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Volumn 54, Issue 7, 2004, Pages 406-415

Evaluation of anti-prion activity of congo red and its derivatives in experimentally infected hamsters

Author keywords

Bovine spongiform encephalopatdy (BSE); CAS 573 58 0; Congo Red, anti prion activity, derivatives, hamster; Prion protein

Indexed keywords

ANTIVIRUS AGENT; BENZIDINE(4,4' DIAMINOBIPHENYL); CAS 573580; CONGO RED; UNCLASSIFIED DRUG;

EID: 3242786318     PISSN: 00044172     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0031-1296992     Document Type: Article
Times cited : (29)

References (63)
  • 2
    • 0019127305 scopus 로고
    • Comparative activity of 4,4′diaminobiphenyl (benzidine) and its terphenyl analogue, 4,4′-diaminoterphenyl, in two in vitro assays for potential carcinogenicity
    • Ashby, J., Styles, J., Callander, R. D., Comparative activity of 4,4′diaminobiphenyl (benzidine) and its terphenyl analogue, 4,4′-diaminoterphenyl, in two in vitro assays for potential carcinogenicity. Carcinogenesis 1, 801 (1980)
    • (1980) Carcinogenesis , vol.1 , pp. 801
    • Ashby, J.1    Styles, J.2    Callander, R.D.3
  • 3
    • 0030801497 scopus 로고    scopus 로고
    • Inhibitors of Ab peptide aggregation as potential anti-Alzheimer agents
    • Bandiera, T., Lansen, J., Post, G. et al., Inhibitors of Ab peptide aggregation as potential anti-Alzheimer agents. Curr. Med. Chem. 4, 159 (1997)
    • (1997) Curr. Med. Chem. , vol.4 , pp. 159
    • Bandiera, T.1    Lansen, J.2    Post, G.3
  • 4
    • 0034044948 scopus 로고    scopus 로고
    • Opposite effects of Dextran Sulfate 500, the polyene antibiotic MS-8209, and Congo Red on accumulation on the protease-resistant isoform of PrP in the spleens of mice inoculated intraperitoneally with the scrapie agent
    • Beringue, V., Adjou, K. T., Lamoury, F. et al., Opposite effects of Dextran Sulfate 500, the polyene antibiotic MS-8209, and Congo Red on accumulation on the protease-resistant isoform of PrP in the spleens of mice inoculated intraperitoneally with the scrapie agent. J. Virol. 74, 5432 (2000)
    • (2000) J. Virol. , vol.74 , pp. 5432
    • Beringue, V.1    Adjou, K.T.2    Lamoury, F.3
  • 5
    • 0012856184 scopus 로고
    • The essential role of the intestinal flora in the toxification of orally-administered benzidine-based dyes: Internal exposure of rats to benzidine after intestinal azo reduction
    • Bos, R. P, Koopman, J. P., Theuws, J. L., The essential role of the intestinal flora in the toxification of orally-administered benzidine-based dyes: internal exposure of rats to benzidine after intestinal azo reduction. Mutat. Res. 181, 327 (1987)
    • (1987) Mutat. Res. , vol.181 , pp. 327
    • Bos, R.P.1    Koopman, J.P.2    Theuws, J.L.3
  • 6
    • 0033999635 scopus 로고    scopus 로고
    • Cultured cells sublines highly susceptible to prion infection
    • Bosque, P. J., Prusiner, S. B., Cultured cells sublines highly susceptible to prion infection. J. Virol. 74, 4377 (2000)
    • (2000) J. Virol. , vol.74 , pp. 4377
    • Bosque, P.J.1    Prusiner, S.B.2
  • 7
    • 0034533064 scopus 로고    scopus 로고
    • PrPsc-like prion protein peptide inhibits the function of cellular prion protein
    • Brown, D. R., PrPsc-like prion protein peptide inhibits the function of cellular prion protein. Biochem. J. 352, 511 (2000)
    • (2000) Biochem. J. , vol.352 , pp. 511
    • Brown, D.R.1
  • 8
    • 0032488921 scopus 로고    scopus 로고
    • The antiprion activity of Congo Red. Putative mechanism
