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Volumn 83, Issue 6, 2005, Pages 1455-1476

Prion biology relevant to bovine spongiform encephalopathy

Author keywords

Bovine Spongiform Encephalopathy; Chronic Wasting Disease; Prion

Indexed keywords

ANIMALIA; BOVIDAE; BOVINAE; CERVIDAE; MAMMALIA;

EID: 33646017123     PISSN: 00218812     EISSN: None     Source Type: Journal    
DOI: 10.2527/2005.8361455x     Document Type: Review
Times cited : (43)

References (217)
  • 1
    • 10044264196 scopus 로고    scopus 로고
    • Assoc. Am. Feed Control Officials, Oxford, IN
    • AAFFCO. 2004. Official Publication. Assoc. Am. Feed Control Officials, Oxford, IN.
    • (2004) Official Publication
  • 2
    • 0344021409 scopus 로고    scopus 로고
    • Prions and the immune system: A journey through gut, spleen, and nerves
    • Aguzzi, A. 2003. Prions and the immune system: A journey through gut, spleen, and nerves. Adv. Immunol. 81:123-171.
    • (2003) Adv. Immunol. , vol.81 , pp. 123-171
    • Aguzzi, A.1
  • 3
    • 2642531891 scopus 로고    scopus 로고
    • Recent advances in prion biology
    • Aguzzi, A., and G. Miele. 2004. Recent advances in prion biology. Curr. Opin. Neurol. 17:337-342.
    • (2004) Curr. Opin. Neurol. , vol.17 , pp. 337-342
    • Aguzzi, A.1    Miele, G.2
  • 7
    • 0035140891 scopus 로고    scopus 로고
    • Heat stability of prion rods and recombinant prion protein in water, lipid and lipid-water mixtures
    • Appel, T., M. Wolff, F. von Rheinbaben, M. Heinzel, and D. Riesner. 2001. Heat stability of prion rods and recombinant prion protein in water, lipid and lipid-water mixtures. J. Gen. Virol. (Pt 2) 82:465-473.
    • (2001) J. Gen. Virol. , vol.82 , Issue.PART 2 , pp. 465-473
    • Appel, T.1    Wolff, M.2    Von Rheinbaben, F.3    Heinzel, M.4    Riesner, D.5
  • 9
    • 17144452771 scopus 로고    scopus 로고
    • Chronic wasting disease in a Rocky Mountain elk
    • Ball, K. 2002. Chronic wasting disease in a Rocky Mountain elk. Can. Vet. J. 43:880-882.
    • (2002) Can. Vet. J. , vol.43 , pp. 880-882
    • Ball, K.1
  • 10
    • 0034749390 scopus 로고    scopus 로고
    • Molecular analysis of the abnormal prion protein during co-infection of mice with a bovine encephalopathy and a scrapie agent
    • Baron, T. G., and A. G. Biacabe. 2001. Molecular analysis of the abnormal prion protein during co-infection of mice with a bovine encephalopathy and a scrapie agent. J. Virol. 75:107-114.
    • (2001) J. Virol. , vol.75 , pp. 107-114
    • Baron, T.G.1    Biacabe, A.G.2
  • 12
    • 0036091743 scopus 로고    scopus 로고
    • Retrograde transport of transmissible mink encephalopathy within descending motor tracts
    • Bartz, J. C., A. E. Kincaid, and R. A. Bessen. 2002. Retrograde transport of transmissible mink encephalopathy within descending motor tracts. J. Virol. 76:5759-5768.
    • (2002) J. Virol. , vol.76 , pp. 5759-5768
    • Bartz, J.C.1    Kincaid, A.E.2    Bessen, R.A.3
  • 13
    • 0037213933 scopus 로고    scopus 로고
    • Rapid prion neuroinvasion following tongue infection
    • Bartz, J. C., A. E. Kincaid, and R. A. Bessen. 2003. Rapid prion neuroinvasion following tongue infection. J. Virol. 77:583-591.
    • (2003) J. Virol. , vol.77 , pp. 583-591
    • Bartz, J.C.1    Kincaid, A.E.2    Bessen, R.A.3
  • 14
    • 0032567088 scopus 로고    scopus 로고
    • The host range of chronic wasting disease is altered on passage in ferrets
    • Bartz, J. C., R. F. March, D. I. McKenzie, and J. M. Aiken. 1998. The host range of chronic wasting disease is altered on passage in ferrets. J. Virol. 251:297-301.
    • (1998) J. Virol. , vol.251 , pp. 297-301
    • Bartz, J.C.1    March, R.F.2    McKenzie, D.I.3    Aiken, J.M.4
  • 15
  • 17
    • 0028997297 scopus 로고
    • Non-genetic propagation of strain-specific properties of scrapie prion protein
    • Bessen, R. A., D. A. Kocisko, G. J. Raymond, S. Nandan, P. T. Lansbury, and B. Caughey. 1995. Non-genetic propagation of strain-specific properties of scrapie prion protein. Nature 375:698-700.
    • (1995) Nature , vol.375 , pp. 698-700
    • Bessen, R.A.1    Kocisko, D.A.2    Raymond, G.J.3    Nandan, S.4    Lansbury, P.T.5    Caughey, B.6
  • 18
    • 1242321022 scopus 로고    scopus 로고
    • Distinct molecular phenotypes in bovine prion diseases
    • Biacabe, A. G., J. L. Laplanche, S. Ryder, and T. G. Baron. 2004. Distinct molecular phenotypes in bovine prion diseases. EMBO Rep. 5(1):110-115.
    • (2004) EMBO Rep. , vol.5 , Issue.1 , pp. 110-115
    • Biacabe, A.G.1    Laplanche, J.L.2    Ryder, S.3    Baron, T.G.4
  • 21
    • 0032612107 scopus 로고    scopus 로고
    • BSE transmission studies with particular reference to blood
    • Bradley, R. 1999. BSE transmission studies with particular reference to blood. Dev. Biol. Stand. 99:35-40.
    • (1999) Dev. Biol. Stand. , vol.99 , pp. 35-40
    • Bradley, R.1
  • 22
    • 0026031118 scopus 로고
    • Survival of scrapie virus after 3 years' interment
    • Brown, P., and D. C. Gajdusek. 1991. Survival of scrapie virus after 3 years' interment. Lancet 337:269-270.
    • (1991) Lancet , vol.337 , pp. 269-270
    • Brown, P.1    Gajdusek, D.C.2
  • 23
    • 0020032352 scopus 로고
    • Effect of chemicals, heat, and histopathologic processing on high-infectivity hamster-adapted scrapie virus
    • Brown, P., R. G. Rohwer, E. M. Green, and D. C. Gajdusek. 1982. Effect of chemicals, heat, and histopathologic processing on high-infectivity hamster-adapted scrapie virus. J. Infect. Dis. 145:683-687.
    • (1982) J. Infect. Dis. , vol.145 , pp. 683-687
    • Brown, P.1    Rohwer, R.G.2    Green, E.M.3    Gajdusek, D.C.4
  • 26
    • 3543092761 scopus 로고    scopus 로고
    • The distribution of infectivity in blood components and plasma derivatives in experimental models of transmissible spongiform encephalopathy
    • Brown, P., R. G. Rohwer, B. C. Dunstan, C. MacAuley, D. C. Gajdusek, and W. N. Drohan. 1998. The distribution of infectivity in blood components and plasma derivatives in experimental models of transmissible spongiform encephalopathy. Transfusion 38:810-816.
    • (1998) Transfusion , vol.38 , pp. 810-816
    • Brown, P.1    Rohwer, R.G.2    Dunstan, B.C.3    MacAuley, C.4    Gajdusek, D.C.5    Drohan, W.N.6
  • 28
    • 0035138695 scopus 로고    scopus 로고
    • Blood infectivity and the prospects for a diagnostic screening test in Creutzfeldt-Jakob disease
    • Brown P., L. Cervenakova, and H. Diringer. 2001. Blood infectivity and the prospects for a diagnostic screening test in Creutzfeldt-Jakob disease. J. Lab. Clin. Med. 137:5-13.
    • (2001) J. Lab. Clin. Med. , vol.137 , pp. 5-13
    • Brown, P.1    Cervenakova, L.2    Diringer, H.3
  • 29
    • 0141515178 scopus 로고    scopus 로고
    • TSE strain variation
    • Bruce, M. E. 2003. TSE strain variation. Br. Med. Bull. 66:99-108.
