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

The DOI matches its Crossref record.

[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

Open this paper in CoChat — free account

Integrity signals

Registry

Crossref · 10.1016/s0076-6879(99)09020-5

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

No references could be resolved yet.

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

Sorted by citations

Items 601–700 of 1,003

Transthyretin Aggregate-Specific Antibodies Recognize Cryptic Epitopes on Patient-Derived Amyloid Fibrils
Phay, M., Blinder, V., Macy, S., Greene, M. J., Wooliver, D. C., Liu, W., Planas, A., Walsh, D., Connors, L., Primmer, S., et al. (2014) · Rejuvenation Research · doi:10.1089/rej.2013.1524 · Cited by 25
High throughput prediction of the long-term stability of pharmaceutical macromolecules from short-term multi-instrument spectroscopic data.
Maddux, N. R., Iyer, V. G., Cheng, W., Youssef, A., Joshi, S., Volkin, D., Ralston, J., Winter, G., & Middaugh, C. (2014) · Journal of Pharmacy and Science · doi:10.1002/jps.23849 · Cited by 25
Chronic Administration of Anti-Stroke Herbal Medicine TongLuoJiuNao Reduces Amyloidogenic Processing of Amyloid Precursor Protein in a Mouse Model of Alzheimer’s Disease
He, P., Li, P., Hua, Q., Liu, Y., Staufenbiel, M., Li, R., & Shen, Y. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058181 · Cited by 22
Heterodivalent Linked Macrocyclic β-Sheets with Enhanced Activity against Aβ Aggregation: Two Sites Are Better Than One
Cheng, P.-N., Spencer, R. K., Woods, R. J., Glabe, C. G., & Nowick, J. S. (2012) · Journal of the American Chemical Society · doi:10.1021/ja305416a · Cited by 28
Amyloid-Like Fibril Formation by Tachykinin Neuropeptides and Its Relevance to Amyloid β-Protein Aggregation and Toxicity
Singh, P., & Maji, S. (2012) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-012-9364-z · Cited by 25
“fibrils possess many common physical properties including their cross-b-sheet structure [2, 3], binding to amyloidspecific dyes such as congo red (CR) [4] and thioflavin T (ThT) [5] and morphology consisting mostly of 2–3 protofilaments [6, 7].”
Background
An Empirical Phase Diagram–High‐Throughput Screening Approach to the Characterization and Formulation of Biopharmaceuticals
Joshi, S., Bhambhani, A., Zeng, Y.-H., & Middaugh, C. (2010) · doi:10.1002/9780470595886.ch8 · Cited by 25
Inhibiting protein–amyloid interactions with small molecules: A surface chemistry approach
Inbar, P., & Yang, J. (2005) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2005.10.067 · Cited by 24
Inhibition of amyloid-β-induced cell death in human brain pericytes in vitro
Rensink, A. A. M., Verbeek, M. M., Otte‐Höller, I., ten Donkelaar, H. J., de Waal, R. M. W., & Kremer, B. P. H. (2002) · Brain Research · doi:10.1016/s0006-8993(02)03218-3 · Cited by 27
Cross-β-sheet supersecondary structure in amyloid folds: techniques for detection and characterization.
Sabaté, R., & Ventura, S. (2013) · Methods in molecular biology · doi:10.1007/978-1-62703-065-6_15 · Cited by 25
Nucleo-cytoplasmic environment modulates spatiotemporal p53 phase separation
Datta, D., Navalkar, A., Sakunthala, A., Paul, A., Patel, K. M., Masurkar, S. A., Gadhe, L. G., Manna, S., Bhattacharyya, A., Sengupta, S., et al. (2024) · Science Advances · doi:10.1126/sciadv.ads0427 · Cited by 33
Multi-Target Effects of Novel Synthetic Coumarin Derivatives Protecting Aβ-GFP SH-SY5Y Cells against Aβ Toxicity
Huang, C.-C., Chang, K., Chiu, Y., Chen, Y., Lung, T.-H., Hsieh‐Li, H. M., Su, M., Sun, Y., Chen, C., Lin, W., et al. (2021) · Cells · doi:10.3390/cells10113095 · Cited by 25
