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[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

LeVine, Harry·1999·Methods in Enzymology

DOI 10.1016/s0076-6879(99)09020-5

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Vassar, 1959, Arch. Pathol., 68, 487
Kelenyi, 1967, J. Histochem. Cytochem., 15, 172, 10.1177/15.3.172 · DOI
Puchtler, 1983, Histochemistry, 77, 431, 10.1007/BF00495799 · DOI
Klunk, 1989, J. Histochem Cytochem., 37, 1273, 10.1177/37.8.2666510 · DOI
Klunk, 1999, Methods Enzymol., 309
Ashburn, 1996, Chem Biol., 3, 351, 10.1016/S1074-5521(96)90118-0 · DOI
Klunk, 1994, Neurobiol. Aging, 15, 691, 10.1016/0197-4580(94)90050-7 · DOI
W. E. Klunk, J. W. Pettigrew, and C. A. Mathis, Jr., International Patent WO 96/34853 (1996). · DOI
Naiki, 1989, Anal. Biochem., 177, 244, 10.1016/0003-2697(89)90046-8 · DOI
Naiki, 1990, Lab. Invest., 62, 768
Naiki, 1991, Lab. Invest., 65, 104
LeVine, 1993, Prot. Sci., 2, 404, 10.1002/pro.5560020312 · DOI
LeVine, 1995, Amyloid Int. J. Exp. Clin. Invest., 2, 1
Bonifacio, 1996, Biochim. Biophys. Acta, 1316, 35, 10.1016/0925-4439(96)00014-2 · DOI
Naiki, 1993, Lab. Invest., 68, 332
Maury, 1997, Biochem. Biophys. Res. Commun., 235, 249, 10.1006/bbrc.1997.6336 · DOI
Tagouri, 1996, Lab. Invest., 74, 290
Schweers, 1995, 92, 8463
Maury, 1994, Lab. Invest., 70, 558
Brancaccio, 1991, Biochem. Biophys. Res. Commun., 176, 1037, 10.1016/0006-291X(91)90387-M · DOI
LeVine, 1997, Arch. Biochem. Biophys., 342, 306, 10.1006/abbi.1997.0137 · DOI
Jao, 1997, Amyloid Int. J. Exp. Clin. Invest., 4, 240
Roher, 1988, J. Cell Biol., 107, 2703, 10.1083/jcb.107.6.2703 · DOI
Wood, 1996, Biochemistry, 35, 12623, 10.1021/bi961074j · DOI
Barrow, 1992, J. Mol Biol., 225, 1075, 10.1016/0022-2836(92)90106-T · DOI
Naiki, 1996, Lab. Invest., 74, 374
Evans, 1995, 92, 763
Chan, 1996, Biochemistry, 35, 7123, 10.1021/bi952852v · DOI
Burdick, 1997, Brain Res., 746, 275, 10.1016/S0006-8993(96)01262-0 · DOI · Paper page
Wood, 1996, J. Mol. Biol., 256, 870, 10.1006/jmbi.1996.0133 · DOI
Garzon-Rodriguez, 1997, J. Biol. Chem., 272, 21037, 10.1074/jbc.272.34.21037 · DOI