    • (2003) Br. Med. Bull. , vol.66 , pp. 99-108
    • Bruce, M.E.1
  • 32
    • 1542357669 scopus 로고    scopus 로고
    • Identification of a second bovine amyloidotic spongiform encephalopathy: Molecular similarities with sporadic Creutzfeldt-Jakob disease
    • Casalone, C., G. Zanusso, P. Acutis, S. Ferrari, L. Capucci, F. Tagliavini, S. Monaco, and M. Caramelli. 2004. Identification of a second bovine amyloidotic spongiform encephalopathy: Molecular similarities with sporadic Creutzfeldt-Jakob disease. Proc. Natl. Acad. Sci. USA 101:3065-3070.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3065-3070
    • Casalone, C.1    Zanusso, G.2    Acutis, P.3    Ferrari, S.4    Capucci, L.5    Tagliavini, F.6    Monaco, S.7    Caramelli, M.8
  • 34
    • 0028256222 scopus 로고
    • Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red
    • Caughey, B., K. Brown, G. J. Raymond, G. E. Katzenstein, and W. Thresher. 1994. Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red. J. Virol. 68:2135-2141.
    • (1994) J. Virol. , vol.68 , pp. 2135-2141
    • Caughey, B.1    Brown, K.2    Raymond, G.J.3    Katzenstein, G.E.4    Thresher, W.5
  • 35
    • 0026638150 scopus 로고
    • Potent inhibition of scrapie-associated PrP accumulation by congo red
    • Caughey, B., and R. E. Race. 1992. Potent inhibition of scrapie-associated PrP accumulation by congo red. J. Neurochem. 59:768-771.
    • (1992) J. Neurochem. , vol.59 , pp. 768-771
    • Caughey, B.1    Race, R.E.2
  • 36
    • 0032514682 scopus 로고    scopus 로고
    • Inhibition of protease-resistant prion protein formation by porphyrins and phthalocyanines
    • Caughey, W. S., L. D. Raymond, M. Horiuchi, and B. Caughey. 1998. Inhibition of protease-resistant prion protein formation by porphyrins and phthalocyanines. Proc. Natl. Acad. Sci. USA 95:12117-12122.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12117-12122
    • Caughey, W.S.1    Raymond, L.D.2    Horiuchi, M.3    Caughey, B.4
  • 37
    • 0345165981 scopus 로고    scopus 로고
    • Similar levels of infectivity in the blood of mice infected with human-derived vCJD and GSS strains of transmissible spongiform encephalopathy
    • Cervenakova., L., O. Yakovleva, C. McKenzie, S. Kolchinsky, L. McShane, W. N. Drohan, and P. Brown. 2003. Similar levels of infectivity in the blood of mice infected with human-derived vCJD and GSS strains of transmissible spongiform encephalopathy. Transfusion 43:1687-1694.
    • (2003) Transfusion , vol.43 , pp. 1687-1694
    • Cervenakova, L.1    Yakovleva, O.2    McKenzie, C.3    Kolchinsky, S.4    McShane, L.5    Drohan, W.N.6    Brown, P.7
  • 38
    • 84858871536 scopus 로고    scopus 로고
    • 5.1.7. Canadian Food Inspection Agency
    • CFIA. 2004. Approved feed ingredients Schedule IV, Part 1, 5.1.7. Canadian Food Inspection Agency. Available: http://www. inspection.gc.ca/ english/anima/feebet/feebete.shtml. Accessed Nov. 4, 2004.
    • (2004) Approved Feed Ingredients Schedule IV, Part 1
  • 39
    • 0000048085 scopus 로고
    • Experimental scrapie in the mouse
    • Chandler, R. L. 1963. Experimental scrapie in the mouse. Res. Vet. Sci. 4:269-275.
    • (1963) Res. Vet. Sci. , vol.4 , pp. 269-275
    • Chandler, R.L.1
  • 40
    • 0021065669 scopus 로고
    • Scrapie in France: Some possible predisposing factors in the naturally-acquired disease of sheep
    • Chatelain, J., N. Delasnerie-Laupretre, F. Cathala, and P. Brown. 1983. Scrapie in France: Some possible predisposing factors in the naturally-acquired disease of sheep. Vet. Microbiol. 8:511-515.
    • (1983) Vet. Microbiol. , vol.8 , pp. 511-515
    • Chatelain, J.1    Delasnerie-Laupretre, N.2    Cathala, F.3    Brown, P.4
  • 41
    • 0035168351 scopus 로고    scopus 로고
    • Prion diseases: What is the neurotoxic molecule?
    • Chiesa, R., and D. A. Harris. 2001. Prion diseases: What is the neurotoxic molecule? Neurobiol. Dis. 8:743-763.
    • (2001) Neurobiol. Dis. , vol.8 , pp. 743-763
    • Chiesa, R.1    Harris, D.A.2
  • 42
    • 1142275103 scopus 로고    scopus 로고
    • The similarity of the physical sign frequencies of bovine spongiform encephalopathy and selected differential diagnoses
    • Cockcroft, P. D. 2004. The similarity of the physical sign frequencies of bovine spongiform encephalopathy and selected differential diagnoses. Vet. J. 167:175-180.
    • (2004) Vet. J. , vol.167 , pp. 175-180
    • Cockcroft, P.D.1
  • 43
    • 33646025403 scopus 로고    scopus 로고
    • Title 21, Parts 589, U.S. Government Printing Office, Washington, DC
    • Code of Federal Regulations. 2000. Substances Prohibited from Use in Animal Food or Feed. Title 21, Vol. 6, Parts 589, 523-526. U.S. Government Printing Office, Washington, DC.
    • (2000) Substances Prohibited from Use in Animal Food or Feed , vol.6 , pp. 523-526
  • 44
    • 0040178162 scopus 로고    scopus 로고
    • Current Official Standards. Codex Standard 211, Part 2.4.1. FAO, WHO, United Nations, Geneva, Switzerland
    • Codex Alimentarius. 1998. Food Labelling Complete Texts. Current Official Standards. Codex Standard 211, Part 2.4.1. FAO, WHO, United Nations, Geneva, Switzerland.
    • (1998) Food Labelling Complete Texts
  • 46
    • 0025859996 scopus 로고
    • Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease
    • Collinge, J., M. S. Palmer, and A. J. Dryden. 1991. Genetic predisposition to iatrogenic Creutzfeldt-Jakob disease. Lancet 337:1441-1442.
    • (1991) Lancet , vol.337 , pp. 1441-1442
    • Collinge, J.1    Palmer, M.S.2    Dryden, A.J.3
  • 48
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
    • Collinge, J., K. C. Sidle, J. Meads, J. Ironside, A. F. Hill. 1996. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383:685-690.
    • (1996) Nature , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 50
    • 0036877388 scopus 로고    scopus 로고
    • Quantitative exposure assessment for the combustion of meat and bone meal derived from specified risk material in the context of BSE in Ireland
    • Cummins, E. J., P. M. Grace, D. J. Fry, K. P. McDonnell, S. F. Colgan, and S. M. Ward. 2002. Quantitative exposure assessment for the combustion of meat and bone meal derived from specified risk material in the context of BSE in Ireland. J. Agric. Saf. Health 8:365-383.
    • (2002) J. Agric. Saf. Health , vol.8 , pp. 365-383
    • Cummins, E.J.1    Grace, P.M.2    Fry, D.J.3    McDonnell, K.P.4    Colgan, S.F.5    Ward, S.M.6
  • 51
    • 0036158152 scopus 로고    scopus 로고
    • Use of a marker organism to model the spread of central nervous system tissue in cattle and the abattoir environment during commercial stunning and carcass dressing
    • Daly, D. J., D. M. Prendergast, J. J. Sheridan, I. S. Blair, and D. A. McDowell. 2002. Use of a marker organism to model the spread of central nervous system tissue in cattle and the abattoir environment during commercial stunning and carcass dressing. Appl. Environ. Microbiol. 68:791-798.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 791-798
    • Daly, D.J.1    Prendergast, D.M.2    Sheridan, J.J.3    Blair, I.S.4    McDowell, D.A.5
  • 53
    • 0003866499 scopus 로고    scopus 로고
    • Her Majesty's Stationary Office, London
    • DEFRA. 2000. The BSE inquiry: The Report. House of Commons papers 1999-2000. Her Majesty's Stationary Office, London. Available: http://www.bseinquiry.gov.uk/report/index.html. Accessed Nov. 4, 2004.
