메뉴 건너뛰기




Volumn 9, Issue 3, 2008, Pages 290-297

High pressure/temperature treatments to inactivate highly infectious prion subpopulations

Author keywords

263K strain; EIA; Enzyme immunoassay; High pressure; Inactivation kinetics; Prion inactivation; Prion infectivity; Scrapie prions

Indexed keywords

BIOASSAY; BIOMOLECULES; CHEMICAL STABILITY; FOOD PRESERVATION; HYDROSTATIC PRESSURE; INDUSTRIAL APPLICATIONS; KINETIC PARAMETERS;

EID: 43849083214     PISSN: 14668564     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ifset.2007.07.013     Document Type: Article
Times cited : (16)

References (41)
  • 2
    • 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., and Pocchiari M. Ultra-high-pressure inactivation of prion infectivity in processed meat: A practical method to prevent human infection. Proceedings of the National Academy of Sciences USA 100 (2003) 6093-6097
    • (2003) Proceedings of the National Academy of Sciences USA , vol.100 , pp. 6093-6097
    • Brown, P.1    Meyer, R.2    Cardone, F.3    Pocchiari, M.4
  • 4
    • 33646016587 scopus 로고    scopus 로고
    • Inactivation of transmissible spongiform encephalopathy agents in food products by ultra high pressure-temperature treatment
    • Cardone F., Brown P., Meyer R., and Pocchiari M. Inactivation of transmissible spongiform encephalopathy agents in food products by ultra high pressure-temperature treatment. Biochimica et Biophysica Acta-Proteins and Proteomics 1764 (2006) 558-562
    • (2006) Biochimica et Biophysica Acta-Proteins and Proteomics , vol.1764 , pp. 558-562
    • Cardone, F.1    Brown, P.2    Meyer, R.3    Pocchiari, M.4
  • 5
    • 0032006763 scopus 로고    scopus 로고
    • Heat resistance of prions and food processing
    • Casolari A. Heat resistance of prions and food processing. Food Microbiology 15 (1998) 59-63
    • (1998) Food Microbiology , vol.15 , pp. 59-63
    • Casolari, A.1
  • 6
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy
    • Caughey B.W., Dong A., Bhat K.S., Ernst D., Hayes S.F., and Caughey W.S. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochemistry 30 (1991) 7672-7680
    • (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
  • 7
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders
    • Caughey B., and Lansbury P.T. Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annual Review Neuroscience 26 (2003) 267-298
    • (2003) Annual Review Neuroscience , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 8
    • 3543030409 scopus 로고    scopus 로고
    • Hydration and packing effects on prion folding and beta-sheet conversion: High-pressure spectroscopy and pressure perturbation calorimetry studies
    • Cordeiro Y., Kraineva J., Ravindra R., Lima M.L.T.R., Gomes M.P.B., Foguel D., et al. Hydration and packing effects on prion folding and beta-sheet conversion: High-pressure spectroscopy and pressure perturbation calorimetry studies. Journal of Biological Chemistry 279 (2004) 32354-32359
    • (2004) Journal of Biological Chemistry , vol.279 , pp. 32354-32359
    • Cordeiro, Y.1    Kraineva, J.2    Ravindra, R.3    Lima, M.L.T.R.4    Gomes, M.P.B.5    Foguel, D.6
  • 10
    • 0037368005 scopus 로고    scopus 로고
    • Perspectives on prion biology, prion disease pathogenesis, and pharmacologic approaches to treatment
    • DeArmond S.J., and Prusiner S.B. Perspectives on prion biology, prion disease pathogenesis, and pharmacologic approaches to treatment. Clinical Chemistry and Laboratory Medicine 23 (2003) 1-41
    • (2003) Clinical Chemistry and Laboratory Medicine , vol.23 , pp. 1-41
    • DeArmond, S.J.1    Prusiner, S.B.2
  • 12
    • 0027405681 scopus 로고
    • Comparative analysis of scrapie agent inactivation methods
    • Ernst D.R., and Race R.E. Comparative analysis of scrapie agent inactivation methods. Journal of Virological Methods 41 (1993) 193-202
    • (1993) Journal of Virological Methods , vol.41 , pp. 193-202
    • Ernst, D.R.1    Race, R.E.2
  • 17
    • 33646010324 scopus 로고    scopus 로고
    • Protein conformation determines the sensibility to high pressure treatment of infectious scrapie prions