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Liu, B., Moloney, A. M., Meehan, S., Morris, K. L., Thomas, S. E., Serpell, L. C., Hider, R. C., Marciniak, S. J., Lomas, D. A., & Crowther, D. C. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.158980 · Cited by 222
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Furukawa, Y., Kaneko, K., Yamanaka, K., O’Halloran, T. V., & Nukina, N. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802083200 · Cited by 207
The Kinetics of Nucleated Polymerizations at High Concentrations: Amyloid Fibril Formation Near and Above the “Supercritical Concentration”
Powers, E. T., & Powers, D. L. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.073767 · Cited by 212
ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization
DiDonato, M., Craig, L., Huff, M. E., THAYER, M. M., Cardoso, R. M. F., Kassmann, C. J., Lo, T. P., Bruns, C. K., Powers, E. T., Kelly, J. W., et al. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00889-1 · Cited by 209
Spectral Properties of Thioflavin T and Its Complexes with Amyloid Fibrils
Voropai, E. S., Samtsov, M., Kaplevskii, K. N., Maskevich, A., Stepuro, V., Povarova, O., Kuznetsova, I. M., Turoverov, K., Fink, A. L., & Uverskii, V. N. (2003) · doi:10.1023/b:japs.0000016303.37573.7e · Cited by 206
Cross‐seeding effects of amyloid β‐protein and α‐synuclein
Ono, K., Takahashi, R., Ikeda, T., & Yamada, M. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07847.x · Cited by 222
“We used a well-characterized assay of fibril formation, thioflavin dye binding (LeVine 1999), to determine the effects of fibrils or cross-linked oligomers on peptide assembly.”
Method
Amyloid peptides and proteins in review
Harrison, R. S., Sharpe, P. C., Singh, Y., & Fairlie, D. P. (2007) · Springer eBooks · doi:10.1007/112_2007_0701 · Cited by 222
Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers
Luibl, V. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25843 · Cited by 203
Mechanisms of Protein Fibril Formation: Nucleated Polymerization with Competing Off-Pathway Aggregation
Powers, E. T., & Powers, D. L. (2007) · Biophysical Journal · doi:10.1529/biophysj.107.117168 · Cited by 207
Small Molecule Modulators of Copper-Induced Aβ Aggregation
Hindo, S. S., Mancino, A. M., Braymer, J. J., Liu, Y., Vivekanandan, S., Ramamoorthy, A., & Lim, M. H. (2009) · Journal of the American Chemical Society · doi:10.1021/ja907045h · Cited by 203
Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation
Ghosh, D., Singh, P. K., Sahay, S., Jha, N. N., Jacob, R. S., Sen, S., Kumar, A., Riek, R., & Maji, S. K. (2015) · Scientific Reports · doi:10.1038/srep09228 · Cited by 218
Amyloid‐fibril formation
Žerovnik, E. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.03024.x · Cited by 220
Spectral Properties of Thioflavin T in Solvents with Different Dielectric Properties and in a Fibril-Incorporated Form
Maskevich, A. A., Stsiapura, V. I., Kuzmitsky, V. A., Kuznetsova, I. М., Povarova, O. I., Uversky, V. N., & Константинович, Т. К. (2007) · Journal of Proteome Research · doi:10.1021/pr0605567 · Cited by 223
Hierarchical Assembly of β2-Microglobulin Amyloid In Vitro Revealed by Atomic Force Microscopy
Kad, N. M., Myers, S. L., Smith, D. P., Smith, D. A., Radford, S. E., & Thomson, N. H. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00583-7 · Cited by 204
The green tea polyphenol (−)‐epigallocatechin gallate prevents the aggregation of tau protein into toxic oligomers at substoichiometric ratios
Wobst, H. J., Sharma, A. M., Diamond, M. I., Wanker, E. E., & Bieschke, J. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.11.026 · Cited by 207
“ThT increases fluorescence on binding to b-sheet rich amyloid-like structures [25].”
Background
Prion Disease Blood Test Using Immunoprecipitation and Improved Quaking-Induced Conversion
Orrú, C., Wilham, J. M., Raymond, L., Kuhn, F., Schroeder, B., Raeber, A., & Caughey, B. (2011) · mBio · doi:10.1128/mbio.00078-11 · Cited by 195
Amyloid Fibril Formation by Lens Crystallin Proteins and Its Implications for Cataract Formation*
Meehan, S., Berry, Y. J., Luisi, B., Dobson, C., Carver, J., & MacPhee, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m308203200 · Cited by 195
Novel donepezil-based inhibitors of acetyl- and butyrylcholinesterase and acetylcholinesterase-induced beta-amyloid aggregation.
Camps, P., Formosa, X., Galdeano, C., Gómez, T., Muñoz-Torrero, D., Scarpellini, M., Viayna, E., Badía, A., Clos, M. V., Camins, A., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm8001313 · Cited by 194
Insights into the Mechanism of Aggregation and Fibril Formation from Bovine Serum Albumin
Bhattacharya, M., Jain, N., & Mukhopadhyay, S. (2011) · The Journal of Physical Chemistry B · doi:10.1021/jp111528c · Cited by 211
SDS-Induced Fibrillation of α-Synuclein: An Alternative Fibrillation Pathway
Giehm, L., Oliveira, C. L. P., Christiansen, G., Pedersen, J. S., & Otzen, D. E. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.060 · Cited by 198
“We quantify fibrillation through the fluorescent probe thioflavin T (ThT) whose emission intensity at 485 nm increases by several orders of magnitude in the presence of fibrils.(43) We incubated 20 μM αSN with 0–10 mM SDS without agitation”
Effects of Grape Seed-derived Polyphenols on Amyloid β-Protein Self-assembly and Cytotoxicity*
Ono, K., Condron, M. M., Ho, L., Wang, J., Zhao, W., Pasinetti, G. M., & Teplow, D. B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806154200 · Cited by 190
Metabolite-initiated protein misfolding may trigger Alzheimer's disease
Zhang, Q., Powers, E. T., Nieva, J. J., Huff, M. E., Dendle, M. A., Bieschke, J., Glabe, C. G., Eschenmoser, A., Wentworth, P., Lerner, R. A., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400924101 · Cited by 197
α-Synuclein Alters Toll-Like Receptor Expression
Béraud, D., Twomey, M. A., Bloom, B., Mittereder, A., Ton, V., Neitzke, K., Chasovskikh, S., Mhyre, T. R., & Maguire‐Zeiss, K. A. (2011) · Frontiers in Neuroscience · doi:10.3389/fnins.2011.00080 · Cited by 203
“, Liu, F., Pristupa, Z. B., and Niznik, H. B. (2001). Direct binding and functional coupling of alpha-synuclein to the dopamine transporters accelerate dopamine-induced apoptosis. FASEB J. 15, 916–926. Lee, H. J., Patel, S., and Lee, S. J. (2005). Intravesicular localization and exocytosis of alpha-synuclein and its a…”
BackgroundInfluential
Nanomaterials: amyloids reflect their brighter side
Mankar, S., Arunagiri, A., Sen, S., & Maji, S. K. (2011) · Nano Reviews · doi:10.3402/nano.v2i0.6032 · Cited by 182
Self healing hydrogels composed of amyloid nano fibrils for cell culture and stem cell differentiation
Jacob, R. S., Ghosh, D., Singh, P. K., Basu, S. K., Jha, N. N., Das, S., Sukul, P. K., Patil, S. P., Sathaye, S., Kumar, A., et al. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.03.002 · Cited by 200
Structural properties of pore-forming oligomers of alpha-synuclein.
Kim, H.-Y., Cho, M.-K., Kumar, A., Maier, E., Siebenhaar, C., Becker, S., Fernández, C., Lashuel, H., Benz, R., Lange, A., et al. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9077599 · Cited by 185
Synthesis of a library of oligothiophenes and their utilization as fluorescent ligands for spectral assignment of protein aggregates
Klingstedt, T., Åslund, A., Simon, R., Johansson, L. B. G., Mason, J., Nyström, S., Hammarström, P., & Nilsson, K. P. (2011) · Organic and biomolecular chemistry · doi:10.1039/c1ob05637a · Cited by 183
Structural mechanism of serum amyloid A-mediated inflammatory amyloidosis
Lu, J., Yu, Y., Zhu, I., Cheng, Y., & Sun, P. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1322357111 · Cited by 180
“1 and carried out fibril formation assays using thioflavin T (ThT) staining (29).”
Method
Aβ amyloid fibrils possess a core structure highly resistant to hydrogen exchange
Kheterpal, I., Zhou, S., Cook, K. D., & Wetzel, R. B. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.250288897 · Cited by 168
Multicomponent peptide assemblies
Raymond, D. M., & Nilsson, B. L. (2018) · Chemical Society Reviews · doi:10.1039/c8cs00115d · Cited by 348
Fluorescence Quantum Yield of Thioflavin T in Rigid Isotropic Solution and Incorporated into the Amyloid Fibrils
Sulatskaya, A. I., Maskevich, A. A., Kuznetsova, I. М., Uversky, V. N., & Константинович, Т. К. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015385 · Cited by 172

