The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Structural and Dynamic Features of Alzheimer's Aβ Peptide in Amyloid Fibrils Studied by Site-directed Spin Labeling
Open accessAbstract
Electron paramagnetic resonance spectroscopy analysis of 19 spin-labeled derivatives of the Alzheimer's amyloid beta (Abeta) peptide was used to reveal structural features of amyloid fibril formation. In the fibril, extensive regions of the peptide show an in-register, parallel arrangement. Based on the parallel arrangement and side chain mobility analysis we find the amyloid structure to be mostly ordered and specific, but we also identify more dynamic regions (N and C termini) and likely turn or bend regions (around residues 23-26). Despite their different aggregation properties and roles in disease, the two peptides, Abeta40 and Abeta42, homogeneously co-mix in amyloid fibrils suggesting that they possess the same structural architecture.
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Cited by
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Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
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Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils
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Metadata
- Authors
- Török, M., Milton, S., Kayed, R., Wu, P., McIntire, T., Glabe, C. G., & Langen, R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2002-10
- Volume
- 277
- Issue
- 43
- Pages
- 40810-40815
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2080399081
- Cited by
- 373
- References
- 44
- FWCI
- 11.02
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Török, M., Milton, S., Kayed, R., Wu, P., McIntire, T., Glabe, C. G., & Langen, R. (2002). Structural and Dynamic Features of Alzheimer's Aβ Peptide in Amyloid Fibrils Studied by Site-directed Spin Labeling. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m205659200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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