메뉴 건너뛰기




Volumn 188, Issue 11, 2003, Pages 1782-1789

Enzymatic Degradation of Prion Protein in Brain Stem from Infected Cattle and Sheep

Author keywords

[No Author keywords available]

Indexed keywords

DETERGENT; PROTEINASE; PROTEINASE 2; PROTEINASE K; SUBTILISIN; UNCLASSIFIED DRUG;

EID: 0346882925     PISSN: 00221899     EISSN: None     Source Type: Journal    
DOI: 10.1086/379664     Document Type: Article
Times cited : (133)

References (48)
  • 1
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl N, Baldwin MA, Teplow DB, et al. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 1993; 32:1991-2002.
    • (1993) Biochemistry , vol.32 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3
  • 2
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey BW, Dong A, Bhat KS, Ernst D, Hayes SF, Caughey WS. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 1991; 30:7672-80.
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 3
    • 0027332116 scopus 로고
    • Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins
    • Pan KM, Baldwin M, Nguyen J, et al. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 1993; 90:10962-6.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Baldwin, M.2    Nguyen, J.3
  • 5
    • 0021383523 scopus 로고
    • A rapid and efficient method to enrich SAF-protein from scrapie brains of hamsters
    • Hilmert H, Diringer H. A rapid and efficient method to enrich SAF-protein from scrapie brains of hamsters. Biosci Rep 1984; 4:165-70.
    • (1984) Biosci Rep , vol.4 , pp. 165-170
    • Hilmert, H.1    Diringer, H.2
  • 6
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • Prusiner SB. Novel proteinaceous infectious particles cause scrapie. Science 1982; 216:136-44.
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 8
    • 0027405681 scopus 로고
    • Comparative analysis of scrapie agent inactivation methods
    • Ernst DR, Race RE. Comparative analysis of scrapie agent inactivation methods. J Virol Methods 1993; 41:193-201.
    • (1993) J Virol Methods , vol.41 , pp. 193-201
    • Ernst, D.R.1    Race, R.E.2
  • 9
    • 0033629344 scopus 로고    scopus 로고
    • Inactivation of transmissible degenerative encephalopathy agents: A review
    • Taylor DM. Inactivation of transmissible degenerative encephalopathy agents: a review. Vet J 2000; 159:10-7.
    • (2000) Vet J , vol.159 , pp. 10-17
    • Taylor, D.M.1
  • 10
    • 0032474023 scopus 로고    scopus 로고
    • Studies on the efficacy of hyperbaric rendering procedures in inactivating bovine spongiform encephalopathy (BSE) and scrapie agents
    • Schreuder BEC, Geertsma RE, VanKeulen LJM, et al. Studies on the efficacy of hyperbaric rendering procedures in inactivating bovine spongiform encephalopathy (BSE) and scrapie agents. Vet Rec 1998; 142:474-80.
    • (1998) Vet Rec , vol.142 , pp. 474-480
    • Schreuder, B.E.C.1    Geertsma, R.E.2    VanKeulen, L.J.M.3
  • 12
    • 0018220615 scopus 로고
    • Resistance of scrapie agent to decontamination
    • Dickinson AG, Taylor DM. Resistance of scrapie agent to decontamination. N Engl J Med 1978; 299:1413-4.
    • (1978) N Engl J Med , vol.299 , pp. 1413-1414
    • Dickinson, A.G.1    Taylor, D.M.2
  • 13
    • 0037192848 scopus 로고    scopus 로고
    • Characterisation of thermodynamic diversity between transmissible spongiform encephalopathy agent strains and its theoretical implications
    • Somerville RA, Oberthür RC, Havekotte U, MacDonald F, Taylor DM, Dickinson AG. Characterisation of thermodynamic diversity between transmissible spongiform encephalopathy agent strains and its theoretical implications. J Biol Chem 2002; 277:11084-9.
    • (2002) J Biol Chem , vol.277 , pp. 11084-11089
    • Somerville, R.A.1    Oberthür, R.C.2    Havekotte, U.3    MacDonald, F.4    Taylor, D.M.5    Dickinson, A.G.6