    • (2000) The BSE Inquiry: The Report. House of Commons Papers 1999-2000
  • 54
    • 84858869704 scopus 로고    scopus 로고
    • U.K. Dept. Environ. Food and Rural Affairs
    • DEFRA. 2004a. Animal Health and Welfare, Bovine Spongiform Encephalopathy of BSE. U.K. Dept. Environ. Food and Rural Affairs. Available: http://www.defra.gov.uk/animalh/bse/index. html. Accessed Nov. 4, 2004.
    • (2004) Animal Health and Welfare, Bovine Spongiform Encephalopathy of BSE
  • 57
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation
    • Doh-ura, K., T. Iwaki, and B. Caughey. 2000. Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation. J. Virol. 74:4894-4897.
    • (2000) J. Virol. , vol.74 , pp. 4894-4897
    • Doh-ura, K.1    Iwaki, T.2    Caughey, B.3
  • 60
    • 0027405681 scopus 로고
    • Comparative analysis of scrapie agent inactivation methods
    • Ernst, D. R., and R. E. Race. 1993. Comparative analysis of scrapie agent inactivation methods. J. Virol. Methods 41:193-201.
    • (1993) J. Virol. Methods , vol.41 , pp. 193-201
    • Ernst, D.R.1    Race, R.E.2
  • 61
    • 0037798369 scopus 로고    scopus 로고
    • EC Scientific Steering Committee
    • European Commission. 2002a. Opinion on TSE infectivity distribution in ruminant tissues. EC Scientific Steering Committee. Available: http://www.europa.eu.int/comm/food/fs/sc/ssc/outcome_en.html. Accessed Nov. 4, 2004.
    • (2002) Opinion on TSE Infectivity Distribution in Ruminant Tissues
  • 66
    • 0034707048 scopus 로고    scopus 로고
    • Binding of disease-associated prion protein to plasminogen
    • Fischer, M. B., C. Roeckl, P. Parizek, H. P. Schwarz, and A. Aguzzi. 2000. Binding of disease-associated prion protein to plasminogen. Nature 408:479-483.
    • (2000) Nature , vol.408 , pp. 479-483
    • Fischer, M.B.1    Roeckl, C.2    Parizek, P.3    Schwarz, H.P.4    Aguzzi, A.5
  • 69
    • 0027906543 scopus 로고
    • Transmission of bovine spongiform encephalopathy to sheep and goats
    • Foster J. D., J. Hope, and H. Fraser. 1993. Transmission of bovine spongiform encephalopathy to sheep and goats. Vet. Rec. 133:339-441.
    • (1993) Vet. Rec. , vol.133 , pp. 339-441
    • Foster, J.D.1    Hope, J.2    Fraser, H.3
  • 70
  • 72
    • 1642436839 scopus 로고    scopus 로고
    • Hereditary Creutzfeldt-Jakob disease and fatal familial insomnia
    • Gambetti, P., P. Parchi, and S. G. Chen. 2003. Hereditary Creutzfeldt-Jakob disease and fatal familial insomnia. Clin. Lab. Med. 23:43-64.
    • (2003) Clin. Lab. Med. , vol.23 , pp. 43-64
    • Gambetti, P.1    Parchi, P.2    Chen, S.G.3
  • 73
    • 0018936053 scopus 로고
    • Oral transmission of Kuru, Creutzfeldt-Jakob Disease, and Scrapie to non-human primates
    • Gibbs, Jr., C. J., H. L. Amyx, A. Bacoate, C. I. Masters, and D. C. Gajdusek. 1980. Oral transmission of Kuru, Creutzfeldt-Jakob Disease, and Scrapie to non-human primates. J. Infect. Dis. 142:205-208.
    • (1980) J. Infect. Dis. , vol.142 , pp. 205-208
    • Gibbs Jr., C.J.1    Amyx, H.L.2    Bacoate, A.3    Masters, C.I.4    Gajdusek, D.C.5
  • 75
    • 0026017096 scopus 로고
    • Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein-coding exon
    • Goldmann, W., N. Hunter, G. Benson, J. D. Foster, and J. Hope. 1991. Different forms of the bovine PrP gene have five or six copies of a short, G-C-rich element within the protein-coding exon. J. Gen. Virol. (Pt. 1) 72:201-204.
    • (1991) J. Gen. Virol. , vol.72 , Issue.PART 1 , pp. 201-204
    • Goldmann, W.1    Hunter, N.2    Benson, G.3    Foster, J.D.4    Hope, J.5
  • 76
    • 0028349264 scopus 로고
    • PrP genotype and agent effects in scrapie: Change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie
    • Goldmann, W., N. Hunter, G. Smith, J. Foster, and I. Hope. 1994. PrP genotype and agent effects in scrapie: change in allelic interaction with different isolates of agent in sheep, a natural host of scrapie. J. Gen. Virol. 75(Pt 5):989-995.
    • (1994) J. Gen. Virol. , vol.75 , Issue.PART 5 , pp. 989-995
    • Goldmann, W.1    Hunter, N.2    Smith, G.3    Foster, J.4    Hope, I.5
  • 79
    • 1942448804 scopus 로고    scopus 로고
    • Inactivation of the bovine spongiform encephalopathy (BSE) agent by the acid and alkaline processes for manufacturing of bone gelatine
    • Grobben, A. H., P. J. Steele, R. A. Somerville, D. M. Taylor. 2003. Inactivation of the bovine spongiform encephalopathy (BSE) agent by the acid and alkaline processes for manufacturing of bone gelatine. Biotechnol. Appl. Biochem. 39:329-338.
    • (2003) Biotechnol. Appl. Biochem. , vol.39 , pp. 329-338
    • Grobben, A.H.1    Steele, P.J.2    Somerville, R.A.3    Taylor, D.M.4
  • 81
    • 0742270049 scopus 로고    scopus 로고
    • Failure to detect prion protein (PrPres) by immunohistochemistry in striated muscle tissues of animals experimentally inoculated with agents of transmissible spongiform encephalopathy
    • Hamir, A. N., J. M. Miller and R. C. Cutlip. 2004a. Failure to detect prion protein (PrPres) by immunohistochemistry in striated muscle tissues of animals experimentally inoculated with agents of transmissible spongiform encephalopathy. Vet. Pathol. 41:78-81.
    • (2004) Vet. Pathol. , vol.41 , pp. 78-81
    • Hamir, A.N.1    Miller, J.M.2    Cutlip, R.C.3
  • 83
    • 1142267004 scopus 로고    scopus 로고
    • Peripheral tissue involvement in sporadic, iatrogenic, and variant Creutzfeldt-Jakob disease: An immunohistochemical, quantitative, and biochemical study
    • Head, M. W., D. Ritchie, N. Smith, V. McLoughlin, W. Nailon, S. Samad, S. Masson, M. Bishop, L. McCardle, J. W. Ironside. 2004. Peripheral tissue involvement in sporadic, iatrogenic, and variant Creutzfeldt-Jakob disease: An immunohistochemical, quantitative, and biochemical study. Am. J. Pathol. 164:143-153.
    • (2004) Am. J. Pathol. , vol.164 , pp. 143-153
    • Head, M.W.1    Ritchie, D.2    Smith, N.3    McLoughlin, V.4    Nailon, W.5    Samad, S.6    Masson, S.7    Bishop, M.8    McCardle, L.9    Ironside, J.W.10
  • 86
    • 1942504192 scopus 로고    scopus 로고
    • Dendritic cells and oral transmission of prion diseases
    • Huang, F. P., and G. G. MacPherson. 2004. Dendritic cells and oral transmission of prion diseases. Adv. Drug. Deliv. Rev. 56:901-913.
    • (2004) Adv. Drug. Deliv. Rev. , vol.56 , pp. 901-913
    • Huang, F.P.1    MacPherson, G.G.2
  • 89
    • 0029283933 scopus 로고
    • An investigation of risk factors for cases of bovine spongiform encephalopathy born after the introduction of the "feed ban."
    • Hoinville, L. J., J. W. Wilesmith and M. S. Richards. 1995. An investigation of risk factors for cases of bovine spongiform encephalopathy born after the introduction of the "feed ban." Vet. Rec. 136:312-318.
