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Volumn 70, Issue 5, 2007, Pages 727-733

Cyanine dye-protein interactions: Looking for fluorescent probes for amyloid structures

Author keywords

Amyloid proteins; Cyanine dyes; Fluorescent detection

Indexed keywords

AMYLOID; BENZIMIDAZOLE; BENZOTHIAZOLE; BENZOTHIAZOLE DERIVATIVE; BETA LACTOGLOBULIN; CYANINE DYE; FLUORESCENT DYE; THIOFLAVINE;

EID: 34347387507     PISSN: 0165022X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbbm.2007.03.008     Document Type: Article
Times cited : (67)

References (36)
  • 3
    • 0030822582 scopus 로고    scopus 로고
    • Prion diseases and the BSE crisis
    • Prusiner S.B. Prion diseases and the BSE crisis. Science 278 (1997) 245-251
    • (1997) Science , vol.278 , pp. 245-251
    • Prusiner, S.B.1
  • 4
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • Kelly J.F. Alternative conformations of amyloidogenic proteins govern their behavior. Curr Opin Struct Biol 6 (1996) 11-17
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 11-17
    • Kelly, J.F.1
  • 7
    • 0036784667 scopus 로고    scopus 로고
    • A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea
    • Hamada D., and Dobson C.M. A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea. Protein sci 11 (2002) 2417-2426
    • (2002) Protein sci , vol.11 , pp. 2417-2426
    • Hamada, D.1    Dobson, C.M.2
  • 8
    • 0023425365 scopus 로고
    • Synthetic peptide homologous to β protein from Alzheimer disease forms amyloid-like fibrils in vitro
    • Kirschner D.A., Inouye H., Duffy L.K., Sinclair A., Lind M., and Selkoe D.J. Synthetic peptide homologous to β protein from Alzheimer disease forms amyloid-like fibrils in vitro. Proc Natl Acad Sci 84 (1987) 6953-6957
    • (1987) Proc Natl Acad Sci , vol.84 , pp. 6953-6957
    • Kirschner, D.A.1    Inouye, H.2    Duffy, L.K.3    Sinclair, A.4    Lind, M.5    Selkoe, D.J.6
  • 9
    • 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
  • 10
    • 0027502784 scopus 로고
    • Thioflavin T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine III H. Thioflavin T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci 2 (1993) 404-410
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 11
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo Red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • Klunk W.E., Pettegrew J.W., and Abraham D.J. Quantitative evaluation of Congo Red binding to amyloid-like proteins with a beta-pleated sheet conformation. J Histochem Cytochem 37 (1989) 1273-1281
    • (1989) J Histochem Cytochem , vol.37 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 12
    • 0032855076 scopus 로고    scopus 로고
    • Staining methods for identification of amyloid in tissue
    • Westermark G.T., Johnson K.H., and Westermark P. Staining methods for identification of amyloid in tissue. Methods Enzymol 309 (1999) 3-25
    • (1999) Methods Enzymol , vol.309 , pp. 3-25
    • Westermark, G.T.1    Johnson, K.H.2    Westermark, P.3
  • 14
    • 0025440053 scopus 로고
    • Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: use of the fluorescent indicator, Thioflavin T
    • Naiki H., Higuchi K., Matsushima K., Shimada A., Chen W.-H., Hosokawa M., et al. Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: use of the fluorescent indicator, Thioflavin T. Lab Invest 62 (1990) 768-773
    • (1990) Lab Invest , vol.62 , pp. 768-773
    • Naiki, H.1    Higuchi, K.2    Matsushima, K.3    Shimada, A.4    Chen, W.-H.5    Hosokawa, M.6
  • 15
    • 33645227600 scopus 로고    scopus 로고
    • Congo Red interaction with α-proteins
    • Sereikaite J., and Bumelis V.-A. Congo Red interaction with α-proteins. Acta Biochim Pol 53 (2006) 87-91
