The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Thioflavine T interaction with amyloid β-sheet structures
Abstract
Thioflavine T (ThT) interacts in tissue sections with amyloid deposits comprised of a variety of protein species giving a characteristic fluorescent complex. Binding of the dye to amyloid fibrils in suspension generates an amyloid-specific fluorescent signal. This interaction with amyloid fibrils formed from different polypeptides and proteins containing antiparallel β-pleated sheet secondary structure is selective, occurring strongly with amyloid fibrils formed from insulin, transthyretin, polyglycine(I), Aβ (1–40), and weakly with β2–microglobulin. No fluorescence changes were seen with β-sheet fibrillar poly-L-lysine, islet amyloid peptide (20–29), or poly-L-serine. Native forms of transthyretin, insulin, β2-microglobulin, poly-L-lysine, Aβ(1–40), or several proteins containing high percentages of β-sheet were also unreactive. The affinity of the amyloid fibrils for ThT varied: (apparent Kd's 0.033 – 10 μ Amyloid A protein <insulin <ApoAII <polyglycine <transthyretin
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Cites
Assembly and aggregation properties of synthetic Alzheimer's A4/beta amyloid peptide analogs.
Burdick, D., Soreghan, B., Kwon, M., Kosmoski, J., Knauer, M., Henschen, A., Yates, J., Cotman, C., & Glabe, C. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48529-8 · Cited by 1,014
Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation.
Westermark, P., Engström, U., Johnson, K. H., Westermark, G. T., & Betsholtz, C. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.13.5036 · Cited by 807
Cited by
Seeding Specificity in Amyloid Growth Induced by Heterologous Fibrils
O'Nuallain, B., Williams, A. D., Westermark, P., & Wetzel, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311300200 · Cited by 423
Dual Effect of Amino Modified Polystyrene Nanoparticles on Amyloid β Protein Fibrillation
Cabaleiro-Lago, C., Quinlan-Pluck, F., Lynch, I., Dawson, K. A., & Linse, S. (2010) · ACS Chemical Neuroscience · doi:10.1021/cn900027u · Cited by 275
Rodríguez-Rodríguez, C., Sánchez de Groot, N., Rimola, A., Álvarez-Larena, Á., Lloveras, V., Vidal-Gancedo, J., Ventura, S., Vendrell, J., Sodupe, M., & González-Duarte, P. (2009) · Journal of the American Chemical Society · doi:10.1021/ja806062g · Cited by 210
Rodríguez-Rodríguez, C., Telpoukhovskaia, M., & Orvig, C. (2012) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2012.03.008 · Cited by 151
Huang, Q., Zhao, Q., Peng, J., Yu, Y., Wang, C., Zou, Y., Su, Y., Zhu, L., Wang, C., & Yang, Y. (2019) · ACS Omega · doi:10.1021/acsomega.8b02797 · Cited by 25
Metadata
- Authors
- LeVine, H.
- Venue
- Amyloid
- Publisher
- Informa UK Limited
- Published
- 1995-01
- Volume
- 2
- Issue
- 1
- Pages
- 1-6
- ISSN
- 1350-6129 (ISSN-L)
- 1744-2818
- OpenAlex
- W2004593644
- Cited by
- 253
- References
- 2
- FWCI
- 0.84
- Type
- journal article
- Language
- en
- Open access
- closed
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