The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact register
Open accessAbstract
The pathognomonic plaques of Alzheimer’s disease are composed primarily of the 39- to 43-aa β-amyloid (Aβ) peptide. Crosslinking of Aβ peptides by tissue transglutaminase (tTg) indicates that Gln 15 of one peptide is proximate to Lys 16 of another in aggregated Aβ. Here we report how the fibril structure is resolved by mapping interstrand distances in this core region of the Aβ peptide chain with solid-state NMR. Isotopic substitution provides the source points for measuring distances in aggregated Aβ. Peptides containing a single carbonyl 13 C label at Gln 15 , Lys 16 , Leu 17 , or Val 18 were synthesized and evaluated by NMR dipolar recoupling methods for the measurement of interpeptide distances to a resolution of 0.2 Å. Analysis of these data establish that this central core of Aβ consists of a parallel β-sheet structure in which identical residues on adjacent chains are aligned directly, i.e., in register. Our data, in conjunction with existing structural data, establish that the Aβ fibril is a hydrogen-bonded, parallel β-sheet defining the long axis of the Aβ fibril propagation.
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The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
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Protein aggregation and neurodegenerative disease
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Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development
Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965
Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils
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Experimental Constraints on Quaternary Structure in Alzheimer's β-Amyloid Fibrils
Petkova, A. T., Yau, W.-M., & Tycko, R. (2006) · Biochemistry · doi:10.1021/bi051952q · Cited by 1,044
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Metadata
- Authors
- Benzinger, T. L. S., Gregory, D. M., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Botto, R. E., & Meredith, S. C.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1998-11-10
- Volume
- 95
- Issue
- 23
- Pages
- 13407-13412
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W1965973197
- Cited by
- 389
- References
- 5
- FWCI
- 8.63
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact register. https://app.cochat.ai/papers/10.1073/pnas.95.23.13407
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- Benzinger, T. L. S., Gregory, D. M., Burkoth, T. S., Miller-Auer, H., Lynn, D. G., Botto, R. E., & Meredith, S. C. (1998). Propagating structure of Alzheimer’s β-amyloid (10–35) is parallel β-sheet with residues in exact register. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.95.23.13407
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