Design, synthesis and preliminary in-vitro studies of novel boronated monocarbonyl analogues of Curcumin (BMAC) for antitumor and β-amiloyd disaggregation activity.
Azzi, E., Alberti, D., Parisotto, S., Oppedisano, A., Protti, N., Altieri, S., Crich, S. G., & Deagostino, A. (2019) · Bioorganic chemistry (Print) · doi:10.1016/j.bioorg.2019.103324 · Cited by 24
pH-Dependent fibril maturation of a Pmel17 repeat domain isoform revealed by tryptophan fluorescence
Dean, D. N., & Lee, J. C. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.01.012 · Cited by 37
Identification of key regions and residues controlling Aβ folding and assembly
Hayden, E. Y., Hoi, K. K., Lopez, J., Inayathullah, M., Condron, M. M., & Teplow, D. B. (2017) · Scientific Reports · doi:10.1038/s41598-017-10845-6 · Cited by 29
Glucose directs amyloid-beta into membrane-active oligomers
Kedia, N., Almisry, M., & Bieschke, J. (2017) · Physical Chemistry Chemical Physics · doi:10.1039/c7cp02849k · Cited by 28
Photophysical Properties of Fluorescent Probe Thioflavin T in Crowded Milieu
Rodina, N., Sulatsky, M., Sulatskaya, A. I., Kuznetsova, I., Uversky, V., & Turoverov, K. K. (2017) · Journal of Spectroscopy · doi:10.1155/2017/2365746 · Cited by 24
Repositioning nordihydroguaiaretic acid as a potent inhibitor of systemic amyloidosis and associated cellular toxicity.
Nusrat, S., Zaidi, N., Zaman, M., Islam, S., Ajmal, M., Siddiqi, M., Santra, M., & Khan, R. H. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.10.014 · Cited by 24
Morphology and aggregation of RADA‐16‐I peptide Studied by AFM, NMR and molecular dynamics simulations
Bagrov, D., Gazizova, Y. A., Podgorsky, V. V., Udovichenko, I., Danilkovich, A., Prusakov, K., & Klinov, D. (2016) · Biopolymers · doi:10.1002/bip.22755 · Cited by 24
Thermally induced degradation pathways of three different antibody-based drug development candidates.
Fincke, A., Winter, J., Bunte, T., & Olbrich, C. (2014) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2014.05.014 · Cited by 24
Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II)
PANDEY, N. K., Ghosh, S., May, N. V., & Dasgupta, S. (2013) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2013.819300 · Cited by 24
“The fluorescence of ThT is a hallmark signature of amyloid fibril formation as it shows a significant increase in fluorescence intensity around 482 nm upon binding with the β-sheet structure of fibrils when excited at 450 nm (Levine, 1993; Levine, 1999; Nilsson, 2004).”
Background
Modulators of amyloid protein aggregation and toxicity: EGCG and CLR01
Attar, A., Rahimi, F., & Bitan, G. (2013) · Translational Neuroscience · doi:10.2478/s13380-013-0137-y · Cited by 24
Self-assembly and bioactivity of a polymer/peptide conjugate containing the RGD cell adhesion motif and PEG
Castelletto, V., Gouveia, R. M., Connon, C., & Hamley, I. (2013) · doi:10.1016/j.eurpolymj.2013.02.016 · Cited by 24
Probing and Trapping a Sensitive Conformation: Amyloid-β Fibrils, Oligomers, and Dimers
Fawver, J. N., Duong, K. T., Wise-Scira, O., Chapa, R. P., Schall, H. E., Coskuner‐Weber, O., Zhu, X., Colom, L. V., & Murray, I. V. J. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120880 · Cited by 24
Zinc(II) modulates specifically amyloid formation and structure in model peptides
Aliès, B., Pradines, V., Llorens, I., Sayen, S., Guillon, E., Hureau, C., & Faller, P. (2010) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-010-0729-8 · Cited by 28
Structurally distinct toxicity inhibitors bind at common loci on β‐amyloid fibril
Keshet, B., Gray, J. J., & Good, T. A. (2010) · Protein Science · doi:10.1002/pro.509 · Cited by 23
Multi-scale modelling of amyloid formation from unfolded proteins using a set of theory derived rate constants.
