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 401–500 of 1,003

On the Stability of the Soluble Amyloid Aggregates
Sahoo, B., Nag, S., Sengupta, P., & Maiti, S. (2009) · Biophysical Journal · doi:10.1016/j.bpj.2009.05.055 · Cited by 47
“The solution is also probed for thio-T binding, which is supposed to report the formation of the repeated b-sheet structures in a protein (43).”
Background
Amyloid peptides in different assembly states and related effects on isolated and cellular proteasomes
Cecarini, V., Bonfili, L., Amici, M., Angeletti, M., Keller, J. N., & Eleuteri, A. M. (2008) · Brain Research · doi:10.1016/j.brainres.2008.03.003 · Cited by 46
Disrupting Self-Assembly and Toxicity of Amyloidogenic Protein Oligomers by “ Molecular Tweezers” - from the Test Tube to Animal Models
Attar, A., & Bitan, G. (2014) · Current Pharmaceutical Design · doi:10.2174/13816128113199990496 · Cited by 48
Novel Mannitol-Based Small Molecules for Inhibiting Aggregation of α-Synuclein Amyloids in Parkinson's Disease
Paul, A., Zhang, B., Mohapatra, S., Gao, L., Li, Y., Gazit, E., & Segal, D. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00016 · Cited by 50
“Its level of fluorescence is commonly used to monitor the amount of fibrils present in the solution (LeVine, 1999). α-Syn was dissolved in PBS buffer (pH 7.4, 100mM) to obtained a final working concentration of 10µM and was Frontiers in Molecular Biosciences | www.frontiersin.org 4 March 2019 |…”
MethodInfluential
Synergistic Inhibitory Effect of Peptide–Organic Coassemblies on Amyloid Aggregation
Niu, L., Liu, L., Xi, W., Han, Q., Li, Q., Yu, Y., Huang, Q., Qu, F., Xu, M., Li, Y., et al. (2016) · ACS Nano · doi:10.1021/acsnano.5b07396 · Cited by 53
“brils leads to increased fluorescence emission at 482 nm upon excitation at 450 nm, which has been widely used for screening inhibitors.(44) In Figure 6a, typical sigmoidal curve of Aβ42 peptide (50 μM)”
Method
Arresting Amyloid with Coulomb’s Law: Acetylation of ALS-Linked SOD1 by Aspirin Impedes Aggregation
Abdolvahabi, A., Shi, Y., Rhodes, N. R., Cook, N. P., Martı́, A. A., & Shaw, B. F. (2015) · Biophysical Journal · doi:10.1016/j.bpj.2015.01.014 · Cited by 49
Thioflavin-S Staining of Bacterial Inclusion Bodies for the Fast, Simple, and Inexpensive Screening of Amyloid Aggregation Inhibitors
Pouplana, S., Espargaró, A., Galdeano, C., Viayna, E., Sola, I., Ventura, S., Muñoz‐Torrero, D., & Sabaté, R. (2014) · Current Medicinal Chemistry · doi:10.2174/09298673113206660256 · Cited by 50
“Keywords: Amyloid formation, Alzheimer’s disease, Bacterial inclusion bodies, Beta-amyloid peptide, Conformational diseases, Tau protein, Thioflavin-S Short “running title”: Simple Screening of A42 and Tau Aggregation Inhibitors in Intact E. coli Cells 1”
Background
Crocetin inhibits beta-amyloid fibrillization and stabilizes beta-amyloid oligomers
Ahn, J. H., Hu, Y., Hernandez, M. X., & Kim, J. R. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.09.025 · Cited by 45
Role of zinc along with ascorbic acid and folic acid during long-termin vitroalbumin glycation
Tupe, R. S., & Agte, V. V. (2009) · British Journal Of Nutrition · doi:10.1017/s0007114509991929 · Cited by 41
Characterization of ordered aggregates of cerato-platanin and their involvement in fungus-host interactions.
