메뉴 건너뛰기




Volumn 356, Issue 1, 2007, Pages 245-248

Prion inactivation by the Maillard reaction

Author keywords

Bioassay; Maillard reaction; Meat and bone meal; Prion inactivation; Protein misfolding cyclic amplification

Indexed keywords

BICARBONATE; GLUCOSE; PRION PROTEIN;

EID: 33947146522     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.02.113     Document Type: Article
Times cited : (10)

References (24)
  • 1
    • 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
  • 2
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein PrP27-30 in water by infrared spectroscopy
    • Caughey B.W., Dong A., Bhat K.S., Ernst D., Hayes S.F., and Caughey F.S. Secondary structure analysis of the scrapie-associated protein PrP27-30 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, F.S.6
  • 4
    • 0034724227 scopus 로고    scopus 로고
    • New studies on the heat resistance of hamster-adapted scrapie agent: threshold survival after ashing at 600 degrees C suggests an inorganic template of replication
    • Brown P., Rau E.H., Johnson B.K., Bacote A.E., Gibbs C.J., and Gajdusek D.C. New studies on the heat resistance of hamster-adapted scrapie agent: threshold survival after ashing at 600 degrees C suggests an inorganic template of replication. Proc. Natl. Acad. Sci. USA 97 (2000) 3418-3421
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3418-3421
    • Brown, P.1    Rau, E.H.2    Johnson, B.K.3    Bacote, A.E.4    Gibbs, C.J.5    Gajdusek, D.C.6
  • 5
    • 0035757574 scopus 로고    scopus 로고
    • Resistance of transmissible spongiform encephalopathy agents to decontamination
    • Rabenau H.F., Ciantl J., and Doerr H.W. (Eds), Karger, Basel
    • Taylor D.M. Resistance of transmissible spongiform encephalopathy agents to decontamination. In: Rabenau H.F., Ciantl J., and Doerr H.W. (Eds). Prions. A challenge for science, medicine and public health system (2001), Karger, Basel 58-67
    • (2001) Prions. A challenge for science, medicine and public health system , pp. 58-67
    • Taylor, D.M.1
  • 7
    • 0024290760 scopus 로고
    • Bovine spongiform encephalopathy: epidemiological studies
    • Wilesmith J.W., Wells G.A.H., Cranwell M.P., and Ryan J.B. Bovine spongiform encephalopathy: epidemiological studies. Vet. Rec. 123 (1988) 638-644
    • (1988) Vet. Rec. , vol.123 , pp. 638-644
    • Wilesmith, J.W.1    Wells, G.A.H.2    Cranwell, M.P.3    Ryan, J.B.4
  • 8
    • 0026412979 scopus 로고
    • Bovine spongiform encephalopathy: epidemiological studies on the origin
    • Wilesmith J.W., Ryan J.B.M., and Atkinson M.J. Bovine spongiform encephalopathy: epidemiological studies on the origin. Vet. Rec. 128 (1991) 199-203
    • (1991) Vet. Rec. , vol.128 , pp. 199-203
    • Wilesmith, J.W.1    Ryan, J.B.M.2    Atkinson, M.J.3
  • 9
    • 0026813024 scopus 로고
    • Bovine spongiform encephalopathy: epidemiological features 1985 to 1990
    • Wilesmith J.W., Ryan J.B.M., Hueston W.D., and Hoinville L.J. Bovine spongiform encephalopathy: epidemiological features 1985 to 1990. Vet. Rec. 130 (1992) 90-94
    • (1992) Vet. Rec. , vol.130 , pp. 90-94
    • Wilesmith, J.W.1    Ryan, J.B.M.2    Hueston, W.D.3    Hoinville, L.J.4
  • 10
    • 0021285458 scopus 로고
    • Nonenzymatic glucosylation of lysine residues in albumin
    • Baynes J.W., Thorpe S.R., and Murtiashaw M.H. Nonenzymatic glucosylation of lysine residues in albumin. Methods Enzymol. 106 (1984) 88-98
    • (1984) Methods Enzymol. , vol.106 , pp. 88-98
    • Baynes, J.W.1    Thorpe, S.R.2    Murtiashaw, M.H.3
  • 11
    • 0035968307 scopus 로고    scopus 로고
    • Formation pathways for lysine-arginine cross-links derived from hexoses and pentoses by Maillard processes
    • Biemel K.M., Reihl O., Conrad J., and Lederer M.O. Formation pathways for lysine-arginine cross-links derived from hexoses and pentoses by Maillard processes. J. Biol. Chem. 276 (2001) 23405-23412
    • (2001) J. Biol. Chem. , vol.276 , pp. 23405-23412
    • Biemel, K.M.1    Reihl, O.2    Conrad, J.3    Lederer, M.O.4
  • 12
    • 0036441178 scopus 로고    scopus 로고
    • Oxidative deamination of lysine residue in plasma protein of diabetic rats. Novel mechanism via the Maillard reaction
    • Akagawa M., Sasaki T., and Suyama K. Oxidative deamination of lysine residue in plasma protein of diabetic rats. Novel mechanism via the Maillard reaction. Eur. J. Biochem. 269 (2002) 5451-5458
    • (2002) Eur. J. Biochem. , vol.269 , pp. 5451-5458
    • Akagawa, M.1    Sasaki, T.2    Suyama, K.3
  • 13
    • 0346731073 scopus 로고    scopus 로고
    • Maillard reaction products in tissue proteins: new products and new perspectives