Hall, D., & Hirota, N. (2009) · Biophysical Chemistry · doi:10.1016/j.bpc.2008.11.013 · Cited by 24
A single mutation in an SH3 domain increases amyloid aggregation by accelerating nucleation, but not by destabilizing thermodynamically the native state
Varela, L., Morel, B., Azuaga, A. I., & Conejero-Lara, F. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.01.033 · Cited by 24
Deficiency of Disulfide Bonds Facilitating Fibrillogenesis of Endostatin
He, Y., Zhou, H., Tang, H., & Luo, Y. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507745200 · Cited by 24
Pathogenesis, manifestations, diagnosis, and management of CNS complications in hereditary ATTR amyloidosis
Sekijima, Y., & Sousa, L. (2024) · Amyloid · doi:10.1080/13506129.2024.2435573 · Cited by 24
“These tracers all have a fundamental structure that is similar to thioflavin-T and are thought to bind to the β-pleated motif of amyloid fibrils [83], which explains why they are believed to bind to amyloid fibrils of any type.”
Characterization and kinetics of whey protein isolate amyloid fibril aggregates under moderate electric fields.
Leal, R., Pereira, R. S., Rodrigues, R. M., & Pereira, R. N. (2024) · Food Research International · doi:10.1016/j.foodres.2024.115033 · Cited by 23
Efficient Amyloid Fibrillation Inhibition and Remodeling of Preformed Fibrils of Bovine Insulin by Propolis Polyphenols-Based Nanosheets.
Ramezani, M., Hesami, M., Rafiei, Y., Ghareghozloo, E. R., Meratan, A., & Nikfarjam, N. (2021) · ACS Applied Bio Materials · doi:10.1021/acsabm.1c00068 · Cited by 23
Chinese Herbal Medicine Glycyrrhiza inflata Reduces Aβ Aggregation and Exerts Neuroprotection through Anti-Oxidation and Anti-Inflammation
Chiu, Y., Lee, C.-M., Lin, T., Lin, H.-Y., Lee, S.-Y., Mesri, M., Chang, K., Lin, J., Lee‐Chen, G., & Chen, C. (2018) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x18500799 · Cited by 27
Conformation and Aggregation of Selectively PEGylated and Lipidated Gastric Peptide Hormone Human PYY3-36.
Castelletto, V., Hamley, I., Seitsonen, J., Ruokolainen, J., Harris, G., Bellmann-Sickert, K., & Beck-Sickinger, A. (2018) · Biomacromolecules · doi:10.1021/acs.biomac.8b01209 · Cited by 23
“(a) Ensemble of conformations from solution NMR (pdb file: 2dez) of human PYY(3-36).”
Background
De novo designed alpha-sheet peptides inhibit functional amyloid formation of Streptococcus mutans biofilms
Paranjapye, N., & Daggett, V. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.07.005 · Cited by 23
Ovalbumin self-assembles into amyloid nanosheets that elicit immune responses and facilitate sustained drug release
Tufail, S., Sherwani, M. A., Shoaib, S., Azmi, S., Owais, M., & Islam, N. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002550 · Cited by 27
Host regulation by the ectophagous parasitoid wasp Bracon nigricans.
Becchimanzi, A., Avolio, M., Lelio, I. D., Marinelli, A., Varricchio, P., Grimaldi, A., de Eguileor, M., Pennacchio, F., & Caccia, S. (2017) · Journal of insect physiology · doi:10.1016/j.jinsphys.2017.07.002 · Cited by 23
Stepwise oligomerization of murine amylin and assembly of amyloid fibrils.
Palmieri, L., Melo-Ferreira, B., Braga, C., Fontes, G. N., Mattos, L., & Lima, L. M. T. R. (2013) · Biophysical Chemistry · doi:10.1016/j.bpc.2013.07.013 · Cited by 23
“However, wild-type murine amylin has been shown to bind thioflavin T (ThT) [20,22], a known dye indicative for amyloid fibrils [46].”
Background
Association of β-amyloid peptide fragments with neuronal nitric oxide synthase: Implications in the etiology of Alzheimers disease
Padayachee, E., Ngqwala, N., & Whiteley, C. (2012) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2011.590805 · Cited by 23