Pazzagli, L., Zoppi, C., Carresi, L., Tiribilli, B., Sbrana, F., Schiff, S., Pertinhez, T., Scala, A., & Cappugi, G. (2009) · Biochimica et Biophysica Acta · doi:10.1016/j.bbagen.2009.07.014 · Cited by 45
The effects of the flavonoid baicalein and osmolytes on the Mg 2+ accelerated aggregation/fibrillation of carboxymethylated bovine 1SS-α-lactalbumin
Bomhoff, G., Sloan, K., McLain, C., Gogol, E. P., & Fisher, M. T. (2006) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2006.02.001 · Cited by 44
Ginsenoside derivatives inhibit advanced glycation end-product formation and glucose-fructose mediated protein glycation in vitro via a specific structure-activity relationship.
Ali, M. Y., Jannat, S., & Rahman, M. M. (2021) · Bioorganic chemistry (Print) · doi:10.1016/j.bioorg.2021.104844 · Cited by 44
Design, synthesis, and biological evaluation of ferulic acid based 1,3,4-oxadiazole hybrids as multifunctional therapeutics for the treatment of Alzheimer's disease.
Tripathi, A., Choubey, P. K., Sharma, P., Seth, A., Saraf, P., & Shrivastava, S. (2019) · Bioorganic chemistry (Print) · doi:10.1016/j.bioorg.2019.103506 · Cited by 44
Lipopolysaccharide-binding protein (LBP) reverses the amyloid state of fibrin seen in plasma of type 2 diabetics with cardiovascular co-morbidities
Pretorius, E., Mbotwe, S., & Kell, D. B. (2017) · Scientific Reports · doi:10.1038/s41598-017-09860-4 · Cited by 46
Amyloidogenesis of the amylin analogue pramlintide
da Silva, D. C., Fontes, G. N., Erthal, L. C. S., & Lima, L. M. T. R. (2016) · Biophysical Chemistry · doi:10.1016/j.bpc.2016.09.007 · Cited by 43
Human Apolipoprotein A-I Natural Variants: Molecular Mechanisms Underlying Amyloidogenic Propensity
Ramella, N., Schinella, G., Ferreira, S., Prieto, E., Vela, M., Ríos, J., Tricerri, M., & Rimoldi, O. (2012) · PLoS ONE · doi:10.1371/journal.pone.0043755 · Cited by 44
Analysis of monomeric Aβ (1–40) peptide by capillary electrophoresis
Picou, R. A., Moses, J. P., Wellman, A. D., Kheterpal, I., & Gilman, S. D. (2010) · The Analyst · doi:10.1039/c0an00080a · Cited by 48
Design and synthesis of new trehalose‐conjugated pentapeptides as inhibitors of Aβ(1–42) fibrillogenesis and toxicity
Bona, P. D., Giuffrida, M. L., Caraci, F., Copani, A., Pignataro, B., Attanasio, F., Cataldo, S., Pappalardo, G., & Rizzarelli, E. (2009) · Journal of Peptide Science · doi:10.1002/psc.1109 · Cited by 48
The hydrophobic environment of Met35 of Alzheimer's Aβ(1–42) is important for the neurotoxic and oxidative properties of the peptide
Kański, J., Aksenova, M. V., & Butterfield, D. A. (2002) · Neurotoxicity Research · doi:10.1080/10298420290023945 · Cited by 58
α-Synuclein Conformational Strains as Drivers of Phenotypic Heterogeneity in Neurodegenerative Diseases
So, R. W. L., & Watts, J. C. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168011 · Cited by 46
α-Synuclein Aggregation Modulation: An Emerging Approach for the Treatment of Parkinson'S Disease
Singh, S. K., Dutta, A. K., & Modi, G. P. (2017) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0016 · Cited by 47
Luminescent Ru(II) Phenanthroline Complexes as a Probe for Real-Time Imaging of Aβ Self-Aggregation and Therapeutic Applications in Alzheimer’s Disease
Silva, D. E. S., Cali, M. P., Pazin, W. M., Carlos-Lima, E., Trevisan, M. T. S., Venâncio, T., Arcísio-Miranda, M., Ito, A. S., & Carlos, R. M. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01130 · Cited by 57
Solvent Polarity Effect on Nonradiative Decay Rate of Thioflavin T
Stsiapura, V. I., Kurhuzenkau, S. A., Kuzmitsky, V. A., Bouganov, O. V., & Тихомиров, С. А. (2016) · The Journal of Physical Chemistry A · doi:10.1021/acs.jpca.6b02577 · Cited by 51
Glycation of bovine serum albumin by ascorbate in vitro: Possible contribution of the ascorbyl radical?
