ArticleProceedings of the National Academy of Sciences of the United States of America2015
Nanomechanics and intermolecular forces of amyloid revealed by four-dimensional electron microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Repositioning of polyubiquitin alters the pathologic tau filament structure.Nature structural & molecular biology · 2026Article
- Spontaneous aging of mature amyloids alters structural stability, cytotoxicity, and susceptibility to biological clearance.Cell death discovery · 2026Article
- Catalytic Amyloids: Turning Fibrils Into Biocatalysts.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Relativistic ultrafast electron diffraction at high repetition rates.Structural dynamics (Melville, N.Y.) · 2023Article
- Time-resolved transmission electron microscopy for nanoscale chemical dynamics.Nature reviews. Chemistry · 2023Review
- Article
- Computer Simulations Aimed at Exploring Protein Aggregation and Dissociation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- 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
- α-Synuclein fibril-induced inclusion spread in rats and mice correlates with dopaminergic Neurodegeneration.Neurobiology of disease · 2017Article
- Ultrafast atomic-scale visualization of acoustic phonons generated by optically excited quantum dots.Structural dynamics (Melville, N.Y.) · 2017Article
- Mapping the Broad Structural and Mechanical Properties of Amyloid Fibrils.Biophysical journal · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amyloid state of polypeptides is a stable, highly organized structural form consisting of laterally associated β-sheet protofilaments that may be adopted as an alternative to the functional, native state. Identifying the balance of forces stabilizing amyloid is fundamental to understanding the wide accessibility of this state to peptides and proteins with unrelated primary sequences, various chain lengths, and widely differing native structures. Here, we use four-dimensional electron microscopy to demonstrate that the forces acting to stabilize amyloid at the atomic level are highly anisotropic, that an optimized interbackbone hydrogen-bonding network within β-sheets confers 20 times more rigidity on the structure than sequence-specific sidechain interactions between sheets, and that electrostatic attraction of protofilaments is only slightly stronger than these weak amphiphilic interactions. The potential biological relevance of the deposition of such a highly anisotropic biomaterial in vivo is discussed.
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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.