Authors: LeVine, H.
Corresponding author: LeVine, Harry
Venue: Methods in Enzymology
Publisher: Elsevier
Published: 1999
Volume: 309
Pages: 274-284
ISSN: 0076-6879 (ISSN-L)
DOI: 10.1016/s0076-6879(99)09020-5
OpenAlex: W1588296570
Cited by: 1,365
References: 25
Citations by year: 2026: 26 · 2025: 34 · 2024: 56 · 2023: 42 · 2022: 51 · 2021: 54 · 2020: 60 · 2019: 78 · 2018: 86 · 2017: 69 · 2016: 61 · 2015: 67 · 2014: 78 · 2013: 58 · 2012: 66
FWCI: 28.63
Type: book chapter
Language: en
Open access: closed
Locations: Methods in enzymology on CD-ROM/Methods in enzymology (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
Health Sciences › Medicine › Internal Medicine › Amyloidosis: Diagnosis, Treatment, Outcomes
Keywords: thioflavin T, amyloid fibrils, beta-sheet, amyloid quantification, Congo red, amyloid staining, amyloid fibril formation, fluorescence spectroscopy, Congo red birefringence
MeSH terms: Fluorescence, Hydrogen-Ion Concentration, Protein Binding, Spectrum Analysis, Thiazoles, Amyloid beta-Peptides, Protein Structure, Secondary, Benzothiazoles

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[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

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