    • (1995) Vet. Rec. , vol.136 , pp. 312-318
    • Hoinville, L.J.1    Wilesmith, J.W.2    Richards, M.S.3
  • 90
    • 0028874995 scopus 로고
    • A cellular form of prion protein (PrPC) exists in many non-neuronal tissues of sheep
    • Horiuchi, M., N. Yamazaki, T. Ikeda, N. Ishiguro, and M. Shinagawa. 1995. A cellular form of prion protein (PrPC) exists in many non-neuronal tissues of sheep. J. Gen. Virol. (Pt. 10) 76:2583-2587.
    • (1995) J. Gen. Virol. , vol.76 , Issue.PART 10 , pp. 2583-2587
    • Horiuchi, M.1    Yamazaki, N.2    Ikeda, T.3    Ishiguro, N.4    Shinagawa, M.5
  • 92
    • 0004201081 scopus 로고    scopus 로고
    • Review prepared for the UK Dept. Environ., Food and Rural Affairs
    • Horn, G., M. Bobrow, M. Bruce, M. Goedert, A. McLean, and J. Webster. 2001. Review of the origin of BSE. Review prepared for the UK Dept. Environ., Food and Rural Affairs. Available: http://www.defra.gov.uk/animalh/bse/ publications/bseorigin.pdf. Accessed Nov. 4, 2004.
    • (2001) Review of the Origin of BSE
    • Horn, G.1    Bobrow, M.2    Bruce, M.3    Goedert, M.4    McLean, A.5    Webster, J.6
  • 94
    • 0346496093 scopus 로고    scopus 로고
    • Comparative evaluation of the performance of two commercial kits for the detection of central nervous system tissue in meat
    • Hughson, E., P. Reece, M. J. Dennis, and S. Oehlschlager. 2003. Comparative evaluation of the performance of two commercial kits for the detection of central nervous system tissue in meat. Food Addit. Contam. 20:1034-1043.
    • (2003) Food Addit. Contam. , vol.20 , pp. 1034-1043
    • Hughson, E.1    Reece, P.2    Dennis, M.J.3    Oehlschlager, S.4
  • 95
    • 0141626026 scopus 로고    scopus 로고
    • Scrapie and experimental BSE in sheep
    • Hunter, N. 2003. Scrapie and experimental BSE in sheep. Br. Med. Bull. 66:171-183.
    • (2003) Br. Med. Bull. , vol.66 , pp. 171-183
    • Hunter, N.1
  • 96
    • 28444441684 scopus 로고    scopus 로고
    • Sheep and goats: Natural and experimental TSEs and factors influencing incidence of disease
    • Hunter, N., W. Goldmann, E. Marshall, and G. O'Neill. 2000. Sheep and goats: natural and experimental TSEs and factors influencing incidence of disease. Arch. Virol. Suppl. 16:181-188.
    • (2000) Arch. Virol. Suppl. , vol.16 , pp. 181-188
    • Hunter, N.1    Goldmann, W.2    Marshall, E.3    O'Neill, G.4
  • 98
    • 0141609860 scopus 로고    scopus 로고
    • Variant Creutzfeldt-Jakob disease and its transmission by blood
    • Ironside, J. W., and M. W. Head. 2003. Variant Creutzfeldt-Jakob disease and its transmission by blood. J. Thromb. Haemost. 1:1479-1486.
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 1479-1486
    • Ironside, J.W.1    Head, M.W.2
  • 100
    • 0034941197 scopus 로고    scopus 로고
    • Oral inoculation of sheep with the agent of bovine spongiform encephalopathy (BSE). 1. Onset and distribution of disease-specific PrP accumulation in brain and viscera
    • Jeffrey, M., S. Ryder, S. Martin, S. A. Hawkins, L. Terry, C. Berthelin-Baker, and S. J. Bellworthy. 2001. Oral inoculation of sheep with the agent of bovine spongiform encephalopathy (BSE). 1. Onset and distribution of disease-specific PrP accumulation in brain and viscera. J. Comp. Pathol. 124:280-289.
    • (2001) J. Comp. Pathol. , vol.124 , pp. 280-289
    • Jeffrey, M.1    Ryder, S.2    Martin, S.3    Hawkins, S.A.4    Terry, L.5    Berthelin-Baker, C.6    Bellworthy, S.J.7
  • 101
    • 2442662470 scopus 로고    scopus 로고
    • Prion protein gene heterogeneity in free-ranging white-tailed deer within the chronic wasting disease affected region of Wisconsin
    • Johnson, C., J. Johnson, M. Clayton, D. McKenzie and J. Aiken. 2003. Prion protein gene heterogeneity in free-ranging white-tailed deer within the chronic wasting disease affected region of Wisconsin. J. Wildlife Dis. 39:576-581.
    • (2003) J. Wildlife Dis. , vol.39 , pp. 576-581
    • Johnson, C.1    Johnson, J.2    Clayton, M.3    McKenzie, D.4    Aiken, J.5
  • 102
    • 1942531594 scopus 로고    scopus 로고
    • Prion protein is ubiquitinated after developing protease resistance in the brains of scrapie-infected mice
    • Kang, S. C., D. R. Brown, M. Whiteman, R. Li, T. Pan, G. Perry, T. Wisniewski, M. S. Sy, B. S. Wong. 2004. Prion protein is ubiquitinated after developing protease resistance in the brains of scrapie-infected mice. J. Pathol. 203:603-608.
    • (2004) J. Pathol. , vol.203 , pp. 603-608
    • Kang, S.C.1    Brown, D.R.2    Whiteman, M.3    Li, R.4    Pan, T.5    Perry, G.6    Wisniewski, T.7    Sy, M.S.8    Wong, B.S.9
  • 103
    • 0033853584 scopus 로고    scopus 로고
    • An evaluation of methods for the detection of spinal cord in product derived from advanced meat recovery systems
    • Kelley, L. C., S. Hafner, P. C. McCaskey, M. T. Button, and K. A. Langheinrich. 2000. An evaluation of methods for the detection of spinal cord in product derived from advanced meat recovery systems. J. Food Prot. 63:1107-1112.
    • (2000) J. Food Prot. , vol.63 , pp. 1107-1112
    • Kelley, L.C.1    Hafner, S.2    McCaskey, P.C.3    Button, M.T.4    Langheinrich, K.A.5
  • 105
    • 0024519176 scopus 로고
    • The role of the spleen in the neuroinvasion of scrapie in mice
    • Kimberlin, R. H., and C. A. Walker. 1989. The role of the spleen in the neuroinvasion of scrapie in mice. Virus Res. 12:201-211.
    • (1989) Virus Res. , vol.12 , pp. 201-211
    • Kimberlin, R.H.1    Walker, C.A.2
  • 107
    • 0028779748 scopus 로고
    • Epidemiological observations on spongiform encephalopathies in captive wild animals in the British Isles
    • Kirkwood, J. K., and A. A. Cunningham. 1994. Epidemiological observations on spongiform encephalopathies in captive wild animals in the British Isles. Vet. Rec. 135:296-303.
    • (1994) Vet. Rec. , vol.135 , pp. 296-303
    • Kirkwood, J.K.1    Cunningham, A.A.2
  • 112
    • 0031828358 scopus 로고    scopus 로고
    • Prion's progress: Patterns and rates of molecular evolution in relation to spongiform disease
    • Krakauer, D. C., P. M. Zanotto, and M. Pagel. 1998. Prion's progress: Patterns and rates of molecular evolution in relation to spongiform disease. J. Mol. Evol. 47:133-145.
    • (1998) J. Mol. Evol. , vol.47 , pp. 133-145
    • Krakauer, D.C.1    Zanotto, P.M.2    Pagel, M.3
  • 114
    • 0028911161 scopus 로고
    • The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system
    • Kurschner, C., and J. L. Morgan. 1995. The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system. Brain Res. Mol. Brain Res. 30:165-168.
    • (1995) Brain Res. Mol. Brain Res. , vol.30 , pp. 165-168
    • Kurschner, C.1    Morgan, J.L.2
  • 116
    • 0036525729 scopus 로고    scopus 로고
    • Metal ions and prion diseases
    • Lehmann, S. 2002. Metal ions and prion diseases. Curr. Opin. Chem Biol. 6:187-192.
