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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Research works printed but not linked: 31

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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Background
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“Inhibition of self-induced Aβ1–42 aggregation was assayed, as described elsewhere [34].”
Method
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Sulatskaya, A. I., Rodina, N., Polyakov, D., Sulatsky, M., Artamonova, T., Khodorkovskii, M., Shavlovsky, M., Kuznetsova, I., & Turoverov, K. K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092762 · Cited by 29
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“ThT is a small dye and one of themost commonly used for amyloid detection [26].”
Background
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Lempart, J., Tse, E., Lauer, J. A., Ivanova, M. I., Sutter, A., Yoo, N. G., Huettemann, P., Southworth, D. R., & Jakob, U. (2019) · Life Science Alliance · doi:10.26508/lsa.201900486 · Cited by 30
“…formation by nucleating α -synuclein oligomers Amyloid ﬁ bril formation is most commonly monitored by measuring the ﬂ uorescence of thio ﬂ avin T (ThT), a small molecular dye that becomes highly emissive when intercalated into the β -sheets of amyloidogenic oligomers and ﬁ brils (LeVine, 1999).”
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Takahashi, H., Adachi, N., Shirafuji, T., Danno, S., Ueyama, T., Vendruscolo, M., Shuvaev, А. N., Sugimoto, T., Seki, T., Hamada, D., et al. (2014) · Human Molecular Genetics · doi:10.1093/hmg/ddu472 · Cited by 26
Studying the effects of chaperones on amyloid fibril formation.
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A thienoquinoxaline and a styryl-quinoxaline as new fluorescent probes for amyloid-β fibrils
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A chemical screening approach reveals that indole fluorescence is quenched by pre-fibrillar but not fibrillar amyloid-β
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Doxycycline Interferes With Tau Aggregation and Reduces Its Neuronal Toxicity
Medina, L., González‐Lizárraga, F., Dominguez‐Meijide, A., Ploper, D., Parrales, V., Sequeira, S., Cima‐Omori, M., Zweckstetter, M., Bel, E. A. D., Michel, P. P., et al. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.635760 · Cited by 34
“Formation of cross-β structures during tau aggregation was followed by addition of Thioflavin T (ThT) fluorescent probe on aliquots withdrawn from the incubation mixture at different times, according to LeVine (1993, 1999).”
Method
Gly25-Ser26 Amyloid β-Protein Structural Isomorphs Produce Distinct Aβ42 Conformational Dynamics and Assembly Characteristics
Roychaudhuri, R., Lomakin, A., Bernstein, S. L., Zheng, X., Condron, M. M., Benedek, G. B., Bowers, M. T., & Teplow, D. B. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.04.004 · Cited by 30
The Mutation V42M Distorts the Compact Packing of the Human Gamma-S-Crystallin Molecule, Resulting in Congenital Cataract
Vendra, V., Chandani, S., & Balasubramanian, D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051401 · Cited by 27
Secondary Nucleating Sequences Affect Kinetics and Thermodynamics of Tau Aggregation
Moore, C. L., Huang, M. H., Robbennolt, S., Voss, K., Combs, B., Gamblin, T. C., & Goux, W. J. (2011) · Biochemistry · doi:10.1021/bi2014745 · Cited by 28
“The kinetics of aggregation of tau peptides was measured in MOPS-Cl-HMWH by following the time dependence of ThS fluorescence at 490 nm, and fitting the data to Gompertz growth curves (20,40,41,45,47,48).”
Method
Conjugation of β-sheet peptides to modify the rheological properties of hyaluronic acid.
Elder, A. N., D'Angelo, N., Kim, S. C., & Washburn, N. (2011) · Biomacromolecules · doi:10.1021/bm200393k · Cited by 27
The N-terminal fragment of human islet amyloid polypeptide is non-fibrillogenic in the presence of membranes and does not cause leakage of bilayers of physiologically relevant lipid composition.
Khemtemourian, L., Engel, M. F., Liskamp, R., Höppener, J., & Killian, J. (2010) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamem.2010.05.022 · Cited by 27
“We first investigated whether hIAPP1–19 can form amyloid fibrils in the absence of membranes by using transmission electron microscopy (TEM) and we followed the kinetics of fibril formation using the amyloid specific thioflavin (ThT) binding assays [25].”