    • Caspi, S., Halimi, M., Yanai, A. et al., The antiprion activity of Congo Red. Putative mechanism. J. Biol. Chem. 273, 3484 (1998)
    • (1998) J. Biol. Chem. , vol.273 , pp. 3484
    • Caspi, S.1    Halimi, M.2    Yanai, A.3
  • 9
    • 0028256222 scopus 로고
    • Binding of protease-sensitive form of prion protein PrP to sulfated glycosaminoglycan and Congo Red
    • Caughey, B., Brown, K., Raymond, G. J. et al., Binding of protease-sensitive form of prion protein PrP to sulfated glycosaminoglycan and Congo Red. J. Virol. 68, 2135 (1994)
    • (1994) J. Virol. , vol.68 , pp. 2135
    • Caughey, B.1    Brown, K.2    Raymond, G.J.3
  • 10
    • 0031080867 scopus 로고    scopus 로고
    • Prion protein and the transmissible spongiform encephalopathies
    • Caughey, B., Chesebro, B., Prion protein and the transmissible spongiform encephalopathies. Trends Cell Biol. 7, 56 (1997)
    • (1997) Trends Cell Biol. , vol.7 , pp. 56
    • Caughey, B.1    Chesebro, B.2
  • 11
    • 0026638150 scopus 로고
    • Potent inhibition of scrapie-associated PrP accumulation by Congo Red
    • Caughey, B., Race, R. E., Potent inhibition of scrapie-associated PrP accumulation by Congo Red. J. Neurochem. 59, 768 (1992)
    • (1992) J. Neurochem. , vol.59 , pp. 768
    • Caughey, B.1    Race, R.E.2
  • 12
    • 0033946710 scopus 로고    scopus 로고
    • Prions, peptides and protein misfolding
    • Cohen, F. E., Prions, peptides and protein misfolding. Mol. Med. Today 6, 292 (2000)
    • (2000) Mol. Med. Today , vol.6 , pp. 292
    • Cohen, F.E.1
  • 13
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • Collinge, J., Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24, 519 (2001)
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 519
    • Collinge, J.1
  • 14
    • 0030778819 scopus 로고    scopus 로고
    • Late treatment with polyene antibiotics can prolong the survival time of scrapie-infected animals
    • Demaimay, R., Adjou, K., Beringue, V. et al., Late treatment with polyene antibiotics can prolong the survival time of scrapie-infected animals. J. Virol. 71, 9685 (1997)
    • (1997) J. Virol. , vol.71 , pp. 9685
    • Demaimay, R.1    Adjou, K.2    Beringue, V.3
  • 15
    • 0028015941 scopus 로고
    • Pharmacological studies of a new derivative of amphotericin B, MS-8209, in mouse and hamster scrapie
    • Demaimay, R., Adjou, K., Lasmezas, C. et al., Pharmacological studies of a new derivative of amphotericin B, MS-8209, in mouse and hamster scrapie. J. Gen. Virol. 75, 2499 (1994)
    • (1994) J. Gen. Virol. , vol.75 , pp. 2499
    • Demaimay, R.1    Adjou, K.2    Lasmezas, C.3
  • 16
    • 28444498432 scopus 로고    scopus 로고
    • Inhibition of formation of protease-resistant prion protein by Trypan blue, Sirius Red and other Congo Red analogues
    • Demaimay, R., Chesebro, B., Caughey, B., Inhibition of formation of protease-resistant prion protein by Trypan blue, Sirius Red and other Congo Red analogues. Arch. Virol. Suppl. 16, 277 (2000)
    • (2000) Arch. Virol. Suppl. , vol.16 , pp. 277
    • Demaimay, R.1    Chesebro, B.2    Caughey, B.3
  • 17
    • 0031797266 scopus 로고    scopus 로고
    • Structural aspects of Congo Red as an inhibitor of protease-resistant prion protein formation
    • Demaimay, R., Harper, J., Gordon, H. et al., Structural aspects of Congo Red as an inhibitor of protease-resistant prion protein formation. J. Neurochem. 71, 2534 (1998)
    • (1998) J. Neurochem. , vol.71 , pp. 2534