    • (2002) Curr. Opin. Chem Biol. , vol.6 , pp. 187-192
    • Lehmann, S.1
  • 117
    • 0030006902 scopus 로고    scopus 로고
    • Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform
    • Lehmann, S., and D. A. Harris. 1996. Two mutant prion proteins expressed in cultured cells acquire biochemical properties reminiscent of the scrapie isoform. Proc. Natl. Acad. Sci. USA 93:5610-5614.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5610-5614
    • Lehmann, S.1    Harris, D.A.2
  • 119
  • 121
    • 0036009766 scopus 로고    scopus 로고
    • Studies on contamination of beef with tissues of the central nervous system (CNS) as pertaining to slaughtering technology and human BSE-exposure risk
    • Lucker, E., B. Schlottermuller, and A. Martin. 2002. Studies on contamination of beef with tissues of the central nervous system (CNS) as pertaining to slaughtering technology and human BSE-exposure risk. Berl. Munch. Tierarztl. Wochenschr. 115:118-121.
    • (2002) Berl. Munch. Tierarztl. Wochenschr. , vol.115 , pp. 118-121
    • Lucker, E.1    Schlottermuller, B.2    Martin, A.3
  • 122
    • 0037195647 scopus 로고    scopus 로고
    • Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol
    • Ma, J., R. Wollmann, and S. Lindquist. 2002. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298:1781-1785.
    • (2002) Science , vol.298 , pp. 1781-1785
    • Ma, J.1    Wollmann, R.2    Lindquist, S.3
  • 123
    • 0346847520 scopus 로고    scopus 로고
    • Prion disease: Bridging the spleen-nerve gap
    • Mabbott, N. A., and M. E. Bruce. 2003. Prion disease: Bridging the spleen-nerve gap. Nat. Med. 9:1463-1464.
    • (2003) Nat. Med. , vol.9 , pp. 1463-1464
    • Mabbott, N.A.1    Bruce, M.E.2
  • 124
    • 0035938902 scopus 로고    scopus 로고
    • Plasminogen binds to disease-associated prion protein of multiple species
    • Maissen, M., C. Roeckl, M. Glatzel, W. Goldmann, and A. Aguzzi. 2001. Plasminogen binds to disease-associated prion protein of multiple species. Lancet 357:2026-2028.
    • (2001) Lancet , vol.357 , pp. 2026-2028
    • Maissen, M.1    Roeckl, C.2    Glatzel, M.3    Goldmann, W.4    Aguzzi, A.5
  • 125
    • 0031059831 scopus 로고    scopus 로고
    • Decontamination of Creutzfeldt-Jakob disease and other transmissible agents
    • Manuelidis, L. 1997. Decontamination of Creutzfeldt-Jakob disease and other transmissible agents. J. Neurovirol. 3:62-65.
    • (1997) J. Neurovirol. , vol.3 , pp. 62-65
    • Manuelidis, L.1
  • 127
    • 0027925797 scopus 로고
    • Failure to transmit bovine spongiform encephalopathy to mice by feeding them with extraneural tissues of affected cattle
    • Middleton, D. J., and R. M. Barlow. 1993. Failure to transmit bovine spongiform encephalopathy to mice by feeding them with extraneural tissues of affected cattle. Vet. Rec. 132:545-547.
    • (1993) Vet. Rec. , vol.132 , pp. 545-547
    • Middleton, D.J.1    Barlow, R.M.2
  • 128
    • 0032110683 scopus 로고    scopus 로고
    • Epidemiology of chronic wasting disease in captive Rocky Mountain elk
    • Miller, M. W., M. A. Wild, and E. S. Williams. 1998. Epidemiology of chronic wasting disease in captive Rocky Mountain elk. J. Wildlife Dis. 34:532-538.
    • (1998) J. Wildlife Dis. , vol.34 , pp. 532-538
    • Miller, M.W.1    Wild, M.A.2    Williams, E.S.3
  • 129
    • 0041822083 scopus 로고    scopus 로고
    • Prion disease: Horizontal prion transmission in muledeer
    • Miller, M. W., and E. S. Williams. 2003. Prion disease: Horizontal prion transmission in muledeer. Nature 425:35-36.
    • (2003) Nature , vol.425 , pp. 35-36
    • Miller, M.W.1    Williams, E.S.2
  • 132
  • 133
    • 10644241804 scopus 로고    scopus 로고
    • Protease-resistant human prion protein and ferritin are cotransported across Caco-2 epithelial cells: Implications for species barrier in prion uptake from the intestine
    • Mishra, R. S., S. Basu, Y. Gu, X. Luo, W. Q. Zou, R. Mishra, R. Li, S. G. Chen, P. Gambetti, H. Fujioka and N. Singh. 2004. Protease-resistant human prion protein and ferritin are cotransported across Caco-2 epithelial cells: Implications for species barrier in prion uptake from the intestine. J. Neurosci. 24:11280-11290.
    • (2004) J. Neurosci. , vol.24 , pp. 11280-11290
    • Mishra, R.S.1    Basu, S.2    Gu, Y.3    Luo, X.4    Zou, W.Q.5    Mishra, R.6    Li, R.7    Chen, S.G.8    Gambetti, P.9    Fujioka, H.10    Singh, N.11
  • 134
    • 0034904789 scopus 로고    scopus 로고
    • Cellular prion protein status in sheep: Tissue-specific biochemical signatures
    • Moudjou, M., Y. Frobert, J. Grassi, and C. La Bonnardiere. 2001. Cellular prion protein status in sheep: Tissue-specific biochemical signatures. J. Gen. Virol. (Pt. 8) 82:2017-2024.
    • (2001) J. Gen. Virol. , vol.82 , Issue.PART 8 , pp. 2017-2024
    • Moudjou, M.1    Frobert, Y.2    Grassi, J.3    La Bonnardiere, C.4
  • 135
    • 2942630618 scopus 로고    scopus 로고
    • Prion infection of skeletal muscle cells and papillae in the tongue
    • Mulcahy, E. R., J. C. Bartz, A. E. Kincaid, and R. A. Bessen. 2004. Prion infection of skeletal muscle cells and papillae in the tongue. J. Virol. 78:6792-6798.
    • (2004) J. Virol. , vol.78 , pp. 6792-6798
    • Mulcahy, E.R.1    Bartz, J.C.2    Kincaid, A.E.3    Bessen, R.A.4
  • 137
    • 84858872553 scopus 로고    scopus 로고
    • National Center for Biotechnology Information
    • NCBI. 2004. Protein sequence database. National Center for Biotechnology Information. Available: http://www.ncbi.nlm.nih.gov/. Accessed Nov. 4, 2004.
    • (2004) Protein Sequence Database
  • 138
    • 0028925377 scopus 로고
    • Prion protein peptides induce alpha-helix to beta-sheet conformational transitions
    • Nguyen, J., M. A. Baldwin, F. E. Cohen, and S. B. Prusiner. 1995. Prion protein peptides induce alpha-helix to beta-sheet conformational transitions. Biochemistry 34:4186-4192.
    • (1995) Biochemistry , vol.34 , pp. 4186-4192
    • Nguyen, J.1    Baldwin, M.A.2    Cohen, F.E.3    Prusiner, S.B.4
  • 141
    • 2442643832 scopus 로고    scopus 로고
    • Polymorphisms in the prion precursor functional gene but not the pseudogene are associated with susceptibility to chronic wasting disease in white-tailed deer
    • O'Rourke, K. I., T. R. Spraker, L. K. Hamburg, T. E. Besser, K. A. Brayton, and D. P. Knowles. 2004. Polymorphisms in the prion precursor functional gene but not the pseudogene are associated with susceptibility to chronic wasting disease in white-tailed deer. J. Gen. Virol. 85(Pt 5):1339-1346.
    • (2004) J. Gen. Virol. , vol.85 , Issue.PART 5 , pp. 1339-1346
    • O'Rourke, K.I.1    Spraker, T.R.2    Hamburg, L.K.3    Besser, T.E.4    Brayton, K.A.5    Knowles, D.P.6
  • 143
    • 0025820942 scopus 로고
    • Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease
    • Palmer, M. S., A. J . Dryden, J. T. Hughes, and J. Collinge. 1991. Homozygous prion protein genotype predisposes to sporadic Creutzfeldt-Jakob disease. Nature 352:340-342.
    • (1991) Nature , vol.352 , pp. 340-342
    • Palmer, M.S.1    Dryden, A.J.2    Hughes, J.T.3    Collinge, J.4
  • 144
    • 26744431792 scopus 로고
    • Further observations on the production of scrapie in sheep by oral dosing with foetal membranes from scrapie-infected sheep
    • Pattison, I. H., M. N. Hoare, J. N. Jebbett, and W. A. Watson. 1972. Further observations on the production of scrapie in sheep by oral dosing with foetal membranes from scrapie-infected sheep. Br. Vet. J. 130:1xv-1xvii.
