The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
3D structure of Alzheimer's amyloid-β(1–42) fibrils
Open accessAbstract
Alzheimer's disease is the most fatal neurodegenerative disorder wherein the process of amyloid-β (Aβ) amyloidogenesis appears causative. Here, we present the 3D structure of the fibrils comprising Aβ(1–42), which was obtained by using hydrogen-bonding constraints from quenched hydrogen/deuterium-exchange NMR, side-chain packing constraints from pairwise mutagenesis studies, and parallel, in-register β-sheet arrangement from previous solid-state NMR studies. Although residues 1–17 are disordered, residues 18–42 form a β-strand–turn–β-strand motif that contains two intermolecular, parallel, in-register β-sheets that are formed by residues 18–26 (β1) and 31–42 (β2). At least two molecules of Aβ(1–42) are required to achieve the repeating structure of a protofilament. Intermolecular side-chain contacts are formed between the odd-numbered residues of strand β1 of the n th molecule and the even-numbered residues of strand β2 of the ( n – 1)th molecule. This interaction pattern leads to partially unpaired β-strands at the fibrillar ends, which explains the sequence selectivity, the cooperativity, and the apparent unidirectionality of Aβ fibril growth. It also provides a structural basis for fibrillization inhibitors.
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Cites
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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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Clearance systems in the brain—implications for Alzheimer disease
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In vivo demonstration that α-synuclein oligomers are toxic
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Self-citationStructural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111
Metadata
- Authors
- Lührs, T., Ritter, C., Adrian, M., Riek-Loher, D., Bohrmann, B., Döbeli, H., Schubert, D., & Riek, R.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2005-11-17
- Volume
- 102
- Issue
- 48
- Pages
- 17342-17347
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2122294662
- Cited by
- 1,996
- References
- 10
- FWCI
- 37.59
- Type
- journal article
- Language
- en
- Open access
- green
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