The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structures for amyloid fibrils
Open accessAbstract
Alzheimer's disease and Creutzfeldt–Jakob disease are the best‐known examples of a group of diseases known as the amyloidoses. They are characterized by the extracellular deposition of toxic, insoluble amyloid fibrils. Knowledge of the structure of these fibrils is essential for understanding the process of pathology of the amyloidoses and for the rational design of drugs to inhibit or reverse amyloid formation. Structural models have been built using information from a wide variety of techniques, including X‐ray diffraction, electron microscopy, solid state NMR and EPR. Recent advances have been made in understanding the architecture of the amyloid fibril. Here, we describe and compare postulated structural models for the mature amyloid fibril and discuss how the ordered structure of amyloid contributes to its stability.
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Cites
Rationalization of the effects of mutations on peptide andprotein aggregation rates
Chiti, F., Stefani, M., Taddei, N., Ramponi, G., & Dobson, C. M. (2003) · Nature · doi:10.1038/nature01891 · Cited by 1,072
Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats
Perutz, M. F., & Windle, A. H. (2001) · Nature · doi:10.1038/35084141 · Cited by 199
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Reinke, A. A., & Gestwicki, J. E. (2007) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2007.00557.x · Cited by 329
Structural Basis for Increased Toxicity of Pathological Aβ42:Aβ40 Ratios in Alzheimer Disease
Pauwels, K., Williams, T. L., Morris, K. L., Jonckheere, W., Vandersteen, A., Kelly, G., Schymkowitz, J., Rousseau, F., Pastore, A., Serpell, L. C., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.264473 · Cited by 253
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Zucca, F. A., Basso, E., Cupaioli, F. A., Ferrari, E., Sulzer, D., Casella, L., & Zecca, L. (2014) · Neurotoxicity Research · doi:10.1007/s12640-013-9435-y · Cited by 243
Zecca, L., Bellei, C., Costi, P., Albertini, A., Monzani, E., Casella, L., Gallorini, M., Bergamaschi, L., Moscatelli, A., Turro, N. J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808768105 · Cited by 240
Metadata
- Authors
- Makin, O. S., & Serpell, L. C.
- Venue
- The FEBS Journal
- Publisher
- Wiley
- Published
- 2005-11-16
- Volume
- 272
- Issue
- 23
- Pages
- 5950-5961
- ISSN
- 1742-464X (ISSN-L)
- 1742-4658
- OpenAlex
- W1856532105
- Cited by
- 461
- References
- 2
- FWCI
- 18.25
- 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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