Neutron Scattering Reveals Enhanced Protein Dynamics in Concanavalin A Amyloid Fibrils.
Schirò, G., Vetri, V., Frick, B., Militello, V., Leone, M., & Cupane, A. (2012) · Journal of Physical Chemistry Letters · doi:10.1021/jz300082x · Cited by 23
Characterization of Heparin-induced Glyceraldehyde-3-phosphate Dehydrogenase Early Amyloid-like Oligomers and Their Implication in α-Synuclein Aggregation*
Torres-Bugeau, C. M., Ávila, C., Raisman-Vozari, R., Papy-Garcia, D., Itri, R., Barbosa, L. R. S., Cortez, L. M., Sim, V. L., & Chehín, R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.303503 · Cited by 23
Study of thioflavin-T immobilized in porous silicon and the effect of different organic vapors on the fluorescence lifetime.
Hutter, T., Amdursky, N., Gepshtein, R., Elliott, S., & Huppert, D. (2011) · Langmuir · doi:10.1021/la200875k · Cited by 23
Thioflavin T fluorescence assay for beta-lactoglobulin fibrils hindered by DAPH.
Kroes-Nijboer, A., Lubbersen, Y. S., Venema, P., & van der Linden, E. (2009) · Journal of Structural Biology · doi:10.1016/j.jsb.2008.11.003 · Cited by 23
Amyloid fibrils: modulation of formation and structure by copper(ii)
Pradines, V., Stroia, A. J., & Faller, P. (2008) · New Journal of Chemistry · doi:10.1039/b719556g · Cited by 25
Denaturant effect on amyloid fibrils: Declasterization, depolymerization, denaturation and reassembly.
Sulatsky, M., Sulatskaya, A. I., Stepanenko, O., Povarova, O., Kuznetsova, I. M., & Turoverov, K. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.01.290 · Cited by 22
Xanthohumol inhibits tau protein aggregation and protects cells against tau aggregates
Zhang, M., Wu, Q., Yao, X., Zhao, J., Zhong, W., Liu, Q., & Xiao, S. (2019) · Food & Function · doi:10.1039/c9fo02133g · Cited by 33
Effect of glycation on human serum albumin–zinc interaction: a biophysical study
Iqbal, S., Qais, F. A., Alam, M. M., & Naseem, I. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1554-8 · Cited by 22
A Human Monoclonal IgG That Binds Aβ Assemblies and Diverse Amyloids Exhibits Anti-Amyloid ActivitiesIn VitroandIn Vivo
Levites, Y., O’Nuallain, B., Puligedda, R. D., Ondrejčák, T., Adekar, S. P., Chen, C. S., Cruz, P. E., Rosario, A. M., Macy, S. D., Mably, A. J., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.5109-14.2015 · Cited by 21
“The reaction was monitored by ThT fluorescence and was judged complete when the fluorescent signal reached a maximum plateau value (LeVine, 1999).”
Method
Structure-activity relationships of sugar-based peptidomimetics as modulators of amyloid β-peptide early oligomerization and fibrillization.
Kaffy, J., Brinet, D., Soulier, J., Khemtemourian, L., Lequin, O., Taverna, M., Crousse, B., & Ongeri, S. (2014) · European journal of medicinal chemistry · doi:10.1016/j.ejmech.2014.09.031 · Cited by 22
Pharmacodynamics of Cholinesterase Inhibitors Suggests Add-on Therapy with a Low-Dose Carbamylating Inhibitor in Patients on Long-Term Treatment with Rapidly Reversible Inhibitors
Darreh‐Shori, T., Hosseini, S. M., & Nordberg, A. K. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-130845 · Cited by 23
l-Arginine reduces thioflavin T fluorescence but not fibrillation of bovine serum albumin
Liu, K.-N., Wang, H.-Y., Chen, C.-Y., & Wang, S. S. (2010) · Amino Acids · doi:10.1007/s00726-010-0536-0 · Cited by 22
Non-native Proteins as Newly-Identified Targets of Heavy Metals and Metalloids
Sharma, S., Goloubinoff, P., & Christen, P. (2011) · Springer eBooks · doi:10.1007/978-94-007-0428-2_12 · Cited by 23
Prion seeded conversion and amplification assays
Orrú, C., & Caughey, B. (2011) · Topics in current chemistry · doi:10.1007/128_2011_184 · Cited by 22
