The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence
Open accessAbstract
Real-time monitoring of fibril growth is essential to clarify the mechanism of amyloid fibril formation. Thioflavin T (ThT) is a reagent known to become strongly fluorescent upon binding to amyloid fibrils. Here, we show that, by monitoring ThT fluorescence with total internal reflection fluorescence microscopy (TIRFM), amyloid fibrils of beta2-microgobulin (beta2-m) can be visualized without requiring covalent fluorescence labeling. One of the advantages of TIRFM would be that we selectively monitor fibrils lying along the slide glass, so that we can obtain the exact length of fibrils. This method was used to follow the kinetics of seed-dependent beta2-m fibril extension. The extension was unidirectional with various rates, suggesting the heterogeneity of the amyloid structures. Since ThT binding is common to all amyloid fibrils, the present method will have general applicability for the analysis of amyloid fibrils. We confirmed this with the octapeptide corresponding to the C terminus derived from human medin and the Alzheimer's amyloid beta-peptide.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Structure of the human class I histocompatibility antigen, HLA-A2
Bjorkman, P. J., Saper, M. A., Samraoui, B., Bennett, W. S., Strominger, J. L., & Wiley, D. C. (1987) · Nature · doi:10.1038/329506a0 · Cited by 3,472
Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
Naiki, H., Higuchi, K., Hosokawa, M., & Takeda, T. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90046-8 · Cited by 1,223
Self-citationFunatsu, T., Harada, Y., Tokunaga, M., Saito, K., & Yanagida, T. (1995) · Nature · doi:10.1038/374555a0 · Cited by 1,047
Gejyo, F., Yamada, T., Odani, S., Nakagawa, Y., Arakawa, M., Kunitomo, T., Kataoka, H., Suzuki, M., Hirasawa, Y., Shirahama, T., et al. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)91948-5 · Cited by 980
The Structure of Amyloid Fibrils by Electron Microscopy and X-Ray Diffraction
SUNDE, M., & BLAKE, C. (1997) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60320-4 · Cited by 767
The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
Fandrich, M. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf573 · Cited by 525
Sipe, J. D. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.004503 · Cited by 352
Protein-misfolding diseases: Getting out of shape
Dobson, C. M. (2002) · Nature · doi:10.1038/418729a · Cited by 341
Watching amyloid fibrils grow by time-lapse atomic force microscopy 1 1Edited by W. Baumeister
Goldsbury, C., Kistler, J., Aebi, U., Arvinte, T., & Cooper, G. J. S. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.2299 · Cited by 326
Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange
Hoshino, M., Katou, H., Hagihara, Y., Hasegawa, K., Naiki, H., & Goto, Y. (2002) · Nature Structural Biology · doi:10.1038/nsb792 · Cited by 315
Self-citation
Cited by
Mechanism of thioflavin T binding to amyloid fibrils
Khurana, R., Coleman, C., Ionescu-Zanetti, C., Carter, S. A., Krishna, V., Grover, R. K., Roy, R., & Singh, S. (2005) · Journal of Structural Biology · doi:10.1016/j.jsb.2005.06.006 · Cited by 831
The chemistry of Alzheimer’s disease
Rauk, A. (2009) · Chemical Society Reviews · doi:10.1039/b807980n · Cited by 417
Molecular Rotors: What Lies Behind the High Sensitivity of the Thioflavin-T Fluorescent Marker
Amdursky, N., Erez, Y., & Huppert, D. (2012) · Accounts of Chemical Research · doi:10.1021/ar300053p · Cited by 411
Functional amyloid in Pseudomonas
Dueholm, M. S., Petersen, S. V., Sønderkær, M., Larsen, P., Christiansen, G., Hein, K. L., Enghild, J. J., Nielsen, J. L., Nielsen, K. L., Nielsen, P. H., et al. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07269.x · Cited by 300
Atamna, H., & Boyle, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0600134103 · Cited by 290
Metadata
- Authors
- Ban, T., Hamada, D., Hasegawa, K., Naiki, H., & Goto, Y.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2003-05
- Volume
- 278
- Issue
- 19
- Pages
- 16462-16465
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2006510253
- Cited by
- 345
- References
- 20
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence. https://app.cochat.ai/papers/10.1074/jbc.c300049200
- The paper
- Ban, T., Hamada, D., Hasegawa, K., Naiki, H., & Goto, Y. (2003). Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.c300049200
Data sources
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.