    • Demaimay, R.1    Harper, J.2    Gordon, H.3
  • 18
    • 0025971881 scopus 로고
    • Chemoprophylaxis of scrapie in mice
    • Diringer, H., Ehlers, B. J., Chemoprophylaxis of scrapie in mice J. Gen. Virol. 72, 457 (1991)
    • (1991) J. Gen. Virol. , vol.72 , pp. 457
    • Diringer, H.1    Ehlers, B.J.2
  • 19
    • 0021282464 scopus 로고
    • Dextran sulfate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen
    • Ehlers, B., Diringer, H., Dextran sulfate 500 delays and prevents mouse scrapie by impairment of agent replication in spleen. J. Gen. Virol. 65, 1325 (1984)
    • (1984) J. Gen. Virol. , vol.65 , pp. 1325
    • Ehlers, B.1    Diringer, H.2
  • 20
    • 0033537348 scopus 로고    scopus 로고
    • Prophylactic potential of pentosan polysulphate in transmissible spongiform encephalopathies
    • Farquhar, C., Dickinson, A., Bruce, M., Prophylactic potential of pentosan polysulphate in transmissible spongiform encephalopathies. Lancet 353, 117 (1999)
    • (1999) Lancet , vol.353 , pp. 117
    • Farquhar, C.1    Dickinson, A.2    Bruce, M.3
  • 21
    • 2442694517 scopus 로고    scopus 로고
    • Analysis of time risk (survival) data
    • J.P.T.M. Noordhuizen, K. Frankena, C. M. van der Hoof et al. (eds.), Wageningen, Wageningen Pers, The Netherlands
    • Frankena, K., Graat, E. A. M., Analysis of time risk (survival) data, J.P.T.M. Noordhuizen, K. Frankena, C. M. van der Hoof et al. (eds.), Application of quantitative methods in veterinary epidemiology, p. 181, Wageningen, Wageningen Pers, The Netherlands (1997)
    • (1997) Application of Quantitative Methods in Veterinary Epidemiology , vol.181
    • Frankena, K.1    Graat, E.A.M.2
  • 22
    • 0034116880 scopus 로고    scopus 로고
    • Peripheral pathogenesis of prion diseases
    • Glatzel, M., Aguzzi, A., Peripheral pathogenesis of prion diseases. Microbes Infect. 2, 613 (2000)
    • (2000) Microbes Infect. , vol.2 , pp. 613
    • Glatzel, M.1    Aguzzi, A.2
  • 23
    • 0018868515 scopus 로고
    • Amyloid deposits and amyloidosis. The beta-fibrilloses
    • Glenner, G., Amyloid deposits and amyloidosis. The beta-fibrilloses. N. Engl. J. Med. 302, 1333 (1980)
    • (1980) N. Engl. J. Med. , vol.302 , pp. 1333
    • Glenner, G.1
  • 24
    • 70449647008 scopus 로고
    • Proportional hazard test and diagnostic based on weighted residual
    • Grambsh, P. M., Therneau, T. M., Proportional hazard test and diagnostic based on weighted residual. Biometrika 81, 515 (1994)
    • (1994) Biometrika , vol.81 , pp. 515
    • Grambsh, P.M.1    Therneau, T.M.2
  • 25
    • 77957178266 scopus 로고
    • The effects of prenatal administration of azo dyes on testicular development in the mouse: Structure activity profile of dyes derived from benzidine, dimethylbenzidine or dimethoxybenzidine
    • Gray, L. E., Ostby, J. S., The effects of prenatal administration of azo dyes on testicular development in the mouse: structure activity profile of dyes derived from benzidine, dimethylbenzidine or dimethoxybenzidine. Fund. Appl. Toxicol. 20, 177 (1993)
    • (1993) Fund. Appl. Toxicol. , vol.20 , pp. 177
    • Gray, L.E.1    Ostby, J.S.2
  • 26
    • 0032802332 scopus 로고    scopus 로고
    • Cellular biology of prion diseases
    • Harris, D. A., Cellular biology of prion diseases. Clinical Microbiol. Rev. 12, 429 (1999)
    • (1999) Clinical Microbiol. Rev. , vol.12 , pp. 429
    • Harris, D.A.1
  • 27
    • 0030820354 scopus 로고    scopus 로고
    • The same prion strain cause vCJD and BSE