Distribution and progression of cerebral amyloid angiopathy in early-onset V30M (p.V50M) hereditary ATTR amyloidosis
Takahashi, Y., Oguchi, K., Mochizuki, Y., Takasone, K., Ezawa, N., Matsushima, A., Katoh, N., Yazaki, M., & Sekijima, Y. (2022) · Amyloid: Journal of Protein Folding Disorders · doi:10.1080/13506129.2022.2128331 · Cited by 21
Solution structure of recombinant Pvfp-5β reveals insights into mussel adhesion
Morando, M. A., Venturella, F., Sollazzo, M., Monaca, E., Sabbatella, R., Vetri, V., Passantino, R., Pastore, A., & Alfano, C. (2022) · Communications Biology · doi:10.1038/s42003-022-03699-w · Cited by 25
Conformational distortion in a fibril-forming oligomer arrests alpha-Synuclein fibrillation and minimizes its toxic effects
Chakraborty, R., Dey, S., Sil, P., Paul, S., Bhattacharyya, D., Bhunia, A., Sengupta, J., & Chattopadhyay, K. (2021) · Communications Biology · doi:10.1038/s42003-021-02026-z · Cited by 21
CMT-3 targets different α-synuclein aggregates mitigating their toxic and inflammogenic effects
González‐Lizárraga, F., Ploper, D., Ávila, C. L., Socías, S. B., Pereira, M. D. S., Machín, B., Bel, E. A. D., Michel, P. P., Pietrasanta, L. I., Raisman‐Vozari, R., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-76927-0 · Cited by 23
Ruthenium(III) complexes with imidazole ligands that modulate the aggregation of the amyloid-β peptide via hydrophobic interactions
Yawson, G. K., Huffman, S. E., Fisher, S. S., Bothwell, P. J., Platt, D. C., Jones, M. A., Ferrence, G. M., Hamaker, C. G., & Webb, M. I. (2020) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2020.111303 · Cited by 26
Alpha-B-Crystallin Effect on Mature Amyloid Fibrils: Different Degradation Mechanisms and Changes in Cytotoxicity
Stepanenko, O., Sulatsky, M., Mikhailova, E., Stepanenko, O., Povarova, O., Kuznetsova, I. M., Turoverov, K., & Sulatskaya, A. I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207659 · Cited by 21
Flavonoids with Vicinal Hydroxyl Groups Inhibit Human Calcitonin Amyloid Formation
Lantz, R., Busbee, B., Wojcikiewicz, E. P., & Du, D. (2020) · Chemistry - A European Journal · doi:10.1002/chem.202002027 · Cited by 25
Inhibition of amyloid fibrillation, enzymatic degradation and cytotoxicity of insulin at carboxyl tailored gold-aryl nanoparticles surface
AlBab, N. D., Hameed, M. K., Marešová, A., Ahmady, I. M., Arooj, M., Han, C., Workie, B., Chehimi, M. M., & Mohamed, A. A. M. (2019) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2019.124279 · Cited by 25
The small molecule inhibitor anle145c thermodynamically traps human islet amyloid peptide in the form of non-cytotoxic oligomers
Sadasivam, S. M., Ryazanov, S., Leonov, A., Nicolai, J., Praest, P., Giese, A., Winter, R., Khemtémourian, L., Griesinger, C., & Killian, J. A. (2019) · Scientific Reports · doi:10.1038/s41598-019-54919-z · Cited by 28
Unravelling the inhibitory and cytoprotective potential of diuretics towards amyloid fibrillation
Malik, S., Siddiqi, M. K., Majid, N., Masroor, A., Ali, S. M., & Khan, R. H. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.10.137 · Cited by 20
Novel compound VB‐037 inhibits A&bgr; aggregation and promotes neurite outgrowth through enhancement of HSP27 and reduction of P38 and JNK‐mediated inflammation in cell models for Alzheimer's disease
Chiu, Y.-J., Hsieh, Y.-H., Lin, T.-H., Lee, G.-C., Hsiu, M.-H.-L., Sun, Y.-C., Chen, C.-M., Chang, K.-H., & Lee-Chen, G. (2019) · Neurochemistry International · doi:10.1016/j.neuint.2019.01.021 · Cited by 21
“The results of the thioflavin T assay, which was widely used to measure the misfolded level of amyloid (LeVine, 1999), indicated that curcumin, VB-030, and VB-037 all demonstrated significant aggregation inhibition, with half-maximal effective concentration (EC50) of 5, 30, and 8 μM, respectively…”
