The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status
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Citations
Cites
Protein folding and misfolding
Dobson, C. M. (2003) · Nature · doi:10.1038/nature02261 · Cited by 4,791
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
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases
Bucciantini, M., Giannoni, E., Chiti, F., Baroni, F., Formigli, L., Zurdo, J., Taddei, N., Ramponi, G., Dobson, C. M., & Stefani, M. (2002) · Nature · doi:10.1038/416507a · Cited by 2,434
[18] Quantification of β-sheet amyloid fibril structures with thioflavin T
LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365
The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation
Nilsberth, C., Westlind-Danielsson, A., Eckman, C. B., Condron, M. M., Axelman, K., Forsell, C., Stenh, C., Luthman, J., Teplow, D. B., Younkin, S. G., et al. (2001) · Nature Neuroscience · doi:10.1038/nn0901-887 · Cited by 1,209
Klunk, W. E., Jacob, R. F., & Mason, R. P. (1999) · Analytical Biochemistry · doi:10.1006/abio.1998.2933 · Cited by 310
Lockhart, A., Ye, L., Judd, D. B., Merritt, A. T., Lowe, P. N., Morgenstern, J. L., Hong, G., Gee, A. D., & Brown, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m412056200 · Cited by 213
Cited by
ThT 101: a primer on the use of thioflavin T to investigate amyloid formation
Gade Malmos, K., Blancas-Mejia, L. M., Weber, B., Buchner, J., Ramirez-Alvarado, M., Naiki, H., & Otzen, D. (2017) · Amyloid · doi:10.1080/13506129.2017.1304905 · Cited by 445
Amyloid-binding compounds maintain protein homeostasis during ageing and extend lifespan
Alavez, S., Vantipalli, M. C., Zucker, D. J. S., Klang, I. M., & Lithgow, G. J. (2011) · Nature · doi:10.1038/nature09873 · Cited by 361
Wang, W., Liu, M., Gao, W., Sun, Y., & Dong, X. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c17267 · Cited by 53
Losev, Y., Paul, A., Frenkel-Pinter, M., Abu-Hussein, M., Khalaila, I., Gazit, E., & Segal, D. (2019) · Scientific Reports · doi:10.1038/s41598-019-39218-x · Cited by 50
Stefanescu, R., Stanciu, G. D., Luca, A., Paduraru, L., & Tamba, B.-I. (2020) · Biomolecules · doi:10.3390/biom10060870 · Cited by 35
Metadata
- Authors
- Groenning, M.
- Venue
- Journal of Chemical Biology
- Published
- 2009-08-20
- Volume
- 3
- Issue
- 1
- Pages
- 1-18
- ISSN
- 1864-6158 (ISSN-L)
- 1864-6166
- OpenAlex
- W2009604591
- Cited by
- 643
- References
- 7
- FWCI
- 16.14
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Groenning, M. (2010). Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils—current status. Journal of Chemical Biology. https://doi.org/10.1007/s12154-009-0027-5
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