Sadowska‐Bartosz, I., Stefaniuk, I., Galiniak, S., & Bartosz, G. (2015) · Redox Biology · doi:10.1016/j.redox.2015.06.017 · Cited by 46
“Formation of amyloid cross-β structure was measured using thioflavin T [25,26].”
Method
Benzofuran–Chalcone Hybrids as Potential Multifunctional Agents against Alzheimer’s Disease: Synthesis and in vivo Studies with Transgenic Caenorhabditis elegans
Sashidhara, K. V., Modukuri, R. K., Jadiya, P., Dodda, R. P., Kumar, M., Sridhar, B., Kumar, V., Haque, R., Siddiqi, M. I., & Nazir, A. (2014) · ChemMedChem · doi:10.1002/cmdc.201402291 · Cited by 49
Dutch and arctic mutant peptides of β amyloid1–40 differentially affect the FGF-2 pathway in brain endothelium
Solito, R., Corti, F., Fossati, S., Mezhericher, E., Donnini, S., Ghiso, J. A., Giachetti, A., Rostagno, A. A., & Ziche, M. (2008) · Experimental Cell Research · doi:10.1016/j.yexcr.2008.11.002 · Cited by 38
“Thioflavin T binding assay Thioflavin T binding was assessed essentially as previously described [17,18].”
Method
Amyloid Imaging: From Benchtop to Bedside
Wu, C., Pike, V. W., & Wang, Y. (2005) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(05)70008-9 · Cited by 45
Anti-Aging and Neuroprotective Properties of Grifola frondosa and Hericium erinaceus Extracts
Tripodi, F., Falletta, E., Leri, M., Angeloni, C., Beghelli, D., Giusti, L., Milanesi, R., Sampaio-Marques, B., Ludovico, P., Goppa, L., et al. (2022) · Nutrients · doi:10.3390/nu14204368 · Cited by 42
“The ThT binding assay was performed according to LeVine [42], using a 25 μM ThT solution in 20 mM sodium phosphate buffer, pH 7.”
MethodInfluential
Design, synthesis, and evaluation of N-benzylpyrrolidine and 1,3,4-oxadiazole as multitargeted hybrids for the treatment of Alzheimer’s disease
Choubey, P. K., Tripathi, A., Tripathi, M. K., Seth, A., & Shrivastava, S. K. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104922 · Cited by 53
Design and development of novel N-(pyrimidin-2-yl)-1,3,4-oxadiazole hybrids to treat cognitive dysfunctions
Tripathi, P. N., Srivastava, P., Sharma, P. A., Seth, A., & Shrivastava, S. K. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.02.031 · Cited by 42
The Potential of LPS-Binding Protein to Reverse Amyloid Formation in Plasma Fibrin of Individuals With Alzheimer-Type Dementia
Pretorius, E., Bester, J., Pagé, M., & Kell, D. B. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00257 · Cited by 47
“We added Thioflavin T (ThT) (a well-established amyloid stain; LeVine, 1999; Biancalana et al., 2009; Biancalana and Koide, 2010; Groenning, 2010; Sulatskaya et al., 2011, 2012; Kuznetsova et al., 2012; Picken and Herrera, 2012; Younan and Viles, 2015; Kuznetsova et al., 2016; Rybicka et al., 2016)…”
An Azobenzene Photoswitch Sheds Light on Turn Nucleation in Amyloid-β Self-Assembly
Doran, T. M., Anderson, E. A., Latchney, S. E., Opanashuk, L. A., & Nilsson, B. L. (2012) · ACS Chemical Neuroscience · doi:10.1021/cn2001188 · Cited by 40
Structural dynamics of the ΔE22 (Osaka) familial Alzheimer’s disease-linked amyloid β-protein
Inayathullah, M., & Teplow, D. B. (2011) · Amyloid · doi:10.3109/13506129.2011.580399 · Cited by 43
A Strategy for Designing a Peptide Probe for Detection of β‐Amyloid Oligomers
Hu, Y., Su, B., Kim, C., Hernandez, M. X., Rostagno, A. A., Ghiso, J. A., & Kim, J. R. (2010) · ChemBioChem · doi:10.1002/cbic.201000435 · Cited by 43
Plug‐Based Microfluidics with Defined Surface Chemistry to Miniaturize and Control Aggregation of Amyloidogenic Peptides
