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Volumn 149, Issue 1, 2005, Pages 30-37

The binding of thioflavin-T to amyloid fibrils: Localisation and implications

Author keywords

Amyloid fibrils; Confocal microscopy; Congo red; Spherulites; Thioflavin T

Indexed keywords

AMYLOID; POLYVINYL ALCOHOL; THIOFLAVINE;

EID: 11144222595     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2004.08.002     Document Type: Article
Times cited : (646)

References (54)
  • 1
    • 0033009148 scopus 로고    scopus 로고
    • Primary amyloid tumor (amyloidoma) of the jejunum with spheroid type of amyloid
    • E. Acebo, M. Mayorga, and J.F. Val-Bernal Primary amyloid tumor (amyloidoma) of the jejunum with spheroid type of amyloid Pathology 31 1999 8 11
    • (1999) Pathology , vol.31 , pp. 8-11
    • Acebo, E.1    Mayorga, M.2    Val-Bernal, J.F.3
  • 4
    • 0037356379 scopus 로고    scopus 로고
    • Polymer spherulites: A modern assessment
    • D.C. Bassett Polymer spherulites: a modern assessment J. Macromol. Sci. B Phys. 42 2003 227 256
    • (2003) J. Macromol. Sci. B Phys. , vol.42 , pp. 227-256
    • Bassett, D.C.1
  • 5
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • M. Bouchard, J. Zurdo, E.J. Nettleton, C.M. Dobson, and C.V. Robinson Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy Protein Sci. 9 2000 1960 1967
    • (2000) Protein Sci. , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 8
    • 0031960745 scopus 로고    scopus 로고
    • A model for structure-dependent binding of Congo red to Alzheimer β-amyloid fibrils
    • D.B. Carter, and K.-C. Chou A model for structure-dependent binding of Congo red to Alzheimer β-amyloid fibrils Neurobiol. Aging 19 1998 37 40
    • (1998) Neurobiol. Aging , vol.19 , pp. 37-40
    • Carter, D.B.1    Chou, K.-C.2
  • 9
    • 0016287131 scopus 로고
    • Selective amyloid staining as a function of amyloid composition and structure
    • J.H. Cooper Selective amyloid staining as a function of amyloid composition and structure Lab. Invest. 31 1974 232 238
    • (1974) Lab. Invest. , vol.31 , pp. 232-238
    • Cooper, J.H.1
  • 10
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 13
    • 0015408029 scopus 로고
    • The relation of the properties of Congo red-stained amyloid fibrils to the β-conformation
    • G.G. Glenner, E.G. Eanes, and D.L. Page The relation of the properties of Congo red-stained amyloid fibrils to the β-conformation J. Histochem. Cytochem. 20 1972 821 826
    • (1972) J. Histochem. Cytochem. , vol.20 , pp. 821-826
    • Glenner, G.G.1    Eanes, E.G.2    Page, D.L.3
  • 14
    • 1042267371 scopus 로고    scopus 로고
    • Amyloid fibrillogenesis of silkmoth chorion protein peptide-analogues via a liquid-crystalline intermediate phase
    • S.J. Hamodrakas, A. Hoenger, and V.A. Iconomidou Amyloid fibrillogenesis of silkmoth chorion protein peptide-analogues via a liquid-crystalline intermediate phase J. Struct. Biol. 145 2004 226 235
    • (2004) J. Struct. Biol. , vol.145 , pp. 226-235
    • Hamodrakas, S.J.1    Hoenger, A.2    Iconomidou, V.A.3
  • 15
    • 0028773889 scopus 로고
    • Volume changes on protein folding
    • Y. Harpaz, M. Gerstein, and C. Chothia Volume changes on protein folding Structure 2 1994 641 649
    • (1994) Structure , vol.2 , pp. 641-649
    • Harpaz, Y.1    Gerstein, M.2    Chothia, C.3
  • 18
    • 0028076051 scopus 로고
    • Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease
    • W.E. Klunk, M.L. Debmath, and J.W. Pettergrew Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease Neurobiol. Aging 15 1994 691 698
    • (1994) Neurobiol. Aging , vol.15 , pp. 691-698
    • Klunk, W.E.1    Debmath, M.L.2    Pettergrew, J.W.3
  • 19
    • 0024352110 scopus 로고
    • Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation
    • W.E. Klunk, J.W. Pettegrew, and D.J. Abraham 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
  • 21
    • 0035902875 scopus 로고    scopus 로고
    • Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain
    • W.E. Klunk, Y. Wang, G. Huang, M.L. Debmath, D.P. Holt, and C.A. Mathis Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain Life Sci. 69 2001 1471 1484
    • (2001) Life Sci. , vol.69 , pp. 1471-1484
    • Klunk, W.E.1    Wang, Y.2    Huang, G.3    Debmath, M.L.4    Holt, D.P.5    Mathis, C.A.6
  • 22
  • 25
