Cited by 1,365Alzheimer's disease research and treatmentsPrion Diseases and Protein MisfoldingAmyloidosis: Diagnosis, Treatment, Outcomes

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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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Shivaprasad, S., & Wetzel, R. B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505091200 · Cited by 71
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Ho, L., Zhao, D., Ono, K., Ruan, K., Mogno, I., Tsuji, M., Carry, E., Brathwaite, J. S., Sims, S. L., Frolinger, T., et al. (2018) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2018.10.019 · Cited by 74
Rational Design and Identification of a Non‐Peptidic Aggregation Inhibitor of Amyloid‐β Based on a Pharmacophore Motif Obtained from cyclo[‐Lys‐Leu‐Val‐Phe‐Phe‐]
Arai, T., Araya, T., Sasaki, D., Taniguchi, A., Sato, T., Sohma, Y., & Kanai, M. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201405109 · Cited by 84
Long-Term Treatment of Thalidomide Ameliorates Amyloid-Like Pathology through Inhibition of β-Secretase in a Mouse Model of Alzheimer’s Disease
He, P., Cheng, X., Staufenbiel, M., Li, R., & Shen, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055091 · Cited by 75
The osmolyte betaine promotes protein misfolding and disruption of protein aggregates
Natalello, A., Liu, J. L., Ami, D., Doglia, S. M., & de Marco, A. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22266 · Cited by 74
Adsorption of Frog Foam Nest Proteins at the Air-Water Interface
Cooper, A., Kennedy, M. W., Fleming, R. I., Wilson, E. H., Videler, H., Wokosin, D. L., Su, T.-J., Green, R. J., & Lu, J. R. (2004) · Biophysical Journal · doi:10.1529/biophysj.104.046268 · Cited by 71
Enhanced in vitro production of amyloid-like fibrils from mutant (S20G) islet amyloid polypeptide
Ma, Z., Westermark, G., Sakagashira, S., Sanke, T., Gustavsson, Å., Sakamoto, H., Engström, U., Nanjo, K., & Westermark, P. (2001) · Amyloid: Journal of Protein Folding Disorders · doi:10.3109/13506120108993820 · Cited by 69
Peptide-Stabilized Emulsions and Gels from an Arginine-Rich Surfactant-like Peptide with Antimicrobial Activity
Castelletto, V., Edwards-Gayle, C., Hamley, I., Barrett, G. A., Seitsonen, J., & Ruokolainen, J. (2019) · ACS Applied Materials and Interfaces · doi:10.1021/acsami.9b00581 · Cited by 68
The amyloid architecture provides a scaffold for enzyme-like catalysts
Al‐Garawi, Z. S., McIntosh, B. A., Neill‐Hall, D., Hatimy, A. A., Sweet, S. M. M., Bagley, M. C., & Serpell, L. C. (2017) · Nanoscale · doi:10.1039/c7nr02675g · Cited by 120
Both lipopolysaccharide and lipoteichoic acids potently induce anomalous fibrin amyloid formation: assessment with novel Amytracker™ stains
Pretorius, E., Page, M., Hendricks, L. M., Nkosi, N. B., Benson, S. R., & Kell, D. (2017) · bioRxiv · doi:10.1098/rsif.2017.0941 · Cited by 68
“[11, 34-50]), a considerable number of other fluorogenic stains have been shown to illuminate amyloids (e.”
Coassembly of amphiphilic peptide EAK16-II with histidinylated analogues and implications for functionalization of β-sheet fibrils in vivo.
Wen, Y., Roudebush, S. L., Buckholtz, G. A., Goehring, T., Giannoukakis, N., Gawalt, E., & Meng, W. S. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.03.009 · Cited by 68
Promising in Vitro anti-Alzheimer Properties for a Ruthenium(III) Complex.
Messori, L., Camarri, M., Ferraro, T., Gabbiani, C., & Franceschini, D. (2013) · ACS Medicinal Chemistry Letters · doi:10.1021/ml3003567 · Cited by 68
A New Trend in the Experimental Methodology for the Analysis of the Thioflavin T Binding to Amyloid Fibrils
Kuznetsova, I. М., Sulatskaya, A. I., Uversky, V. N., & Константинович, Т. К. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8272-y · Cited by 69
Kinetics of insulin aggregation: disentanglement of amyloid fibrillation from large-size cluster formation.