    • Thorpe S.R., and Baynes J.W. Maillard reaction products in tissue proteins: new products and new perspectives. Amino Acids 25 (2003) 275-281
    • (2003) Amino Acids , vol.25 , pp. 275-281
    • Thorpe, S.R.1    Baynes, J.W.2
  • 14
    • 23744453195 scopus 로고    scopus 로고
    • Formation of α-aminoadipic and γ-glutamic semialdehydes in proteins by the Maillard reaction
    • Akagawa M., Sasaki D., Kurota Y., and Suyama K. Formation of α-aminoadipic and γ-glutamic semialdehydes in proteins by the Maillard reaction. Ann. N. Y. Acad. Sci. 1043 (2005) 129-134
    • (2005) Ann. N. Y. Acad. Sci. , vol.1043 , pp. 129-134
    • Akagawa, M.1    Sasaki, D.2    Kurota, Y.3    Suyama, K.4
  • 15
    • 0034470581 scopus 로고    scopus 로고
    • On the influence of the carbohydrate moiety on chromophore formation during food-related Maillard reaction of pentoses, hexoses, and disaccharides
    • Frank O., and Hofmann T. On the influence of the carbohydrate moiety on chromophore formation during food-related Maillard reaction of pentoses, hexoses, and disaccharides. Helv. Chim. Acta 83 (2000) 3246-3264
    • (2000) Helv. Chim. Acta , vol.83 , pp. 3246-3264
    • Frank, O.1    Hofmann, T.2
  • 16
    • 33645185054 scopus 로고
    • Preparation of N-substituted 1-amino-1-deoxy-d-arabino-hexuloses of arginine, histidine, and lysine
    • Lowy P.H., and Noak H. Preparation of N-substituted 1-amino-1-deoxy-d-arabino-hexuloses of arginine, histidine, and lysine. J. Am. Chem. Soc. 78 (1956) 3175-3179
    • (1956) J. Am. Chem. Soc. , vol.78 , pp. 3175-3179
    • Lowy, P.H.1    Noak, H.2
  • 17
    • 0035859102 scopus 로고    scopus 로고
    • Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding
    • Saborio G.P., Permanne B., and Soto C. Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411 (2001) 810-813
    • (2001) Nature , vol.411 , pp. 810-813
    • Saborio, G.P.1    Permanne, B.2    Soto, C.3
  • 18
    • 33845944898 scopus 로고    scopus 로고
    • Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification
    • Saá P., Castilla J., and Soto C. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J. Biol. Chem. 281 (2006) 35245-35252
    • (2006) J. Biol. Chem. , vol.281 , pp. 35245-35252
    • Saá, P.1    Castilla, J.2    Soto, C.3
  • 20
    • 33947137941 scopus 로고
    • Lysine-catalyzed Maillard browning of sugar-related compounds smaller than tetrose, in neutral and alkaline solution
    • Takagi M., and Morita N. Lysine-catalyzed Maillard browning of sugar-related compounds smaller than tetrose, in neutral and alkaline solution. Dev. Food Sci. 13 (1985) 49-57
    • (1985) Dev. Food Sci. , vol.13 , pp. 49-57
    • Takagi, M.1    Morita, N.2
  • 21
    • 0000792774 scopus 로고
    • The effect of activity of water, of pH, and of temperature on the primary reaction between casein and glucose
    • Lea C.H., and Hannan R.S. The effect of activity of water, of pH, and of temperature on the primary reaction between casein and glucose. Biochem. Biophys. Acta 3 (1949) 315-325
    • (1949) Biochem. Biophys. Acta , vol.3 , pp. 315-325
    • Lea, C.H.1    Hannan, R.S.2
  • 22
    • 84982334315 scopus 로고
    • Browning of sugar solutions. 3. Effects of pH on the color produced in dilute glucose solutions containing amino acid with amino group in different positions in molecule
    • Underwood J.C., Lento H.G., and Willets C.O. Browning of sugar solutions. 3. Effects of pH on the color produced in dilute glucose solutions containing amino acid with amino group in different positions in molecule. J. Chem. Soc. 1959 (1959) 181-184
    • (1959) J. Chem. Soc. , vol.1959 , pp. 181-184
    • Underwood, J.C.1    Lento, H.G.2    Willets, C.O.3
  • 23
    • 0028876414 scopus 로고
    • Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent
    • Race R.E., Priola S.A., Bessen R.A., Ernst D., Dockter J., Rall G.F., Mucke L., Chesebro B., and Oldstone M.B. Neuron-specific expression of a hamster prion protein minigene in transgenic mice induces susceptibility to hamster scrapie agent. Neuron 15 (1995) 1183-1191
    • (1995) Neuron , vol.15 , pp. 1183-1191
    • Race, R.E.1    Priola, S.A.2    Bessen, R.A.3    Ernst, D.4    Dockter, J.5    Rall, G.F.6    Mucke, L.7    Chesebro, B.8    Oldstone, M.B.9
  • 24
    • 22444432021 scopus 로고    scopus 로고
    • Historical perspective of the Maillard reaction in food science, the Maillard reaction-chemistry at the interface of nutrition, aging and disease
    • Finot P.A. Historical perspective of the Maillard reaction in food science, the Maillard reaction-chemistry at the interface of nutrition, aging and disease. Ann. N. Y. Acad. Sci. 1043 (2005) 1-8
    • (2005) Ann. N. Y. Acad. Sci. , vol.1043 , pp. 1-8
    • Finot, P.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.