The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Structural polymorphism of Alzheimer Aβ and other amyloid fibrils
Open accessAbstract
Deposits of amyloid fibrils characterize a diverse group of human diseases that includes Alzheimer's disease, Creutzfeldt-Jakob disease and type II diabetes. Amyloid fibrils formed from different polypeptides contain a common cross-beta spine. Nevertheless, amyloid fibrils formed from the same polypeptide can occur in a range of structurally different morphologies. The heterogeneity of amyloid fibrils reflects different types of polymorphism: (i) variations in the protofilament number, (ii) variations in the protofilament arrangement and (iii) different polypeptide conformations. Amyloid fibril polymorphism implies that fibril 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
Exogenous Induction of Cerebral ß-Amyloidogenesis Is Governed by Agent and Host
Meyer-Luehmann, M., Coomaraswamy, J., Bolmont, T., Kaeser, S., Schaefer, C., Kilger, E., Neuenschwander, A., Abramowski, D., Frey, P., Jaton, A. L., et al. (2006) · Science · doi:10.1126/science.1131864 · Cited by 971
Prions of fungi: inherited structures and biological roles
Wickner, R. B., Edskes, H. K., Shewmaker, F., & Nakayashiki, T. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1708 · Cited by 231
Cited by
Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases
Soto, C., & Pritzkow, S. (2018) · Nature Neuroscience · doi:10.1038/s41593-018-0235-9 · Cited by 1,180
Multicomponent peptide assemblies
Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 346
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-citationAtomic-level differences between brain parenchymal- and cerebrovascular-seeded Aβ fibrils
Scherpelz, K. P., Wang, S., Pytel, P., Madhurapantula, R. S., Srivastava, A. K., Sachleben, J. R., Orgel, J., Ishii, Y., & Meredith, S. C. (2021) · Scientific Reports · doi:10.1038/s41598-020-80042-5 · Cited by 12
Metadata
- Authors
- Fändrich, M., Meinhardt, J., & Grigorieff, N.
- Venue
- Prion
- Publisher
- Informa UK Limited
- Published
- 2009-04
- Volume
- 3
- Issue
- 2
- Pages
- 89-93
- ISSN
- 1933-6896 (ISSN-L)
- 1933-690X
- OpenAlex
- W1964976698
- Cited by
- 258
- References
- 3
- FWCI
- 12.01
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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