  • 14
    • 0030347375 scopus 로고    scopus 로고
    • Analysis of risk to biomedical products developed from animal sources (with special emphasis on the spongiform encephalopathy agents, scrapie and BSE)
    • Rohwer RG. Analysis of risk to biomedical products developed from animal sources (with special emphasis on the spongiform encephalopathy agents, scrapie and BSE). Dev Biol Stand 1996; 88:247-56.
    • (1996) Dev Biol Stand , vol.88 , pp. 247-256
    • Rohwer, R.G.1
  • 15
    • 0035341334 scopus 로고    scopus 로고
    • Creutzfeldt-Jakob disease: Recommendations for disinfection and sterilization
    • Rutala WA, Weber DJ. Creutzfeldt-Jakob disease: recommendations for disinfection and sterilization. Clin Infect Dis 2001; 32:1348-56.
    • (2001) Clin Infect Dis , vol.32 , pp. 1348-1356
    • Rutala, W.A.1    Weber, D.J.2
  • 16
    • 0037947523 scopus 로고    scopus 로고
    • Ultra-high-pressure inactivation of prion infectivity in processed meat: A practical method to prevent human infection
    • Brown P, Meyer R, Cardone F, Pocchiari M. Ultra-high-pressure inactivation of prion infectivity in processed meat: a practical method to prevent human infection. Proc Natl Acad Sci USA 2003; 100:6093-7.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6093-6097
    • Brown, P.1    Meyer, R.2    Cardone, F.3    Pocchiari, M.4
  • 17
    • 0037162510 scopus 로고    scopus 로고
    • Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance
    • Jung G, Jones G, Masison DC. Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance. Proc Natl Acad Sci USA 2002; 99:9936-41.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9936-9941
    • Jung, G.1    Jones, G.2    Masison, D.C.3
  • 18
    • 0014438991 scopus 로고
    • Further studies of the infectivity and stability of extracts and homogenates derived from scrapie affected mouse brains
    • Hunter GD, Gibbons RA, Kimberlin RH, Millson GC. Further studies of the infectivity and stability of extracts and homogenates derived from scrapie affected mouse brains. J Comp Pathol 1969; 79:101-8.
    • (1969) J Comp Pathol , vol.79 , pp. 101-108
    • Hunter, G.D.1    Gibbons, R.A.2    Kimberlin, R.H.3    Millson, G.C.4
  • 19
    • 84903245545 scopus 로고
    • The enigma of the scrapie agent: Biochemical approaches and the involvement of membranes and nucleic acids
    • Prusiner SB, Hadlow W, eds. New York: Academic Press
    • Hunter GD. The enigma of the scrapie agent: biochemical approaches and the involvement of membranes and nucleic acids. In: Prusiner SB, Hadlow W, eds. Slow transmissible diseases of the nervous system. Vol. 2. New York: Academic Press, 1979:365-86.
    • (1979) Slow Transmissible Diseases of the Nervous System , vol.2 , pp. 365-386
    • Hunter, G.D.1
  • 21
    • 0021023167 scopus 로고
    • A protease-resistant protein is a structural component of the scrapie prion
    • McKinley MP, Bolton DC, Prusiner SB. A protease-resistant protein is a structural component of the scrapie prion. Cell 1983; 35:57-62.
    • (1983) Cell , vol.35 , pp. 57-62
    • McKinley, M.P.1    Bolton, D.C.2    Prusiner, S.B.3
  • 22
    • 0028240984 scopus 로고
    • Properties of the scrapie prion protein: Quantitative analysis of protease resistance
    • Oesch B, Jensen M, Nilsson P, Fogh J. Properties of the scrapie prion protein: quantitative analysis of protease resistance. Biochemistry 1994; 33:5926-31.
    • (1994) Biochemistry , vol.33 , pp. 5926-5931
    • Oesch, B.1    Jensen, M.2    Nilsson, P.3    Fogh, J.4
  • 23
    • 0021672620 scopus 로고
    • Molecular characteristics of the major scrapie prion protein
    • Bolton DC, McKinley MP, Prusiner SB. Molecular characteristics of the major scrapie prion protein. Biochemistry 1984; 23:5898-906.