    • (1972) Br. Vet. J. , vol.130
    • Pattison, I.H.1    Hoare, M.N.2    Jebbett, J.N.3    Watson, W.A.4
  • 145
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly, P. C., and D. A. Harris. 1998. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273:33107-33110.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 148
    • 84858870527 scopus 로고    scopus 로고
    • Univ. of Washington and Joseph Felsenstein
    • PHYLIP. 2004. The Phylogeny Inference Package. Univ. of Washington and Joseph Felsenstein. Available: http://evolution.gs.washington.edu/phylip.html. Accessed Nov. 4, 2004.
    • (2004) The Phylogeny Inference Package
  • 150
    • 0028928498 scopus 로고
    • Allelic variations in apolipoprotein e and prion protein genotype related to plaque formation and age of onset in sporadic Creutzfeldt-Jakob disease
    • Pickering-Brown, S. M., D. M. A. Mann, F. Owen, J. W. Ironside, R. de Silva, D. A. Roberts, D. J. Balderson, and P. N. Cooper. 1995. Allelic variations in apolipoprotein E and prion protein genotype related to plaque formation and age of onset in sporadic Creutzfeldt-Jakob disease. Neurosci. Lett. 187:127-129.
    • (1995) Neurosci. Lett. , vol.187 , pp. 127-129
    • Pickering-Brown, S.M.1    Mann, D.M.A.2    Owen, F.3    Ironside, J.W.4    De Silva, R.5    Roberts, D.A.6    Balderson, D.J.7    Cooper, P.N.8
  • 151
    • 0346656570 scopus 로고    scopus 로고
    • Dissemination of central nervous system tissue during the slaughter of cattle in three Irish abattoirs
    • Prendergast, D. M., J. J. Sheridan, D. J. Daly, D. A. McDowell, and I. S. Blair. 2004. Dissemination of central nervous system tissue during the slaughter of cattle in three Irish abattoirs. Vet. Rec. 154:21-24.
    • (2004) Vet. Rec. , vol.154 , pp. 21-24
    • Prendergast, D.M.1    Sheridan, J.J.2    Daly, D.J.3    McDowell, D.A.4    Blair, I.S.5
  • 153
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner, S. B. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216:136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 154
    • 0003661592 scopus 로고    scopus 로고
    • Cold Spring Harbor Monograph Series, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Prusiner, S. B. 2004. Prion Biology and Diseases. 2nd ed. Cold Spring Harbor Monograph Series, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2004) Prion Biology and Diseases. 2nd Ed.
    • Prusiner, S.B.1
  • 158
    • 0028789745 scopus 로고    scopus 로고
    • The myth of maternal transmission of spongiform encephalopathy
    • Ridley, R. M., and H. F. Baker. 1999. The myth of maternal transmission of spongiform encephalopathy. Br. Med. J. 311(7012):1071-1075.
    • (1999) Br. Med. J. , vol.311 , Issue.7012 , pp. 1071-1075
    • Ridley, R.M.1    Baker, H.F.2
  • 159
    • 0141515202 scopus 로고    scopus 로고
    • Biochemistry and structure of PrP(C) and PrP(Sc)
    • Riesner, D. 2003. Biochemistry and structure of PrP(C) and PrP(Sc). Br. Med. Bull. 66:21-33.
    • (2003) Br. Med. Bull. , vol.66 , pp. 21-33
    • Riesner, D.1
  • 160
    • 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., S. Vasiljevic, R. M. Hennion, C. R. Birkett, J. Hope, and I. H. Gilbert. 2000. Screening Congo Red and its analogues for their ability to prevent the formation of PrP-res in scrapie-infected cells. J. Gen. Virol. 81:1155-1164.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1155-1164
    • Rudyk, H.1    Vasiljevic, S.2    Hennion, R.M.3    Birkett, C.R.4    Hope, J.5    Gilbert, I.H.6
  • 161
    • 0035341334 scopus 로고    scopus 로고
    • Creutzfeldt-Jakob disease: Recommendations for disinfection and sterilization
    • Rutala, W. A., and D. J. Weber. 2001. Creutzfeldt-Jakob disease: Recommendations for disinfection and sterilization. Clin. Infect. Dis. 32:1348-1356.
    • (2001) Clin. Infect. Dis. , vol.32 , pp. 1348-1356
    • Rutala, W.A.1    Weber, D.J.2
  • 162
    • 28444457804 scopus 로고    scopus 로고
    • Quantitative traits of prion strains are enciphered in the conformation of the prion protein
    • Safar, J., F. E. Cohen, and S. B. Prusiner. 2000. Quantitative traits of prion strains are enciphered in the conformation of the prion protein. Arch. Virol. Suppl. 2000:227-235.
    • (2000) Arch. Virol. Suppl. , vol.2000 , pp. 227-235
    • Safar, J.1    Cohen, F.E.2    Prusiner, S.B.3
  • 165
    • 0033120473 scopus 로고    scopus 로고
    • Potential for disruption of central nervous system tissue in beef cattle by different types of captive bolt stunners
    • Schmidt, G. R., K. L. Hossner, R. S. Yemm, and D. H. Gould. 1999. Potential for disruption of central nervous system tissue in beef cattle by different types of captive bolt stunners. J. Food Prot. 62:390-393.
    • (1999) J. Food Prot. , vol.62 , pp. 390-393
    • Schmidt, G.R.1    Hossner, K.L.2    Yemm, R.S.3    Gould, D.H.4
  • 166
    • 0035542809 scopus 로고    scopus 로고
    • The detection of central nervous system tissue on beef carcasses and in comminuted beef
    • Schmidt, G. R., R. S. Yemm, K. D. Childs, J. P. O'Callaghan, and K. L. Hossner. 2001. The detection of central nervous system tissue on beef carcasses and in comminuted beef. J. Food Prot. 64:2047-2052.
    • (2001) J. Food Prot. , vol.64 , pp. 2047-2052
    • Schmidt, G.R.1    Yemm, R.S.2    Childs, K.D.3    O'Callaghan, J.P.4    Hossner, K.L.5
  • 167
    • 0027710719 scopus 로고
    • General aspects of spongiform encephalopathies and hypotheses on the agents
    • Schreuder, B. E. C. 1994. General aspects of spongiform encephalopathies and hypotheses on the agents. Vet. Q. 15:167-174.
    • (1994) Vet. Q. , vol.15 , pp. 167-174
    • Schreuder, B.E.C.1
  • 168
    • 0027712781 scopus 로고
    • Gelatine production, the six steps to maximum safety
    • Schrieber, R., and U. Seybold. 1993. Gelatine production, the six steps to maximum safety. Dev. Biol. Stand. 80:195-198.
    • (1993) Dev. Biol. Stand. , vol.80 , pp. 195-198
    • Schrieber, R.1    Seybold, U.2
  • 170
    • 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. M., Y. Shaked, Z. Kariv-Inbal, M. Halimi, I. Avraham, and R. Gabizon. 2001. A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases. J. Biol. Chem. 276:31479-31482.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31479-31482
    • Shaked, G.M.1    Shaked, Y.2    Kariv-Inbal, Z.3    Halimi, M.4    Avraham, I.5    Gabizon, R.6
  • 171
    • 0032883356 scopus 로고    scopus 로고
    • Oral transmission and early lymphoid tropism of chronic wasting disease PrPres in mule deer fawns (Odocoileus hemionus)
    • Sigurdson, C. J., E. S. Williams, M. S. Miller, T. R. Spraker, K. I. O'-Rourke, and E. A. Hoover. 1999. Oral transmission and early lymphoid tropism of chronic wasting disease PrPres in mule deer fawns (Odocoileus hemionus). J. Gen. Virol. 80:2757-2764.
    • (1999) J. Gen. Virol. , vol.80 , pp. 2757-2764
    • Sigurdson, C.J.1    Williams, E.S.2    Miller, M.S.3    Spraker, T.R.4    O'-Rourke, K.I.5    Hoover, E.A.6
  • 172
    • 0030599770 scopus 로고    scopus 로고
    • BSE in Great Britain: Consistency of the neurohistopathological findings in two random annual samples of clinically suspect cases
    • Simmons, M. M., P. Harris, M. Jeffrey, S. C. Meek, I. W. Blamire, G. A. Wells. 1996. BSE in Great Britain: Consistency of the neurohistopathological findings in two random annual samples of clinically suspect cases. Vet. Rec. 138:175-177.