Architecture and physicochemical characterization of Bacillus biofilm as a potential enzyme immobilization factory.
Romero, C. M., Martorell, P., Lopez, A., Peñalver, C. G. N., Chaves, S., & Mechetti, M. (2018) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2017.11.057 · Cited by 21
Excited-State Dynamics of Thioflavin T: Planar Stable Intermediate Revealed by Nuclear Wave Packet Spectroscopies
Kim, J., Kim, D. E., & Joo, T. (2018) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.7b11951 · Cited by 24
Morphological Effects of CuO Nanostructures on Fibrillation of Human Serum Albumin.
Konar, S., Sen, S., & Pathak, A. (2017) · Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.7b08432 · Cited by 21
trans -Stilbenoids with Extended Fluorescence Lifetimes for the Characterization of Amyloid Fibrils
Zhang, J., Sandberg, A., Wu, X., Nyström, S., Lindgren, M., Konradsson, P., & Hammarström, P. (2017) · ACS Omega · doi:10.1021/acsomega.7b00535 · Cited by 23
3D compartmented model to study the neurite-related toxicity of Aβ aggregates included in collagen gels of adaptable porosity
Labour, M.-N., Vigier, S., Lerner, D. A., Marcilhac, A., & Belamie, E. (2016) · Acta Biomaterialia · doi:10.1016/j.actbio.2016.04.001 · Cited by 22
Substoichiometric molecular control and amplification of the initiation and nature of amyloid fibril formation: lessons from and for blood clottingPreprint
Kell, D. B., & Pretorius, E. (2016) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/054734 · Cited by 14
“fibrils a substantially enhanced ThT fluorescence is observed, with excitation and emission maxima at about 440/450 and 480/490 nm, respectively [188-204].”
Background
Investigating the structural impact of the glutamine repeat in huntingtin assembly.
Perevozchikova, T., Stanley, C., McWilliams-Koeppen, H. P., Rowe, E. L., & Berthelier, V. (2014) · Biophysical Journal · doi:10.1016/j.bpj.2014.06.002 · Cited by 21
“in Thioflavin T (ThT) fluorescence (21) using an LS 55 fluorescence spec-”
Method
In vitrobinding of [3H]PIB to human amyloid deposits of different types
Hellström‐Lindahl, E., Westermark, P., Antoni, G., & Estrada, S. (2013) · Amyloid · doi:10.3109/13506129.2013.860895 · Cited by 23
High fluorescence of thioflavin T confined in mesoporous silica xerogels.
D'Amico, M., Schirò, G., Cupane, A., D'Alfonso, L., Leone, M., Militello, V., & Vetri, V. (2013) · Langmuir · doi:10.1021/la402406g · Cited by 21
Adsorption and detection of amyloid marker thioflavin T on Ag nanoparticles by surface-enhanced raman scattering
López-Tobar, E., Antalík, M., Jancura, D., Cañamares, M. V., Garcia-Leis, A., Fedunova, D., Fabriciová, G., & Sánchez-Cortés, S. (2013) · doi:10.1021/jp310619c · Cited by 21
The neurotransmitter serotonin interrupts α-synuclein amyloid maturation
Falsone, S. F., Leitinger, G., Karner, A., Kungl, A. J., Kosol, S., Cappai, R., & Zangger, K. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.02.008 · Cited by 19
Enzymatically active fibrils generated by the self-assembly of the ApoA-I fibrillogenic domain functionalized with a catalytic moiety.
Guglielmi, F., Monti, D., Arciello, A., Torrassa, S., Cozzolino, F., Pucci, P., Relini, A., & Piccoli, R. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2008.10.036 · Cited by 21
Surface plasmon resonance characterization of specific binding of polyglutamine aggregation inhibitors to the expanded polyglutamine stretch.
Okamoto, Y., Nagai, Y., Fujikake, N., Popiel, H., Yoshioka, T., Toda, T., & Inui, T. (2009) · Biochemical and Biophysical Research Communications - BBRC · doi:10.1016/j.bbrc.2008.11.094 · Cited by 21
