ArticleBiophysical journal2017
Mapping the Broad Structural and Mechanical Properties of Amyloid Fibrils.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
20 citing papers in PubMed, 48 citations in OpenAlex.
- From Pathology to Materials Science and Engineering: Harnessing the Amyloid State for Biotechnological Applications.ACS applied materials & interfaces · 2025Review
- Strategies for Making High-Performance Artificial Spider Silk Fibers.Advanced functional materials · 2024Review
- ZBP1 condensate formation synergizes Z-NAs recognition and signal transduction.Cell death & disease · 2024Article
- HSPA8 acts as an amyloidase to suppress necroptosis by inhibiting and reversing functional amyloid formation.Cell research · 2023Article
- Morphoscanner2.0: A new python module for analysis of molecular dynamics simulations.PloS one · 2023Article
- Catalytically Active Amyloids as Future Bionanomaterials.Nanomaterials (Basel, Switzerland) · 2022Review
- What makes functional amyloids work?Critical reviews in biochemistry and molecular biology · 2022Review
- A central role for amyloid fibrin microclots in long COVID/PASC: origins and therapeutic implications.The Biochemical journal · 2022Review
- The Protein Folding Problem: The Role of Theory.Journal of molecular biology · 2021Review
- Self-assembly of aramid amphiphiles into ultra-stable nanoribbons and aligned nanoribbon threads.Nature nanotechnology · 2021Article
- Adjusting the length of supramolecular polymer bottlebrushes by top-down approaches.Beilstein journal of organic chemistry · 2021Article
- Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amyloid Fibrils Converting into Microcrystals.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Atomic Force Microscopy Imaging and Nanomechanical Properties of Six Tau Isoform Assemblies.Biophysical journal · 2020Article
- Probing mechanical properties and failure mechanisms of fibrils of self-assembling peptides.Nanoscale advances · 2020Article
- Design Parameters of Tissue-Engineering Scaffolds at the Atomic Scale.Angewandte Chemie (International ed. in English) · 2019Article
- Dissolution of a fibrous peptide by terahertz free electron laser.Scientific reports · 2019Article
- Autophagy regulates inflammatory programmed cell death via turnover of RHIM-domain proteins.eLife · 2019Article
- Atomic force microscopy for single molecule characterisation of protein aggregation.Archives of biochemistry and biophysics · 2019Review
- Selective autophagy of the adaptor TRIF regulates innate inflammatory signaling.Nature immunology · 2018Article
- High Tensile Strength of Engineered β-Solenoid Fibrils via Sonication and Pulling.Biophysical journal · 2017Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
Amyloids are fibrillar nanostructures of proteins that are assembled in several physiological processes in human cells (e.g., hormone storage) but also during the course of infectious (prion) and noninfectious (nonprion) diseases such as Creutzfeldt-Jakob and Alzheimer's diseases, respectively. How the amyloid state, a state accessible to all proteins and peptides, can be exploited for functional purposes but also have detrimental effects remains to be determined. Here, we measure the nanomechanical properties of different amyloids and link them to features found in their structure models. Specifically, we use shape fluctuation analysis and sonication-induced scission in combination with full-atom molecular dynamics simulations to reveal that the amyloid fibrils of the mammalian prion protein PrP are mechanically unstable, most likely due to a very low hydrogen bond density in the fibril structure. Interestingly, amyloid fibrils formed by HET-s, a fungal protein that can confer functional prion behavior, have a much higher Young's modulus and tensile strength than those of PrP, i.e., they are much stiffer and stronger due to a tighter packing in the fibril structure. By contrast, amyloids of the proteins RIP1/RIP3 that have been shown to be of functional use in human cells are significantly stiffer than PrP fibrils but have comparable tensile strength. Our study demonstrates that amyloids are biomaterials with a broad range of nanomechanical properties, and we provide further support for the strong link between nanomechanics and β-sheet characteristics in the amyloid core.
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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.