메뉴 건너뛰기




Volumn , Issue , 2013, Pages

Small-molecule theranostic probes: A promising future in neurodegenerative diseases

Author keywords

[No Author keywords available]

Indexed keywords

ACRIDINE DERIVATIVE; AMPHOTERICIN B; ANTHRACYCLINE; AZO DYE; CONGO RED; MEMANTINE; MEPACRINE; PENTOSAN POLYSULFATE; PHENANTHRIDINE DERIVATIVE; PHTHALOCYANINE; POLYAMINE; PORPHYRIN; STILBENE; STILBENE DERIVATIVE; THIOFLAVINE;

EID: 84890052132     PISSN: 16878876     EISSN: 16878884     Source Type: Journal    
DOI: 10.1155/2013/150952     Document Type: Review
Times cited : (39)

References (182)
  • 2
    • 59249096066 scopus 로고    scopus 로고
    • Radiation dosimetry of beta-amyloid tracers 11c-Pib and 18f-bay94-9172
    • O'keefe G. J., Saunder T. H., Ng S., Radiation dosimetry of beta-amyloid tracers 11c-Pib and 18f-bay94-9172. Journal of Nuclear Medicine 50 309 315
    • Journal of Nuclear Medicine , vol.50 , pp. 309-315
    • O'Keefe, G.J.1    Saunder, T.H.2    Ng, S.3
  • 3
    • 66149104129 scopus 로고    scopus 로고
    • Whole-body biodistribution and radiation dosimetry of 18F-GE067: A radioligand for in vivo brain amyloid imaging
    • 2-s2.0-66149104129 10.2967/jnumed.108.060756
    • Koole M., Lewis D. M., Buckley C., Nelissen N., Vandenbulcke M., Brooks D. J., Vandenberghe R., Van Laere K., Whole-body biodistribution and radiation dosimetry of 18F-GE067: a radioligand for in vivo brain amyloid imaging. Journal of Nuclear Medicine 2009 50 5 818 822 2-s2.0-66149104129 10.2967/jnumed.108. 060756
    • (2009) Journal of Nuclear Medicine , vol.50 , Issue.5 , pp. 818-822
    • Koole, M.1    Lewis, D.M.2    Buckley, C.3    Nelissen, N.4    Vandenbulcke, M.5    Brooks, D.J.6    Vandenberghe, R.7    Van Laere, K.8
  • 4
    • 81955167935 scopus 로고    scopus 로고
    • Theranostic applications of nanomaterials in cancer: Drug delivery, image-guided therapy, and multifunctional platforms
    • 2-s2.0-81955167935 10.1007/s12010-011-9383-z
    • Fernandez-Fernandez A., Manchanda R., McGoron A. J., Theranostic applications of nanomaterials in cancer: drug delivery, image-guided therapy, and multifunctional platforms. Applied Biochemistry and Biotechnology 2011 165 7-8 1628 1651 2-s2.0-81955167935 10.1007/s12010-011-9383-z
    • (2011) Applied Biochemistry and Biotechnology , vol.165 , Issue.7-8 , pp. 1628-1651
    • Fernandez-Fernandez, A.1    Manchanda, R.2    McGoron, A.J.3
  • 5
    • 80255129385 scopus 로고    scopus 로고
    • Perspectives and opportunities for nanomedicine in the management of atherosclerosis
    • 2-s2.0-80255129385 10.1038/nrd3578
    • Lobatto M. E., Fuster V., Fayad Z. A., Mulder W. J. M., Perspectives and opportunities for nanomedicine in the management of atherosclerosis. Nature Reviews Drug Discovery 2011 10 11 835 852 2-s2.0-80255129385 10.1038/nrd3578
    • (2011) Nature Reviews Drug Discovery , vol.10 , Issue.11 , pp. 835-852
    • Lobatto, M.E.1    Fuster, V.2    Fayad, Z.A.3    Mulder, W.J.M.4
  • 6
    • 79952117075 scopus 로고    scopus 로고
    • Targeting the ischemic penumbra
    • 2-s2.0-79952117075 10.1161/STROKEAHA.110.596684
    • Ramos-Cabrer P., Campos F., Sobrino T., Castillo J., Targeting the ischemic penumbra. Stroke 2011 42 1 S7 S11 2-s2.0-79952117075 10.1161/STROKEAHA.110.596684
    • (2011) Stroke , vol.42 , Issue.1
    • Ramos-Cabrer, P.1    Campos, F.2    Sobrino, T.3    Castillo, J.4
  • 7
    • 84873977399 scopus 로고    scopus 로고
    • A fluorescent styrylquinoline with combined therapeutic and diagnostic activities against Alzheimer's and Prion diseases
    • Staderini M., Aulić S., Bartolini M., A fluorescent styrylquinoline with combined therapeutic and diagnostic activities against Alzheimer's and Prion diseases. ACS Medicinal Chemistry Letters 2013 4 225 229
    • (2013) ACS Medicinal Chemistry Letters , vol.4 , pp. 225-229
    • Staderini, M.1    Aulić, S.2    Bartolini, M.3
  • 8
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner S. B., Molecular biology of prion diseases. Science 1991 252 5012 1515 1522 2-s2.0-0025910229 (Pubitemid 21917065)
    • (1991) Science , vol.252 , Issue.5012 , pp. 1515-1522
    • Prusiner, S.B.1
  • 9
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • DOI 10.1016/0092-8674(93)90635-4
    • Jarrett J. T., Lansbury P. T. Jr., Seeding 'one-dimensional crystallization' of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993 73 6 1055 1058 2-s2.0-0027195933 10.1016/0092-8674(93)90635-4 (Pubitemid 23180480)
    • (1993) Cell , vol.73 , Issue.6 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury Jr., P.T.2
  • 11
    • 84877682799 scopus 로고    scopus 로고
    • Protease-sensitive prions with 144-bp insertion mutations
    • Xiao X., Cali I., Dong Z., Protease-sensitive prions with 144-bp insertion mutations. Aging 2013 5 155 173
    • (2013) Aging , vol.5 , pp. 155-173
    • Xiao, X.1    Cali, I.2    Dong, Z.3
  • 13
    • 0014190760 scopus 로고
    • Nature of the scrapie agent: Self-replication and scrapie
    • 2-s2.0-0014190760 10.1038/2151043a0
    • Griffith J. S., Nature of the scrapie agent: self-replication and scrapie. Nature 1967 215 5105 1043 1044 2-s2.0-0014190760 10.1038/2151043a0
    • (1967) Nature , vol.215 , Issue.5105 , pp. 1043-1044
    • Griffith, J.S.1
  • 14
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner S. B., Novel proteinaceous infectious particles cause scrapie. Science 1982 216 4542 136 144 2-s2.0-0020321767 (Pubitemid 12089840)
    • (1982) Science , vol.216 , Issue.4542 , pp. 136-144
    • Prusiner, S.B.1
  • 15
    • 33746127253 scopus 로고
    • Über eine eigenartige herdförmige erkrankung des zentralnervensystems
    • 2-s2.0-33746127253 10.1007/BF02866081
    • Creutzfeldt H. G., Über eine eigenartige herdförmige erkrankung des zentralnervensystems. Zeitschrift für die Gesamte Neurologie und Psychiatrie 1920 57 1 1 18 2-s2.0-33746127253 10.1007/BF02866081
    • (1920) Zeitschrift für Die Gesamte Neurologie und Psychiatrie , vol.57 , Issue.1 , pp. 1-18
    • Creutzfeldt, H.G.1
  • 16
    • 51849177198 scopus 로고
    • Über eigenartige erkrankungen des zentralnervensystems mit bemerkenswertem anatomischen befunde (Spastische pseudosklerose- encephalomyclopathie mit disseminirrten degenerationsherden.)