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • H. LeVine III Thioflavine T interaction with synthetic Alzheimer's disease β-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
  • 26
    • 0001733723 scopus 로고
    • Thioflavine T interactions with amyloid β-sheet structures
    • H. LeVine III Thioflavine T interactions with amyloid β-sheet structures Amyloid 2 1995 1 6
    • (1995) Amyloid , vol.2 , pp. 1-6
    • LeVine III, H.1
  • 27
    • 0036859441 scopus 로고    scopus 로고
    • Aqueous gel formation of a synthetic peptide derived from the β-sheet domain of platelet factor-4
    • N.A. Lockwood, R. van Tankeren, and K.H. Mayo Aqueous gel formation of a synthetic peptide derived from the β-sheet domain of platelet factor-4 Biomacromolecules 3 2002 1225 1232
    • (2002) Biomacromolecules , vol.3 , pp. 1225-1232
    • Lockwood, N.A.1    Van Tankeren, R.2    Mayo, K.H.3
  • 28
    • 0035394291 scopus 로고    scopus 로고
    • Spherulites: A personal perspective
    • J.H. Magill Spherulites: a personal perspective J. Mater. Sci. 36 2001 3143 3164
    • (2001) J. Mater. Sci. , vol.36 , pp. 3143-3164
    • Magill, J.H.1
  • 29
    • 0030758270 scopus 로고    scopus 로고
    • Evolution of a strain of CJD that induces BSE-like plaques
    • L. Manuelidis, W. Fritch, and Y.-G. Xi Evolution of a strain of CJD that induces BSE-like plaques Science 277 1997 94 98
    • (1997) Science , vol.277 , pp. 94-98
    • Manuelidis, L.1    Fritch, W.2    Y -G. Xi3
  • 30
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
    • H. Naiki, K. Higuchi, M. Hosokawa, and T. Takeda Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T 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
  • 31
    • 0025440053 scopus 로고
    • Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: Use of the fluorescent indicator, thioflavin T
    • H. Naiki, K. Higuchi, K. Matsushima, A. Shimada, W.-H. Chen, M. Hosokawa, and T. Takeda 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    Takeda, T.7
  • 32
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • L. Nielsen, R. Khurana, A. Coats, S. Frokjaer, J. Brange, S. Vyas, V.N. Uversky, and A.L. Fink Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism Biochemistry 40 2001 6036 6046
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 33
    • 0000573263 scopus 로고
    • Configurations of polypeptide chains with favoured orientations around single bonds: Two new pleated sheets
    • L. Pauling, and R.B. Corey Configurations of polypeptide chains with favoured orientations around single bonds: two new pleated sheets Proc. Natl. Acad. Sci. USA 37 1951 729 740
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 729-740
    • Pauling, L.1    Corey, R.B.2
  • 35
    • 0015176952 scopus 로고
    • Selective differentiation between amyloid and connective tissue structures based on the collagen specific topo-optical staining reaction with Congo red
    • G. Romhányi Selective differentiation between amyloid and connective tissue structures based on the collagen specific topo-optical staining reaction with Congo red Virchows Arch. A. 354 1971 209 222
    • (1971) Virchows Arch. A. , vol.354 , pp. 209-222
    • Romhányi, G.1
  • 36
    • 0034096547 scopus 로고    scopus 로고
    • α-l-Iduronidase forms semi-crystalline spherulites with amyloid-like properties
    • L. Ruth, D. Eisenberg, and E.F. Neufeld α-l-Iduronidase forms semi-crystalline spherulites with amyloid-like properties Acta Cryst. D 56 2000 524 528
    • (2000) Acta Cryst. D , vol.56 , pp. 524-528
    • Ruth, L.1    Eisenberg, D.2    Neufeld, E.F.3
  • 37
    • 0036182892 scopus 로고    scopus 로고
    • Mesoscopic structure and viscoelastic properties of β-lactoglobulin gels at low pH and low ionic strength
    • L.M.C. Sagis, C. Veerman, R. Ganzevles, M. Ramaekers, S.G. Bolder, and E. van der Linden Mesoscopic structure and viscoelastic properties of β-lactoglobulin gels at low pH and low ionic strength Food Hydrocoll. 16 2002 207 213
    • (2002) Food Hydrocoll. , vol.16 , pp. 207-213
    • Sagis, L.M.C.1    Veerman, C.2    Ganzevles, R.3    Ramaekers, M.4    Bolder, S.G.5    Van Der Linden, E.6
  • 38
    • 1242310516 scopus 로고    scopus 로고
    • Mesoscopic properties of semiflexible amyloid fibrils
    • L.M.C. Sagis, C. Veerman, and E. van der Linden Mesoscopic properties of semiflexible amyloid fibrils Langmuir 20 2004 924 927
    • (2004) Langmuir , vol.20 , pp. 924-927
