ArticleJournal of the American Chemical Society2016
A Population Shift between Sparsely Populated Folding Intermediates Determines Amyloidogenicity.
Article in Journal of the American Chemical Society, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
21 citing papers in PubMed.
- Integrated Reaction Monitoring and In Situ Structural Elucidation of Reactive Intermediates With Time-Resolved NOAH NMR Supersequences.Magnetic resonance in chemistry : MRC · 2026Article
- Current Understanding of Protein Aggregation in Neurodegenerative Diseases.International journal of molecular sciences · 2025Review
- Detection of an Intermediate in the Unfolding Process of the N-Terminal Domain of TDP-43.ACS omega · 2025Article
- NumSimEX: A method using EXX hydrogen exchange mass spectrometry to map the energetics of protein folding landscapes.Protein science : a publication of the Protein Society · 2025Article
- A Hydrophobic Core Stabilizes the Residual Structure in the RRM2 Intermediate State of the ALS-linked Protein TDP-43.Journal of molecular biology · 2024Article
- Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller.Nature communications · 2024Article
- The effect of mutation on an aggregation-prone protein: An in vivo, in vitro, and in silico analysis.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Generating Ensembles of Dynamic Misfolding Proteins.Frontiers in neuroscience · 2022Review
- Global Proteotoxicity Caused by Human βInternational journal of molecular sciences · 2021Article
- Insight into the Folding and Dimerization Mechanisms of the N-Terminal Domain from Human TDP-43.International journal of molecular sciences · 2020Article
- The role of the IThe Journal of biological chemistry · 2020Article
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- Impact of membrane curvature on amyloid aggregation.Biochimica et biophysica acta. Biomembranes · 2018Review
- Aggregation-primed molten globule conformers of the p53 core domain provide potential tools for studying p53C aggregation in cancer.The Journal of biological chemistry · 2018Article
- Stability of an aggregation-prone partially folded state of human profilin-1 correlates with aggregation propensity.The Journal of biological chemistry · 2018Article
- An efficient combination of BEST and NUS methods in multidimensional NMR spectroscopy for high throughput analysis of proteins.RSC advances · 2018Article
- Biophysical Aspects of Alzheimer's Disease: Implications for Pharmaceutical Sciences : Theme: Drug Discovery, Development and Delivery in Alzheimer's Disease Guest Editor: Davide Brambilla.Pharmaceutical research · 2017Review
- Small molecule probes of protein aggregation.Current opinion in chemical biology · 2017Review
- Effect of Phosphorylation on a Human-like Osteopontin Peptide.Biophysical journal · 2017Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The balance between protein folding and misfolding is a crucial determinant of amyloid assembly. Transient intermediates that are sparsely populated during protein folding have been identified as key players in amyloid aggregation. However, due to their ephemeral nature, structural characterization of these species remains challenging. Here, using the power of nonuniformly sampled NMR methods we investigate the folding pathway of amyloidogenic and nonamyloidogenic variants of β2-microglobulin (β2m) in atomic detail. Despite folding via common intermediate states, we show that the decreased population of the aggregation-prone ITrans state and population of a less stable, more dynamic species ablate amyloid formation by increasing the energy barrier for amyloid assembly. The results show that subtle changes in conformational dynamics can have a dramatic effect in determining whether a protein is amyloidogenic, without perturbation of the mechanism of protein folding.
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Registered trials
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