    • 2-s2.0-51849177198 10.1007/BF02870932
    • Jakob A., Über eigenartige erkrankungen des zentralnervensystems mit bemerkenswertem anatomischen befunde (Spastische pseudosklerose- encephalomyclopathie mit disseminirrten degenerationsherden.). Zeitschrift für die Gesamte Neurologie und Psychiatrie 1921 64 1 147 228 2-s2.0-51849177198 10.1007/BF02870932
    • (1921) Zeitschrift für Die Gesamte Neurologie und Psychiatrie , vol.64 , Issue.1 , pp. 147-228
    • Jakob, A.1
  • 17
    • 0027342789 scopus 로고
    • Human prion diseases (spongiform encephalopathies)
    • 2-s2.0-0027342789
    • Kretzschmar H. A., Human prion diseases (spongiform encephalopathies). Archives of Virology. Supplementum 1993 7 261 293 2-s2.0-0027342789
    • (1993) Archives of Virology. Supplementum , vol.7 , pp. 261-293
    • Kretzschmar, H.A.1
  • 18
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • DOI 10.1146/annurev.neuro.24.1.519
    • Collinge J., Prion diseases of humans and animals: their causes and molecular basis. Annual Review of Neuroscience 2001 24 519 550 2-s2.0-0034916581 10.1146/annurev.neuro.24.1.519 (Pubitemid 32695238)
    • (2001) Annual Review of Neuroscience , vol.24 , pp. 519-550
    • Collinge, J.1
  • 19
    • 0025859996 scopus 로고
    • Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease
    • 2-s2.0-0025859996 10.1016/0140-6736(91)93128-V
    • Collinge J., Palmer M. S., Dryden A. J., Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease. The Lancet 1991 337 8755 1441 1442 2-s2.0-0025859996 10.1016/0140-6736(91)93128-V
    • (1991) The Lancet , vol.337 , Issue.8755 , pp. 1441-1442
    • Collinge, J.1    Palmer, M.S.2    Dryden, A.J.3
  • 20
    • 0025820942 scopus 로고
    • Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease
    • Palmer M. S., Dryden A. J., Hughes J. T., Collinge J., Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 1991 352 6333 340 342 2-s2.0-0025820942 10.1038/352340a0 (Pubitemid 21912354)
    • (1991) Nature , vol.352 , Issue.6333 , pp. 340-342
    • Palmer, M.S.1    Dryden, A.J.2    Hughes, J.T.3    Collinge, J.4
  • 22
    • 0026662717 scopus 로고
    • Familial Creutzfeldt-Jakob disease (codon 200 mutation) with supranuclear palsy
    • 2-s2.0-0026662717 10.1001/jama.268.17.2413
    • Bertoni J. M., Brown P., Goldfarb L. G., Rubenstein R., Gajdusek D. C., Familial Creutzfeldt-Jakob disease (codon 200 mutation) with supranuclear palsy. Journal of the American Medical Association 1992 268 17 2413 2415 2-s2.0-0026662717 10.1001/jama.268.17.2413
    • (1992) Journal of the American Medical Association , vol.268 , Issue.17 , pp. 2413-2415
    • Bertoni, J.M.1    Brown, P.2    Goldfarb, L.G.3    Rubenstein, R.4    Gajdusek, D.C.5
  • 23
    • 0024995430 scopus 로고
    • Mutation of codon 200 of scrapie amyloid protein gene in two clusters of Creutzfeldt-Jakob disease in Slovakia
    • Goldfarb L. G., Mitrova E., Brown P., Toh B. H., Gajdusek D. C., Mutation of codon 200 of scrapie amyloid protein gene in two clusters of Creutzfeldt-Jakob disease in Slovakia. The Lancet 1990 336 8713 514 515 2-s2.0-0024995430 (Pubitemid 20264273)
    • (1990) Lancet , vol.336 , Issue.8713 , pp. 514-515
    • Goldfarb, L.G.1    Mitrova, E.2    Brown, P.3    Toh, B.H.4    Gajdusek, D.C.5
  • 26
    • 0026044686 scopus 로고
    • Familial Creutzfeldt-Jakob disease in Finland: Epidemiological, clinical, pathological and molecular genetic studies
    • 2-s2.0-0026044686
    • Haltia M., Kovanen J., Goldfarb L. G., Brown P., Gajdusek D. C., Familial Creutzfeldt-Jakob disease in Finland: epidemiological, clinical, pathological and molecular genetic studies. European Journal of Epidemiology 1991 7 5 494 500 2-s2.0-0026044686
    • (1991) European Journal of Epidemiology , vol.7 , Issue.5 , pp. 494-500
    • Haltia, M.1    Kovanen, J.2    Goldfarb, L.G.3    Brown, P.4    Gajdusek, D.C.5
  • 27
    • 0026082629 scopus 로고
    • Codon 178 mutation in ethnically diverse Creutzfeldt-Jakob disease families
    • 2-s2.0-0026082629
    • Nieto A., Goldfarb L. G., Brown P., McCombie W. R., Trapp S., Asher D. M., Gajdusek D. C., Codon 178 mutation in ethnically diverse Creutzfeldt-Jakob disease families. The Lancet 1991 337 8741 622 623 2-s2.0-0026082629
    • (1991) The Lancet , vol.337 , Issue.8741 , pp. 622-623
    • Nieto, A.1    Goldfarb, L.G.2    Brown, P.3    McCombie, W.R.4    Trapp, S.5    Asher, D.M.6    Gajdusek, D.C.7
  • 28
    • 0035956518 scopus 로고    scopus 로고
    • Inherited prion disease caused by the V210I mutation: Transmission to transgenic mice
    • Mastrianni J. A., Capellari S., Telling G. C., Han D., Bosque P., Prusiner S. B., DeArmond S. J., Inherited prion disease caused by the V210I mutation: transmission to transgenic mice. Neurology 2001 57 12 2198 2205 2-s2.0-0035956518 (Pubitemid 34016451)
    • (2001) Neurology , vol.57 , Issue.12 , pp. 2198-2205
    • Mastrianni, J.A.1    Capellari, S.2    Telling, G.C.3    Han, D.4    Bosque, P.5    Prusiner, S.B.6    DeArmond, S.J.7
  • 30
  • 32
    • 0031574612 scopus 로고    scopus 로고
    • Predicting the CDJ epidemic in humans
    • DOI 10.1038/385197a0
    • Cousens S. N., Vynnycky E., Zeidier M., Will R. G., Smith P. G., Predicting the CDJ epidemic in humans. Nature 1997 385 6613 197 198 2-s2.0-0031574612 10.1038/385197a0 (Pubitemid 27045728)
    • (1997) Nature , vol.385 , Issue.6613 , pp. 197-198
    • Cousens, S.N.1    Vynnycky, E.2    Zeidier, M.3    Will, R.G.4    Smith, P.G.5
  • 36
    • 0029810684 scopus 로고    scopus 로고
    • New diagnostic tests for prion diseases
    • DOI 10.1056/NEJM199609263351310
    • Collinge J., New diagnostic tests for prion diseases. The New England Journal of Medicine 1996 335 13 963 965 2-s2.0-0029810684 10.1056/ NEJM199609263351310 (Pubitemid 26314452)
    • (1996) New England Journal of Medicine , vol.335 , Issue.13 , pp. 963-965
    • Collinge, J.1
  • 37
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
    • DOI 10.1038/383685a0
    • Collinge J., Sidle K. C. L., Meads J., Ironside J., Hill A. F., Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 1996 383 6602 685 690 2-s2.0-0029831213 10.1038/383685a0 (Pubitemid 26360638)
    • (1996) Nature , vol.383 , Issue.6602 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.L.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 38
    • 4043157677 scopus 로고    scopus 로고
    • Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient
    • DOI 10.1016/S0140-6736(04)16811-6, PII S0140673604168116
    • Peden A. H., Head M. W., Ritchie D. L., Bell P. J. E., Ironside P. J. W., Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. The Lancet 2004 364 9433 527 529 2-s2.0-4043157677 10.1016/S0140- 6736(04)16811-6 (Pubitemid 39070413)
    • (2004) Lancet , vol.364 , Issue.9433 , pp. 527-529
    • Peden, A.H.1    Head, M.W.2    Ritchie, D.L.3    Bell, P.J.E.4    Ironside, P.J.W.5
  • 40
    • 2442735162 scopus 로고    scopus 로고
    • Genetic basis of Creutzfeldt-Jakob disease in the United Kingdom: A systematic analysis of predisposing mutations and allelic variation in the PRNP gene
    • DOI 10.1007/s004390050204
    • Windl O., Dempster M., Estibeiro J. P., Lathe R., De Silva R., Esmonde T., Will R., Springbett A., Campbell T. A., Sidle K. C. L., Palmer M. S., Collinge J., Genetic basis of Creutzfeldt-Jakob disease in the United Kingdom: a systematic analysis of predisposing mutations and allelic variation in the PRNP gene. Human Genetics 1996 98 3 259 264 2-s2.0-2442735162 10.1007/s004390050204 (Pubitemid 26258371)
    • (1996) Human Genetics , vol.98 , Issue.3 , pp. 259-264
    • Windl, O.1    Dempster, M.2    Estibeiro, J.P.3    Lathe, R.4    De Silva, R.5    Esmonde, T.6    Will, R.7    Springbett, A.8    Campbell, T.A.9    Sidle, K.C.L.10    Palmer, M.S.11    Collinge, J.12
  • 41
    • 0025865455 scopus 로고
    • Aminoacid polymorphism in human prion protein and age at death in inherited prion disease
    • 2-s2.0-0025865455
    • Baker H. F., Poulter M., Cros T. J., Frith C. D., Lofthouse R., Ridley R. M., Collinge J., Aminoacid polymorphism in human prion protein and age at death in inherited prion disease. The Lancet 1991 337 8752 1286 2-s2.0-0025865455