Meier, M., Kennedy‐Darling, J., Choi, S. H., Norstrom, E. M., Sisodia, S. S., & Ismagilov, R. F. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200805225 · Cited by 42
α-Synuclein Conformation Affects its Tyrosine-Dependent Oxidative Aggregation
Ruf, R. A. S., Lutz, E. A., Zigoneanu, I. G., & Pielak, G. (2008) · Biochemistry · doi:10.1021/bi801884z · Cited by 42
The Fluorescent Amino Acid p‐Cyanophenylalanine Provides an Intrinsic Probe of Amyloid Formation
Marek, P., Gupta, R., & Raleigh, D. P. (2008) · ChemBioChem · doi:10.1002/cbic.200800052 · Cited by 43
Rapid Assembly of Amyloid-β Peptide at a Liquid/Liquid Interface Produces Unstable β-Sheet Fibers
Nichols, M. R., Moss, M. A., Reed, D. K., Hoh, J. H., & Rosenberry, T. L. (2004) · Biochemistry · doi:10.1021/bi048846t · Cited by 39
Zn2+ Aggravates Tau Aggregation and Neurotoxicity
Li, X., Du, X., & Ni, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030487 · Cited by 48
“The fibrillization of tau-R3 incubated alone or with different cations (Mn2+, Mo5+, Fe3+, or Zn2+) was examined by a ThT fluorescence assay [31,32].”
Macromolecular and Small Molecular Crowding Have Similar Effects on α‐Synuclein Structure
Bai, J. Q. A., Liu, M., Pielak, G. J., & Li, C. (2016) · ChemPhysChem · doi:10.1002/cphc.201601097 · Cited by 48
Real-Time Quaking-Induced Conversion Analysis for the Diagnosis of Sporadic Creutzfeldt-Jakob Disease in Korea
Park, J.-H., Choi, Y.-G., Lee, Y.-J., Park, S., Choi, H., Choi, K., Choi, E., & Kim, Y.-S. (2015) · Journal of Clinical Neurology · doi:10.3988/jcn.2016.12.1.101 · Cited by 41
Fructose restrains fibrillogenesis in human serum albumin.
Pandey, N., Ghosh, S., & Dasgupta, S. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2013.08.006 · Cited by 41
9‐(4‐Dimethylaminophenyl)benzo[ b ]quinolizinium: A Near‐Infrared Fluorophore for the Multicolor Analysis of Proteins and Nucleic Acids in Living Cells
Bortolozzi, R., Ihmels, H., Thomas, L., Tian, M., & Viola, G. (2013) · Chemistry - A European Journal · doi:10.1002/chem.201301164 · Cited by 54
Aβ Interacts with Both the Iron Center and the Porphyrin Ring of Heme: Mechanism of Heme’s Action on Aβ Aggregation and Disaggregation
Yuan, C., & Gao, Z. (2013) · Chemical Research in Toxicology · doi:10.1021/tx300441e · Cited by 49
EGCG disaggregates amyloid-like fibrils formed by Plasmodium falciparum merozoite surface protein 2
Chandrashekaran, I., Adda, C., MacRaild, C., Anders, R., & Norton, R. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.07.008 · Cited by 41
Dual amyloid domains promote differential functioning of the chaplin proteins during Streptomyces aerial morphogenesis
Capstick, D. S., Jomaa, A., Hanke, C., Ortega, J., & Elliot, M. (2011) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1018715108 · Cited by 41
Highly sensitive amyloid detection enabled by thioflavin T dimers.
Qin, L.-H., Vastl, J., & Gao, J.-M. (2010) · Molecular Biosystems · doi:10.1039/c005255h · Cited by 41
Aggregation of lysozyme and of poly(ethylene glycol)-modified lysozyme after adsorption to silica.
Daly, S., Przybycien, T., & Tilton, R. D. (2007) · Colloids and Surfaces B: Biointerfaces · doi:10.1016/j.colsurfb.2007.01.007 · Cited by 41
Requirement of aggregation propensity of Alzheimer amyloid peptides for neuronal cell surface binding
Bateman, D. A., McLaurin, J., & Chakrabartty, A. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-29 · Cited by 36
Freezing of a fish antifreeze protein results in amyloid fibril formation.