    • (2006) Acta Biochim Pol , vol.53 , pp. 87-91
    • Sereikaite, J.1    Bumelis, V.-A.2
  • 16
    • 0029083059 scopus 로고
    • Chrysamine-G binding to Alzheimer and control brain: autopsy study of a new amyloid probe
    • Klunk W.E., Debnath M.L., and Pettegrew J.W. Chrysamine-G binding to Alzheimer and control brain: autopsy study of a new amyloid probe. Neurobiol Aging 16 (1995) 541-548
    • (1995) Neurobiol Aging , vol.16 , pp. 541-548
    • Klunk, W.E.1    Debnath, M.L.2    Pettegrew, J.W.3
  • 17
    • 0033857342 scopus 로고    scopus 로고
    • X-34, a fluorescent derivative of Congo Red: a novel histochemical stain for Alzheimer's disease pathology
    • Styren S.D., Hamilton R.L., Styren G.C., and Klunk W.E. X-34, a fluorescent derivative of Congo Red: a novel histochemical stain for Alzheimer's disease pathology. J Histochem Cytochem 48 (2000) 1223-1232
    • (2000) J Histochem Cytochem , vol.48 , pp. 1223-1232
    • Styren, S.D.1    Hamilton, R.L.2    Styren, G.C.3    Klunk, W.E.4
  • 19
    • 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., et al. 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
  • 21
    • 0032500717 scopus 로고    scopus 로고
    • Chrysamine-G, a lipophilic analogue of Congo Red, inhibits A beta-induced toxicity in PC12 cells
    • Klunk W.E., Debnath M.L., Koros A.M., and Pettegrew J.W. Chrysamine-G, a lipophilic analogue of Congo Red, inhibits A beta-induced toxicity in PC12 cells. Life Sci 63 (1998) 1807-1814
    • (1998) Life Sci , vol.63 , pp. 1807-1814
    • Klunk, W.E.1    Debnath, M.L.2    Koros, A.M.3    Pettegrew, J.W.4
  • 30
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis. The betafibrilloses (first of two parts)
    • Glenner G.G. Amyloid deposits and amyloidosis. The betafibrilloses (first of two parts). N Engl J Med 302 (1980) 1283-1292
    • (1980) N Engl J Med , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 31
    • 11144222595 scopus 로고    scopus 로고
    • The binding of Thioflavin-T to amyloid fibrils: localization and implications
    • Krebs M.R.H., Bromley E.H.C., and Donald A.M. The binding of Thioflavin-T to amyloid fibrils: localization and implications. J Struct Biol 149 (2005) 30-37
    • (2005) J Struct Biol , vol.149 , pp. 30-37
    • Krebs, M.R.H.1    Bromley, E.H.C.2    Donald, A.M.3
  • 33
    • 0016287131 scopus 로고
    • Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo Red, standardized toluidine blue, and iodine methods
    • Cooper J.H. Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo Red, standardized toluidine blue, and iodine methods. Lab Invest 31 (1974) 232-238
    • (1974) Lab Invest , vol.31 , pp. 232-238
    • Cooper, J.H.1
  • 35
    • 0035811461 scopus 로고    scopus 로고
    • Isomerization of (Z,Z) to (E,E)1-bromo-2,5-bis-(3-hydroxycarbonyl-4-hydroxy)styrylbenzene in strong base: probes for amyloid plaques in the brain
    • Lee C.W., Zhuang Z.P., Kung M.P., Plossl K., Skovronsky D., Gur T., et al. Isomerization of (Z,Z) to (E,E)1-bromo-2,5-bis-(3-hydroxycarbonyl-4-hydroxy)styrylbenzene in strong base: probes for amyloid plaques in the brain. J Med Chem 44 (2001) 2270-2275
    • (2001) J Med Chem , vol.44 , pp. 2270-2275
    • Lee, C.W.1    Zhuang, Z.P.2    Kung, M.P.3    Plossl, K.4    Skovronsky, D.5    Gur, T.6
  • 36
    • 0142011533 scopus 로고    scopus 로고
    • Dimethylamino-fluorenes: ligands for detecting beta-amyloid plaques in the brain
    • Lee C.W., Kung M.P., Hou C., and Kung H.F. Dimethylamino-fluorenes: ligands for detecting beta-amyloid plaques in the brain. Nucl Med Biol 30 (2003) 573-580
    • (2003) Nucl Med Biol , vol.30 , pp. 573-580
    • Lee, C.W.1    Kung, M.P.2    Hou, C.3    Kung, H.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.