    • Sagis, L.M.C.1    Veerman, C.2    Van Der Linden, E.3
  • 39
    • 0020991935 scopus 로고
    • Structural properties of protein β-sheets
    • F.R. Salemme Structural properties of protein β-sheets Prog. Biophys. mol. Biol. 42 1983 95 133
    • (1983) Prog. Biophys. Mol. Biol. , vol.42 , pp. 95-133
    • Salemme, F.R.1
  • 40
    • 0347987853 scopus 로고    scopus 로고
    • Folding proteins in fatal ways
    • D.J. Selkoe Folding proteins in fatal ways Nature 426 2003 900 904
    • (2003) Nature , vol.426 , pp. 900-904
    • Selkoe, D.J.1
  • 42
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • J.D. Sipe, and A.S. Cohen Review: history of the amyloid fibril J. Struct. Biol. 130 2000 88 98
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 43
    • 0028082136 scopus 로고
    • An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar Aβ-amyloid in rat brain
    • A.D. Snow, R. Sekiguchi, D. Nochlin, P. Fraser, K. Kimata, A. Mizutani, M. Arai, W.A. Schreier, and D.G. Morgan An important role of heparan sulfate proteoglycan (perlecan) in a model system for the deposition and persistence of fibrillar Aβ-amyloid in rat brain Neuron 12 1994 219 234
    • (1994) Neuron , vol.12 , pp. 219-234
    • Snow, A.D.1    Sekiguchi, R.2    Nochlin, D.3    Fraser, P.4    Kimata, K.5    Mizutani, A.6    Arai, M.7    Schreier, W.A.8    Morgan, D.G.9
  • 44
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • M. Sunde, and C.C.F. Blake The structure of amyloid fibrils by electron microscopy and X-ray diffraction Adv. Protein Chem. 50 1997 123 159
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.C.F.2
  • 46
    • 0011753041 scopus 로고
    • Polarized absorption spectroscopy of molecules aligned in stretched polymers
    • E.W. Thulstrup, and J. Michl Polarized absorption spectroscopy of molecules aligned in stretched polymers Spectrochim. Acta 44A 1988 767 782
    • (1988) Spectrochim. Acta , vol.44 , pp. 767-782
    • Thulstrup, E.W.1    Michl, J.2
  • 47
    • 0026451628 scopus 로고
    • Binding of the dye Congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences
    • W.G. Turnell, and J.T. Finch Binding of the dye Congo red to the amyloid protein pig insulin reveals a novel homology amongst amyloid-forming peptide sequences J. Mol. Biol. 227 1992 1205
    • (1992) J. Mol. Biol. , vol.227 , pp. 1205
    • Turnell, W.G.1    Finch, J.T.2
  • 48
    • 36549102907 scopus 로고
    • Determination of transition moment directions in molecules of low symmetry using polarized fluorescence I
    • M. van Gurp, and Y.K. Levine Determination of transition moment directions in molecules of low symmetry using polarized fluorescence I Theory J. Chem. Phys. 90 1989 4095 4102
    • (1989) Theory J. Chem. Phys. , vol.90 , pp. 4095-4102
    • Van Gurp, M.1    Levine, Y.K.2
  • 49
    • 36549097035 scopus 로고
    • Determination of transition moment directions in molecules of low symmetry using polarized fluorescence. II. Applications to pyranine, perylene, and DPH
    • M. van Gurp, T. van Heijnsbergen, G. van Ginkel, and Y.K. Levine Determination of transition moment directions in molecules of low symmetry using polarized fluorescence. II. Applications to pyranine, perylene, and DPH J. Chem. Phys. 90 1989 4103 4111
    • (1989) J. Chem. Phys. , vol.90 , pp. 4103-4111
    • Van Gurp, M.1    Van Heijnsbergen, T.2    Van Ginkel, G.3    Levine, Y.K.4
  • 52
    • 0022085842 scopus 로고
    • Amyloid in canine mammary tumors
    • J.H. Vos, and E. Gruys Amyloid in canine mammary tumors Vet. Pathol. 22 1985 347 354
    • (1985) Vet. Pathol. , vol.22 , pp. 347-354
    • Vos, J.H.1    Gruys, E.2
  • 53
    • 0000335935 scopus 로고
    • A fibrous modification of insulin
    • D.F. Waugh A fibrous modification of insulin J. Am. Chem. Soc. 68 1946 247 250
    • (1946) J. Am. Chem. Soc. , vol.68 , pp. 247-250
    • Waugh, D.F.1
  • 54
    • 0035846576 scopus 로고    scopus 로고
    • Spontaneous in vitro formation of supramolecular β-amyloid structures, "β amy balls" by amyloid 1-40 peptide
    • A. Westlind-Danielsson, and G. Arnerup Spontaneous in vitro formation of supramolecular β-amyloid structures, "β amy balls" by amyloid 1-40 peptide Biochemistry 40 2001 14736 14743
    • (2001) Biochemistry , vol.40 , pp. 14736-14743
    • Westlind-Danielsson, A.1    Arnerup, G.2


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