The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease
Open accessAbstract
Increasing evidence has suggested that formation and propagation of misfolded aggregates of 42-residue human amyloid β (Aβ(1–42)), rather than of the more abundant Aβ(1–40), provokes the Alzheimer's disease cascade. However, structural details of misfolded Aβ(1–42) have remained elusive. Here we present the atomic model of an Aβ(1–42) amyloid fibril, from solid-state NMR (ssNMR) data. It displays triple parallel-β-sheet segments that differ from reported structures of Aβ(1–40) fibrils. Remarkably, Aβ(1–40) is incompatible with the triple-β-motif, because seeding with Aβ(1–42) fibrils does not promote conversion of monomeric Aβ(1–40) into fibrils via cross-replication. ssNMR experiments suggest that C-terminal Ala42, absent in Aβ(1–40), forms a salt bridge with Lys28 to create a self-recognition molecular switch that excludes Aβ(1–40). The results provide insight into the Aβ(1–42)-selective self-replicating amyloid-propagation machinery in early-stage Alzheimer's disease.
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Structural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
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Amyloid β Protein (Aβ) in Alzheimeri's Disease Brain
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Cited by
Cryo-EM structure of islet amyloid polypeptide fibrils reveals similarities with amyloid-β fibrils
Röder, C., Kupreichyk, T., Gremer, L., Schäfer, L. U., Pothula, K. R., Ravelli, R. B. G., Willbold, D., Hoyer, W., & Schröder, G. F. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0442-4 · Cited by 180
Structure of Crenezumab Complex with Aβ Shows Loss of β-Hairpin
Ultsch, M., Li, B., Maurer, T., Mathieu, M., Adolfsson, O., Muhs, A., Pfeifer, A., Pihlgren, M., Bainbridge, T. W., Reichelt, M., et al. (2016) · Scientific Reports · doi:10.1038/srep39374 · Cited by 124
Green Tea Extracts EGCG and EGC Display Distinct Mechanisms in Disrupting Aβ42 Protofibril
Zhan, C., Chen, Y., Tang, Y., & Wei, G. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00277 · Cited by 115
Riad, A., Lengyel-Zhand, Z., Zeng, C., Weng, C.-C., Lee, V. M.-Y., Trojanowski, J. Q., & Mach, R. H. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01988-1 · Cited by 81
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Metadata
- Authors
- Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M., Nussinov, R., & Ishii, Y.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2015-05-04
- Volume
- 22
- Issue
- 6
- Pages
- 499-505
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W1961186421
- Cited by
- 818
- References
- 7
- FWCI
- 58.97
- Type
- journal article
- Language
- en
- Open access
- green
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- Xiao, Y., Ma, B., McElheny, D., Parthasarathy, S., Long, F., Hoshi, M., Nussinov, R., & Ishii, Y. (2015). Aβ(1–42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.2991
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