ArticleCommunications biology2021
Breakdown of supersaturation barrier links protein folding to amyloid formation.
Article in Communications biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- The temperature dependence of amyloidProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Quantitative Analysis of Amyloid Fibril Nucleation by Linking Folding and Nucleation Pathways Using a Robust Ultrasonic Assay.ACS omega · 2026Article
- Ultrasonic frequency and intensity dependence in βUltrasonics sonochemistry · 2025Article
- AmyloGram reveals amyloidogenic potential in stroke thrombus proteomes.The Biochemical journal · 2025Article
- To What Extent is Anfinsen's Thermodynamic Hypothesis Consistent With the Formation and Polymorphism of Amyloid Fibrils?Journal of molecular biology · 2025Review
- Deciphering Amyloid Fibril Formation through Protein Concentration by Optical Trapping.JACS Au · 2025Article
- Interactions of Sucrose and Trehalose with Lysozyme in Different Media: A Perspective from Atomistic Molecular Dynamics Simulations.Molecular pharmaceutics · 2025Article
- Direct comparison of the structural dynamics between spontaneous and ligand-induced folding of staphylococcal nuclease.Protein science : a publication of the Protein Society · 2025Article
- Initiation of transthyretin aggregation at neutral pH by fluid agitation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Decoding Solubility Signatures from Amyloid Monomer Energy Landscapes.Journal of chemical theory and computation · 2025Article
- Guide to the structural characterization of protein aggregates and amyloid fibrils by CD spectroscopy.Protein science : a publication of the Protein Society · 2025Article
- Accelerated amyloid fibril formation at the interface of liquid-liquid phase-separated droplets by depletion interactions.Protein science : a publication of the Protein Society · 2025Article
- Beyond Misfolding: A New Paradigm for the Relationship Between Protein Folding and Aggregation.International journal of molecular sciences · 2024Review
- Aggregation of Transthyretin by Fluid Agitation.bioRxiv : the preprint server for biology · 2024Article
- The State-of-the-Art Overview to Application of Deep Learning in Accurate Protein Design and Structure Prediction.Topics in current chemistry (Cham) · 2024Review
- Review
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Hydroxytyrosol-Donepezil Hybrids Play a Protective Role in an In Vitro Induced Alzheimer's Disease Model and in Neuronal Differentiated Human SH-SY5Y Neuroblastoma Cells.International journal of molecular sciences · 2023Article
- Protein nanocondensates: the next frontier.Biophysical reviews · 2023Review
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Authors and funding
16 authors.
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Abstract
The thermodynamic hypothesis of protein folding, known as the "Anfinsen's dogma" states that the native structure of a protein represents a free energy minimum determined by the amino acid sequence. However, inconsistent with the Anfinsen's dogma, globular proteins can misfold to form amyloid fibrils, which are ordered aggregates associated with diseases such as Alzheimer's and Parkinson's diseases. Here, we present a general concept for the link between folding and misfolding. We tested the accessibility of the amyloid state for various proteins upon heating and agitation. Many of them showed Anfinsen-like reversible unfolding upon heating, but formed amyloid fibrils upon agitation at high temperatures. We show that folding and amyloid formation are separated by the supersaturation barrier of a protein. Its breakdown is required to shift the protein to the amyloid pathway. Thus, the breakdown of supersaturation links the Anfinsen's intramolecular folding universe and the intermolecular misfolding universe.
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