorescence. An analysis of the products formed indicated that excessively strong ultrasonic power generated fibrillar aggregates that retained β-structures but without high efficiency as seeds. On the other hand, when the spontaneous fibrillation of β2m was induced at higher concentrations of NaCl at pH 2.0 with stirring, amorphous aggregates became more dominant than amyloid fibrils. These apparent complexities in fibrillation were explained comprehensively by a competitive mechanism in which supersaturation-limited reactions competed with supersaturation-unlimited reactions. We link the kinetics of protein aggregation and a conformational phase diagram, in which supersaturation played important roles.
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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.