Albumin fibrillization induces apoptosis via integrin/FAK/Akt pathway
Huang, C.-Y., Liang, C., Chu, C.-L., & Liang, S. (2009) · BMC Biotechnology · doi:10.1186/1472-6750-9-2 · Cited by 21
Trehalose effects on α-crystallin aggregates
Attanasio, F., Cascio, C., Fisichella, S., Nicoletti, V., Pignataro, B., Savarino, A., & Rizzarelli, E. (2007) · doi:10.1016/j.bbrc.2007.01.061 · Cited by 21
“Fluorescence emission spectra of ThT are shifted towards the long-wave region upon incorporation into b-sheet aggregates structures [27,28].”
Background
Effects of confinement on insulin amyloid fibrils formation
Librizzi, F., Foderà, V., Vetri, V., LoPresti, C., & Leone, M. (2007) · European Biophysics Journal · doi:10.1007/s00249-007-0137-3 · Cited by 21
“ThT is widely used as a selective probe for the detection of amyloid W brils, since in the presence of W brils it brightly X uoresces, with excitation and emission maxima at approximately 450 and 482 nm, respectively (Naiki et al. 1989; Levine 1999; Krebs et al. 2005).”
Characterization of the native and fibrillar conformation of the human Nα‐acetyltransferase ARD1
Sánchez‐Puig, N., & Fersht, A. (2006) · Protein Science · doi:10.1110/ps.062264006 · Cited by 21
“4A,B) (Klunk et al. 1999; LeVine 1999).”
Dequalinium-induced Protofibril Formation of α-Synuclein
Lee, C., Kim, H. J., Lee, J., Cho, H.-J., Kim, J., Chung, K. C., Jung, S., & Paik, S. R. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505307200 · Cited by 24
Studying Protein Misfolding and Aggregation by Fluorescence Spectroscopy
Bhattacharya, M., & Mukhopadhyay, S. (2015) · Reviews in fluorescence · doi:10.1007/978-3-319-24609-3_1 · Cited by 21
Investigating by circular dichroism some amyloidogenic elastin-derived polypeptides.
Tamburro, A., Lorusso, M., Ibriş, N., Pepe, A., & Bochicchio, B. (2010) · Chirality · doi:10.1002/chir.20869 · Cited by 21
Inhibition of tau amyloid formation and disruption of its preformed fibrils by Naphthoquinone–Dopamine hybrid
Paul, A., Viswanathan, G. K., Huber, A., Arad, E., Engel, H., Jelinek, R., Gazit, E., & Segal, D. (2021) · FEBS Journal · doi:10.1111/febs.15741 · Cited by 26
Identification of aplysinopsin as a blood-brain barrier permeable scaffold for anti-cholinesterase and anti-BACE-1 activity
Nuthakki, V. K., Bheemanaboina, R. R. Y., & Bharate, S. B. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104568 · Cited by 27
Interaction with zinc oxide nanoparticle kinetically traps α-synuclein fibrillation into off-pathway non-toxic intermediates
Asthana, S., Bhattacharyya, D., Kumari, S., Nayak, P. S., Saleem, M., Bhunia, A., & Jha, S. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.01.269 · Cited by 23
Blue autofluorescence in protein aggregates “lighted on” by UV induced oxidation
Fricano, A., Librizzi, F., Rao, E., Alfano, C., & Vetri, V. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.07.011 · Cited by 26
Fabrication of an amyloid fibril-palladium nanocomposite: a sustainable catalyst for C–H activation and the electrooxidation of ethanol
Jayarajan, R., Kumar, R., Gupta, J., Dev, G., Kadu, P., Chatterjee, D., Bahadur, D., Maiti, D., & Maji, S. (2019) · Journal of Materials Chemistry A · doi:10.1039/c8ta11134k · Cited by 20
Functional amyloidogenesis in immunocytes from the colonial ascidian Botryllus schlosseri: Evolutionary perspective
Franchi, N., Ballarin, L., Peronato, A., Cima, F., Grimaldi, A., Girardello, R., & de Eguileor, M. (2019) · Developmental and Comparative Immunology · doi:10.1016/j.dci.2018.09.010 · Cited by 20
Amyloid properties of the yeast cell wall protein Toh1 and its interaction with prion proteins Rnq1 and Sup35
