ArticleJournal of the American Chemical Society2013
Crystal structure of a human prion protein fragment reveals a motif for oligomer formation.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- The structure of complexes between zinc(ii) cations and histidine-rich repeats from the unstructured N-terminal domain of human prion protein.RSC advances · 2025Review
- Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer's Disease, Parkinson's Disease and Prionopathies.International journal of molecular sciences · 2024Review
- Probing differences among Aβ oligomers with two triangular trimers derived from Aβ.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Amyloid oligomers as on-pathway precursors or off-pathway competitors of fibrils.Frontiers in molecular biosciences · 2023Review
- Origin, toxicity and characteristics of two amyloid oligomer polymorphs.RSC chemical biology · 2021Article
- Exploring amyloid oligomers with peptide model systems.Current opinion in chemical biology · 2021Review
- In Silico Modeling of the Influence of Environment on Amyloid Folding Using FOD-M Model.International journal of molecular sciences · 2021Article
- X-ray Crystallography Reveals Parallel and Antiparallel β-Sheet Dimers of a β-Hairpin Derived from AβACS chemical neuroscience · 2020Article
- Article
- The polar clasps of a bank vole PrP(168-176) prion protofibril revisiting.Journal of molecular modeling · 2019Article
- Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease.Scientific reports · 2018Article
- Origin of metastable oligomers and their effects on amyloid fibril self-assembly.Chemical science · 2018Article
- Controlling the Oligomerization State of Aβ-Derived Peptides with Light.Journal of the American Chemical Society · 2018Article
- Elucidating the Structures of Amyloid Oligomers with Macrocyclic β-Hairpin Peptides: Insights into Alzheimer's Disease and Other Amyloid Diseases.Accounts of chemical research · 2018Review
- A Hexamer of a Peptide Derived from AβBiochemistry · 2017Article
- Toward the Atomic Structure of PrPCold Spring Harbor perspectives in biology · 2017Review
- Theory of amyloid fibril nucleation from folded proteins.Israel journal of chemistry · 2017Article
- Crystal Structure of the DFNKF Segment of Human Calcitonin Unveils Aromatic Interactions between Phenylalanines.Chemistry (Weinheim an der Bergstrasse, Germany) · 2017Article
- The Biological Function of the Prion Protein: A Cell Surface Scaffold of Signaling Modules.Frontiers in molecular neuroscience · 2017Article
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Authors and funding
3 authors.
Funding
Abstract
The structural transition of the prion protein from α-helical- to β-sheet-rich underlies its conversion into infectious and disease-associated isoforms. Here we describe the crystal structure of a fragment from human prion protein consisting of the disulfide-bond-linked portions of helices 2 and 3. Instead of forming a pair-of-sheets steric zipper structure characteristic of amyloid fibers, this fragment crystallized into a β-sheet-rich assembly of hexameric oligomers. This study reveals a never before observed structural motif for ordered protein aggregates and suggests a possible mechanism for self-propagation of misfolded conformations by such nonamyloid oligomers.
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