    • (1991) The Lancet , vol.337 , Issue.8752 , pp. 1286
    • Baker, H.F.1    Poulter, M.2    Cros, T.J.3    Frith, C.D.4    Lofthouse, R.5    Ridley, R.M.6    Collinge, J.7
  • 43
    • 0028984802 scopus 로고
    • Gerstmann-Straussler-Scheinker disease and the Indiana kindred
    • 10.1111/j.1750-3639.1995.tb00578.x
    • Ghetti B., Dlouhy S. R., Giaccone G., Gerstmann-Straussler-Scheinker disease and the Indiana kindred. Brain Pathology 1995 5 61 75 10.1111/j.1750-3639.1995.tb00578.x
    • (1995) Brain Pathology , vol.5 , pp. 61-75
    • Ghetti, B.1    Dlouhy, S.R.2    Giaccone, G.3
  • 44
    • 0019778656 scopus 로고
    • Creutzfeldt-Jakob disease virus isolations from the Gerstmann-Straussler syndrome. With an analysis of the various forms of amyloid plaque deposition in the virus-induced spongiform encephalopathies
    • Masters C. L., Gajdusek D. C., Gibbs C. J. Jr., Creutzfeldt-Jakob disease virus isolations from the Gerstmann-Straussler syndrome with an analysis of the various forms of amyloid plaque deposition in the virus-induced spongiform encephalopathies. Brain 1981 104 559 588 (Pubitemid 12202196)
    • (1981) Brain , vol.104 , Issue.3 , pp. 559-588
    • Masters, C.L.1    Gajdusek, D.C.2    Gibbs Jr., C.J.3
  • 45
    • 51849178459 scopus 로고
    • Über eine eigenartige hereditär-familiäre Erkrankung des Zentralnervensystems. Zugleich ein Beitrag zur Frage des vorzeitigen lokalen Alterns
    • Gerstmann J., Sträussler E., Scheinker I., Über eine eigenartige hereditär-familiäre Erkrankung des Zentralnervensystems. Zugleich ein Beitrag zur Frage des vorzeitigen lokalen Alterns. Zeitschrift für die Gesamte Neurologie und Psychiatrie 1936 154 736 762
    • (1936) Zeitschrift für Die Gesamte Neurologie und Psychiatrie , vol.154 , pp. 736-762
    • Gerstmann, J.1    Sträussler, E.2    Scheinker, I.3
  • 46
    • 0024519771 scopus 로고
    • Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome
    • DOI 10.1038/338342a0
    • Hsiao K., Baker H. F., Crow T. J., Poulter M., Owen F., Terwilliger J. D., Westaway D., Ott J., Prusiner S. B., Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. Nature 1989 338 6213 342 345 2-s2.0-0024519771 (Pubitemid 19082975)
    • (1989) Nature , vol.338 , Issue.6213 , pp. 342-345
    • Hsiao, K.1    Baker, H.F.2    Crow, T.J.3    Poulter, M.4    Owen, F.5    Terwilliger, J.D.6    Westaway, D.7    Ott, J.8    Prusiner, S.B.9
  • 47
    • 0027729337 scopus 로고
    • A missense mutation at codon 105 with codon 129 polymorphism of the prion protein gene in a new variant of Gerstmann-Straussler-Scheinker disease
    • Yamada M., Itoh Y., Fujigasaki H., Naruse S., Kaneko K., Kitamoto T., Tateishi J., Otomo E., Hayakawa M., Tanaka J., Matsushita M., Miyatake T., A missense mutation at codon 105 with codon 129 polymorphism of the prion protein gene in a new variant of Gerstmann-Straussler-Scheinker disease. Neurology 1993 43 12 I 2723 2724 2-s2.0-0027729337 (Pubitemid 24004583)
    • (1993) Neurology , vol.43 , Issue.I12 , pp. 2723-2724
    • Yamada, M.1    Itoh, Y.2    Fujigasaki, H.3    Naruse, S.4    Kaneko, K.5    Kitamoto, T.6    Tateishi, J.7    Otomo, E.8    Hayakawa, M.9    Tanaka, J.10    Matsushita, M.11    Miyatake, T.12
  • 48
    • 0024473899 scopus 로고
    • Pro→Leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome
    • DOI 10.1016/0006-291X(89)92317-6
    • Doh-ura K., Tateishi J., Sasaki H., Kitamoto T., Sakaki Y., Pro→Leu change at position 102 of prion protein is the most common but not the sole mutation related to Gerstmann-Straussler syndrome. Biochemical and Biophysical Research Communications 1989 163 2 974 979 2-s2.0-0024473899 (Pubitemid 19236945)
    • (1989) Biochemical and Biophysical Research Communications , vol.163 , Issue.2 , pp. 974-979
    • Doh-ura, K.1    Tateishi, J.2    Sasaki, H.3    Kitamoto, T.4    Sakaki, Y.5
  • 52
    • 77749237271 scopus 로고    scopus 로고
    • Conformational flexibility of Y145stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy
    • 2-s2.0-77749237271 10.1021/ja909827v
    • Helmus J. J., Surewicz K., Surewicz W. K., Jaroniec C. P., Conformational flexibility of Y145stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy. Journal of the American Chemical Society 2010 132 7 2393 2403 2-s2.0-77749237271 10.1021/ja909827v
    • (2010) Journal of the American Chemical Society , vol.132 , Issue.7 , pp. 2393-2403
    • Helmus, J.J.1    Surewicz, K.2    Surewicz, W.K.3    Jaroniec, C.P.4
  • 54
    • 0036459944 scopus 로고    scopus 로고
    • Mutations of the prion protein gene: Phenotypic spectrum
    • DOI 10.1007/s00415-002-0896-9
    • Kovács G. G., Trabattoni G., Hainfellner J. A., Ironside J. W., Knight R. S. G., Budka H., Mutations of the prion protein gene: phenotypic spectrum. Journal of Neurology 2002 249 11 1567 1582 2-s2.0-0036459944 10.1007/s00415-002-0896-9 (Pubitemid 35477900)
    • (2002) Journal of Neurology , vol.249 , Issue.11 , pp. 1567-1582
    • Kovacs, G.G.1    Trabattoni, G.2    Hainfellner, J.A.3    Ironside, J.W.4    Knight, R.S.G.5    Budka, H.6
  • 55
    • 78651248344 scopus 로고    scopus 로고
    • A novel seven-octapeptide repeat insertion in the prion protein gene (PRNP) in a Dutch pedigree with Gerstmann-Sträussler-Scheinker disease phenotype: Comparison with similar cases from the literature
    • 2-s2.0-78651248344 10.1007/s00401-010-0656-3
    • Jansen C., Voet W., Head M. W., Parchi P., Yull H., Verrips A., Wesseling P., Meulstee J., Baas F., Van Gool W. A., Ironside J. W., Rozemuller A. J. M., A novel seven-octapeptide repeat insertion in the prion protein gene (PRNP) in a Dutch pedigree with Gerstmann-Sträussler-Scheinker disease phenotype: comparison with similar cases from the literature. Acta Neuropathologica 2011 121 1 59 68 2-s2.0-78651248344 10.1007/s00401-010-0656-3
    • (2011) Acta Neuropathologica , vol.121 , Issue.1 , pp. 59-68
    • Jansen, C.1    Voet, W.2    Head, M.W.3    Parchi, P.4    Yull, H.5    Verrips, A.6    Wesseling, P.7    Meulstee, J.8    Baas, F.9    Van Gool, W.A.10    Ironside, J.W.11    Rozemuller, A.J.M.12
  • 56
    • 0022447484 scopus 로고
    • Fatal familial insomnia and dysautonomia with selective degeneration of thalamic nuclei
    • Lugaresi E., Medori R., Montagna P., Fatal familial insomnia and dysautonomia with selective degeneration of thalamic nuclei. The New England Journal of Medicine 1986 315 16 997 1003 2-s2.0-0022447484 (Pubitemid 16028581)
    • (1986) New England Journal of Medicine , vol.315 , Issue.16 , pp. 997-1003
    • Lugaresi, E.1    Medori, R.2    Montagna, P.3
  • 58
    • 0029989832 scopus 로고    scopus 로고
    • A panencephalopathic type of Creutzfeldt-Jakob disease with selective lesions of the thalamic nuclei in 2 Swiss patients
    • Carota A., Pizzolato G. P., Gailloud P., Macchi G., Fasel J., Le Floch J., Cardone F., A panencephalopathic type of Creutzfeldt-Jakob disease with selective lesions of the thalamic nuclei in 2 Swiss patients. Clinical Neuropathology 1996 15 3 125 134 2-s2.0-0029989832 (Pubitemid 26164822)
    • (1996) Clinical Neuropathology , vol.15 , Issue.3 , pp. 125-134
    • Carota, A.1    Pizzolato, G.P.2    Gailloud, P.3    Macchi, G.4    Fasel, J.5    Le Floch, J.6    Cardone, F.7
  • 60
    • 0030821246 scopus 로고    scopus 로고
    • The D178N (cis-129M) 'fatal familial insomnia' mutation associated with diverse clinicopathologic phenotypes in an Australian kindred
    • 2-s2.0-0030821246
    • McLean C. A., Storey E., Gardner R. J. M., Tannenberg A. E. G., Cervenáková L., Brown P., The D178N (cis-129M) 'fatal familial insomnia' mutation associated with diverse clinicopathologic phenotypes in an Australian kindred. Neurology 1997 49 2 552 558 2-s2.0-0030821246
    • (1997) Neurology , vol.49 , Issue.2 , pp. 552-558
    • McLean, C.A.1    Storey, E.2    Gardner, R.J.M.3    Tannenberg, A.E.G.4    Cervenáková, L.5    Brown, P.6
  • 61
    • 0029961971 scopus 로고    scopus 로고
    • Fatal familial insomnia with a mutation at codon 178 of the priori protein gene: First report from Japan
    • Nagayama M., Shinohara Y., Furukawa H., Kitamoto T., Fatal familial insomnia with a mutation at codon 178 of the priori protein gene: first report from Japan. Neurology 1996 47 5 1313 1316 2-s2.0-0029961971 (Pubitemid 26374905)
