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Chemical Compound Review

Thioflavine t,CI 49005     4-(3,6-dimethylbenzothiazol- 2-yl)-N,N...

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Disease relevance of Setoflavin T


Psychiatry related information on Setoflavin T


High impact information on Setoflavin T


Biological context of Setoflavin T


Anatomical context of Setoflavin T


Associations of Setoflavin T with other chemical compounds


Gene context of Setoflavin T

  • By using Thioflavin T, a dye that specifically binds to beta-sheet structures, we found that highly toxic forms of Abeta-aggregates were formed at the initial stage of fibrillogenesis, which is consistent with recent reports on Abeta oligomers [27].
  • Thioflavin T binding assays confirmed that this effect was not mediated by interference with h-IAPP oligomerization [28].
  • The fibrils have all the classical characteristics of amyloid: they have a diameter of 6-7 nm and bind both Congo red and thioflavin-T [29].
  • In addition, hARD1 forms protofilaments under physiological conditions of pH and temperature, as judged by electron microscopy and staining with the dyes Congo red and thioflavin T [30].
  • Here, we prepared nanoparticles as carriers for the model drugs thioflavin T and thioflavin S that bind fibrillar amyloid beta peptides (Abeta) [31].

Analytical, diagnostic and therapeutic context of Setoflavin T


  1. N-Methylated peptide inhibitors of beta-amyloid aggregation and toxicity. Optimization of the inhibitor structure. Kokkoni, N., Stott, K., Amijee, H., Mason, J.M., Doig, A.J. Biochemistry (2006) [Pubmed]
  2. Characterization of two highly amyloidogenic mutants of transthyretin. Goldsteins, G., Andersson, K., Olofsson, A., Dacklin, I., Edvinsson, A., Baranov, V., Sandgren, O., Thylén, C., Hammarstrom, S., Lundgren, E. Biochemistry (1997) [Pubmed]
  3. Single Chain Fv Antibodies against the 25-35 Abeta Fragment Inhibit Aggregation and Toxicity of Abeta42. Zameer, A., Schulz, P., Wang, M.S., Sierks, M.R. Biochemistry (2006) [Pubmed]
  4. Light chain deposition disease restricted to the brain: the first case report. Popovi??, M., Tav??ar, R., Glavac, D., Volavsek, M., Pirtosek, Z., Vizjak, A. Hum. Pathol. (2007) [Pubmed]
  5. Thioflavin T fluorescence in membranoproliferative glomerulonephritis. Date, A., Neela, P., Shastry, J.C. Nephron (1982) [Pubmed]
  6. Evidence for the presence of three distinct binding sites for the thioflavin T class of Alzheimer's disease PET imaging agents on beta-amyloid peptide fibrils. Lockhart, A., Ye, L., Judd, D.B., Merritt, A.T., Lowe, P.N., Morgenstern, J.L., Hong, G., Gee, A.D., Brown, J. J. Biol. Chem. (2005) [Pubmed]
  7. Evidence for cholinergic neurites in senile plaques. Kitt, C.A., Price, D.L., Struble, R.G., Cork, L.C., Wainer, B.H., Becher, M.W., Mobley, W.C. Science (1984) [Pubmed]
  8. A role for protein misfolding in immunogenicity of biopharmaceuticals. Maas, C., Hermeling, S., Bouma, B., Jiskoot, W., Gebbink, M.F. J. Biol. Chem. (2007) [Pubmed]
