The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials
Abstract
Amyloid fibers constitute one of the most abundant and important naturally occurring self‐associated assemblies. A variety of protein and peptide molecules with various amino acid sequences form these highly stable and well‐organized assemblies under diverse conditions. These assemblies display phase states ranging from liquid crystals to rigid nanotubes. The potential applications of these supramolecular assemblies exceed those of synthetic polymers since the building blocks may introduce biological function in addition to mechanical properties. Here we review the structural characteristics of amyloidal supramolecular assemblies, their potential use as either natural or de novo designed sequences, and the range of applications that have been demonstrated so far.
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Cites
Bacterial Biofilms: A Common Cause of Persistent Infections
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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506
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Cited by
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade
Chiti, F., & Dobson, C. M. (2017) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-045115 · Cited by 2,629
Self-assembly and application of diphenylalanine-based nanostructures
Yan, X., Zhu, P., & Li, J. (2010) · Chemical Society Reviews · doi:10.1039/b915765b · Cited by 1,044
Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Dominguez, L., Shea, J.-E., Dokholyan, N. V., De Simone, A., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 678
Pathogenic protein seeding in Alzheimer disease and other neurodegenerative disorders
Jucker, M., & Walker, L. C. (2011) · Annals of Neurology · doi:10.1002/ana.22615 · Cited by 622
“This ‘cross-seeding’ is generally less potent than is homologous seeding, but the potential corruption of proteins by exogenous nanoscale materials, some of which may feature amyloid-like structural properties 103, 104 , should be factored into safety evaluations of such materials 41 .”
Background
Metadata
- Authors
- Cherny, I., & Gazit, E.
- Venue
- Angewandte Chemie International Edition
- Publisher
- Wiley
- Published
- 2008-05-09
- Volume
- 47
- Issue
- 22
- Pages
- 4062-4069
- ISSN
- 1433-7851 (ISSN-L)
- 1521-3773
- OpenAlex
- W1970736092
- Cited by
- 561
- References
- 5
- FWCI
- 16.88
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