    • (1996) Neurology , vol.47 , Issue.5 , pp. 1313-1316
    • Nagayama, M.1    Shinohara, Y.2    Furukawa, H.3    Kitamoto, T.4
  • 66
    • 0041851001 scopus 로고    scopus 로고
    • Familial and sporadic fatal insomnia
    • DOI 10.1016/S1474-4422(03)00323-5
    • Montagna P., Gambetti P., Cortelli P., Lugaresi E., Familial and sporadic fatal insomnia. The Lancet Neurology 2003 2 3 167 176 2-s2.0-0041851001 10.1016/S1474-4422(03)00323-5 (Pubitemid 37443320)
    • (2003) Lancet Neurology , vol.2 , Issue.3 , pp. 167-176
    • Montagna, P.1    Gambetti, P.2    Cortelli, P.3    Lugaresi, E.4
  • 67
    • 78651041685 scopus 로고
    • Degenerative disease of the central nervous system in New Guinea, the endemic occurrence of kuru in the native population
    • 2-s2.0-78651041685
    • Gajdusek D. C., Zigas V., Degenerative disease of the central nervous system in New Guinea, the endemic occurrence of kuru in the native population. The New England Journal of Medicine 1957 257 20 974 978 2-s2.0-78651041685
    • (1957) The New England Journal of Medicine , vol.257 , Issue.20 , pp. 974-978
    • Gajdusek, D.C.1    Zigas, V.2
  • 68
    • 34249936265 scopus 로고    scopus 로고
    • C): Its physiological function and role in disease
    • DOI 10.1016/j.bbadis.2007.02.011, PII S0925443907000609, Prion-Related Disorders
    • Westergard L., Christensen H. M., Harris D. A., The cellular prion protein (PrPC): its physiological function and role in disease. Biochimica et Biophysica Acta 2007 1772 6 629 644 2-s2.0-34249936265 10.1016/j.bbadis.2007.02. 011 (Pubitemid 46880208)
    • (2007) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1772 , Issue.6 , pp. 629-644
    • Westergard, L.1    Christensen, H.M.2    Harris, D.A.3
  • 69
    • 34249947609 scopus 로고    scopus 로고
    • Motor behavioral and neuropathological deficits in mice deficient for normal prion protein expression
    • DOI 10.1016/j.bbadis.2007.04.004, PII S0925443907001019, Prion-Related Disorders
    • Nazor K. E., Seward T., Telling G. C., Motor behavioral and neuropathological deficits in mice deficient for normal prion protein expression. Biochimica et Biophysica Acta 2007 1772 6 645 653 2-s2.0-34249947609 10.1016/j.bbadis.2007.04.004 (Pubitemid 46880209)
    • (2007) Biochimica et Biophysica Acta - Molecular Basis of Disease , vol.1772 , Issue.6 , pp. 645-653
    • Nazor, K.E.1    Seward, T.2    Telling, G.C.3
  • 70
    • 0026600865 scopus 로고
    • Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein
    • 2-s2.0-0026600865 10.1038/356577a0
    • Bueler H., Fischer M., Lang Y., Bluethmann H., Lipp H.-P., DeArmond S. J., Prusiner S. B., Aguet M., Weissmann C., Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 1992 356 6370 577 582 2-s2.0-0026600865 10.1038/356577a0
    • (1992) Nature , vol.356 , Issue.6370 , pp. 577-582
    • Bueler, H.1    Fischer, M.2    Lang, Y.3    Bluethmann, H.4    Lipp, H.-P.5    Dearmond, S.J.6    Prusiner, S.B.7    Aguet, M.8    Weissmann, C.9
  • 71
    • 0028420937 scopus 로고
    • 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal
    • 2-s2.0-0028420937 10.1007/BF02780662
    • Manson J. C., Clarke A. R., Hooper M. L., Aitchison L., McConnell I., Hope J., 129/Ola mice carrying a null mutation in PrP that abolishes mRNA production are developmentally normal. Molecular Neurobiology 1994 8 2-3 121 127 2-s2.0-0028420937 10.1007/BF02780662
    • (1994) Molecular Neurobiology , vol.8 , Issue.2-3 , pp. 121-127
    • Manson, J.C.1    Clarke, A.R.2    Hooper, M.L.3    Aitchison, L.4    McConnell, I.5    Hope, J.6
  • 72
    • 0027319326 scopus 로고
    • Mice devoid of PrP are resistant to scrapie
    • DOI 10.1016/0092-8674(93)90360-3
    • Bueler H., Aguzzi A., Sailer A., Greiner R.-A., Autenried P., Aguet M., Weissmann C., Mice devoid of PrP are resistant to scrapie. Cell 1993 73 7 1339 1347 2-s2.0-0027319326 10.1016/0092-8674(93)90360-3 (Pubitemid 23201147)
    • (1993) Cell , vol.73 , Issue.7 , pp. 1339-1347
    • Bueler, H.1    Aguzzi, A.2    Sailer, A.3    Greiner, R.-A.4    Autenried, P.5    Aguet, M.6    Weissmann, C.7
  • 73
    • 0029112533 scopus 로고
    • Ultrastructural localization of cellular prion protein (PrPc) in synaptic boutons of normal hamster hippocampus
    • 2-s2.0-0029112533
    • Fournier J.-G., Escaig-Haye F., de Villemeur T. B., Robain O., Ultrastructural localization of cellular prion protein (PrPc) in synaptic boutons of normal hamster hippocampus. Comptes Rendus de l'Academie des Sciences 1995 318 3 339 344 2-s2.0-0029112533
    • (1995) Comptes Rendus de l'Academie des Sciences , vol.318 , Issue.3 , pp. 339-344
    • Fournier, J.-G.1    Escaig-Haye, F.2    De Villemeur, T.B.3    Robain, O.4
  • 75
    • 0031866162 scopus 로고    scopus 로고
    • Cellular prion protein localization in rodent and primate brain
    • DOI 10.1046/j.1460-9568.1998.00258.x
    • Salès N., Rodolfo K., Hässig R., Faucheux B., Di Giamberardino L., Moya K. L., Cellular prion protein localization in rodent and primate brain. European Journal of Neuroscience 1998 10 7 2464 2471 2-s2.0-0031866162 10.1046/j.1460-9568.1998.00258.x (Pubitemid 28302347)
    • (1998) European Journal of Neuroscience , vol.10 , Issue.7 , pp. 2464-2471
    • Sales, N.1    Rodolfo, K.2    Hassig, R.3    Faucheux, B.4    Di Giamberardino, L.5    Moya, K.L.6
  • 79
    • 0032585594 scopus 로고    scopus 로고
    • Creutzfeldt-Jakob disease and related transmissible spongiform encephalopathies
    • DOI 10.1056/NEJM199812313392707
    • Johnson R. T., Gibbs C. J. Jr., Creutzfeldt-Jakob disease and related transmissible spongiform encephalopathies. The New England Journal of Medicine 1998 339 27 1994 2004 2-s2.0-0032585594 10.1056/NEJM199812313392707 (Pubitemid 29024133)
    • (1998) New England Journal of Medicine , vol.339 , Issue.27 , pp. 1994-2004
    • Johnson, R.T.1    Gibbs Jr., C.J.2
  • 82
    • 0031720905 scopus 로고    scopus 로고
    • Eight prion strains have PrP(Sc) molecules with different conformations
    • DOI 10.1038/2654
    • Safar J., Wille H., Itri V., Groth D., Serban H., Torchia M., Cohen F. E., Prusiner S. B., Eight prion strains have PrP(Sc) molecules with different conformations. Nature Medicine 1998 4 10 1157 1165 2-s2.0-0031720905 10.1038/2654 (Pubitemid 28468829)
    • (1998) Nature Medicine , vol.4 , Issue.10 , pp. 1157-1165
    • Safar, J.1    Wille, H.2    Itri, V.3    Groth, D.4    Serban, H.5    Torchia, M.6    Cohen, F.E.7    Prusiner, S.B.8
  • 86
    • 26444434251 scopus 로고    scopus 로고
    • Selective precipitation of prions by polyoxometalate complexes
    • DOI 10.1021/ja055219y
    • Lee I. S., Long J. R., Prusiner S. B., Safar J. G., Selective precipitation of prions by polyoxometalate complexes. Journal of the American Chemical Society 2005 127 40 13802 13803 2-s2.0-26444434251 10.1021/ja055219y (Pubitemid 41437025)
    • (2005) Journal of the American Chemical Society , vol.127 , Issue.40 , pp. 13802-13803
    • Lee, I.S.1    Long, J.R.2    Prusiner, S.B.3    Safar, J.G.4
  • 87
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • DOI 10.1038/35081095
    • Saborio G. P., Permanne B., Soto C., Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 2001 411 6839 810 813 2-s2.0-0035859102 10.1038/35081095 (Pubitemid 32588105)
    • (2001) Nature , vol.411 , Issue.6839 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 88
    • 33845944898 scopus 로고    scopus 로고
    • Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification
    • DOI 10.1074/jbc.M603964200
    • Saá P., Castilla J., Soto C., Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. The Journal of Biological Chemistry 2006 281 46 35245 35252 2-s2.0-33845944898 10.1074/jbc.M603964200 (Pubitemid 46036562)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.46 , pp. 35245-35252
    • Saa, P.1    Castilla, J.2    Soto, C.3
  • 89
    • 84855936004 scopus 로고    scopus 로고
    • The oral secretion of infectious scrapie prions occurs in preclinical sheep with a range of PRNP genotypes
    • 2-s2.0-84855936004 10.1128/JVI.05579-11