Sergeeva, A. V., Sopova, J. V., Belashova, T. A., Siniukova, V. A., Chirinskaite, A. V., Galkin, A. P., & Zadorsky, S. P. (2018) · Prion · doi:10.1080/19336896.2018.1558763 · Cited by 23
“detergents, such as sodium dodecyl sulfate (SDS), and proteases [1–3], and propensity to bind amyloid-specific dyes thioflavines T and S [4], andCongo red [5].”
Background
Aptamers Selected for Recognizing Amyloid β-Protein—A Case for Cautious Optimism
Rahimi, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030668 · Cited by 18
“(7) The selected aptamers—and the naïve library—could track progression of β-sheet formation and fibrillization in Aβ40 and insulin with ~16-fold higher sensitively than the thioflavin T fluorescence assay, which is commonly used to assess fibril formation by many amyloidogenic proteins [158,159].”
Background
Reversible association of proteins into sub-visible amorphous aggregates using short solubility controlling peptide tags
Kabir, M. G., Islam, M. M., & Kuroda, Y. (2017) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2017.09.012 · Cited by 17
Tetrahydroacridine derivatives with fluorobenzoic acid moiety as multifunctional agents for Alzheimer’s disease treatment
Czarnecka, K., Szymański, P., Girek, M. K., Mikiciuk‐Olasik, E., Skibiński, R., Kabziński, J., Majsterek, I., Malawska, B., Jończyk, J., & Bajda, M. (2017) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2017.05.003 · Cited by 22
Evidence of two oxidation states of copper during aggregation of hen egg white lysozyme (HEWL)
Ghosh, S., PANDEY, N. K., Bhattacharya, S., Roy, A., May, N. V., & Dasgupta, S. (2015) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2015.02.014 · Cited by 21
The Chaperone-Like Activity of α-Synuclein Attenuates Aggregation of Its Alternatively Spliced Isoform, 112-Synuclein In Vitro: Plausible Cross-Talk between Isoforms in Protein Aggregation
Manda, K. M., Yedlapudi, D., Korukonda, S., Sreedhar, B., & Kalivendi, S. V. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098657 · Cited by 25
Ferrocene tripeptide Gly-Pro-Arg conjugates: Synthesis and inhibitory effects on Alzheimer’s Aβ1–42 fibrillogenesis and Aβ-induced cytotoxicity in vitro
Zhou, B., Li, C., Hao, Y., Chabu, J. M., Liu, Y., & Li, J. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.11.030 · Cited by 21
Inhibitory mechanism of pancreatic amyloid fibril formation: formation of the complex between tea catechins and the fragment of residues 22-27.
Kamihira-Ishijima, M., Nakazawa, H., Kira, A., Naito, A., & Nakayama, T. (2012) · Biochemistry · doi:10.1021/bi3012274 · Cited by 20
Enzyme-Linked Immunosorbent Assay-Based Method to Quantify the Association of Small Molecules with Aggregated Amyloid Peptides
Capule, C. C., & Yang, J. (2012) · Analytical Chemistry · doi:10.1021/ac2030859 · Cited by 21
Protein Aggregates in Pathological Inclusions of Amyotrophic Lateral Sclerosis
Furukawa, Y. (2012) · InTech eBooks · doi:10.5772/30897 · Cited by 15
“Given that the typical amyloid aggregates lead to ~1000-fold increase in the intensity of ThT fluorescence and red-shift a spectrum of Congo Red (Klunk et al., 1999; LeVine, 1999), TFE-induced SOD1 S-S aggregates will not be categorized as a typical amyloid.”
Partially Folded Glycated State of Human Serum Albumin Tends to Aggregate
Khan, T., Saleemuddin, M., & Naeem, A. (2011) · International Journal of Peptide Research and Therapeutics · doi:10.1007/s10989-011-9267-7 · Cited by 20

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

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

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

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Metadata

Record

About these checks