    • Hill, A. F., Desbrulais, M., Joiner, S. et al., The same prion strain cause vCJD and BSE. Nature 389, 448 (1997)
    • (1997) Nature , vol.389 , pp. 448
    • Hill, A.F.1    Desbrulais, M.2    Joiner, S.3
  • 28
    • 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. J. Virol. 69, 506 (1995)
    • (1995) J. Virol. , vol.69 , pp. 506
    • Ingrosso, L.1    Ladogana, A.2    Pocchiari, M.3
  • 29
    • 0030931519 scopus 로고    scopus 로고
    • Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation
    • Kaneko, K., Zulianello, L., Scott, M. et al., Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl. Acad. Sci. USA 94, 10069 (1997)
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10069
    • Kaneko, K.1    Zulianello, L.2    Scott, M.3
  • 30
    • 0021046367 scopus 로고
    • The antiviral compound HPA-23 can prevent scrapie when administered at the time of infection
    • Kimberlin, R. H., Walker, C. A., The antiviral compound HPA-23 can prevent scrapie when administered at the time of infection. Arch. Virol. 78, 9 (1983)
    • (1983) Arch. Virol. , vol.78 , pp. 9
    • Kimberlin, R.H.1    Walker, C.A.2
  • 31
    • 0017336439 scopus 로고
    • Characteristics of a short incubation model of scrapie in the golden hamster
    • Kimberlin, R. H., Walker, C. A., Characteristics of a short incubation model of scrapie in the golden hamster. J. Gen. Viro. 34, 295 (1977)
    • (1977) J. Gen. Viro. , vol.34 , pp. 295
    • Kimberlin, R.H.1    Walker, C.A.2
  • 32
    • 0022629053 scopus 로고
    • Pathogenesis of scrapie (strain 263K) in hamsters infected intracerebrally, intraperitoneally or intraocularly
    • Kimberlin, R. H., Walker, C. A., Pathogenesis of scrapie (strain 263K) in hamsters infected intracerebrally, intraperitoneally or intraocularly. J. Gen. Virol. 67, 255 (1986)
    • (1986) J. Gen. Virol. , vol.67 , pp. 255
    • Kimberlin, R.H.1    Walker, C.A.2
  • 33
    • 0022450560 scopus 로고
    • Suppression of scrapie infection in mice by heteropolyanion 23, dextran sulfate, and some other polyanions
    • Kimberlin, R. H., Walker, C. A., Suppression of scrapie infection in mice by heteropolyanion 23, dextran sulfate, and some other polyanions. Antimicrob. Agents Chemother. 30, 409 (1986)
    • (1986) Antimicrob. Agents Chemother. , vol.30 , pp. 409
    • Kimberlin, R.H.1    Walker, C.A.2
  • 34
    • 0031444295 scopus 로고    scopus 로고
    • A crucial role for B cells in neuroinvasive scrapie
    • Klein, M. A., Frigg, R., Raeber, A. J. et al., A crucial role for B cells in neuroinvasive scrapie. Nature 390, 687 (1997)
    • (1997) Nature , vol.390 , pp. 687
    • Klein, M.A.1    Frigg, R.2    Raeber, A.J.3
  • 35
    • 0030030927 scopus 로고    scopus 로고
    • Immune system-dependent and independent replication of the scrapie agent
    • Lazmesas, C. I., Cesbron, J. Y., Deslys, J. O. et al., Immune system-dependent and independent replication of the scrapie agent. J. Virol. 70, 1292 (1996)
    • (1996) J. Virol. , vol.70 , pp. 1292
    • Lazmesas, C.I.1    Cesbron, J.Y.2    Deslys, J.O.3
  • 36
    • 0034097242 scopus 로고    scopus 로고
    • Amphotericin B inhibits the generation of the scrapie isoform of the prion protein in infected cultures
    • Mangè, A., Nishida, N., Milhavet, O. et al., Amphotericin B inhibits the generation of the scrapie isoform of the prion protein in infected cultures. J. Virol. 74, 3135 (2000)
    • (2000) J. Virol. , vol.74 , pp. 3135
    • Mangè, A.1    Nishida, N.2    Milhavet, O.3
  • 37
    • 0027074778 scopus 로고