    • (1996) Vet. Rec. , vol.138 , pp. 175-177
    • Simmons, M.M.1    Harris, P.2    Jeffrey, M.3    Meek, S.C.4    Blamire, I.W.5    Wells, G.A.6
  • 174
    • 11444251657 scopus 로고    scopus 로고
    • Transmissible spongiform encephalopathy strain, PrP genotype and brain region all affect the degree of glycosylation of PrPSc
    • Somerville, R. A., S. Hamilton and K. Fernie. 2005. Transmissible spongiform encephalopathy strain, PrP genotype and brain region all affect the degree of glycosylation of PrPSc. J. Gen. Virol. (Pt. 1) 86:241-246.
    • (2005) J. Gen. Virol. , vol.86 , Issue.PART 1 , pp. 241-246
    • Somerville, R.A.1    Hamilton, S.2    Fernie, K.3
  • 175
    • 4844220510 scopus 로고    scopus 로고
    • Diagnosing prion diseases: Needs, challenges and hopes
    • Soto, C. 2004. Diagnosing prion diseases: needs, challenges and hopes. Nat. Rev. Microbiol. 2:809-819.
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 809-819
    • Soto, C.1
  • 176
    • 0035977053 scopus 로고    scopus 로고
    • PrPC directly interacts with proteins involved in signaling pathways
    • Spielhaupter, C., and H. M. Schatzl. 2001. PrPC directly interacts with proteins involved in signaling pathways. J. Biol. Chem. 276:44604-44612.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44604-44612
    • Spielhaupter, C.1    Schatzl, H.M.2
  • 177
    • 0030636097 scopus 로고    scopus 로고
    • Spongiform encephalopathy in free-ranging mule deer (Odocoileus hemionus), white-tailed deer (Odocoileus virginianus) and Rocky Mountain elk (Cervus elaphus nelsoni) in north central Colorado
    • Spraker, T. R., M. W. Miller, E. S. Williams, D. M. Getzy, W. J. Adrian, G. G. Schoonveld, R. A. Spowart, K. I. O'Rourke, J. M. Miller, and P. A. Merz. 1997. Spongiform encephalopathy in free-ranging mule deer (Odocoileus hemionus), white-tailed deer (Odocoileus virginianus) and Rocky Mountain elk (Cervus elaphus nelsoni) in north central Colorado. J. Wildlife Dis. 33:1-6.
    • (1997) J. Wildlife Dis. , vol.33 , pp. 1-6
    • Spraker, T.R.1    Miller, M.W.2    Williams, E.S.3    Getzy, D.M.4    Adrian, W.J.5    Schoonveld, G.G.6    Spowart, R.A.7    O'Rourke, K.I.8    Miller, J.M.9    Merz, P.A.10
  • 178
    • 8644261692 scopus 로고    scopus 로고
    • The first Canadian indigenous case of bovine spongiform encephalopathy (BSE) has molecular characteristics for prion protein that are similar to those of BSE in the United Kingdom but differ from those of chronic wasting disease in captive elk and deer
    • Stack, M. J., A. Balachandran, M. Chaplin, L. Davis, S. Czub and B. Miller. 2004. The first Canadian indigenous case of bovine spongiform encephalopathy (BSE) has molecular characteristics for prion protein that are similar to those of BSE in the United Kingdom but differ from those of chronic wasting disease in captive elk and deer. Can. Vet. J. 45:825-830.
    • (2004) Can. Vet. J. , vol.45 , pp. 825-830
    • Stack, M.J.1    Balachandran, A.2    Chaplin, M.3    Davis, L.4    Czub, S.5    Miller, B.6
  • 179
    • 84858880936 scopus 로고    scopus 로고
    • The Swiss Institute of Bioinformatics and the European Bioinformatics Institute
    • Swiss-Prot/TrEMBL. 2004. Protein Knowledge Base. The Swiss Institute of Bioinformatics and the European Bioinformatics Institute. Available: http://us.expasy.org/. Accessed Nov. 4, 2004.
    • (2004) Protein Knowledge Base
  • 183
    • 0007292277 scopus 로고
    • Absence of disease in mice receiving milk from cows with bovine spongiform encephalopathy
    • Taylor, D. M., C. E. Ferguson, C. J. Bostock, and M. Dawson. 1995a. Absence of disease in mice receiving milk from cows with bovine spongiform encephalopathy. Vet. Rec. 136:592-596.
    • (1995) Vet. Rec. , vol.136 , pp. 592-596
    • Taylor, D.M.1    Ferguson, C.E.2    Bostock, C.J.3    Dawson, M.4
  • 184
    • 0029897787 scopus 로고    scopus 로고
    • Exposure to autoclaving or sodium-hydroxide extends the dose-response curve of the 263K strain of scrapie agent in hamsters
    • Taylor, D. M., and K. Fernie. 1996. Exposure to autoclaving or sodium-hydroxide extends the dose-response curve of the 263K strain of scrapie agent in hamsters. J. Gen. Virol. 77:811-813.
    • (1996) J. Gen. Virol. , vol.77 , pp. 811-813
    • Taylor, D.M.1    Fernie, K.2
  • 185
    • 0029640538 scopus 로고
    • Inactivation of the bovine spongiform encephalopathy agent by rendering procedures
    • Taylor, D. M., S. L. Woodgate, and M. J. Atkinson. 1995b. Inactivation of the bovine spongiform encephalopathy agent by rendering procedures. Vet. Rec. 136:605-610.
    • (1995) Vet. Rec. , vol.136 , pp. 605-610
    • Taylor, D.M.1    Woodgate, S.L.2    Atkinson, M.J.3
  • 186
    • 0029884496 scopus 로고    scopus 로고
    • Scrapie infection can be established readily through skin scarification in immunocompetent but not immunodeficient mice
    • Taylor, D. M., I. McConnell, and H. Fraser. 1996. Scrapie infection can be established readily through skin scarification in immunocompetent but not immunodeficient mice. J. Gen. Virol. 77:1595-1599.
    • (1996) J. Gen. Virol. , vol.77 , pp. 1595-1599
    • Taylor, D.M.1    McConnell, I.2    Fraser, H.3
  • 189
    • 0037471890 scopus 로고    scopus 로고
    • Detection of disease-specific PrP in the distal ileum of cattle exposed orally to the agent of bovine spongiform encephalopathy
    • Terry, L. A., S. Marsh, S. J. Ryder, S. A. Hawkins, G. A. Wells, and Y. I. Spencer. 2003. Detection of disease-specific PrP in the distal ileum of cattle exposed orally to the agent of bovine spongiform encephalopathy. Vet. Rec. 152:387-392.
    • (2003) Vet. Rec. , vol.152 , pp. 387-392
    • Terry, L.A.1    Marsh, S.2    Ryder, S.J.3    Hawkins, S.A.4    Wells, G.A.5    Spencer, Y.I.6
  • 190
    • 0038110004 scopus 로고    scopus 로고
    • Widespread PrPSc accumulation in muscles of hamsters orally infected with scrapie
    • Thomzig, A., C. Kratzel, G. Lenz, D. Kruger, and M. Beekes. 2003. Widespread PrPSc accumulation in muscles of hamsters orally infected with scrapie. EMBO Rep. 4:530-533.
    • (2003) EMBO Rep. , vol.4 , pp. 530-533
    • Thomzig, A.1    Kratzel, C.2    Lenz, G.3    Kruger, D.4    Beekes, M.5
  • 191
    • 2942592731 scopus 로고    scopus 로고
    • Preclinical deposition of pathological prion protein PrP(Sc) in muscles of hamsters orally exposed to scrapie
    • Thomzig, A., W. Schulz-Schaeffer, C. Kratzel, J. Mai, and M. Beekes. 2004. Preclinical deposition of pathological prion protein PrP(Sc) in muscles of hamsters orally exposed to scrapie. J. Clin. Invest. 113:1465-1472.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1465-1472
    • Thomzig, A.1    Schulz-Schaeffer, W.2    Kratzel, C.3    Mai, J.4    Beekes, M.5
  • 192
    • 0036220673 scopus 로고    scopus 로고
    • Influence of the prion protein gene, Prnp, on scrapie susceptibility in sheep
    • Tranulis, M. A. 2002. Influence of the prion protein gene, Prnp, on scrapie susceptibility in sheep. APMIS 110:33-43.