Graether, S., Slupsky, C., & Sykes, B. (2003) · Biophysical Journal · doi:10.1016/s0006-3495(03)74874-7 · Cited by 41
“…dye ThT To provide further evidence that the type I AFP fibrils were amyloidotic in nature, we examined the AFP gel in the Biophysical Journal 84(1) 552–557 presence of the fluorescent dye ThT. ThT undergoes a specific excitation and emission redshift when bound to amyloid fibrils (LeVine, 1999).”
BackgroundMethod
Ability of soy protein derived amyloid fibrils to stabilize aqueous two-phase system and effect of pH on the system
Gao, Y., Xu, Z.-J., Jin, M., Wang, X., Fan, Z., Jiang, L.-Z., & Sui, X.-N. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109084 · Cited by 40
Amentoflavone: A Bifunctional Metal Chelator that Controls the Formation of Neurotoxic Soluble Aβ42 Oligomers
Sun, L., Sharma, A., Han, B., & Mirica, L. M. (2020) · ACS Chemical Neuroscience · doi:10.26434/chemrxiv.12445505.v1 · Cited by 40
Lipopolysaccharide-binding protein (LBP) can reverse the amyloid state of fibrin seen or induced in Parkinson's disease
Pretorius, E., Pagé, M., Mbotwe, S., & Kell, D. B. (2018) · PLoS ONE · doi:10.1371/journal.pone.0192121 · Cited by 47
Binding of thioflavin T by albumins: An underestimated role of protein oligomeric heterogeneity.
Rovnyagina, N., Sluchanko, N., Tikhonova, T., Fadeev, V., Litskevich, A. Y., Maskevich, A., & Shirshin, E. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2017.12.002 · Cited by 40
The Bacterial Amyloid Curli Is Associated with Urinary Source Bloodstream Infection
Hung, C. S., Marschall, J., Burnham, C., Byun, A. S., & Henderson, J. P. (2014) · PLoS ONE · doi:10.1371/journal.pone.0086009 · Cited by 40
Auramine-O as a fluorescence marker for the detection of amyloid fibrils.
Amdursky, N., & Huppert, D. (2012) · Journal of Physical Chemistry B · doi:10.1021/jp310232b · Cited by 40
Amyloid formation from an α-helix peptide bundle is seeded by 3(10)-helix aggregates.
Singh, Y., Sharpe, P., Hoang, H. N., Lucke, A. J., Mcdowall, A., Bottomley, S., & Fairlie, D. (2011) · Chemistry · doi:10.1002/chem.201002500 · Cited by 40
Wheat glutenin proteins assemble into a nanostructure with unusual structural features
Mackintosh, S. H., Meade, S. J., Healy, J., Sutton, K., Larsen, N., Squires, A., & Gerrard, J. (2009) · doi:10.1016/j.jcs.2008.08.003 · Cited by 40
Phase-Transited Lysozyme with Secondary Reactivity for Moisture-Permeable Antibacterial Wool Fabric
Zhang, N., Deng, Z., Wang, Q., Zhou, M., Wang, P., & Yu, Y. (2021) · Chemical Engineering Journal · doi:10.1016/j.cej.2021.134198 · Cited by 39
Imperfect repeats in the functional amyloid protein FapC reduce the tendency to fragment during fibrillation
Rasmussen, C. B., Christiansen, G., Vad, B. S., Lynggaard, C., Enghild, J. J., Andreasen, M., & Otzen, D. E. (2018) · Protein Science · doi:10.1002/pro.3566 · Cited by 41
A multi‐pathway perspective on protein aggregation: Implications for control of the rate and extent of amyloid formation
Hall, D. R., Kardos, J., Edskes, H. K., Carver, J. A., & Goto, Y. (2015) · FEBS Letters · doi:10.1016/j.febslet.2015.01.032 · Cited by 41
“Another frequently-used procedure for recording the kinetics of amyloid formation involves the use of amyloid specific dyes such as Thioflavin T [29,32] and Congo Red [33].”
BackgroundMethod
Inhibition by flavonoids of amyloid-like fibril formation by Plasmodium falciparum merozoite surface protein 2.
Chandrashekaran, I., Adda, C., MacRaild, C., Anders, R., & Norton, R. (2010) · Biochemistry · doi:10.1021/bi902197x · Cited by 39
Control of amyloid beta-peptide protofibril formation by a designed template assembly.
