The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Atomic structure and hierarchical assembly of a cross-β amyloid fibril
Open accessAbstract
The cross-β amyloid form of peptides and proteins represents an archetypal and widely accessible structure consisting of ordered arrays of β-sheet filaments. These complex aggregates have remarkable chemical and physical properties, and the conversion of normally soluble functional forms of proteins into amyloid structures is linked to many debilitating human diseases, including several common forms of age-related dementia. Despite their importance, however, cross-β amyloid fibrils have proved to be recalcitrant to detailed structural analysis. By combining structural constraints from a series of experimental techniques spanning five orders of magnitude in length scale—including magic angle spinning nuclear magnetic resonance spectroscopy, X-ray fiber diffraction, cryoelectron microscopy, scanning transmission electron microscopy, and atomic force microscopy—we report the atomic-resolution (0.5 Å) structures of three amyloid polymorphs formed by an 11-residue peptide. These structures reveal the details of the packing interactions by which the constituent β-strands are assembled hierarchically into protofilaments, filaments, and mature fibrils.
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Cites
Protein Misfolding, Functional Amyloid, and Human Disease
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Self-citationSoluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
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Atomic structures of amyloid cross-β spines reveal varied steric zippers
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Cited by
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
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Self-citationCryo-EM structures of tau filaments from Alzheimer’s disease
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Metadata
- Authors
- Fitzpatrick, A. W. P., Debelouchina, G. T., Bayro, M. J., Clare, D. K., Caporini, M. A., Bajaj, V. S., Jaroniec, C. P., Wang, L., Ladizhansky, V., Müller, S. A., MacPhee, C. E., Waudby, C. A., Mott, H. R., De Simone, A., Knowles, T. P. J., Saibil, H. R., Vendruscolo, M., Orlova, E. V., Griffin, R. G., & Dobson, C. M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2013-03-19
- Volume
- 110
- Issue
- 14
- Pages
- 5468-5473
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2146656482
- Cited by
- 565
- References
- 43
- FWCI
- 36.11
- Type
- journal article
- Language
- en
- Open access
- bronze
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- The paper
- Fitzpatrick, A. W. P., Debelouchina, G. T., Bayro, M. J., Clare, D. K., Caporini, M. A., Bajaj, V. S., Jaroniec, C. P., Wang, L., Ladizhansky, V., Müller, S. A., MacPhee, C. E., Waudby, C. A., Mott, H. R., De Simone, A., Knowles, T. P. J., Saibil, H. R., Vendruscolo, M., Orlova, E. V., Griffin, R. G., & Dobson, C. M. (2013). Atomic structure and hierarchical assembly of a cross-β amyloid fibril. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.1219476110
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