    • PrP protein is associated with FDC cells of spleens and lymphonodes in uninfected and scrapie-infected mice
    • McBride, P. A., Eikelenboom, P., Kraal, G. et al., PrP protein is associated with FDC cells of spleens and lymphonodes in uninfected and scrapie-infected mice. J. Pathol. 168, 413 (1992)
    • (1992) J. Pathol. , vol.168 , pp. 413
    • McBride, P.A.1    Eikelenboom, P.2    Kraal, G.3
  • 38
    • 0036124813 scopus 로고    scopus 로고
    • Oxidative stress and the prion protein in transmissible spongiform encephalopathies
    • Milhavet, O., Lehmann, S., Oxidative stress and the prion protein in transmissible spongiform encephalopathies. Brain Res. Rev. 38, 328 (2002)
    • (2002) Brain Res. Rev. , vol.38 , pp. 328
    • Milhavet, O.1    Lehmann, S.2
  • 39
    • 0033961817 scopus 로고    scopus 로고
    • Effect of Congo Red on wild-type and mutated Prion Proteins in cultured cells
    • Milhavet, O., Mangé, A., Casanova, D. et al., Effect of Congo Red on wild-type and mutated Prion Proteins in cultured cells, J. Neurochem. 74, 222 (2000)
    • (2000) J. Neurochem. , vol.74 , pp. 222
    • Milhavet, O.1    Mangé, A.2    Casanova, D.3
  • 40
    • 0033988236 scopus 로고    scopus 로고
    • Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cells lines overexpressing wild-type mouse protein
    • Nishida, N., Harris, D. A., Vilette, D. et al., Successful transmission of three mouse-adapted scrapie strains to murine neuroblastoma cells lines overexpressing wild-type mouse protein. J. Virol. 74, 320 (2000)
    • (2000) J. Virol. , vol.74 , pp. 320
    • Nishida, N.1    Harris, D.A.2    Vilette, D.3
  • 41
    • 0035813151 scopus 로고    scopus 로고
    • Novel differences between two human prion strains revealed by two dimensional gel electrophoresis
    • Pan, T., Colucci, M., Wong, B. S. et al., Novel differences between two human prion strains revealed by two dimensional gel electrophoresis. J. Biol. Chem. 276, 37284 (2001)
    • (2001) J. Biol. Chem. , vol.276 , pp. 37284
    • Pan, T.1    Colucci, M.2    Wong, B.S.3
  • 42
    • 0034705043 scopus 로고    scopus 로고
    • Mimicking dominant negative inhibition of prion replication through structure-based drug design
    • Perrier, V., Wallace, A. C., Kaneko, K. et al., Mimicking dominant negative inhibition of prion replication through structure-based drug design. Proc. Natl. Acad. Sci. USA 97, 6073 (2000)
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6073
    • Perrier, V.1    Wallace, A.C.2    Kaneko, K.3
  • 43
    • 0025219885 scopus 로고
    • Immunohistochemical localization of prion protein in spongiform encephalopathies and normal brain tissues
    • Piccardo, P., Safar, J., Ceroni, M. et al., Immunohistochemical localization of prion protein in spongiform encephalopathies and normal brain tissues. Neurology 40, 518 (1990)
    • (1990) Neurology , vol.40 , pp. 518
    • Piccardo, P.1    Safar, J.2    Ceroni, M.3
  • 44
    • 0037170759 scopus 로고    scopus 로고
    • Determination of sodium 3,4-diaminonaphthalene-1-sulfonate, a Congo Red derivative, in plasma and brain of hamsters by high-performance liquid chromatography after solid-phase extraction and ultraviolet absorbance
    • Pirola, R., Gervasoni, M., Pollera, C. et al., Determination of sodium 3,4-diaminonaphthalene-1-sulfonate, a Congo Red derivative, in plasma and brain of hamsters by high-performance liquid chromatography after solid-phase extraction and ultraviolet absorbance. J. Chromatog. B 769, 27 (2002)