  9. Formation of tau inclusions in knock-in mice with familial Alzheimer disease (FAD) mutation of presenilin 1 (PS1). Tanemura, K., Chui, D.H., Fukuda, T., Murayama, M., Park, J.M., Akagi, T., Tatebayashi, Y., Miyasaka, T., Kimura, T., Hashikawa, T., Nakano, Y., Kudo, T., Takeda, M., Takashima, A. J. Biol. Chem. (2006) [Pubmed]
  10. p25alpha Stimulates alpha-synuclein aggregation and is co-localized with aggregated alpha-synuclein in alpha-synucleinopathies. Lindersson, E., Lundvig, D., Petersen, C., Madsen, P., Nyengaard, J.R., Højrup, P., Moos, T., Otzen, D., Gai, W.P., Blumbergs, P.C., Jensen, P.H. J. Biol. Chem. (2005) [Pubmed]
  11. Does the cytotoxic effect of transient amyloid oligomers from common equine lysozyme in vitro imply innate amyloid toxicity? Malisauskas, M., Ostman, J., Darinskas, A., Zamotin, V., Liutkevicius, E., Lundgren, E., Morozova-Roche, L.A. J. Biol. Chem. (2005) [Pubmed]
  12. Thioflavin T is a fluorescent probe of the acetylcholinesterase peripheral site that reveals conformational interactions between the peripheral and acylation sites. De Ferrari, G.V., Mallender, W.D., Inestrosa, N.C., Rosenberry, T.L. J. Biol. Chem. (2001) [Pubmed]
  13. Relationship between stability of folding intermediates and amyloid formation for the yeast prion Ure2p: a quantitative analysis of the effects of pH and buffer system. Zhu, L., Zhang, X.J., Wang, L.Y., Zhou, J.M., Perrett, S. J. Mol. Biol. (2003) [Pubmed]
  14. Direct Observation of Oligomeric Species formed in the Early Stages of Amyloid Fibril Formation using Electrospray Ionisation Mass Spectrometry. Smith, A.M., Jahn, T.R., Ashcroft, A.E., Radford, S.E. J. Mol. Biol. (2006) [Pubmed]
  15. Unmasking tandem site interaction in human acetylcholinesterase. Substrate activation with a cationic acetanilide substrate. Johnson, J.L., Cusack, B., Davies, M.P., Fauq, A., Rosenberry, T.L. Biochemistry (2003) [Pubmed]
  16. A peptide motif consisting of glycine, alanine, and valine is required for the fibrillization and cytotoxicity of human alpha-synuclein. Du, H.N., Tang, L., Luo, X.Y., Li, H.T., Hu, J., Zhou, J.W., Hu, H.Y. Biochemistry (2003) [Pubmed]
  17. Failure to find amyloidosis in dogs treated with long-term intravenous insulin delivered by a totally implantable pump. Mauer, S.M., Buchwald, H., Groppoli, T.J., Rohde, T.D., Wigness, B.D., Rupp, W.M., Steffes, M.W. Diabetologia (1983) [Pubmed]
  18. Cerebrospinal fluid of Alzheimer patients promotes beta-amyloid fibril formation in vitro. Ono, K., Noguchi, M., Matsumoto, Y., Yanase, D., Iwasa, K., Naiki, H., Yamada, M. Neurobiol. Dis. (2005) [Pubmed]
  19. Cardiac nonamyloidotic immunoglobulin deposition disease. Toor, A.A., Ramdane, B.A., Joseph, J., Thomas, M., O'Hara, C., Barlogie, B., Walker, P., Joseph, L. Mod. Pathol. (2006) [Pubmed]
  20. Thiazole orange: a new dye for reticulocyte analysis. Lee, L.G., Chen, C.H., Chiu, L.A. Cytometry. (1986) [Pubmed]
  21. Emission of thioflavin T and its off-on control in polymer membranes. Raj, C.R., Ramaraj, R. Photochem. Photobiol. (2001) [Pubmed]
  22. Amyloid-like fibril formation in an all beta-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation. Srisailam, S., Kumar, T.K., Rajalingam, D., Kathir, K.M., Sheu, H.S., Jan, F.J., Chao, P.C., Yu, C. J. Biol. Chem. (2003) [Pubmed]
