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Volumn 360, Issue 1, 2007, Pages 135-138

Thioflavin T fluorescence anisotropy: An alternative technique for the study of amyloid aggregation

Author keywords

Amyloid; Anisotropy; Dye binding; Fibril polymerisation; Fibrillogenesis; Kinetic aggregation; Podospora anserina; Prion; Protein aggregation; Thioflavin T

Indexed keywords

AMYLOID; PRION PROTEIN; THIOFLAVINE;

EID: 34250890734     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.06.063     Document Type: Article
Times cited : (58)

References (27)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., and Dobson C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006) 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, Thioflavin T1
    • Naiki H., Higuchi K., Hosokawa M., and Takeda T. Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, Thioflavin T1. Anal. Biochem. 177 (1989) 244-249
    • (1989) Anal. Biochem. , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 3
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with Thioflavin T
    • LeVine H. Quantification of β-sheet amyloid fibril structures with Thioflavin T. Methods Enzymol. 309 (1999) 274-284
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • LeVine, H.1
  • 5
    • 0242580170 scopus 로고    scopus 로고
    • Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease
    • Murakami K., Irie K., Morimoto A., Ohigashi H., Shindo M., Nagao M., Shimizu T., and Shirasawa T. Neurotoxicity and physicochemical properties of Aβ mutant peptides from cerebral amyloid angiopathy: implication for the pathogenesis of cerebral amyloid angiopathy and Alzheimer's disease. J. Biol. Chem. 278 (2003) 46179-46187
    • (2003) J. Biol. Chem. , vol.278 , pp. 46179-46187
    • Murakami, K.1    Irie, K.2    Morimoto, A.3    Ohigashi, H.4    Shindo, M.5    Nagao, M.6    Shimizu, T.7    Shirasawa, T.8
  • 6
    • 27944455577 scopus 로고    scopus 로고
    • Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: an induced circular dichroism/DFT study
    • Dzwolak W., and Pecul M. Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: an induced circular dichroism/DFT study. FEBS Lett. 579 (2005) 6601-6603
    • (2005) FEBS Lett. , vol.579 , pp. 6601-6603
    • Dzwolak, W.1    Pecul, M.2
  • 8
    • 23144434344 scopus 로고    scopus 로고
    • Stimulatory and inhibitory effects of alkyl bromide surfactants on beta-amyloid fibrillogenesis
    • Sabaté R., and Estelrich J. Stimulatory and inhibitory effects of alkyl bromide surfactants on beta-amyloid fibrillogenesis. Langmuir 21 (2005) 6944-6949
    • (2005) Langmuir , vol.21 , pp. 6944-6949
    • Sabaté, R.1    Estelrich, J.2
  • 9
    • 0038795608 scopus 로고    scopus 로고
    • An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid
    • Sabaté R., Gallardo M., and Estelrich J. An autocatalytic reaction as a model for the kinetics of the aggregation of beta-amyloid. Biopolymers 71 (2003) 190-195
    • (2003) Biopolymers , vol.71 , pp. 190-195
    • Sabaté, R.1    Gallardo, M.2    Estelrich, J.3
  • 10
    • 0028872558 scopus 로고
    • Apolipoprotein E is a kinetic but not thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease
    • Evans K.C., Berger E., Cho C., and Weisgraber K.H. Apolipoprotein E is a kinetic but not thermodynamic inhibitor of amyloid formation: implications for the pathogenesis and treatment of Alzheimer disease. Proc. Natl. Acad. Sci. USA 92 (1995) 763-767
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 763-767
    • Evans, K.C.1    Berger, E.2    Cho, C.3    Weisgraber, K.H.4
  • 13
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants
    • Lomakin A., Chung D.S., Benedek G.B., and Kirschner D.A. On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. USA 93 (1996) 1125-1129
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4
  • 14
    • 0036407227 scopus 로고    scopus 로고
    • Peptide aggregation in neurodegenerative disease
    • Murphy R.M. Peptide aggregation in neurodegenerative disease. Annu. Rev. Biomed. Eng. 4 (2002) 155-174
    • (2002) Annu. Rev. Biomed. Eng. , vol.4 , pp. 155-174
    • Murphy, R.M.1
  • 15
    • 0032855484 scopus 로고    scopus 로고
    • Kinetic analysis of amyloid fibril formation
    • Naiki H., and Gejyo F. Kinetic analysis of amyloid fibril formation. Methods Enzymol. 309 (1999) 305-318
    • (1999) Methods Enzymol. , vol.309 , pp. 305-318
    • Naiki, H.1    Gejyo, F.2
  • 18
    • 11144243803 scopus 로고    scopus 로고
    • Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid
    • Koo B.W., and Miranker A.D. Contribution of the intrinsic disulfide to the assembly mechanism of islet amyloid. Protein Sci. 14 (2005) 231-239
    • (2005) Protein Sci. , vol.14 , pp. 231-239
    • Koo, B.W.1    Miranker, A.D.2
  • 19
    • 0038047044 scopus 로고    scopus 로고
    • Structural transformations of oligomeric intermedietes in the fibrillation of the immunoglobulin light chain LEN
    • Souillac P.O., Uversky V.N., and Fink A.L. Structural transformations of oligomeric intermedietes in the fibrillation of the immunoglobulin light chain LEN. Biochemistry 42 (2003) 8094-8104
    • (2003) Biochemistry , vol.42 , pp. 8094-8104
    • Souillac, P.O.1    Uversky, V.N.2    Fink, A.L.3
  • 20
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie
    • Harper J.D., and Lansbury P.T. Models of amyloid seeding in Alzheimer's disease and scrapie. Annu. Rev. Biochem. 66 (1997) 385-407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 23
    • 0242611913 scopus 로고    scopus 로고
    • Pinacyanol as effective probe of fibrillar β-amyloid peptide: Comparative study with Congo Red
    • Sabaté R., and Estelrich J. Pinacyanol as effective probe of fibrillar β-amyloid peptide: Comparative study with Congo Red. Biopolymers 72 (2003) 455-463
    • (2003) Biopolymers , vol.72 , pp. 455-463
    • Sabaté, R.1    Estelrich, J.2
  • 26
    • 34247093347 scopus 로고    scopus 로고
    • Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of the stacked beta-solenoid model of HET-s prion fibrils
    • Sen A., Baxa U., Simon M.N., Wall J.S., Sabate R., Saupe S.J., and Steven A.C. Mass analysis by scanning transmission electron microscopy and electron diffraction validate predictions of the stacked beta-solenoid model of HET-s prion fibrils. J. Biol. Chem. 282 (2007) 5545-5550
    • (2007) J. Biol. Chem. , vol.282 , pp. 5545-5550
    • Sen, A.1    Baxa, U.2    Simon, M.N.3    Wall, J.S.4    Sabate, R.5    Saupe, S.J.6    Steven, A.C.7
  • 27
    • 0034714351 scopus 로고    scopus 로고
    • Nucleated conformational conversion and the replication of conformational information by a prion determinant
    • Serio T., Cashikar A., Kowal A., Sawicki G., Moslehi J., Serpell L., Arnsdorf M., and Lindquist S. Nucleated conformational conversion and the replication of conformational information by a prion determinant. Science 289 (2000) 1317-1321
    • (2000) Science , vol.289 , pp. 1317-1321
    • Serio, T.1    Cashikar, A.2    Kowal, A.3    Sawicki, G.4    Moslehi, J.5    Serpell, L.6    Arnsdorf, M.7    Lindquist, S.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.