    • Gough K. C., Baker C. A., Rees H. C., Terry L. A., Spiropoulos J., Thorne L., Maddison B. C., The oral secretion of infectious scrapie prions occurs in preclinical sheep with a range of PRNP genotypes. Journal of Virology 2012 86 1 566 571 2-s2.0-84855936004 10.1128/JVI.05579-11
    • (2012) Journal of Virology , vol.86 , Issue.1 , pp. 566-571
    • Gough, K.C.1    Baker, C.A.2    Rees, H.C.3    Terry, L.A.4    Spiropoulos, J.5    Thorne, L.6    Maddison, B.C.7
  • 90
    • 80052009162 scopus 로고    scopus 로고
    • Detection of prions in the faeces of sheep naturally infected with classical scrapie
    • 2-s2.0-80052009162 10.1186/1297-9716-42-65
    • Terry L. A., Howells L., Bishop K., Baker C. A., Everest S., Thorne L., Maddison B. C., Gough K. C., Detection of prions in the faeces of sheep naturally infected with classical scrapie. Veterinary Research 2011 42 1, article 65 2-s2.0-80052009162 10.1186/1297-9716-42-65
    • (2011) Veterinary Research , vol.42
    • Terry, L.A.1    Howells, L.2    Bishop, K.3    Baker, C.A.4    Everest, S.5    Thorne, L.6    Maddison, B.C.7    Gough, K.C.8
  • 93
    • 58149380989 scopus 로고    scopus 로고
    • In vitro amplification of PrPSc derived from the brain and blood of sheep infected with scrapie
    • 2-s2.0-58149380989 10.1099/vir.0.2008/004226-0
    • Thorne L., Terry L. A., In vitro amplification of PrPSc derived from the brain and blood of sheep infected with scrapie. Journal of General Virology 2008 89 12 3177 3184 2-s2.0-58149380989 10.1099/vir.0.2008/004226-0
    • (2008) Journal of General Virology , vol.89 , Issue.12 , pp. 3177-3184
    • Thorne, L.1    Terry, L.A.2
  • 96
    • 79960163849 scopus 로고    scopus 로고
    • Prion disease blood test using immunoprecipitation and improved quaking-induced conversion
    • 2-s2.0-79960163849 10.1128/mBio.00078-11
    • Orrú C. D., Wilham J. M., Raymond L. D., Kuhn F., Schroeder B., Raeber A. J., Caughey B., Prion disease blood test using immunoprecipitation and improved quaking-induced conversion. mBio 2011 2 3 e00078 e00011 2-s2.0-79960163849 10.1128/mBio.00078-11
    • (2011) MBio , vol.2 , Issue.3
    • Orrú, C.D.1    Wilham, J.M.2    Raymond, L.D.3    Kuhn, F.4    Schroeder, B.5    Raeber, A.J.6    Caughey, B.7
  • 98
    • 70349211719 scopus 로고    scopus 로고
    • Human variant Creutzfeldt-Jakob disease and sheep scrapie PrPres detection using seeded conversion of recombinant prion protein
    • 2-s2.0-70349211719 10.1093/protein/gzp031
    • Orrú C. D., Wilham J. M., Hughson A. G., Raymond L. D., McNally K. L., Bossers A., Ligios C., Caughey B., Human variant Creutzfeldt-Jakob disease and sheep scrapie PrPres detection using seeded conversion of recombinant prion protein. Protein Engineering, Design and Selection 2009 22 8 515 521 2-s2.0-70349211719 10.1093/protein/gzp031
    • (2009) Protein Engineering, Design and Selection , vol.22 , Issue.8 , pp. 515-521
    • Orrú, C.D.1    Wilham, J.M.2    Hughson, A.G.3    Raymond, L.D.4    McNally, K.L.5    Bossers, A.6    Ligios, C.7    Caughey, B.8
  • 100
  • 101
    • 70049114839 scopus 로고    scopus 로고
    • 14-3-3 CSF levels in sporadic Creutzfeldt-Jakob disease differ across molecular subtypes
    • 2-s2.0-70049114839 10.1016/j.neurobiolaging.2008.01.007
    • Gmitterová K., Heinemann U., Bodemer M., Krasnianski A., Meissner B., Kretzschmar H. A., Zerr I., 14-3-3 CSF levels in sporadic Creutzfeldt-Jakob disease differ across molecular subtypes. Neurobiology of Aging 2009 30 11 1842 1850 2-s2.0-70049114839 10.1016/j.neurobiolaging.2008.01.007
    • (2009) Neurobiology of Aging , vol.30 , Issue.11 , pp. 1842-1850
    • Gmitterová, K.1    Heinemann, U.2    Bodemer, M.3    Krasnianski, A.4    Meissner, B.5    Kretzschmar, H.A.6    Zerr, I.7
  • 103
    • 33745113535 scopus 로고    scopus 로고
    • Unsuccessful intraventricular pentosan polysulphate treatment of variant Creutzfeldt-Jakob disease
    • DOI 10.1007/s00701-006-0772-y
    • Whittle I. R., Knight R. S. G., Will R. G., Unsuccessful intraventricular pentosan polysulphate treatment of variant Creutzfeldt-Jakob disease. Acta Neurochirurgica 2006 148 6 677 678 2-s2.0-33745113535 10.1007/s00701-006-0772-y (Pubitemid 43881796)
    • (2006) Acta Neurochirurgica , vol.148 , Issue.6 , pp. 677-678
    • Whittle, I.R.1    Knight, R.S.G.2    Will, R.G.3
  • 104
    • 0032816362 scopus 로고    scopus 로고
    • Inhibitors of protease-resistant prion formation
    • Gilbert I. H., Rudyk H., Inhibitors of protease-resistant prion formation. International Antiviral News 1999 7 5 78 82 2-s2.0-0032816362 (Pubitemid 29374066)
    • (1999) International Antiviral News , vol.7 , Issue.5 , pp. 78-82
    • Gilbert, I.H.1    Rudyk, H.2
  • 105
    • 0242551778 scopus 로고    scopus 로고
    • Emerging therapeutic agents for transmissible spongiform encephalopathies: A review
    • DOI 10.1046/j.1365-2885.2003.00525.x
    • Koster T., Singh K., Zimmermann M., Gruys E., Emerging therapeutic agents for transmissible spongiform encephalopathies: a review. Journal of Veterinary Pharmacology and Therapeutics 2003 26 5 315 326 2-s2.0-0242551778 10.1046/j.1365-2885.2003.00525.x (Pubitemid 37378507)
    • (2003) Journal of Veterinary Pharmacology and Therapeutics , vol.26 , Issue.5 , pp. 315-326
    • Koster, T.1    Singh, K.2    Zimmermann, M.3    Gruys, E.4
  • 107
    • 0037091006 scopus 로고    scopus 로고
    • Pharmacological approaches to prion research
    • DOI 10.1016/S0006-2952(02)00874-2, PII S0006295202008742
    • Supattapone S., Nishina K., Rees J. R., Pharmacological approaches to prion research. Biochemical Pharmacology 2002 63 8 1383 1388 2-s2.0-0037091006 10.1016/S0006-2952(02)00874-2 (Pubitemid 34457952)
    • (2002) Biochemical Pharmacology , vol.63 , Issue.8 , pp. 1383-1388
    • Supattapone, S.1    Nishina, K.2    Rees, J.R.3
  • 108
    • 0033537348 scopus 로고    scopus 로고
    • Prophylactic potential of pentosan polysulphate in transmissible spongiform encephalopathies
    • 2-s2.0-0033537348 10.1016/S0140-6736(98)05395-1
    • Farquhar C., Dickinson A., Bruce M., Prophylactic potential of pentosan polysulphate in transmissible spongiform encephalopathies. The Lancet 1999 353 9147 117 2-s2.0-0033537348 10.1016/S0140-6736(98)05395-1
    • (1999) The Lancet , vol.353 , Issue.9147 , pp. 117
    • Farquhar, C.1    Dickinson, A.2    Bruce, M.3
  • 109
    • 0027280172 scopus 로고
    • Congo red inhibition of scrapie agent replication
    • Caughey B., Ernst D., Race R. E., Congo red inhibition of scrapie agent replication. Journal of Virology 1993 67 10 6270 6272 2-s2.0-0027280172 (Pubitemid 23277541)
    • (1993) Journal of Virology , vol.67 , Issue.10 , pp. 6270-6272
    • Caughey, B.1    Ernst, D.2    Race, R.E.3
  • 110
  • 114
    • 0342409474 scopus 로고    scopus 로고
    • Novel approaches in diagnosis and therapy of Creutzfeldt-Jakob disease
    • 2-s2.0-0342409474 10.1016/S0047-6374(00)00112-3
    • Müller W. E. G., Laplanche J.-L., Ushijima H., Schröder H. C., Novel approaches in diagnosis and therapy of Creutzfeldt-Jakob disease. Mechanisms of Ageing and Development 2000 116 2-3 193 218 2-s2.0-0342409474 10.1016/S0047-6374(00)00112-3
    • (2000) Mechanisms of Ageing and Development , vol.116 , Issue.2-3 , pp. 193-218
    • Müller, W.E.G.1    Laplanche, J.-L.2    Ushijima, H.3    Schröder, H.C.4
  • 115
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie- associated prion protein accumulation
    • DOI 10.1128/JVI.74.10.4894-4897.2000
    • Doh-Ura K., Iwaki T., Caughey B., Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie- associated prion protein accumulation. Journal of Virology 2000 74 10 4894 4897 2-s2.0-0034001444 10.1128/JVI.74.10. 4894-4897.2000 (Pubitemid 30237920)
    • (2000) Journal of Virology , vol.74 , Issue.10 , pp. 4894-4897
    • Doh-Ura, K.1    Iwaki, T.2    Caughey, B.3
  • 119
    • 27444448236 scopus 로고    scopus 로고
    • Promising developments in prion immunotherapy
    • DOI 10.1586/14760584.4.5.607
    • Sigurdsson E. M., Wisniewski T., Promising developments in prion immunotherapy. Expert Review of Vaccines 2005 4 5 607 610 2-s2.0-27444448236 10.1586/14760584.4.5.607 (Pubitemid 41530585)
    • (2005) Expert Review of Vaccines , vol.4 , Issue.5 , pp. 607-610