  23. Amyloid nucleation and hierarchical assembly of Ure2p fibrils. Role of asparagine/glutamine repeat and nonrepeat regions of the prion domains. Jiang, Y., Li, H., Zhu, L., Zhou, J.M., Perrett, S. J. Biol. Chem. (2004) [Pubmed]
  24. Ultrasonication-induced amyloid fibril formation of beta2-microglobulin. Ohhashi, Y., Kihara, M., Naiki, H., Goto, Y. J. Biol. Chem. (2005) [Pubmed]
  25. Oleic Acid Inhibits Amyloid Formation of the Intermediate of alpha-Lactalbumin at Moderately Acidic pH. Yang, F., Zhang, M., Zhou, B.R., Chen, J., Liang, Y. J. Mol. Biol. (2006) [Pubmed]
  26. Amyloid Fibril Formation and Disaggregation of Fragment 1-29 of Apomyoglobin: Insights into the Effect of pH on Protein Fibrillogenesis. Picotti, P., De Franceschi, G., Frare, E., Spolaore, B., Zambonin, M., Chiti, F., de Laureto, P.P., Fontana, A. J. Mol. Biol. (2007) [Pubmed]
  27. Specific compositions of amyloid-beta peptides as the determinant of toxic beta-aggregation. Yoshiike, Y., Chui, D.H., Akagi, T., Tanaka, N., Takashima, A. J. Biol. Chem. (2003) [Pubmed]
  28. Activation of peroxisome proliferator-activated receptor-gamma by rosiglitazone protects human islet cells against human islet amyloid polypeptide toxicity by a phosphatidylinositol 3'-kinase-dependent pathway. Lin, C.Y., Gurlo, T., Haataja, L., Hsueh, W.A., Butler, P.C. J. Clin. Endocrinol. Metab. (2005) [Pubmed]
  29. Amyloid fibril formation by a synthetic peptide from a region of human acetylcholinesterase that is homologous to the Alzheimer's amyloid-beta peptide. Cottingham, M.G., Hollinshead, M.S., Vaux, D.J. Biochemistry (2002) [Pubmed]
  30. Characterization of the native and fibrillar conformation of the human Nalpha-acetyltransferase ARD1. Sánchez-Puig, N., Fersht, A.R. Protein Sci. (2006) [Pubmed]
  31. Thioflavins released from nanoparticles target fibrillar amyloid beta in the hippocampus of APP/PS1 transgenic mice. Siegemund, T., Paulke, B.R., Schmiedel, H., Bordag, N., Hoffmann, A., Harkany, T., Tanila, H., Kacza, J., Härtig, W. Int. J. Dev. Neurosci. (2006) [Pubmed]
  32. Purification, ultrastructure, and chemical analysis of Alzheimer disease amyloid plaque core protein. Roher, A., Wolfe, D., Palutke, M., KuKuruga, D. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
  33. Acceleration of Alzheimer's fibril formation by apolipoprotein E in vitro. Wisniewski, T., Castaño, E.M., Golabek, A., Vogel, T., Frangione, B. Am. J. Pathol. (1994) [Pubmed]
  34. Amyloid-beta protofibrils differ from amyloid-beta aggregates induced in dilute hexafluoroisopropanol in stability and morphology. Nichols, M.R., Moss, M.A., Reed, D.K., Cratic-McDaniel, S., Hoh, J.H., Rosenberry, T.L. J. Biol. Chem. (2005) [Pubmed]
  35. New class of inhibitors of amyloid-beta fibril formation. Implications for the mechanism of pathogenesis in Alzheimer's disease. Lashuel, H.A., Hartley, D.M., Balakhaneh, D., Aggarwal, A., Teichberg, S., Callaway, D.J. J. Biol. Chem. (2002) [Pubmed]
  36. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. Pedersen, J.S., Dikov, D., Flink, J.L., Hjuler, H.A., Christiansen, G., Otzen, D.E. J. Mol. Biol. (2006) [Pubmed]
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