Dolphin, G., Dumy, P., & Garcia, J. (2006) · Angewandte Chemie · doi:10.1002/anie.200600395 · Cited by 39
MOAG-4 promotes the aggregation of α-synuclein by competing with self-protective electrostatic interactions
Yoshimura, Y., Holmberg, M. A., Kukić, P., Andersen, C. B., Mata‐Cabana, A., Falsone, S. F., Vendruscolo, M., Nollen, E. A. A., & Mulder, F. A. A. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.764886 · Cited by 44
“To address this problem, we investigate here the effects of MOAG-4 on the aggregation of -Syn by monitoring the kinetics of this process using thioflavin T (ThT), a dye known to exhibit enhanced fluorescence upon binding amyloid fibrils (8, 9).”
Method
Designed Glycopeptidomimetics Disrupt Protein–Protein Interactions Mediating Amyloid β-Peptide Aggregation and Restore Neuroblastoma Cell Viability
Kaffy, J., Brinet, D., Soulier, J. L., Correia, I., Tonali, N., Fabiana, F. K., Iacone, Y., Hoffmann, A. R. F., Khemtémourian, L., Crousse, B., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01629 · Cited by 54
Interaction of Aβ(1-42) amyloids with lipids promotes "off-pathway" oligomerization and membrane damage.
Henry, S., Vignaud, H., Bobo, C., Decossas, M., Lambert, O., Harté, E., Alves, I., Cullin, C., & Lecomte, S. (2015) · Biomacromolecules · doi:10.1021/bm501837w · Cited by 38
Quantification of Quaternary Structure Stability in Aggregation-Prone Proteins under Physiological Conditions: The Transthyretin Case
Robinson, L. Z., & Reixach, N. (2014) · Biochemistry · doi:10.1021/bi500739q · Cited by 38
Structural Analysis and Aggregation Propensity of Reduced and Nonreduced Glycated Insulin Adducts
Alavi, P., Yousefi, R., Amirghofran, S., Karbalaei-Heidari, H., & Moosavi-Movahedi, A. (2013) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-013-0207-1 · Cited by 38
“To identify the presence of amyloid-like entities in the aggregates of insulin, both ThT and CR assays were performed [28, 29].”
Method
Dissecting the Role of Single Regions of an IAPP Mimic and IAPP in Inhibition of Aβ40 Amyloid Formation and Cytotoxicity
Andreetto, E., Yan, L.-M., Caporale, A., & Kapurniotu, A. (2011) · ChemBioChem · doi:10.1002/cbic.201100192 · Cited by 38
A kinetic assessment of the C. elegans amyloid disaggregation activity enables uncoupling of disassembly and proteolysis
Bieschke, J., Cohen, E., Murray, A. N., Dillin, A. G., & Kelly, J. W. (2009) · Protein Science · doi:10.1002/pro.234 · Cited by 34
Thermally induced denaturation and aggregation of BLG-A: effect of the Cu2+ and Zn2+ metal ions
Stirpe, A., Rizzuti, B., Pantusa, M., Bartucci, R., Sportelli, L., & Guzzi, R. (2008) · European Biophysics Journal · doi:10.1007/s00249-008-0346-4 · Cited by 41
“The ThT dye is widely used to evidence the presence in solution of molecular aggregates with fibrillar structures (LeVine 1999).”
Background
Evidence for fibril-like structure in bovine casein micelles.
Lencki, R. (2007) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(07)72610-3 · Cited by 38
Design of peptide-based inhibitor agent against amyloid-β aggregation: Molecular docking, synthesis and in vitro evaluation
Jokar, S., Erfani, M., Bavi, O., Khazaei, S., Sharifzadeh, M. S., Hajiramezanali, M., Beiki, D., & Shamloo, A. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.104050 · Cited by 43
Self-Assembly, Antimicrobial Activity, and Membrane Interactions of Arginine-Capped Peptide Bola-Amphiphiles
Edwards-Gayle, C., Castelletto, V., Hamley, I., Barrett, G. A., Greco, F., Hermida-Merino, D., Rambo, R., Seitsonen, J., & Ruokolainen, J. (2019) · ACS Applied Bio Materials · doi:10.1021/acsabm.9b00172 · Cited by 37
“Theself-assembly of RA 9 R in water was studied following the same procedure used for RA 6 R. Results from the ThT assay (Figure 2a) shows that RA 9 R aggregates into amyloid ﬁ bers 32 above a cac = (0.18 ± 0.03) wt %.”