    • (2002) J. Chromatog. B , vol.769 , pp. 27
    • Pirola, R.1    Gervasoni, M.2    Pollera, C.3
  • 45
    • 0023243085 scopus 로고
    • Amphotericin B delays the incubation period of scrapie in intracerebrally inoculated hamsters
    • Pocchiari, M., Schmittinger, S., Masullo, C., Amphotericin B delays the incubation period of scrapie in intracerebrally inoculated hamsters. J. Gen. Virol. 68, 219 (1987)
    • (1987) J. Gen. Virol. , vol.68 , pp. 219
    • Pocchiari, M.1    Schmittinger, S.2    Masullo, C.3
  • 46
    • 9144223018 scopus 로고    scopus 로고
    • In vitro evaluation of the anti-prionic activity of newly synthesized Congo Red derivatives
    • Poli, G., Ponti, W., Carcassola, G. et al., In vitro evaluation of the anti-prionic activity of newly synthesized Congo Red derivatives. Arzneim.-Forsch./Drug Res. 53, 875 (2003)
    • (2003) Arzneim.-Forsch./Drug Res. , vol.53 , pp. 875
    • Poli, G.1    Ponti, W.2    Carcassola, G.3
  • 48
    • 0020080097 scopus 로고
    • Measurement of the scrapie agent using an incubation time assay
    • Prusiner, S. B., Cochran, S. P., Groth, D. F. et al., Measurement of the scrapie agent using an incubation time assay. Ann. Neurol. 11, 353 (1982)
    • (1982) Ann. Neurol. , vol.11 , pp. 353
    • Prusiner, S.B.1    Cochran, S.P.2    Groth, D.F.3
  • 49
    • 0033987842 scopus 로고    scopus 로고
    • Entry versus blockade of brain infection following oral or intraperitoneal scrapie administration: Role of prion protein expression in peripheral nerves and spleen
    • Race, R., Oldstone, M., Chesebro, B., Entry versus blockade of brain infection following oral or intraperitoneal scrapie administration: role of prion protein expression in peripheral nerves and spleen. J. Virol. 74, 828 (2000)
    • (2000) J. Virol. , vol.74 , pp. 828
    • Race, R.1    Oldstone, M.2    Chesebro, B.3
  • 50
    • 0034171052 scopus 로고    scopus 로고
    • Beta-sheet breaker peptides reverse conformation of pathogenic prion proteins
    • Reilly, C. E., Beta-sheet breaker peptides reverse conformation of pathogenic prion proteins. J. Neurol. 247, 319 (2000)
    • (2000) J. Neurol. , vol.247 , pp. 319
    • Reilly, C.E.1
  • 51
    • 0034109546 scopus 로고    scopus 로고
    • Screening Congo Red and its analogues for their ability to prevent the formation of PrPres in scrapie-infected cells
    • Rudyk, H., Vasiljevic, S., Hennion, R.M. et al., Screening Congo Red and its analogues for their ability to prevent the formation of PrPres in scrapie-infected cells. J. Gen. Virol. 81, 1155 (2000)
    • (2000) J. Gen. Virol. , vol.81 , pp. 1155
    • Rudyk, H.1    Vasiljevic, S.2    Hennion, R.M.3
  • 52
    • 0035943651 scopus 로고    scopus 로고
    • A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases
    • Shaked, G. R., Shaked, Y., Kariv-Inbal, Z. et al., A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases. J. Biol. Chem. 276, 31479 (2001)
    • (2001) J. Biol. Chem. , vol.276 , pp. 31479
    • Shaked, G.R.1    Shaked, Y.2    Kariv-Inbal, Z.3
  • 54
    • 0033460187 scopus 로고    scopus 로고
    • Elimination of prions by branched polyamines and implications for therapeutics
    • Supattapone, S., Nguyen, H. O., Cohen, F. E. et al., Elimination of prions by branched polyamines and implications for therapeutics. Proc. Natl. Acad. Sci. USA 96, 14529 (1999)
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14529
    • Supattapone, S.1    Nguyen, H.O.2    Cohen, F.E.3
  • 55
    • 0034725536 scopus 로고    scopus 로고