    • (2002) APMIS , vol.110 , pp. 33-43
    • Tranulis, M.A.1
  • 193
    • 0037197975 scopus 로고    scopus 로고
    • Pregnancy status and fetal prion genetics determine PrPSc accumulation in placentomes of scrapie-infected sheep
    • Tuo, W., K. I. O'Rourke, D. Zhuang, W. P. Cheevers, T. R. Spraker, and D. P. Knowles. 2002. Pregnancy status and fetal prion genetics determine PrPSc accumulation in placentomes of scrapie-infected sheep. Proc. Natl. Acad. Sci. USA 99:6310-6315.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 6310-6315
    • Tuo, W.1    O'Rourke, K.I.2    Zhuang, D.3    Cheevers, W.P.4    Spraker, T.R.5    Knowles, D.P.6
  • 196
    • 21544472992 scopus 로고    scopus 로고
    • Prohibition of the use of specified risk materials for human food and requirements for disposition of non-ambulatory disabled cattle
    • Food Safety and Inspection Service
    • USDA. 2004a. Food Safety and Inspection Service. Prohibition of the use of specified risk materials for human food and requirements for disposition of non-ambulatory disabled cattle. Fed. Regis. 69:1861-1874.
    • (2004) Fed. Regis. , vol.69 , pp. 1861-1874
  • 197
    • 33646035058 scopus 로고    scopus 로고
    • Prohibition of the Use of Certain Stunning Devices Used to Immobilize Cattle during Slaughter
    • Food Safety and Inspection Service
    • USDA. 2004b. Food Safety and Inspection Service. Prohibition of the Use of Certain Stunning Devices Used to Immobilize Cattle During Slaughter. Fed. Regis. 69:1885-1891.
    • (2004) Fed. Regis. , vol.69 , pp. 1885-1891
  • 198
    • 33646027183 scopus 로고    scopus 로고
    • Meat Produced by Advanced Meat/Bone Separation Machinery and Meat Recovery (AMR) Systems
    • Food Safety and Inspection Service
    • USDA. 2004c. Food Safety and Inspection Service. Meat Produced by Advanced Meat/Bone Separation Machinery and Meat Recovery (AMR) Systems. Fed. Regis. 69:1874-1885.
    • (2004) Fed. Regis. , vol.69 , pp. 1874-1885
  • 199
    • 84858881292 scopus 로고    scopus 로고
    • USDA:APHIS:VS, CEAH, National Animal Health Monitoring System, Fort Collins, CO
    • USDA. 2004d. Phase II: Scrapie: Ovine Slaughter Surveillance Study. 2002-2003. USDA:APHIS:VS, CEAH, National Animal Health Monitoring System, Fort Collins, CO. Available: http://www.aphis.usda.gov/vs/ceah/ncahs/nahms/sheep/ SOSSphase2.pdf. Accessed Nov. 4, 2004.
    • (2004) Phase II: Scrapie: Ovine Slaughter Surveillance Study. 2002-2003
  • 201
    • 1142285202 scopus 로고    scopus 로고
    • Susceptibility of common fibroblast cell lines to transmissible spongiform encephalopathy agents
    • Vorberg, I., A. Raines, B. Story and S. A. Priola. 2004. Susceptibility of common fibroblast cell lines to transmissible spongiform encephalopathy agents. J. Infect. Dis. 189:431-439.
    • (2004) J. Infect. Dis. , vol.189 , pp. 431-439
    • Vorberg, I.1    Raines, A.2    Story, B.3    Priola, S.A.4
  • 203
    • 0141849458 scopus 로고    scopus 로고
    • Molecular and clinical classification of human prion disease
    • Wadsworth, J. D., A. F. Hill, J. A. Beck, and J. Collinge. 2003. Molecular and clinical classification of human prion disease. Br. Med. Bull. 66:241-254.
    • (2003) Br. Med. Bull. , vol.66 , pp. 241-254
    • Wadsworth, J.D.1    Hill, A.F.2    Beck, J.A.3    Collinge, J.4
  • 204
    • 0035928432 scopus 로고    scopus 로고
    • Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay
    • Wadsworth, J. D., S. Joiner, A. F. Hill, T. A. Campbell, M. Desbruslais, P. J. Luthert, and J. Collinge. 2001. Tissue distribution of protease resistant prion protein in variant Creutzfeldt-Jakob disease using a highly sensitive immunoblotting assay. Lancet 358:171-180.
    • (2001) Lancet , vol.358 , pp. 171-180
    • Wadsworth, J.D.1    Joiner, S.2    Hill, A.F.3    Campbell, T.A.4    Desbruslais, M.5    Luthert, P.J.6    Collinge, J.7
  • 207
    • 0026412979 scopus 로고
    • Bovine spongiform encephalopathy: Epidemiological studies on the origin
    • Wilesmith, J. W., J. B. M. Ryan, and M. J. Atkinson. 1991. Bovine spongiform encephalopathy: Epidemiological studies on the origin. Vet. Rec. 128:199-203.
    • (1991) Vet. Rec. , vol.128 , pp. 199-203
    • Wilesmith, J.W.1    Ryan, J.B.M.2    Atkinson, M.J.3
  • 208
    • 0026813024 scopus 로고
    • Bovine spongiform encephalopathy: Epidemiological features 1985-1990
    • Wilesmith, J. W., J. B. M. Ryan, and W. D. Hueston. 1992. Bovine spongiform encephalopathy: Epidemiological features 1985-1990. Vet. Rec. 130:90-94.
    • (1992) Vet. Rec. , vol.130 , pp. 90-94
    • Wilesmith, J.W.1    Ryan, J.B.M.2    Hueston, W.D.3
  • 209
    • 0024290760 scopus 로고
    • Bovine spongiform encephalopathy: Epidemiological studies
    • Wilesmith, J. W., G. A. Wells, M. P. Cranwell, and J. B. Ryan. 1988. Bovine spongiform encephalopathy: Epidemiological studies. Vet. Rec. 123:638-644.
    • (1988) Vet. Rec. , vol.123 , pp. 638-644
    • Wilesmith, J.W.1    Wells, G.A.2    Cranwell, M.P.3    Ryan, J.B.4
  • 210
    • 0036679120 scopus 로고    scopus 로고
    • Chronic wasting disease in deer and elk in North America
    • Williams, E. S., and M. W. Miller. 2002. Chronic wasting disease in deer and elk in North America. Rev. Sci. Tech. 21:305-316.
    • (2002) Rev. Sci. Tech. , vol.21 , pp. 305-316
    • Williams, E.S.1    Miller, M.W.2
  • 211
    • 0026871312 scopus 로고
    • Spongiform encephalopathies in Cervidae
    • Williams, E. S., and S. Young. 1992. Spongiform encephalopathies in Cervidae. Rev. Sci. Tech. 11:551-567.
    • (1992) Rev. Sci. Tech. , vol.11 , pp. 551-567
    • Williams, E.S.1    Young, S.2
  • 212
    • 0027352768 scopus 로고
    • Neuropathology of chronic wasting disease of mule deer (Odocoileus hemionus) and elk (Cervus elaphus nelsoni)
    • Williams, E. S., and S. Young. 1993. Neuropathology of chronic wasting disease of mule deer (Odocoileus hemionus) and elk (Cervus elaphus nelsoni). Vet. Pathol. 30:36-45.
    • (1993) Vet. Pathol. , vol.30 , pp. 36-45
    • Williams, E.S.1    Young, S.2
  • 215
    • 1942451924 scopus 로고    scopus 로고
    • Infectivity of prion protein bound to stainless steel wires: A model for testing decontamination procedures for transmissible spongiform encephalopathies
    • Yan, Z. X., L. Stitz, P. Heeg, E. Pfaff, and K. Roth. 2004. Infectivity of prion protein bound to stainless steel wires: a model for testing decontamination procedures for transmissible spongiform encephalopathies. Infect. Control Hosp. Epidemiol. 25:280-283.
    • (2004) Infect. Control Hosp. Epidemiol. , vol.25 , pp. 280-283
    • Yan, Z.X.1    Stitz, L.2    Heeg, P.3    Pfaff, E.4    Roth, K.5
  • 216
    • 0028863753 scopus 로고
    • The pathological changes in peripheral organs of scrapie-infected animals
    • Ye, X., and R. I. Carp. 1995. The pathological changes in peripheral organs of scrapie-infected animals. Histol. Histopathol. 10:995-1021.
    • (1995) Histol. Histopathol. , vol.10 , pp. 995-1021
    • Ye, X.1    Carp, R.I.2


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