BackgroundMethodInfluential
Ultrafast twisting dynamics of thioflavin-T: spectroscopy of the twisted intramolecular charge-transfer state.
Ghosh, R., & Palit, D. (2014) · ChemPhysChem · doi:10.1002/cphc.201402317 · Cited by 37
The nematode Caenorhabditis elegans: A versatile model for the study of proteotoxicity and aging
Volovik, Y., Marques, F. C., & Cohen, E. (2014) · Methods · doi:10.1016/j.ymeth.2014.04.014 · Cited by 36
Role of filament annealing in the kinetics and thermodynamics of nucleated polymerization.
Michaels, T., & Knowles, T. (2014) · Journal of Chemical Physics · doi:10.1063/1.4880121 · Cited by 37
Turn Nucleation Perturbs Amyloid β Self-Assembly and Cytotoxicity
Doran, T. M., Anderson, E. A., Latchney, S. E., Opanashuk, L. A., & Nilsson, B. L. (2012) · Journal of Molecular Biology · doi:10.1016/j.jmb.2012.01.055 · Cited by 32
Cholesterol Secosterol Aldehydes Induce Amyloidogenesis and Dysfunction of Wild Type Tumor Protein p53
Nieva, J., Song, B., Rogel, J. K., Kujawara, D., Altobel, L., Izharrudin, A., Boldt, G., Grover, R., Wentworth, A. D., & Wentworth, P. (2011) · Chemistry and Biology · doi:10.1016/j.chembiol.2011.02.018 · Cited by 37
Specificity and sensitivity of the Abeta oligomer ELISA
Klaver, A. C., Patrias, L. M., Finke, J. M., & Loeffler, D. A. (2010) · Journal of Neuroscience Methods · doi:10.1016/j.jneumeth.2010.12.001 · Cited by 33
Distinct Type of Transmission Barrier Revealed by Study of Multiple Prion Determinants of Rnq1
Kadnar, M. L., Articov, G., & Derkatch, I. L. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000824 · Cited by 34
Environmental factors differently affect human and rat IAPP: conformational preferences and membrane interactions of IAPP17-29 peptide derivatives.
Pappalardo, G., Milardi, D., Magrì, A., Attanasio, F., Impellizzeri, G., Rosa, C. L., Grasso, D., & Rizzarelli, E. (2007) · Chemistry · doi:10.1002/chem.200700576 · Cited by 37
Analysis of yeast prion aggregates with amyloid-staining compound in vivo.
Kimura, Y., Koitabashi, S., & Fujita, T. (2003) · Cell Structure and Function · doi:10.1247/csf.28.187 · Cited by 37
“Thioflavin-S is a methylated, sulfonated polymerized primulin preparation (LeVine, 1999).”
Background
Recapitulation of selective nuclear import and export with a perfectly repeated 12mer GLFG peptide
Ng, S. C., Guettler, T., & Görlich, D. (2021) · Nature Communications · doi:10.1038/s41467-021-24292-5 · Cited by 44
New and Evolving Techniques for the Characterization of Peptide Therapeutics
D’Addio, S. M., Bothe, J. R., Neri, C., Walsh, P. L., Zhang, J., Pierson, E. E., Mao, Y. J., Gindy, M. E., Leone, A. M., & Templeton, A. C. (2016) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2016.06.011 · Cited by 41
Detection and Quantification of CWD Prions in Fixed Paraffin Embedded Tissues by Real-Time Quaking-Induced Conversion
Hoover, C. E., Davenport, K., Henderson, D., Pulscher, L., Mathiason, C. K., Zabel, M., & Hoover, E. (2016) · Scientific Reports · doi:10.1038/srep25098 · Cited by 36
Environmental impact of multi-wall carbon nanotubes in a novel model of exposure: systemic distribution, macrophage accumulation, and amyloid deposition
Noonan, D. M., Pagani, A., Pulze, L., Bruno, A., Principi, E., Congiu, T., Grimaldi, A., Bassani, B., Flora, S. D., Gini, E., et al. (2015) · International Journal of Nanomedicine · doi:10.2147/ijn.s85275 · Cited by 41
Two distinct β-sheet structures in Italian-mutant amyloid-beta fibrils: a potential link to different clinical phenotypes
Hubin, E., Deroo, S., Schierle, G. S. K., Kaminski, C. F., Serpell, L. C., Subramaniam, V., van Nuland, N. A. J., Broersen, K., Raussens, V., & Sarroukh, R. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1983-2 · Cited by 36
Aqueous extract of some indigenous medicinal plants inhibits glycation at multiple stages and protects erythrocytes from oxidative damage–an in vitro study
Tupe, R., Sankhe, N. M., Shaikh, S., Phatak, D. V., Parikh, J. U., Khaire, A. A., & Kemse, N. G. (2015) · Journal of food science and technology · doi:10.1007/s13197-013-1211-8 · Cited by 36
“T for 1 h. at room temperature (LeVine 1999).”