Manno, M., Craparo, E. F., Martorana, V., Bulone, D., & Biagio, P. L. S. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.077636 · Cited by 68
Influence of the N‐terminal domain on the aggregation properties of the prion protein
Frankenfield, K. N., Powers, E. T., & Kelly, J. W. (2005) · Protein Science · doi:10.1110/ps.051434005 · Cited by 68
Amyloid aggregates of the prion peptide PrP106–126 are destabilised by oxidation and by the action of dendrimers
Heegaard, P. M. H., Pedersen, H. G., Flink, J. M., & Boas, U. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.09.073 · Cited by 64
Insulin inhibits amyloid β-induced cell death in cultured human brain pericytes
Rensink, A. A. M., Otte‐Höller, I., de Boer, R., Bosch, R. R., ten Donkelaar, H. J., de Waal, R. M. W., Verbeek, M. M., & Kremer, B. P. H. (2003) · Neurobiology of Aging · doi:10.1016/s0197-4580(03)00039-3 · Cited by 82
Intrinsic Fibrillation of Fast-Acting Insulin Analogs
Woods, R. J., Alarcón, J., McVey, E., & Pettis, R. J. (2012) · Journal of Diabetes Science and Technology · doi:10.1177/193229681200600209 · Cited by 75
Copper Alters Aggregation Behavior of Prion Protein and Induces Novel Interactions between Its N- and C-terminal Regions
Thakur, A., Srivastava, A. K., Srinivas, V., Chary, K. R., & Rao, C. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.265645 · Cited by 67
Residue-Specific, Real-Time Characterization of Lag-Phase Species and Fibril Growth During Amyloid Formation: A Combined Fluorescence and IR Study of p-Cyanophenylalanine Analogs of Islet Amyloid Polypeptide
Marek, P., Mukherjee, S. S., Zanni, M. T., & Raleigh, D. P. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.041 · Cited by 76
Thioflavin T fluorescence anisotropy: an alternative technique for the study of amyloid aggregation.
Sabaté, R., & Saupe, S. (2007) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2007.06.063 · Cited by 67
Role of phenylalanine 20 in Alzheimer's amyloid beta-peptide (1-42)-induced oxidative stress and neurotoxicity.
Boyd-Kimball, D., Abdul, H. M., Reed, T. T., Sultana, R., & Butterfield, D. (2004) · Chemical Research in Toxicology · doi:10.1021/tx049796w · Cited by 67
Human apolipoprotein A-I-derived amyloid: its association with atherosclerosis
Ramella, N. A., Rimoldi, O. J., Prieto, E. D., Schinella, G. R., Sanchez, S. A., Jaureguiberry, M. S., Vela, M. E., Ferreira, S. T., & Tricerri, M. A. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022532 · Cited by 66
Immobilization of organophosphate hydrolase on an amyloid fibril nanoscaffold: Towards bioremediation and chemical detoxification
Raynes, J., Pearce, F., Meade, S. J., & Gerrard, J. (2011) · Biotechnology progress (Print) · doi:10.1002/btpr.518 · Cited by 66
“The presence of amyloid fibrils was assessed using Thioflavin T (ThT) based on the methods of LeVine (1999) and transmission electron microscopy (TEM), showing very high reproducibility.49 Crude crystallin proteins were diluted to 5.8 mg/mL in 10% trifluoroethanol, pH 4 and then incubated at 60 C…”
MethodInfluential
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Ashcroft, A. E. (2010) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2010.02.026 · Cited by 65
RNA Aptamers Generated against Oligomeric Aβ40 Recognize Common Amyloid Aptatopes with Low Specificity but High Sensitivity
Rahimi, F., Murakami, K., Summers, J. L., Chen, C. B., & Bitan, G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0007694 · Cited by 68
Amyloid Formation of a Protein in the Absence of Initial Unfolding and Destabilization of the Native State
Soldi, G., Bemporad, F., Torrassa, S., Relini, A., Ramazzotti, M., Taddei, N., & Chiti, F. (2005) · Biophysical Journal · doi:10.1529/biophysj.105.067538 · Cited by 78
Amyloid fibril proteins.
Xing, Y., & Higuchi, K. (2002) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(02)00098-2 · Cited by 66
The structure and protein binding of amyloid-specific dye reagents.
Stopa, B., Piekarska, B., Konieczny, L., Rybarska, J., Spólnik, P., Zemanek, G., Roterman, I., & Król, M. (2003) · Acta Biochimica Polonica · doi:10.18388/abp.2003_3645 · Cited by 66
“Many approaches have been employed to identify the mechanism of complexation and the structure of the protein sites responsible for specific dye attachment (Westermark et al., 1999; Demaimay et al., 1998; Li et al., 1999; Gazit, 2002).”
Method
Design and development of molecular hybrids of 2-pyridylpiperazine and 5-phenyl-1,3,4-oxadiazoles as potential multifunctional agents to treat Alzheimer's disease
Tripathi, A., Choubey, P. K., Sharma, P. A., Seth, A., Tripathi, P. N., Tripathi, M. K., Prajapati, S. K., Krishnamurthy, S., & Shrivastava, S. K. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111707 · Cited by 81
Visualization of multiple organ amyloid involvement in systemic amyloidosis using 11C-PiB PET imaging
Ezawa, N., Katoh, N., Oguchi, K., Yoshinaga, T., Yazaki, M., & Sekijima, Y. (2017) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-017-3814-1 · Cited by 65
“PiB is a derivative of the amyloidbinding dye, thioflavin-T [3], and it can therefore theoretically combine with various amyloid proteins.”

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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