    • Sigurdsson, E.M.1    Wisniewski, T.2
  • 120
    • 19944405458 scopus 로고    scopus 로고
    • Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets
    • DOI 10.1128/JVI.79.12.7785-7791.2005
    • Bertsch U., Winklhofer K. F., Hirschberger T., Bieschke J., Weber P., Hartl F. U., Tavan P., Tatzelt J., Kretzschmar H. A., Giese A., Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets. Journal of Virology 2005 79 12 7785 7791 2-s2.0-19944405458 10.1128/JVI.79.12.7785-7791.2005 (Pubitemid 40756812)
    • (2005) Journal of Virology , vol.79 , Issue.12 , pp. 7785-7791
    • Bertsch, U.1    Winklhofer, K.F.2    Hirschberger, T.3    Bieschke, J.4    Weber, P.5    Hartl, F.U.6    Tavan, P.7    Tatzelt, J.8    Kretzschmar, H.A.9    Giese, A.10
  • 121
    • 0141632823 scopus 로고    scopus 로고
    • New inhibitors of scrapie-associated prion protein formation in a library of 2,000 drugs and natural products
    • DOI 10.1128/JVI.77.19.10288-10294.2003
    • Kocisko D. A., Baron G. S., Rubenstein R., Chen J., Kuizon S., Caughey B., New inhibitors of scrapie-associated prion protein formation in a library of 2,000 drugs and natural products. Journal of Virology 2003 77 19 10288 10294 2-s2.0-0141632823 10.1128/JVI.77.19.10288-10294.2003 (Pubitemid 37129672)
    • (2003) Journal of Virology , vol.77 , Issue.19 , pp. 10288-10294
    • Kocisko, D.A.1    Baron, G.S.2    Rubenstein, R.3    Chen, J.4    Kuizon, S.5    Caughey, B.6
  • 122
    • 0035893245 scopus 로고    scopus 로고
    • Binding characteristics of radiofluorinated 6-dialkylamino-2- naphthylethylidene derivatives as positron emission tomography imaging probes for beta-amyloid plaques in Alzheimer's disease
    • 2-s2.0-0035893245
    • Agdeppa E. D., Kepe V., Liu J., Flores-Torres S., Satyamurthy N., Petric A., Cole G. M., Small G. W., Huang S. C., Barrio J. R., Binding characteristics of radiofluorinated 6-dialkylamino-2-naphthylethylidene derivatives as positron emission tomography imaging probes for beta-amyloid plaques in Alzheimer's disease. Journal of Neuroscience 2001 21 24 RC189 2-s2.0-0035893245
    • (2001) Journal of Neuroscience , vol.21 , Issue.24
    • Agdeppa, E.D.1    Kepe, V.2    Liu, J.3    Flores-Torres, S.4    Satyamurthy, N.5    Petric, A.6    Cole, G.M.7    Small, G.W.8    Huang, S.C.9    Barrio, J.R.10
  • 123
    • 0037448350 scopus 로고    scopus 로고
    • Structure-activity relationship of imidazo[1,2-a]pyridines as ligands for detecting β-amyloid plaques in the brain
    • DOI 10.1021/jm020351j
    • Zhuang Z.-P., Kung M.-P., Wilson A., Lee C.-W., Plössl K., Hou C., Holtzman D. M., Kung H. F., Structure-activity relationship of imidazo[1,2-a]pyridines as ligands for detecting β -amyloid plaques in the brain. Journal of Medicinal Chemistry 2003 46 2 237 243 2-s2.0-0037448350 10.1021/jm020351j (Pubitemid 36078143)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.2 , pp. 237-243
    • Zhuang, Z.-P.1    Kung, M.-P.2    Wilson, A.3    Lee, C.-W.4    Plossl, K.5    Hou, C.6    Holtzman, D.M.7    Kung, H.F.8
  • 124
    • 0041335200 scopus 로고    scopus 로고
    • Molecular-imaging probe 2-(1-{6-[(2-fluoroethyl)(methyl) amino]-2-naphthyl}ethylidene) malononitrile labels prion plaques in vitro
    • Bresjanac M., Smid L. M., Vovko T. D., Petrič A., Barrio J. R., Popovic M., Molecular-imaging probe 2-(1-{6-[(2-fluoroethyl)(methyl) amino]-2-naphthyl}ethylidene) malononitrile labels prion plaques in vitro. Journal of Neuroscience 2003 23 22 8029 8033 2-s2.0-0041335200 (Pubitemid 37082455)
    • (2003) Journal of Neuroscience , vol.23 , Issue.22 , pp. 8029-8033
    • Bresjanac, M.1    Smid, L.M.2    Vovko, T.D.3    Petric, A.4    Barrio, J.R.5    Popovic, M.6
  • 127
    • 20044392910 scopus 로고    scopus 로고
    • 1H MRI detection of amyloid β plaques in vivo
    • DOI 10.1038/nn1422
    • Higuchi M., Iwata N., Matsuba Y., Sato K., Sasamoto K., Saido T. C., 19F and 1H MRI detection of amyloid β plaques in vivo. Nature Neuroscience 2005 8 4 527 533 2-s2.0-20044392910 10.1038/nn1422 (Pubitemid 41007572)
    • (2005) Nature Neuroscience , vol.8 , Issue.4 , pp. 527-533
    • Higuchi, M.1    Iwata, N.2    Matsuba, Y.3    Sato, K.4    Sasamoto, K.5    Saido, T.C.6
  • 129
    • 0142075238 scopus 로고    scopus 로고
    • 11C-labeled stilbene derivatives as Aβ-aggregate-specific PET imaging agents for Alzheimer's disease
    • DOI 10.1016/S0969-8051(03)00049-0
    • Ono M., Wilson A., Nobrega J., Westaway D., Verhoeff P., Zhuang Z.-P., Kung M.-P., Kung H. F., 11C-labeled stilbene derivatives as A β -aggregate-specific PET imaging agents for Alzheimer's disease. Nuclear Medicine and Biology 2003 30 6 565 571 2-s2.0-0142075238 10.1016/S0969-8051(03)00049-0 (Pubitemid 37289318)
    • (2003) Nuclear Medicine and Biology , vol.30 , Issue.6 , pp. 565-571
    • Ono, M.1    Wilson, A.2    Nobrega, J.3    Westaway, D.4    Verhoeff, P.5    Zhuang, Z.-P.6    Kung, M.-P.7    Kung, H.F.8
  • 133
  • 136
    • 0032855076 scopus 로고    scopus 로고
    • Staining methods for identification of amyloid in tissue
    • DOI 10.1016/S0076-6879(99)09003-5
    • Westermark G. T., Johnson K. H., Westermark P., Staining methods for identification of amyloid in tissue. Methods in Enzymology 1999 309 3 25 2-s2.0-0032855076 10.1016/S0076-6879(99)09003-5 (Pubitemid 29446438)
    • (1999) Methods in Enzymology , vol.309 , pp. 3-25
    • Westermark, G.T.1    Johnson, K.H.2    Westermark, P.3
  • 138
    • 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., Abraham D. J., Quantitative evaluation of Congo red binding to amyloid-like proteins with a beta-pleated sheet conformation. Journal of Histochemistry and Cytochemistry 1989 37 8 1273 1281 2-s2.0-0024352110 (Pubitemid 19186029)
    • (1989) Journal of Histochemistry and Cytochemistry , vol.37 , Issue.8 , pp. 1273-1281
    • Klunk, W.E.1    Pettegrew, J.W.2    Abraham, D.J.3
  • 139
    • 0028076051 scopus 로고
    • Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease
    • DOI 10.1016/0197-4580(94)90050-7
    • Klunk W. E., Debnath M. L., Pettegrew J. W., Development of small molecule probes for the beta-amyloid protein of Alzheimer's disease. Neurobiology of Aging 1994 15 6 691 698 2-s2.0-0028076051 10.1016/0197-4580(94) 90050-7 (Pubitemid 24360159)
    • (1994) Neurobiology of Aging , vol.15 , Issue.6 , pp. 691-698
    • Klunk, W.E.1    Debnath, M.L.2    Pettegrew, J.W.3
  • 140
    • 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
    • 2-s2.0-0016287131
    • 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. Laboratory Investigation 1974 31 3 232 238 2-s2.0-0016287131
    • (1974) Laboratory Investigation , vol.31 , Issue.3 , pp. 232-238
    • Cooper, J.H.1
  • 141
    • 33845192482 scopus 로고    scopus 로고
    • Congo red and protein aggregation in neurodegenerative diseases
    • DOI 10.1016/j.brainresrev.2006.08.001, PII S0165017306001019
    • Frid P., Anisimov S. V., Popovic N., Congo red and protein aggregation in neurodegenerative diseases. Brain Research Reviews 2007 53 1 135 160 2-s2.0-33845192482 10.1016/j.brainresrev.2006.08.001 (Pubitemid 44854214)
    • (2007) Brain Research Reviews , vol.53 , Issue.1 , pp. 135-160
    • Frid, P.1    Anisimov, S.V.2    Popovic, N.3
  • 142
    • 0028588694 scopus 로고
    • Congo red protects against toxicity of β -amyloid peptides on rat hippocampal neurones
    • 2-s2.0-0028588694
    • Burgevin M.-C., Passat M., Daniel N., Capet M., Doble A., Congo red protects against toxicity of β -amyloid peptides on rat hippocampal neurones. NeuroReport 1994 5 18 2429 2432 2-s2.0-0028588694
    • (1994) NeuroReport , vol.5 , Issue.18 , pp. 2429-2432
    • Burgevin, M.-C.1    Passat, M.2    Daniel, N.3    Capet, M.4    Doble, A.5
  • 143
    • 0028172886 scopus 로고
    • β-Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • DOI 10.1073/pnas.91.25.12243
    • Lorenzo A., Yankner B. A., β -Amyloid neurotoxicity requires fibril formation and is inhibited by Congo red. Proceedings of the National Academy of Sciences of the United States of America 1994 91 25 12243 12247 2-s2.0-0028172886 10.1073/pnas.91.25.12243 (Pubitemid 24368641)