Background
Advances in electrochemical detection for study of neurodegenerative disorders
Veloso, A. J., & Kerman, K. (2013) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-013-6904-3 · Cited by 38
E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly
Evans, M. L., Schmidt, J., Ilbert, M., Doyle, S. M., Quan, S., Bardwell, J., Jakob, U., Wickner, S., & Chapman, M. (2011) · Prion · doi:10.4161/pri.18555 · Cited by 36
Changes in the physiology of CA1 hippocampal pyramidal neurons in preplaque CRND8 mice
Wykes, R. C., Kalmbach, A., Eliava, M., & Waters, J. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.05.001 · Cited by 31
“To visualize plaques we used thioflavin-S, which binds to amyloid fibrils but not monomers and gives a distinct spectral shift upon binding (Guntern et al., 1992; LeVine, 1999).”
Method
New proteins orthologous to cerato-platanin in various Ceratocystis species and the purification and characterization of cerato-populin from Ceratocystis populicola
Comparini, C., Carresi, L., Pagni, E., Sbrana, F., Sebastiani, F., Luchi, N., Santini, A., Capretti, P., Tiribilli, B., Pazzagli, L., et al. (2009) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-009-1998-4 · Cited by 36
“ThT greatly enhances its fluorescence on binding to amyloid fibrils ( LeVine 1999 ), to protofibrils (Walsh et al. 1999), and to class I hydrophobins (Kwan et al. 2006).”
BackgroundMethod
Promotion of insulin aggregation by protein disulfide isomerase
Maeda, R., Ado, K., Takeda, N., & Taniguchi, Y. (2007) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2007.08.016 · Cited by 38
Supramolecular proteinaceous biofilms as trapping sponges for biologic water treatment and durable catalysis.
Wu, X.-C., Han, X., Lv, L.-L., Li, M.-J., You, J., & Li, C.-X. (2018) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2018.05.036 · Cited by 35
β-Hairpin mimics containing a piperidine–pyrrolidine scaffold modulate the β-amyloid aggregation process preserving the monomer species
Pellegrino, S., Tonali, N., Erba, E., Kaffy, J., Taverna, M., Contini, A., Taylor, M., Allsop, D., Gelmi, M. L., & Ongeri, S. (2016) · Chemical Science · doi:10.1039/c6sc03176e · Cited by 63
Aberrant zinc binding to immature conformers of metal-free copper–zinc superoxide dismutase triggers amorphous aggregation
Leal, S. S., Cristóvão, J. S., Biesemeier, A., Cardoso, I., & Gomes, C. M. (2014) · Metallomics · doi:10.1039/c4mt00278d · Cited by 38
Resting microglia react to Aβ42 fibrils but do not detect oligomers or oligomer-induced neuronal damage
Ferrera, D., Mazzaro, N., Canale, C., & Gasparini, L. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.05.023 · Cited by 33
Xanthene Food Dye, as a Modulator of Alzheimer's Disease Amyloid-beta Peptide Aggregation and the Associated Impaired Neuronal Cell Function
Wong, H. E., & Kwon, I. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025752 · Cited by 34
Discovery and characterization of a mammalian amyloid disaggregation activity
Murray, A. N., Solomon, J. P., Wang, Y., Balch, W. E., & Kelly, J. W. (2010) · Protein Science · doi:10.1002/pro.363 · Cited by 31

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