ArticleNature physics2016
Physical determinants of the self-replication of protein fibrils.
Article in Nature physics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
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The trial behind it
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
49 citing papers in PubMed.
- Article
- Seed Oligomers Regulate Sequence Development through a Templating Effect in Simulated Irreversible Step-Growth Copolymerization.Macromolecules · 2025Article
- Can Prions Carry Biological Information?ACS omega · 2025Article
- Exploring Abeta42 monomer diffusion dynamics on fibril surfaces through molecular simulations.Protein science : a publication of the Protein Society · 2025Article
- Achiral and chiral ligands synergistically harness chiral self-assembly of inorganics.Science advances · 2024Article
- Self-replication of AProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Physicochemical mechanisms of aggregation and fibril formation of α-synuclein and apolipoprotein A-I.Biophysics and physicobiology · 2024Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- Conformational entropy limits the transition from nucleation to elongation in amyloid aggregation.Biophysical journal · 2022Article
- Adsorption free energy predicts amyloid protein nucleation rates.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multi-eGO: An in silico lens to look into protein aggregation kinetics at atomic resolution.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Influence of Cortisol on the Fibril Formation Kinetics of Aβ42 Peptide: A Multi-Technical Approach.International journal of molecular sciences · 2022Article
- Mechanisms of enhanced aggregation and fibril formation of Parkinson's disease-related variants of α-synuclein.Scientific reports · 2022Article
- Single-molecule fluorescence imaging and deep learning reveal highly heterogeneous aggregation of amyloid-β 42.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- General Principles Underpinning Amyloid Structure.Frontiers in neuroscience · 2022Review
- Influence of denaturants on amyloid β42 aggregation kinetics.Frontiers in neuroscience · 2022Article
- Computational Models for the Study of Protein Aggregation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021Review
- Rapid Conversion of Amyloid-Beta 1-40 Oligomers to Mature Fibrils through a Self-Catalytic Bimolecular Process.International journal of molecular sciences · 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
Corrections and comments
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Authors and funding
8 authors.
Funding
Abstract
The ability of biological molecules to replicate themselves, achieved with the aid of a complex cellular machinery, is the foundation of life. However, a range of aberrant processes involve the self-replication of pathological protein structures without any additional factors. A dramatic example is the autocatalytic replication of pathological protein aggregates, including amyloid fibrils and prions, involved in neurodegenerative disorders. Here, we use computer simulations to identify the necessary requirements for the self-replication of fibrillar assemblies of proteins. We establish that a key physical determinant for this process is the affinity of proteins for the surfaces of fibrils. We find that self-replication can only take place in a very narrow regime of inter-protein interactions, implying a high level of sensitivity to system parameters and experimental conditions. We then compare our theoretical predictions with kinetic and biosensor measurements of fibrils formed from the A
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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.