    • (1994) Proceedings of the National Academy of Sciences of the United States of America , vol.91 , Issue.25 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 144
    • 0029117593 scopus 로고
    • Sulfonated dyes attenuate the toxic effects of β -amyloid in a structure-specific fashion
    • 2-s2.0-0029117593 10.1016/0304-3940(95)11939-T
    • Pollack S. J., Sulfonated dyes attenuate the toxic effects of β -amyloid in a structure-specific fashion. Neuroscience Letters 1995 197 3 211 214 2-s2.0-0029117593 10.1016/0304-3940(95)11939-T
    • (1995) Neuroscience Letters , vol.197 , Issue.3 , pp. 211-214
    • Pollack, S.J.1
  • 146
    • 15044339964 scopus 로고    scopus 로고
    • Intraneuronal Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease
    • DOI 10.1016/j.neuroscience.2004.12.025
    • Crowther D. C., Kinghorn K. J., Miranda E., Page R., Curry J. A., Duthie F. A. I., Gubb D. C., Lomas D. A., Intraneuronal A β non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer's disease. Neuroscience 2005 132 1 123 135 2-s2.0-15044339964 10.1016/j.neuroscience.2004. 12.025 (Pubitemid 40380720)
    • (2005) Neuroscience , vol.132 , Issue.1 , pp. 123-135
    • Crowther, D.C.1    Kinghorn, K.J.2    Miranda, E.3    Page, R.4    Curry, J.A.5    Duthie, F.A.I.6    Gubb, D.C.7    Lomas, D.A.8
  • 147
    • 0026638150 scopus 로고
    • Potent inhibition of scrapie-associated PrP accumulation by Congo red
    • 2-s2.0-0026638150 10.1111/j.1471-4159.1992.tb09437.x
    • Caughey B., Race R. E., Potent inhibition of scrapie-associated PrP accumulation by Congo red. Journal of Neurochemistry 1992 59 2 768 771 2-s2.0-0026638150 10.1111/j.1471-4159.1992.tb09437.x
    • (1992) Journal of Neurochemistry , vol.59 , Issue.2 , pp. 768-771
    • Caughey, B.1    Race, R.E.2
  • 148
    • 0028970386 scopus 로고
    • Congo red prolongs the incubation period in scrapie-infected hamsters
    • Ingrosso L., Ladogana A., Pocchiari M., Congo red prolongs the incubation period in scrapie-infected hamsters. Journal of Virology 1995 69 1 506 508 2-s2.0-0028970386 (Pubitemid 24378829)
    • (1995) Journal of Virology , vol.69 , Issue.1 , pp. 506-508
    • Ingrosso, L.1    Ladogana, A.2    Pocchiari, M.3
  • 150
    • 0026673537 scopus 로고
    • Effects of sulfate ions on Alzheimer β /A4 peptide assemblies: Implications for amyloid fibril-proteoglycan interactions
    • 2-s2.0-0026673537
    • Fraser P. E., Nguyen J. T., Chin D. T., Kirschner D. A., Effects of sulfate ions on Alzheimer β /A4 peptide assemblies: implications for amyloid fibril-proteoglycan interactions. Journal of Neurochemistry 1992 59 4 1531 1540 2-s2.0-0026673537
    • (1992) Journal of Neurochemistry , vol.59 , Issue.4 , pp. 1531-1540
    • Fraser, P.E.1    Nguyen, J.T.2    Chin, D.T.3    Kirschner, D.A.4
  • 151
    • 0034109546 scopus 로고    scopus 로고
    • Screening Congo Red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells
    • Rudyk H., Vasiljevic S., Hennion R. M., Birkett C. R., Hope J., Gilbert I. H., Screening Congo red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells. Journal of General Virology 2000 81 4 1155 1164 2-s2.0-0034109546 (Pubitemid 30189659)
    • (2000) Journal of General Virology , vol.81 , Issue.4 , pp. 1155-1164
    • Rudyk, H.1    Vasiljevic, S.2    Hennion, R.M.3    Birkett, C.R.4    Hope, J.5    Gilbert, I.H.6
  • 152
    • 0029083059 scopus 로고
    • Chrysamine-G binding to Alzheimer and control brain: Autopsy study of a new amyloid probe
    • 2-s2.0-0029083059 10.1016/0197-4580(95)00058-M
    • Klunk W. E., Debnath M. L., Pettegrew J. W., Chrysamine-G binding to Alzheimer and control brain: autopsy study of a new amyloid probe. Neurobiology of Aging 1995 16 4 541 548 2-s2.0-0029083059 10.1016/0197-4580(95)00058-M
    • (1995) Neurobiology of Aging , vol.16 , Issue.4 , pp. 541-548
    • Klunk, W.E.1    Debnath, M.L.2    Pettegrew, J.W.3
  • 153
    • 0032500717 scopus 로고    scopus 로고
    • Chrysamine-G, a lipophilic analogue of congo red, inhibits Aβ-induced toxicity in PC12 cells
    • DOI 10.1016/S0024-3205(98)00454-8, PII S0024320598004548
    • Klunk W. E., Debnath M. L., Koros A. M. C., Pettegrew J. W., Chrysamine-G, a lipophilic analogue of Congo red, inhibits A β -induced toxicity in PC12 cells. Life Sciences 1998 63 20 1807 1814 2-s2.0-0032500717 10.1016/S0024-3205(98)00454-8 (Pubitemid 28511613)
    • (1998) Life Sciences , vol.63 , Issue.20 , pp. 1807-1814
    • Klunk, W.E.1    Debnath, M.L.2    Koros, A.M.C.3    Pettegrew, J.W.4
  • 154
    • 0033857342 scopus 로고    scopus 로고
    • X-34, a fluorescent derivative of Congo red: A novel histochemical stain for Alzheimer's disease pathology
    • 2-s2.0-0033857342
    • Styren S. D., Hamilton R. L., Styren G. C., Klunk W. E., X-34, a fluorescent derivative of Congo red: a novel histochemical stain for Alzheimer's disease pathology. Journal of Histochemistry and Cytochemistry 2000 48 9 1223 1232 2-s2.0-0033857342
    • (2000) Journal of Histochemistry and Cytochemistry , vol.48 , Issue.9 , pp. 1223-1232
    • Styren, S.D.1    Hamilton, R.L.2    Styren, G.C.3    Klunk, W.E.4
  • 156
    • 2942672633 scopus 로고    scopus 로고
    • Amyloid imaging probes are useful for detection of prion plaques and treatment of transmissible spongiform encephalopathies
    • DOI 10.1099/vir.0.19754-0
    • Ishikawa K., Doh-ura K., Kudo Y., Nishida N., Murakami-Kubo I., Ando Y., Sawada T., Iwaki T., Amyloid imaging probes are useful for detection of prion plaques and treatment of transmissible spongiform encephalopathies. Journal of General Virology 2004 85 6 1785 1790 2-s2.0-2942672633 10.1099/vir.0.19754-0 (Pubitemid 38807776)
    • (2004) Journal of General Virology , vol.85 , Issue.6 , pp. 1785-1790
    • Ishikawa, K.1    Doh-ura, K.2    Kudo, Y.3    Nishida, N.4    Murakami-Kubo, I.5    Ando, Y.6    Sawada, T.7    Iwaki, T.8
  • 157
    • 0000464103 scopus 로고
    • Fluorescent stains, with special reference to amyloid and connective tissues
    • 2-s2.0-0000464103
    • Vassar P. S., Culling C. F., Fluorescent stains, with special reference to amyloid and connective tissues. Archives of Pathology 1959 68 487 498 2-s2.0-0000464103
    • (1959) Archives of Pathology , vol.68 , pp. 487-498
    • Vassar, P.S.1    Culling, C.F.2
  • 159
    • 0024509805 scopus 로고
    • Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T
    • DOI 10.1016/0003-2697(89)90046-8
    • Naiki H., Higuchi K., Hosokawa M., Takeda T., Fluorometric determination of amyloid fibrils in vitro using the fluorescent dye, thioflavine T. Analytical Biochemistry 1989 177 2 244 249 2-s2.0-0024509805 (Pubitemid 19088253)
    • (1989) Analytical Biochemistry , vol.177 , Issue.2 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 160
    • 0025440053 scopus 로고
    • Methods in laboratory investigation. Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: Use of the fluorescent indicator, Thioflavine T
    • Naiki H., Higuchi K., Matsushima K., Shimada A., Chen W.-H., Hosokawa M., Takeda T., Fluorometric examination of tissue amyloid fibrils in murine senile amyloidosis: use of the fluorescent indicator, Thioflavine T. Laboratory Investigation 1990 62 6 768 773 2-s2.0-0025440053 (Pubitemid 20213696)
    • (1990) Laboratory Investigation , vol.62 , Issue.6 , 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
  • 161
    • 0025826915 scopus 로고
    • Kinetic analysis of amyloid fibril polymerization in vitro
    • 2-s2.0-0025826915
    • Naiki H., Higuchi K., Nakakuki K., Takeda T., Kinetic analysis of amyloid fibril polymerization in vitro. Laboratory Investigation 1991 65 1 104 110 2-s2.0-0025826915
    • (1991) Laboratory Investigation , vol.65 , Issue.1 , pp. 104-110
    • Naiki, H.1    Higuchi, K.2    Nakakuki, K.3    Takeda, T.4
  • 162
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease β -amyloid peptides: Detection of amyloid aggregation in solution
    • 2-s2.0-0027502784
    • LeVine H. III, Thioflavine T interaction with synthetic Alzheimer's disease β -amyloid peptides: detection of amyloid aggregation in solution. Protein Science 1993 2 3 404 410 2-s2.0-0027502784
    • (1993) Protein Science , vol.2 , Issue.3 , pp. 404-410
    • Levine III, H.1
  • 163
    • 0001733723 scopus 로고
