ArticleActa crystallographica. Section D, Biological crystallography2015
The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.
Article in Acta crystallographica. Section D, Biological crystallography, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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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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, 58 citations in OpenAlex.
- Encapsulated Control: Shaping Insulin Fibrillation through Polymer Confinement.Biomacromolecules · 2026Article
- Biomimetic supramolecular protein matrix restores structure and properties of human dental enamel.Nature communications · 2025Article
- Small-angle X-ray microdiffraction from fibrils embedded in tissue thin sections.Journal of applied crystallography · 2022Article
- Diabetes-Associated Mutations in Proinsulin Provide a "Molecular Rheostat" of Nascent Foldability.Current diabetes reports · 2022Review
- Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information.Frontiers in bioengineering and biotechnology · 2021Review
- Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amyloid Fibrils Converting into Microcrystals.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- The Impact of Halogenated Phenylalanine Derivatives on NFGAIL Amyloid Formation.Chembiochem : a European journal of chemical biology · 2020Article
- Liquid-Liquid Phase Separation and Its Mechanistic Role in Pathological Protein Aggregation.Journal of molecular biology · 2020Review
- MIRRAGGE - Minimum Information Required for Reproducible AGGregation Experiments.Frontiers in molecular neuroscience · 2020Review
- Serum amyloid A binds to fibrin(ogen), promoting fibrin amyloid formation.Scientific reports · 2019Article
- Early Stage Alpha-Synuclein Amyloid Fibrils are Reservoirs of Membrane-Binding Species.Scientific reports · 2019Article
- Early stages of aggregation of engineered α-synuclein monomers and oligomers in solution.Scientific reports · 2019Article
- Functional Amyloid and Other Protein Fibers in the Biofilm Matrix.Journal of molecular biology · 2018Review
- No effects without causes: the Iron Dysregulation and Dormant Microbes hypothesis for chronic, inflammatory diseases.Biological reviews of the Cambridge Philosophical Society · 2018Review
- To What Extent Are the Terminal Stages of Sepsis, Septic Shock, Systemic Inflammatory Response Syndrome, and Multiple Organ Dysfunction Syndrome Actually Driven by a Prion/Amyloid Form of Fibrin?Seminars in thrombosis and hemostasis · 2018Review
- The diversity and utility of amyloid fibrils formed by short amyloidogenic peptides.Interface focus · 2017Review
- Competition between crystal and fibril formation in molecular mutations of amyloidogenic peptides.Nature communications · 2017Article
- Lipopolysaccharide-binding protein (LBP) reverses the amyloid state of fibrin seen in plasma of type 2 diabetics with cardiovascular co-morbidities.Scientific reports · 2017Article
- The A2V mutation as a new tool for hindering Aβ aggregation: A neutron and x-ray diffraction study.Scientific reports · 2017Article
- Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Structural analysis of protein fibrillation is inherently challenging. Given the crucial role of fibrils in amyloid diseases, method advancement is urgently needed. A hybrid modelling approach is presented enabling detailed analysis of a highly ordered and hierarchically organized fibril of the GNNQQNY peptide fragment of a yeast prion protein. Data from small-angle X-ray solution scattering, fibre diffraction and electron microscopy are combined with existing high-resolution X-ray crystallographic structures to investigate the fibrillation process and the hierarchical fibril structure of the peptide fragment. The elongation of these fibrils proceeds without the accumulation of any detectable amount of intermediate oligomeric species, as is otherwise reported for, for example, glucagon, insulin and α-synuclein. Ribbons constituted of linearly arranged protofilaments are formed. An additional hierarchical layer is generated via the pairing of ribbons during fibril maturation. Based on the complementary data, a quasi-atomic resolution model of the protofilament peptide arrangement is suggested. The peptide structure appears in a β-sheet arrangement reminiscent of the β-zipper structures evident from high-resolution crystal structures, with specific differences in the relative peptide orientation. The complexity of protein fibrillation and structure emphasizes the need to use multiple complementary methods.
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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.