ArticleBiophysical journal2010
Characterizing the assembly of the Sup35 yeast prion fragment, GNNQQNY: structural changes accompany a fiber-to-crystal switch.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed.
- Cofactor-Free Tau Filaments Are Dynamic and Undergo Structural Evolution Driven by Thermodynamic Control.Journal of the American Chemical Society · 2026Article
- Inhibiting Disulfide Bonding in Truncated Tau297-391 Results in Enhanced Self-Assembly of Tau into Seed-Competent Assemblies.ACS chemical neuroscience · 2026Article
- Energy Landscapes and Heat Capacity Signatures for Monomers and Dimers of Amyloid-Forming Hexapeptides.International journal of molecular sciences · 2023Article
- Stability matters, too - the thermodynamics of amyloid fibril formation.Chemical science · 2022Review
- Linear Dichroism Activity of Chiral Poly(ACS omega · 2021Article
- Understanding and controlling amyloid aggregation with chirality.Current opinion in chemical biology · 2021Review
- Evolution of Conformation, Nanomechanics, and Infrared Nanospectroscopy of Single Amyloid Fibrils Converting into Microcrystals.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Clustering and Fibril Formation during GNNQQNY Aggregation: A Molecular Dynamics Study.Biomolecules · 2020Article
- Half a century of amyloids: past, present and future.Chemical Society reviews · 2020Review
- Amyloid Evolution: Antiparallel Replaced by Parallel.Biophysical journal · 2020Article
- Kinetic Control of Parallel versus Antiparallel Amyloid Aggregation via Shape of the Growing Aggregate.Scientific reports · 2019Article
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- Energetics Underlying Twist Polymorphisms in Amyloid Fibrils.The journal of physical chemistry. B · 2018Article
- 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
- The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.Acta crystallographica. Section D, Biological crystallography · 2015Article
- Article
- Exploring the sequence-structure relationship for amyloid peptides.The Biochemical journal · 2013Article
- Article
- Is photocleavage of DNA by YOYO-1 using a synchrotron radiation light source sequence dependent?European biophysics journal : EBJ · 2011Article
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Authors and funding
7 authors.
Funding
Abstract
Amyloid-like fibrils can be formed by many different proteins and peptides. The structural characteristics of these fibers are very similar to those of amyloid fibrils that are deposited in a number of protein misfolding diseases, including Alzheimer's disease and the transmissible spongiform encephalopathies. The elucidation of two crystal structures from an amyloid-like fibril-forming fragment of the yeast prion, Sup35, with sequence GNNQQNY, has contributed to knowledge regarding side-chain packing of amyloid-forming peptides. Both structures share a cross-beta steric zipper arrangement but vary in the packing of the peptide, particularly in terms of the tyrosine residue. We investigated the fibrillar and crystalline structure and assembly of the GNNQQNY peptide using x-ray fiber diffraction, electron microscopy, intrinsic and quenched tyrosine fluorescence, and linear dichroism. Electron micrographs reveal that at concentrations between 0.5 and 10 mg/mL, fibers form initially, followed by crystals. Fluorescence studies suggest that the environment of the tyrosine residue changes as crystals form. This is corroborated by linear dichroism experiments that indicate a change in the orientation of the tyrosine residue over time, which suggests that a structural rearrangement occurs as the crystals form. Experimental x-ray diffraction patterns from fibers and crystals also suggest that these species are structurally distinct. A comparison of experimental and calculated diffraction patterns contributes to an understanding of the different arrangements accessed by the peptide.
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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.