The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
Insight into Amyloid Structure Using Chemical Probes
Open accessAbstract
Alzheimer’s disease (AD) is a common neurodegenerative disorder characterized by the deposition of amyloids in the brain. One prominent form of amyloid is composed of repeating units of the amyloid‐β (Aβ) peptide. Over the past decade, it has become clear that these Aβ amyloids are not homogeneous; rather, they are composed of a series of structures varying in their overall size and shape and the number of Aβ peptides they contain. Recent theories suggest that these different amyloid conformations may play distinct roles in disease, although their relative contributions are still being discovered. Here, we review how chemical probes, such as Congo red, thioflavin T and their derivatives, have been powerful tools for the better understanding of amyloid structure and function. Moreover, we discuss how design and deployment of conformationally selective probes might be used to test emerging models of AD.
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Citations
Cites
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
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[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
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“One of the first important observations was made by LeVine (25), who proposed that there are multiple binding sites for ThT on amyloids.”
BackgroundStructural conversion of neurotoxic amyloid-β1–42 oligomers to fibrils
Ahmed, M., Davis, J., Aucoin, D., Sato, T., Ahuja, S., Aimoto, S., Elliott, J. I., Van Nostrand, W. E., & Smith, S. O. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1799 · Cited by 1,111
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Amyloid β-Protein Fibrillogenesis
Walsh, D. M., Hartley, D. M., Kusumoto, Y., Fezoui, Y., Condron, M. M., Lomakin, A., Benedek, G. B., Selkoe, D. J., & Teplow, D. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25945 · Cited by 1,046
Arrest of -Amyloid Fibril Formation by a Pentapeptide Ligand
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Synaptic Targeting by Alzheimer's-Related Amyloid β Oligomers
Lacor, P. N., Buniel, M. C., Chang, L., Fernandez, S. J., Gong, Y., Viola, K. L., Lambert, M. P., Velasco, P. T., Bigio, E. H., Finch, C. E., et al. (2004) · The Journal of Neuroscience · doi:10.1523/jneurosci.3432-04.2004 · Cited by 954
Cited by
Smith, M. C., & Gestwicki, J. E. (2012) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2012.10 · Cited by 286
Self-citationRodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151
Reactivity of Diphenylpropynone Derivatives Toward Metal-Associated Amyloid-β Species
Pithadia, A. S., Kochi, A., Soper, M. T., Beck, M. W., Liu, Y., Lee, S., DeToma, A. S., Ruotolo, B. T., & Lim, M. H. (2012) · Inorganic Chemistry · doi:10.1021/ic302084g · Cited by 38
Metadata
- Authors
- Reinke, A. A., & Gestwicki, J. E.
- Venue
- Chemical Biology & Drug Design
- Publisher
- Wiley
- Published
- 2011-04-26
- Volume
- 77
- Issue
- 6
- Pages
- 399-411
- ISSN
- 1747-0277 (ISSN-L)
- 1747-0285
- OpenAlex
- W1532763771
- Cited by
- 169
- References
- 16
- FWCI
- 10.02
- Type
- journal article
- Language
- en
- Open access
- bronze
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