Method
Arginine Metabolising Enzymes as Therapeutic Tools for Alzheimer’s Disease: Peptidyl Arginine Deiminase Catalyses Fibrillogenesis of β-amyloid Peptides
Mohlake, P., & Whiteley, C. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8112-x · Cited by 27
Amidation and Structure Relaxation Abolish the Neurotoxicity of the Prion Peptide PrP106–126 in Vivo and in Vitro*
Bergström, A., Cordes, H., Zsurger, N., Heegaard, P. M., Laursen, H., & Chabry, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500210200 · Cited by 27
A Novel Cu(II)-Binding Peptide Identified by Phage Display Inhibits Cu2+-Mediated Aβ Aggregation
Zhang, X., Zhang, X., Zhong, M., Zhao, P., Guo, C., Li, Y., Xu, H. J., Wang, T., & Gao, H. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22136842 · Cited by 30
“In addition, compared with Aβ1-42 alone, the addition of Cu(II) reduced the ThT fluorescence level, suggesting that Cu(II) triggered the formation of partial Aβ1-42 oligomers because ThT selectively binds to amyloid fibrils but does not interact with unstructured Aβ monomers and oligomers [47,48].”
Background
Differentiating Aβ40 and Aβ42 in amyloid plaques with a small molecule fluorescence probe
Yang, J., Zhu, B., Yin, W. H., Han, Z., Zheng, C., Wang, P., & Ran, C. (2020) · Chemical Science · doi:10.1039/d0sc02060e · Cited by 58
New insights into non-enzymatic glycation of human serum albumin biopolymer: A study to unveil its impaired structure and function
Raghav, A., Ahmad, J., Alam, K., & Khan, A. U. (2017) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.03.086 · Cited by 28
High-affinity Anticalins with aggregation-blocking activity directed against the Alzheimer β-amyloid peptide
Rauth, S., Hinz, D., Borger, M. A., Uhrig, M., Mayhaus, M., Riemenschneider, M. J., & Skerra, A. (2016) · Biochemical Journal · doi:10.1042/bcj20160114 · Cited by 35
Self-Assembly of the Toll-Like Receptor Agonist Macrophage-Activating Lipopeptide MALP-2 and of Its Constituent Peptide
Castelletto, V., Kirkham, S., Hamley, I. W., Kowalczyk, R. M., Rabe, M., Reza, M., & Ruokolainen, J. (2016) · Biomacromolecules · doi:10.1021/acs.biomac.5b01573 · Cited by 27
α-synuclein-lanthanide metal ions interaction: binding sites, conformation and fibrillation
Bai, J. Q. A., Zhang, Z., Liu, M., & Li, C. (2015) · BMC Biophysics · doi:10.1186/s13628-016-0026-1 · Cited by 37
Towards efficient biocatalysts: photo-immobilization of a lipase on novel lysozyme amyloid-like nanofibrils
Chaves, S., Pera, L., Ávila, C., Romero, C., Baigorí, M., Vieyra, F. E. M., Borsarelli, C., & Chehín, R. (2016) · doi:10.1039/c5ra19590j · Cited by 26
Covalent modifier-type aggregation inhibitor of amyloid-β based on a cyclo-KLVFF motif
Kino, R., Araya, T., Arai, T., Sohma, Y., & Kanai, M. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.05.027 · Cited by 32
Fluorescent Filter-Trap Assay for Amyloid Fibril Formation Kinetics in Complex Solutions
Nasir, I., Linse, S. S., & Cabaleiro-Lago, C. (2015) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5b00104 · Cited by 25
Novel neurotrophic phenylbutenoids from Indonesian ginger Bangle, Zingiber purpureum.
Kubo, M., Gima, M., Baba, K., Nakai, M., Harada, K., Suenaga, M., Matsunaga, Y., Kato, E., Hosoda, S., & Fukuyama, Y. (2015) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2015.02.005 · Cited by 26
Increasing Prion Propensity by Hydrophobic Insertion
Nelson, A. C. G., Paul, K. R., Petri, M., Flores, N., Rogge, R. A., Cascarina, S. M., & Ross, E. D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089286 · Cited by 26
Cerato-Populin and Cerato-Platanin, Two Non-Catalytic Proteins from Phytopathogenic Fungi, Interact with Hydrophobic Inanimate Surfaces and Leaves
Martellini, F., Faoro, F., Carresi, L., Pantera, B., Baccelli, I., Maffi, D., Tiribilli, B., Sbrana, F., Luti, S., Comparini, C., et al. (2013) · Molecular Biotechnology · doi:10.1007/s12033-012-9618-4 · Cited by 26
“Self-aggregation of Pop1 was followed by fluorescence spectroscopy by thioflavine T (Tht) according to the literature [39].”
Amino acid sequence determinants in self‐assembly of insulin chiral amyloid superstructures: Role of C‐terminus of B‐chain in association of fibrils
Babenko, V., & Dzwolak, W. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.02.010 · Cited by 26
Early Amyloidogenic Oligomerization Studied through Fluorescence Lifetime Correlation Spectroscopy
Paredes, J. M., Casares, S., Ruedas-Rama, M., Fernández, E., Castello, F., Varela, L., & Orte, Á. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13089400 · Cited by 26
Activation of phospholipase A2 by 1-palmitoyl-2-(9'-oxo-nonanoyl)-sn-glycero-3-phosphocholine in vitro.
