ArticleJournal of the American Chemical Society2011
Characteristics of amyloid-related oligomers revealed by crystal structures of macrocyclic β-sheet mimics.
Article in Journal of the American Chemical Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed.
- Backbone double-mutant cycle analysis quantifies hydrogen-bond energies in proteins.Protein science : a publication of the Protein Society · 2026Article
- Gangliosides GM3 And GD3 Modulate Insulin Aggregation Pathways and Reduce Cytotoxicity Through Structural Remodeling.bioRxiv : the preprint server for biology · 2026Article
- β-Hairpin Alignment Alters Oligomer Formation in Aβ-Derived Peptides.Biochemistry · 2024Article
- Optimizing Epitope Conformational Ensembles Using α-Synuclein Cyclic Peptide "Glycindel" Scaffolds: A Customized Immunogen Method for Generating Oligomer-Selective Antibodies for Parkinson's Disease.ACS chemical neuroscience · 2022Article
- Therapeutic peptides: current applications and future directions.Signal transduction and targeted therapy · 2022Review
- Visualizing and trapping transient oligomers in amyloid assembly pathways.Biophysical chemistry · 2021Review
- Synthesis and study of macrocyclic β-hairpin peptides for investigating amyloid oligomers.Methods in enzymology · 2021Article
- The biofilm adhesion protein Aap fromThe Journal of biological chemistry · 2020Article
- Filamentous Aggregates of Tau Proteins Fulfil Standard Amyloid Criteria Provided by the Fuzzy Oil Drop (FOD) Model.International journal of molecular sciences · 2018Article
- Atomic structures of corkscrew-forming segments of SOD1 reveal varied oligomer conformations.Protein science : a publication of the Protein 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
- The Unexpected Role of Aβ1-42 Monomers in the Pathogenesis of Alzheimer's Disease.Journal of Alzheimer's disease : JAD · 2018Review
- A Hexamer of a Peptide Derived from AβBiochemistry · 2017Article
- Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.Chemical Society reviews · 2017Review
- Somatostatin binds to the human amyloid β peptide and favors the formation of distinct oligomers.eLife · 2017Article
- Chemical Methods to Knock Down the Amyloid Proteins.Molecules (Basel, Switzerland) · 2017Review
- Square channels formed by a peptide derived from transthyretin.Chemical science · 2016Article
- An Atomistic View of Amyloidogenic Self-assembly: Structure and Dynamics of Heterogeneous Conformational States in the Pre-nucleation Phase.Scientific reports · 2016Article
- Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets.The journal of physical chemistry. B · 2016Article
- X-ray Crystallographic Structure of Oligomers Formed by a Toxic β-Hairpin Derived from α-Synuclein: Trimers and Higher-Order Oligomers.Journal of the American Chemical Society · 2016Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Protein amyloid oligomers have been strongly linked to amyloid diseases and can be intermediates to amyloid fibers. β-Sheets have been identified in amyloid oligomers. However, because of their transient and highly polymorphic properties, the details of their self-association remain elusive. Here we explore oligomer structure using a model system: macrocyclic peptides. Key amyloidogenic sequences from Aβ and tau were incorporated into macrocycles, thereby restraining them to β-strands, but limiting the growth of the oligomers so they may crystallize and cannot fibrillate. We determined the atomic structures for four such oligomers, and all four reveal tetrameric interfaces in which β-sheet dimers pair together by highly complementary, dry interfaces, analogous to steric zippers found in fibers, suggesting a common structure for amyloid oligomers and fibers. In amyloid fibers, the axes of the paired sheets are either parallel or antiparallel, whereas the oligomeric interfaces display a variety of sheet-to-sheet pairing angles, offering a structural explanation for the heterogeneity of amyloid oligomers.
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