    • Thioflavine T interaction with amyloid beta-sheet structures
    • 10.3109/13506129509031881
    • LeVine H. I., Thioflavine T interaction with amyloid beta-sheet structures. Amyloid 1995 2 1 1 6 10.3109/13506129509031881
    • (1995) Amyloid , vol.2 , Issue.1 , pp. 1-6
    • Levine, H.I.1
  • 164
    • 33846032313 scopus 로고    scopus 로고
    • Radioligand development for PET imaging of β-amyloid (Aβ)-current status
    • DOI 10.2174/092986707779313471
    • Cai L., Innis R. B., Pike V. W., Radioligand development for PET imaging of β -amyloid (A β)-current status. Current Medicinal Chemistry 2007 14 1 19 52 2-s2.0-33846032313 10.2174/092986707779313471 (Pubitemid 46050302)
    • (2007) Current Medicinal Chemistry , vol.14 , Issue.1 , pp. 19-52
    • Cai, L.1    Innis, R.B.2    Pike, V.W.3
  • 165
    • 0035902875 scopus 로고    scopus 로고
    • Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain
    • DOI 10.1016/S0024-3205(01)01232-2, PII S0024320501012322
    • Klunk W. E., Wang Y., Huang G.-F., Debnath M. L., Holt D. P., Mathis C. A., Uncharged thioflavin-T derivatives bind to amyloid-beta protein with high affinity and readily enter the brain. Life Sciences 2001 69 13 1471 1484 2-s2.0-0035902875 10.1016/S0024-3205(01)01232-2 (Pubitemid 32786721)
    • (2001) Life Sciences , vol.69 , Issue.13 , pp. 1471-1484
    • Klunk, W.E.1    Wang, Y.2    Huang, G.-F.3    Debnath, M.L.4    Holt, D.P.5    Mathis, C.A.6
  • 167
    • 84857047421 scopus 로고    scopus 로고
    • 11C-PiB PET does not detect PrP-amyloid in prion disease patients including variant Creutzfeldt-Jakob disease
    • 10.1136/jnnp.2010.233692
    • Hyare H., Ramlackhansingh A., Gelosa G., 11C-PiB PET does not detect PrP-amyloid in prion disease patients including variant Creutzfeldt-Jakob disease. Journal of Neurology, Neurosurgery & Psychiatry 2012 83 340 341 10.1136/jnnp.2010.233692
    • (2012) Journal of Neurology, Neurosurgery & Psychiatry , vol.83 , pp. 340-341
    • Hyare, H.1    Ramlackhansingh, A.2    Gelosa, G.3
  • 168
    • 0038792263 scopus 로고    scopus 로고
    • 11C-labeled 6-substituted 2-arylbenzothiazoles as amyloid imaging agents
    • DOI 10.1021/jm030026b
    • Mathis C. A., Wang Y., Holt D. P., Huang G.-F., Debnath M. L., Klunk W. E., Synthesis and evaluation of 11C-labeled 6-substituted 2-arylbenzothiazoles as amyloid imaging agents. Journal of Medicinal Chemistry 2003 46 13 2740 2754 2-s2.0-0038792263 10.1021/jm030026b (Pubitemid 36702542)
    • (2003) Journal of Medicinal Chemistry , vol.46 , Issue.13 , pp. 2740-2754
    • Mathis, C.A.1    Wang, Y.2    Holt, D.P.3    Huang, G.-F.4    Debnath, M.L.5    Klunk, W.E.6
  • 172
    • 33748685214 scopus 로고    scopus 로고
    • Styrylbenzoazole derivatives for imaging of prion plaques and treatment of transmissible spongiform encephalopathies
    • DOI 10.1111/j.1471-4159.2006.04035.x
    • Ishikawa K., Kudo Y., Nishida N., Suemoto T., Sawada T., Iwaki T., Doh-Ura K., Styrylbenzoazole derivatives for imaging of prion plaques and treatment of transmissible spongiform encephalopathies. Journal of Neurochemistry 2006 99 1 198 205 2-s2.0-33748685214 10.1111/j.1471-4159.2006. 04035.x (Pubitemid 44395142)
    • (2006) Journal of Neurochemistry , vol.99 , Issue.1 , pp. 198-205
    • Ishikawa, K.1    Kudo, Y.2    Nishida, N.3    Suemoto, T.4    Sawada, T.5    Iwaki, T.6    Doh-Ura, K.7
  • 173
    • 24944586305 scopus 로고    scopus 로고
    • F-18 stilbenes as PET imaging agents for detecting β-amyloid plaques in the brain
    • DOI 10.1021/jm050166g
    • Zhang W., Oya S., Kung M.-P., Hou C., Maier D. L., Kung H. F., F-18 stilbenes as PET imaging agents for detecting β -amyloid plaques in the brain. Journal of Medicinal Chemistry 2005 48 19 5980 5988 2-s2.0-24944586305 10.1021/jm050166g (Pubitemid 41324608)
    • (2005) Journal of Medicinal Chemistry , vol.48 , Issue.19 , pp. 5980-5988
    • Zhang, W.1    Oya, S.2    Kung, M.-P.3    Hou, C.4    Maier, D.L.5    Kung, H.F.6
  • 174
    • 18844406576 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of (E)-3-styrylpyridine derivatives as amyloid imaging agents for Alzheimer's disease
    • DOI 10.1016/j.nucmedbio.2005.01.006, PII S0969805105000442
    • Ono M., Haratake M., Nakayama M., Kaneko Y., Kawabata K., Mori H., Kung M.-P., Kung H. F., Synthesis and biological evaluation of (E)-3-styrylpyridine derivatives as amyloid imaging agents for Alzheimer's disease. Nuclear Medicine and Biology 2005 32 4 329 335 2-s2.0-18844406576 10.1016/j.nucmedbio.2005.01.006 (Pubitemid 40692683)
    • (2005) Nuclear Medicine and Biology , vol.32 , Issue.4 , pp. 329-335
    • Ono, M.1    Haratake, M.2    Nakayama, M.3    Kaneko, Y.4    Kawabata, K.5    Mori, H.6    Kung, M.-P.7    Kung, H.F.8
  • 175
    • 34948887647 scopus 로고    scopus 로고
    • Styryl-based compounds as potential in vivo imaging agents for β-amyloid plaques
    • DOI 10.1002/cbic.200700154
    • Li Q., Min J., Ahn Y.-H., Namm J., Kim E. M., Lui R., Kim H. Y., Ji Y., Wu H., Wisniewski T., Chang Y.-T., Styryl-based compounds as potential in vivo imaging agents for β -amyloid plaques. ChemBioChem 2007 8 14 1679 1687 2-s2.0-34948887647 10.1002/cbic.200700154 (Pubitemid 47523672)
    • (2007) ChemBioChem , vol.8 , Issue.14 , pp. 1679-1687
    • Li, Q.1    Min, J.2    Ahn, Y.-H.3    Namm, J.4    Kim, E.M.5    Lui, R.6    Kim, H.Y.7    Ji, Y.8    Wu, H.9    Wisniewski, T.10    Chang, Y.-T.11
  • 177
    • 78649507705 scopus 로고    scopus 로고
    • Parallel synthesis, evaluation, and preliminary structure-activity relationship of 2,5-diamino-1,4-benzoquinones as a novel class of bivalent anti-prion compound
    • 2-s2.0-78649507705 10.1021/jm100882t
    • Bongarzone S., Tran H. N. A., Cavalli A., Roberti M., Carloni P., Legname G., Bolognesi M. L., Parallel synthesis, evaluation, and preliminary structure-activity relationship of 2,5-diamino-1,4-benzoquinones as a novel class of bivalent anti-prion compound. Journal of Medicinal Chemistry 2010 53 22 8197 8201 2-s2.0-78649507705 10.1021/jm100882t
    • (2010) Journal of Medicinal Chemistry , vol.53 , Issue.22 , pp. 8197-8201
    • Bongarzone, S.1    Tran, H.N.A.2    Cavalli, A.3    Roberti, M.4    Carloni, P.5    Legname, G.6    Bolognesi, M.L.7
  • 179
    • 70449125861 scopus 로고    scopus 로고
    • Optimal parameters for near infrared fluorescence imaging of amyloid plaques in Alzheimer's disease mouse models
    • 2-s2.0-70449125861 10.1088/0031-9155/54/20/011
    • Raymond S. B., Kumar A. T. N., Boas D. A., Bacskai B. J., Optimal parameters for near infrared fluorescence imaging of amyloid plaques in Alzheimer's disease mouse models. Physics in Medicine and Biology 2009 54 20 6201 6216 2-s2.0-70449125861 10.1088/0031-9155/54/20/011
    • (2009) Physics in Medicine and Biology , vol.54 , Issue.20 , pp. 6201-6216
    • Raymond, S.B.1    Kumar, A.T.N.2    Boas, D.A.3    Bacskai, B.J.4
  • 180
    • 70350316758 scopus 로고    scopus 로고
    • Design, synthesis, and testing of difluoroboron-derivatized curcumins as near-infrared probes for in vivo detection of amyloid- β deposits
    • 2-s2.0-70350316758 10.1021/ja9047043
    • Chongzhao R., Xiaoyin X., Raymond S. B., Ferrara B. J., Neal K., Bacskai B. J., Medarova Z., Moore A., Design, synthesis, and testing of difluoroboron-derivatized curcumins as near-infrared probes for in vivo detection of amyloid- β deposits. Journal of the American Chemical Society 2009 131 42 15257 15261 2-s2.0-70350316758 10.1021/ja9047043
    • (2009) Journal of the American Chemical Society , vol.131 , Issue.42 , pp. 15257-15261
    • Chongzhao, R.1    Xiaoyin, X.2    Raymond, S.B.3    Ferrara, B.J.4    Neal, K.5    Bacskai, B.J.6    Medarova, Z.7    Moore, A.8
  • 181
    • 84860203735 scopus 로고    scopus 로고
    • Efficient near-infrared in vivo imaging of amyoid-beta deposits in Alzheimer's disease mouse models
    • Schmidt A., Pahnke J., Efficient near-infrared in vivo imaging of amyoid-beta deposits in Alzheimer's disease mouse models. Journal of Alzheimer's Disease 2012 30 651 664
    • (2012) Journal of Alzheimer's Disease , vol.30 , pp. 651-664
    • Schmidt, A.1    Pahnke, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.