Code, C., Mahalka, A., Bry, K., & Kinnunen, P. (2010) · Biochimica et Biophysica Acta · doi:10.1016/j.bbamem.2010.05.002 · Cited by 26
Amyloid PET Ligands for Dementia
Villemagne, V. L., & Rowe, C. C. (2010) · PET Clinics · doi:10.1016/j.cpet.2009.12.008 · Cited by 31
Bariatric Surgery Normalizes Protein Glycoxidation and Nitrosative Stress in Morbidly Obese Patients
Choromańska, B., Myśliwiec, P., Łuba, M., Wojskowicz, P., Myśliwiec, H., Choromańska, K., Dadan, J., Żendzian‐Piotrowska, M., Zalewska, A., & Maciejczyk, M. (2020) · Antioxidants · doi:10.3390/antiox9111087 · Cited by 30
Molecular Lysine Tweezers Counteract Aberrant Protein Aggregation
Hadrović, I., Rebmann, P., Klärner, F., Bitan, G., & Schrader, T. H. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00657 · Cited by 27
“ThT is an amyloid dye indicator which turns highly fluorescent upon binding to existing β-sheets (LeVine, 1999).”
Background
Allium roseum L. extract inhibits amyloid beta aggregation and toxicity involved in Alzheimer’s disease
Boubakri, A., Leri, M., Bucciantini, M., Najjaa, H., Arfa, A. B., Stefani, M., & Neffati, M. (2019) · bioRxiv · doi:10.1371/journal.pone.0223815 · Cited by 25
Investigation of Anti-SOD1 Antibodies Yields New Structural Insight into SOD1 Misfolding and Surprising Behavior of the Antibodies Themselves
Atlasi, R. S., Malik, R., Corrales, C. I., Tzeplaeff, L., Whitelegge, J. P., Cashman, N. R., & Bitan, G. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00729 · Cited by 30
Recent Advances by In Silico and In Vitro Studies of Amyloid-β 1-42 Fibril Depicted a S-Shape Conformation
Villalobos-Acosta, D. M. Á., Chimal‐Vega, B., Correa‐Basurto, J., Morales, L. G. F., & Rosales‐Hernández, M. C. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082415 · Cited by 26
Does Surface Chirality of Gold Nanoparticles Affect Fibrillation of HSA
Sen, S., Dasgupta, S., & Dasgupta, S. (2017) · doi:10.1021/acs.jpcc.7b05354 · Cited by 25
Macroscopic amyloid fiber formation by staphylococcal biofilm associated SuhB protein.
Dutta, A., Bhattacharyya, S., Kundu, A., Dutta, D., & Das, A. (2016) · Biophysical Chemistry · doi:10.1016/j.bpc.2016.07.006 · Cited by 25
NET amyloidogenic backbone in human activated neutrophils
Pulze, L., Bassani, B., Gini, E., D’Antona, P., Grimaldi, A., Luini, A., Marino, F., Noonan, D. M., Tettamanti, G., Valvassori, R., et al. (2015) · Clinical & Experimental Immunology · doi:10.1111/cei.12730 · Cited by 22
A host–guest complexation based fluorescent probe for the detection of paraquat and diquat herbicides in aqueous solutions
Song, G.-X., Tang, Q., Huang, Y.-H., Wang, R.-B., Xi, Y.-Y., Ni, X.-L., Tao, Z., Xue, S.-F., & Zhang, J.-X. (2015) · doi:10.1039/c5ra18335a · Cited by 25
Golgi-Associated plant Pathogenesis Related protein 1 (GAPR-1) forms amyloid-like fibrils by interaction with acidic phospholipids and inhibits Aβ aggregation
Olrichs, N. K., Mahalka, A. K., Kaloyanova, D. V., Kinnunen, P. K. J., & Helms, J. B. (2014) · Amyloid · doi:10.3109/13506129.2014.882304 · Cited by 32
Amyloid peptides derived from CsgA and FapC modify the viscoelastic properties of biofilm model matrices
Lembré, P., Martino, P. D., & Vendrely, C. (2014) · Biofouling · doi:10.1080/08927014.2014.880112 · Cited by 32
“The Thioflavin T binding assay is the most common assay used to monitor the formation of amyloid fibers because the binding of Thioflavin T fluorescent probe onto amyloid fibers causes an enhancement of its fluorescence intensity at 482 nm after excitation at 450 nm (LeVine 1999).”
Method

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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