    • Tetracycline affects abnormal properties of synthetic PrP peptides and PrP(Sc) in vitro
    • Tagliavini, F., Forloni, G., Colombo, L. et al., Tetracycline affects abnormal properties of synthetic PrP peptides and PrP(Sc) in vitro. J. Mol. Biol. 300, 1309 (2000)
    • (2000) J. Mol. Biol. , vol.300 , pp. 1309
    • Tagliavini, F.1    Forloni, G.2    Colombo, L.3
  • 56
    • 17344382240 scopus 로고    scopus 로고
    • Effectiveness of anthracycline against experimental prion disease in Syrian hamster
    • Tagliavini, F., McArthur, R. A., Canciani, B. et al., Effectiveness of anthracycline against experimental prion disease in Syrian hamster. Science 276, 1119 (1997)
    • (1997) Science , vol.276 , pp. 1119
    • Tagliavini, F.1    McArthur, R.A.2    Canciani, B.3
  • 57
    • 0023639585 scopus 로고
    • The correlation between DNA adducts and chromosomal aberrations in the target organ of benzidine exposed, partially-hepatectomized mice
    • Talaska, G., Au, W. W., Ward, J. B. Jr et al., The correlation between DNA adducts and chromosomal aberrations in the target organ of benzidine exposed, partially-hepatectomized mice. Carcinogenesis 8, 1899 (1987)
    • (1987) Carcinogenesis , vol.8 , pp. 1899
    • Talaska, G.1    Au, W.W.2    Ward Jr., J.B.3
  • 58
    • 0141788017 scopus 로고    scopus 로고
    • Congo red analogues as potential anti-prion agents
    • Villa, S., Cignarella, G., Barlocco, D. et al., Congo red analogues as potential anti-prion agents. Il Farmaco 58, 929 (2003)
    • (2003) Il Farmaco , vol.58 , pp. 929
    • Villa, S.1    Cignarella, G.2    Barlocco, D.3
  • 59
    • 0342951746 scopus 로고    scopus 로고
    • A new variant of Creutzfeldt-Jakob disease in the UK
    • Will, R. G., Ironside, J. W., Zeidler, M. et al., A new variant of Creutzfeldt-Jakob disease in the UK. Lancet 347, 921 (1996)
    • (1996) Lancet , vol.347 , pp. 921
    • Will, R.G.1    Ironside, J.W.2    Zeidler, M.3
  • 60
    • 0032949549 scopus 로고    scopus 로고
    • Construction and characterization of murine neuroblastoma cell clones allowing inducible and high expression of the prion protein
    • Windl, O., Lorenz, H., Behrens, C. et al., Construction and characterization of murine neuroblastoma cell clones allowing inducible and high expression of the prion protein. J. Gen. Virol. 80, 15 (1999)
    • (1999) J. Gen. Virol. , vol.80 , pp. 15
    • Windl, O.1    Lorenz, H.2    Behrens, C.3
  • 61
    • 0034726713 scopus 로고    scopus 로고
    • Prion disease: A loss of antioxidant function?
    • Wong, B. S., Pan, T., Liu, T. et al., Prion disease: a loss of antioxidant function? Biochem. Biophys. Res. Com. 275, 249 (2000)
    • (2000) Biochem. Biophys. Res. Com. , vol.275 , pp. 249
    • Wong, B.S.1    Pan, T.2    Liu, T.3
  • 62
    • 0032476775 scopus 로고    scopus 로고
    • Astrocytosis and amyloid deposition in scrapie infected hamsters
    • Ye, X., Scallet, A. C., Kascsak, R. J. et al., Astrocytosis and amyloid deposition in scrapie infected hamsters. Brain Res. 809, 277 (1998)
    • (1998) Brain Res. , vol.809 , pp. 277
    • Ye, X.1    Scallet, A.C.2    Kascsak, R.J.3
  • 63
    • 0033999341 scopus 로고    scopus 로고
    • Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein
    • Zulianello, L., Kaneko, K., Scott, M. et al., Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein. J. Virol. 74, 4351 (2000)
    • (2000) J. Virol. , vol.74 , pp. 4351
    • Zulianello, L.1    Kaneko, K.2    Scott, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.