The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Peptide Fibrillization
Abstract
The fibrillization of peptides is relevant to many diseases based on the deposition of amyloids. The formation of fibrils is being intensively studied, especially in terms of nanotechnology applications, where fibrillar peptide hydrogels are used for cell scaffolds, as supports for functional and responsive biomaterials, biosensors, and nanowires. This Review is concerned with fundamental aspects of the self‐assembly of peptides into fibrils, and discusses both natural amyloid‐forming peptides and synthetic materials, including peptide fragments, copolymers, and amphiphiles.
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
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Protein folding and misfolding
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Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
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Cited by
Malakoutikhah, M., Peyralans, J. J.-P., Colomb-Delsuc, M., Fanlo-Virgós, H., Stuart, M. C. A., & Otto, S. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4067805 · Cited by 111
Peptides for Vaccine Development
Hamley, I. W. (2022) · ACS Applied Bio Materials · doi:10.1021/acsabm.1c01238 · Cited by 104
Self-citationNeurodegenerative diseases and exposure to the environmental metals Mn, Pb, and Hg
Charlet, L., Chapron, Y., Faller, P., Kirsch, R., Stone, A. T., & Baveye, P. C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.05.012 · Cited by 92
Hu, T., Wang, S., Chen, C., Sun, J., & Yang, X. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04950 · Cited by 28
Vigneswaran, Y., Han, H., De Loera, R., Wen, Y., Zhang, X., Sun, T., Mora-Solano, C., & Collier, J. H. (2016) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.35767 · Cited by 26
Metadata
- Authors
- Hamley, I. W.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2007-10-26
- Volume
- 46
- Issue
- 43
- Pages
- 8128-8147
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W4211167864
- Cited by
- 618
- References
- 20
- FWCI
- 20.88
- Type
- journal article
- Language
- en
- Open access
- closed
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