    • (1984) Biochemistry , vol.23 , pp. 5898-5906
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 24
    • 0026795739 scopus 로고
    • Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain PWD-1
    • Lin X, Lee CG, Casale ES, Shih JCH. Purification and characterization of a keratinase from a feather-degrading Bacillus licheniformis strain PWD-1. Appl Environ Microbiol 1992; 58:3271-5.
    • (1992) Appl Environ Microbiol , vol.58 , pp. 3271-3275
    • Lin, X.1    Lee, C.G.2    Casale, E.S.3    Shih, J.C.H.4
  • 25
    • 0032808211 scopus 로고    scopus 로고
    • Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB-29
    • Wang JJ, Shih J. Fermentation production of keratinase from Bacillus licheniformis PWD-1 and a recombinant B. subtilis FDB-29. J Ind Microbiol Biotechnol 1999; 22:608-16.
    • (1999) J Ind Microbiol Biotechnol , vol.22 , pp. 608-616
    • Wang, J.J.1    Shih, J.2
  • 26
    • 0024973635 scopus 로고
    • Bovine spongiform encephalopathy: Diagnostic significance of vacuolar changes in selected nuclei of the medulla oblongata
    • Wells GA, Hancock RD, Cooley WA, Richards MS, Higgins RJ, David GP. Bovine spongiform encephalopathy: diagnostic significance of vacuolar changes in selected nuclei of the medulla oblongata. Vet Rec 1989; 125:521-4.
    • (1989) Vet Rec , vol.125 , pp. 521-524
    • Wells, G.A.1    Hancock, R.D.2    Cooley, W.A.3    Richards, M.S.4    Higgins, R.J.5    David, G.P.6
  • 27
    • 0029299190 scopus 로고
    • Immunohistochemical detection and localization of prion protein in brain tissue of sheep with natural scrapie
    • VanKeulen LJM, Schreuder BEC, Meloen RH, et al. Immunohistochemical detection and localization of prion protein in brain tissue of sheep with natural scrapie. Vet Pathol 1995; 32:299-308.
    • (1995) Vet Pathol , vol.32 , pp. 299-308
    • VanKeulen, L.J.M.1    Schreuder, B.E.C.2    Meloen, R.H.3
  • 28
    • 0032830886 scopus 로고    scopus 로고
    • Sc detection and its use as a rapid surveillance method for the diagnosis of bovine spongiform encephalopathy (BSE)
    • Sc detection and its use as a rapid surveillance method for the diagnosis of bovine spongiform encephalopathy (BSE). Acta Neuropathol 1999; 98:437-43.
    • (1999) Acta Neuropathol , vol.98 , pp. 437-443
    • Schaller, O.1    Fatzer, R.2    Stack, M.3
  • 29
    • 0000352442 scopus 로고
    • Proteinases as probes of conformation of soluble proteins
    • Beynon RJ, Bond JS eds. Oxford: IRL Press
    • Price NC, Johnson CM. Proteinases as probes of conformation of soluble proteins. In: Beynon RJ, Bond JS eds. Proteolytic enzymes: a practical approach, Oxford: IRL Press, 1989:163-80.
    • (1989) Proteolytic Enzymes: A Practical Approach , pp. 163-180
    • Price, N.C.1    Johnson, C.M.2
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227:680-5.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0026739991 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Biotechnology 1979; 24:145-9.
    • (1979) Biotechnology , vol.24 , pp. 145-149
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 32
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette WN. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal Biochem 1981; 112:195-203.
    • (1981) Anal Biochem , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 33
    • 0033536155 scopus 로고    scopus 로고
    • Tests for BSE evaluated
    • Moynagh J, Schimmel H. Tests for BSE evaluated. Nature 1999; 400: 105.
    • (1999) Nature , vol.400 , pp. 105
    • Moynagh, J.1    Schimmel, H.2
  • 34
    • 0033823648 scopus 로고    scopus 로고
    • Preclinical diagnosis of scrapie by immunohistochemistry of third eyelid lymphoid tissue
