The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Aβ(1-40) Fibril Polymorphism Implies Diverse Interaction Patterns in Amyloid Fibrils
Open accessAbstract
Amyloid fibrils characterize a diverse group of human diseases that includes Alzheimer’s disease, Creutzfeldt-Jakob and type II diabetes. Alzheimer’s amyloid fibrils consist of Aβ peptide and occur in a range of structurally different fibril morphologies. Using electron cryo-microscopy and three-dimensional reconstruction, we have determined here the structural characteristics of twelve single Aβ(1–40) amyloid fibrils, all formed under the same solution conditions. We find that the majority of analyzed fibrils form a range of morphologies that show almost continuously altering structural properties. The observed fibril polymorphism implies that amyloid formation can lead, for the same polypeptide sequence, to many different patterns of inter- or intra-residue interactions. This property differs significantly from native, monomeric protein folding reactions that produce, for one protein sequence, only one ordered conformation and only one set of inter-residue interactions.
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Cites
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650
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Neurodegenerative Diseases: Expanding the Prion Concept
Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361
Neuropathology and biochemistry of Aβ and its aggregates in Alzheimer’s disease
Thal, D. R., Walter, J., Saido, T. C., & Fändrich, M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1375-y · Cited by 319
Self-citationMechanism of amyloid plaque formation suggests an intracellular basis of Aβ pathogenicity
Friedrich, R. P., Tepper, K., Rönicke, R., Soom, M., Westermann, M., Reymann, K., Kaether, C., & Fändrich, M. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904532106 · Cited by 303
Self-citationFibril fragmentation in amyloid assembly and cytotoxicity: When size matters
Xue, W.-F., Hellewell, A. L., Hewitt, E. W., & Radford, S. E. (2010) · Prion · doi:10.4161/pri.4.1.11378 · Cited by 117
AlphaFold and the amyloid landscape
Pinheiro, F., Santos, J., & Ventura, S. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2021.167059 · Cited by 88
Specific Domains of Aβ Facilitate Aggregation on and Association with Lipid Bilayers
Yates, E. A., Owens, S. L., Lynch, M. F., Cucco, E. M., Umbaugh, C. S., & Legleiter, J. (2013) · Journal of Molecular Biology · doi:10.1016/j.jmb.2013.03.022 · Cited by 41
Beal, D. M., Tournus, M., Marchante, R., Purton, T. J., Smith, D. P., Tuite, M. F., Doumic, M., & Xue, W.-F. (2020) · iScience · doi:10.1016/j.isci.2020.101512 · Cited by 29
Metadata
- Authors
- Meinhardt, J., Sachse, C., Hortschansky, P., Grigorieff, N., & Fändrich, M.
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 386
- Issue
- 3
- Pages
- 869-877
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W1987686455
- Cited by
- 300
- References
- 2
- FWCI
- 12.47
- Type
- journal article
- Language
- en
- Open access
- green
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