    • Heindl P., Fernandez Garcia A., Butz P., Pfaff E., and Tauscher B. Protein conformation determines the sensibility to high pressure treatment of infectious scrapie prions. Biochimica et Biophysica Acta 1764 (2006) 552-557
    • (2006) Biochimica et Biophysica Acta , vol.1764 , pp. 552-557
    • Heindl, P.1    Fernandez Garcia, A.2    Butz, P.3    Pfaff, E.4    Tauscher, B.5
  • 18
    • 0031714901 scopus 로고    scopus 로고
    • Protein structure and dynamics at high pressure
    • Heremans K., and Smeller L. Protein structure and dynamics at high pressure. Biochemica et Biophysica Acta 1386 (1998) 353-370
    • (1998) Biochemica et Biophysica Acta , vol.1386 , pp. 353-370
    • Heremans, K.1    Smeller, L.2
  • 22
    • 4444226434 scopus 로고    scopus 로고
    • Polymeric ligands with specificity for aggregated prion proteins
    • Lane A., Stanley C.J., Dealler S., and Wilson S.M. Polymeric ligands with specificity for aggregated prion proteins. Clinical Chemistry 49 (2003) 1774-1775
    • (2003) Clinical Chemistry , vol.49 , pp. 1774-1775
    • Lane, A.1    Stanley, C.J.2    Dealler, S.3    Wilson, S.M.4
  • 23
    • 33645960997 scopus 로고    scopus 로고
    • Protein stability and dynamics in the pressure-temperature plane
    • Meersman F., Smeller L., and Heremans K. Protein stability and dynamics in the pressure-temperature plane. Biochimica et Biophysica Acta 1764 (2006) 346-354
    • (2006) Biochimica et Biophysica Acta , vol.1764 , pp. 346-354
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 24
    • 0023226378 scopus 로고
    • Antisera to scrapie-associated fibril protein and prion protein decorate scrapie associated fibrils
    • Merz P.A., Kascsak R.J., Rubenstein R., Carp R.I., and Wisniewski H.M. Antisera to scrapie-associated fibril protein and prion protein decorate scrapie associated fibrils. Journal of Virology 61 (1987) 42-49
    • (1987) Journal of Virology , vol.61 , pp. 42-49
    • Merz, P.A.1    Kascsak, R.J.2    Rubenstein, R.3    Carp, R.I.4    Wisniewski, H.M.5
  • 26
    • 0030065265 scopus 로고    scopus 로고
    • High pressure effects on protein structure and function
    • Mozhaev V.V., Heremans K., Frank J., Masson P., and Balny C. High pressure effects on protein structure and function. Protein 24 (1996) 81-91
    • (1996) Protein , vol.24 , pp. 81-91
    • Mozhaev, V.V.1    Heremans, K.2    Frank, J.3    Masson, P.4    Balny, C.5
  • 27
    • 0000055079 scopus 로고    scopus 로고
    • Die Inaktivierung von Prionen durch Hitze
    • Hörnlimann B., Riesner D., and Kretzschmar H. (Eds), Walter de Gruyter, Berlin
    • Oberthür R.C. Die Inaktivierung von Prionen durch Hitze. In: Hörnlimann B., Riesner D., and Kretzschmar H. (Eds). Prionen und Prionkrankheiten (2001), Walter de Gruyter, Berlin 389-398
    • (2001) Prionen und Prionkrankheiten , pp. 389-398
    • Oberthür, R.C.1
  • 30
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles causes scrapie
    • Prusiner S.B. Novel proteinaceous infectious particles causes scrapie. Science 216 (1982) 136-144
    • (1982) Science , vol.216 , pp. 136-144
    • Prusiner, S.B.1
  • 32
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner S.B. Molecular biology of prion diseases. Science 252 (1991) 1515-1522
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 35
    • 0037171154 scopus 로고    scopus 로고
    • High hydrostatic pressure as a tool to study protein aggregation and amyloidosis
    • Randolph T.W., Seefeldt M., and Carpenter J.F. High hydrostatic pressure as a tool to study protein aggregation and amyloidosis. Biochemica et Biophysica Acta 1595 (2002) 224-234
    • (2002) Biochemica et Biophysica Acta , vol.1595 , pp. 224-234
    • Randolph, T.W.1    Seefeldt, M.2    Carpenter, J.F.3
  • 36
    • 0021323390 scopus 로고
    • Virus like sensitivity of the scrapie agent to heat inactivation
    • Rohwer R.G. Virus like sensitivity of the scrapie agent to heat inactivation. Science 223 (1984) 600-602
    • (1984) Science , vol.223 , pp. 600-602
    • Rohwer, R.G.1
  • 40
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • Silva J.L., Foguel D., and Royer C. Pressure provides new insights into protein folding, dynamics and structure. Trends in Biochemical Sciences 26 (2001) 612-618
    • (2001) Trends in Biochemical Sciences , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.