    • Rourke KI, Baszler TV, Besser TE, et al. Preclinical diagnosis of scrapie by immunohistochemistry of third eyelid lymphoid tissue. J Clin Microbiol 2000; 38:3254-9.
    • (2000) J Clin Microbiol , vol.38 , pp. 3254-3259
    • Rourke, K.I.1    Baszler, T.V.2    Besser, T.E.3
  • 35
    • 0345540635 scopus 로고    scopus 로고
    • Generation of monoclonal antibodies against prion proteins with an unconventional nucleic acid-based immunization strategy
    • Krasemann S, Jürgens T, Bodemer W. Generation of monoclonal antibodies against prion proteins with an unconventional nucleic acid-based immunization strategy. J Biotechnol 1999; 73:119-29.
    • (1999) J Biotechnol , vol.73 , pp. 119-129
    • Krasemann, S.1    Jürgens, T.2    Bodemer, W.3
  • 36
    • 0029299190 scopus 로고
    • Immunohistochemical detection and localization of prion protein in brain tissue of sheep with natural scrapie
    • VanKeulen LJ, Schreuder BE, Meloen RH, et al. Immunohistochemical detection and localization of prion protein in brain tissue of sheep with natural scrapie. Vet Pathol 1995; 32:299-308.
    • (1995) Vet Pathol , vol.32 , pp. 299-308
    • VanKeulen, L.J.1    Schreuder, B.E.2    Meloen, R.H.3
  • 37
    • 0030613755 scopus 로고    scopus 로고
    • Prion (PrPSc)-specific epitope defined by a monoclonal antibody
    • Korth C, Stierli B, Streit P, et al. Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature 1997; 390:74-7.
    • (1997) Nature , vol.390 , pp. 74-77
    • Korth, C.1    Stierli, B.2    Streit, P.3
  • 39
    • 0035945622 scopus 로고    scopus 로고
    • Screening slaughtered cattle for BSE
    • Deslys JP, Comoy E, Hawkins S, et al. Screening slaughtered cattle for BSE. Nature 2001; 409:476-8.
    • (2001) Nature , vol.409 , pp. 476-478
    • Deslys, J.P.1    Comoy, E.2    Hawkins, S.3
  • 40
  • 41
    • 0029640538 scopus 로고
    • Inactivation of the bovine spongiform encephalopathy agent by rendering procedures
    • Taylor DM, Woodgate SL, Atkinson MJ. Inactivation of the bovine spongiform encephalopathy agent by rendering procedures. Vet Rec 1995; 137:605-10.
    • (1995) Vet Rec , vol.137 , pp. 605-610
    • Taylor, D.M.1    Woodgate, S.L.2    Atkinson, M.J.3
  • 43
    • 0036843448 scopus 로고    scopus 로고
    • Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice
    • Safar JG, Scott M, Monaghan J, et al. Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice. Nat Biotechnol 2002; 20:1147-50.
    • (2002) Nat Biotechnol , vol.20 , pp. 1147-1150
    • Safar, J.G.1    Scott, M.2    Monaghan, J.3
  • 44
    • 0033850051 scopus 로고    scopus 로고
    • Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein
    • Wille H, Prusiner SB, Cohen FE. Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein. J Struct Biol 2000; 130:323-38.
    • (2000) J Struct Biol , vol.130 , pp. 323-338
    • Wille, H.1    Prusiner, S.B.2    Cohen, F.E.3
  • 45
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton DC, McKinley MP, Prusiner SB. Identification of a protein that purifies with the scrapie prion. Science 1982; 218:1309-11.
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 46
    • 0022005315 scopus 로고
    • A cellular gene encodes scrapie PrP 27-30 protein
    • Oesch B, Westaway D, Wälchli M, et al. A cellular gene encodes scrapie PrP 27-30 protein. Cell 1985; 40:735-46.
    • (1985) Cell , vol.40 , pp. 735-746
    • Oesch, B.1    Westaway, D.2    Wälchli, M.3
  • 47
    • 0033081714 scopus 로고    scopus 로고
    • Agents that cause transmissible subacute spongiform encephalopathies
    • Dormont D. Agents that cause transmissible subacute spongiform encephalopathies. Biomed Pharmacother 1999; 53:3-8.
    • (1999) Biomed Pharmacother , vol.53 , pp. 3-8
    • Dormont, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.