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Volumn 392, Issue 2, 2005, Pages 309-312

Recombinant prion protein does not possess SOD-1 activity

Author keywords

Copper (II) ion; Neurodegenerative disorder; Oxidative stress; Prion protein (PrP); Superoxide dismutase (SOD) activity

Indexed keywords

COPPER; DISEASE CONTROL; IONS; OXIDATION; PATHOLOGY; STRESS ANALYSIS;

EID: 29144443530     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20051236     Document Type: Article
Times cited : (72)

References (32)
  • 3
    • 0014211846 scopus 로고
    • Does the agent of scrapie replicate without nucleic acid?
    • Alper, T., Cramp, W. A., Haig, D. A. and Clarke, M. C. (1967) Does the agent of scrapie replicate without nucleic acid? Nature (London) 214, 764-766
    • (1967) Nature (London) , vol.214 , pp. 764-766
    • Alper, T.1    Cramp, W.A.2    Haig, D.A.3    Clarke, M.C.4
  • 4
    • 0014190760 scopus 로고
    • Self replication and scrapie
    • Griffith, J. S. (1967) Self replication and scrapie. Nature (London) 215, 1043-1044
    • (1967) Nature (London) , vol.215 , pp. 1043-1044
    • Griffith, J.S.1
  • 5
    • 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
  • 6
    • 0029831213 scopus 로고    scopus 로고
    • Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD
    • Collinge, J., Sidle, K. C. L., Meads, J., Ironside, J. and Hill, A. F. (1996) Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature (London) 383, 685-690
    • (1996) Nature (London) , vol.383 , pp. 685-690
    • Collinge, J.1    Sidle, K.C.L.2    Meads, J.3    Ironside, J.4    Hill, A.F.5
  • 9
    • 0023663071 scopus 로고
    • Scrapie prion protein contains a phosphalidylinositol glycolipid
    • Stahl, N., Borchelt, D. R., Hsiao, K. and Prusiner, S. B. (1987) Scrapie prion protein contains a phosphalidylinositol glycolipid. Cell 51, 229-240
    • (1987) Cell , vol.51 , pp. 229-240
    • Stahl, N.1    Borchelt, D.R.2    Hsiao, K.3    Prusiner, S.B.4
  • 10
    • 0027534612 scopus 로고
    • Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing
    • Stahl, N., Baldwin, M. A., Teplow, D. B., Hood, L., Gibson, B. W., Burlingame, A. L. and Prusiner, S. B. (1993) Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32, 1991-2002
    • (1993) Biochemistry , vol.32 , pp. 1991-2002
    • Stahl, N.1    Baldwin, M.A.2    Teplow, D.B.3    Hood, L.4    Gibson, B.W.5    Burlingame, A.L.6    Prusiner, S.B.7
  • 12
    • 0030836511 scopus 로고    scopus 로고
    • NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231)
    • Riek, R., Hornemann, S., Wider, G., Glockshuber, R. and Wüthrich, K. (1997) NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413, 282-288
    • (1997) FEBS Lett. , vol.413 , pp. 282-288
    • Riek, R.1    Hornemann, S.2    Wider, G.3    Glockshuber, R.4    Wüthrich, K.5
  • 15
    • 0021672620 scopus 로고
    • Molecular characteristics of the major scrapie prion protein
    • Bolton, D. C., McKinley, M. P. and Prusiner, S. B. (1934) Molecular characteristics of the major scrapie prion protein. Biochemistry 23, 5898-5906
    • (1934) Biochemistry , vol.23 , pp. 5898-5906
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 16
    • 0020490156 scopus 로고
    • Identification of a protein that purifies with the scrapie prion
    • Bolton, D. C., McKinley, M. P. and Prusiner, S. B. (1982) Identification of a protein that purifies with the scrapie prion. Science 218, 1309-1311
    • (1982) Science , vol.218 , pp. 1309-1311
    • Bolton, D.C.1    McKinley, M.P.2    Prusiner, S.B.3
  • 18
  • 19
    • 0028911161 scopus 로고
    • The cellular prion protein (PrP) selectively binds to Bcl-2 in the yeast two-hybrid system
    • Kurschner, C. and Morgan, J. I. (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.I.2
  • 20
    • 0029932071 scopus 로고    scopus 로고
    • Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein
    • Kurschner, C. and Morgan, J. I. (1996) Analysis of interaction sites in homo- and heteromeric complexes containing Bcl-2 family members and the cellular prion protein. Mol. Brain Res. 37, 249-258
    • (1996) Mol. Brain Res. , vol.37 , pp. 249-258
    • Kurschner, C.1    Morgan, J.I.2
  • 23
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly, P. C. and Harris, D. A. (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
  • 24
    • 0031194455 scopus 로고    scopus 로고
    • Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
    • Brown, D. R., Schulz-Schaeffer, W. J., Schmidt, B. and Kretzschmar, H. A. (1997) Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 146, 104-112
    • (1997) Exp. Neurol. , vol.146 , pp. 104-112
    • Brown, D.R.1    Schulz-Schaeffer, W.J.2    Schmidt, B.3    Kretzschmar, H.A.4
  • 26
    • 0036301061 scopus 로고    scopus 로고
    • Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges
    • Gonzalez-Iglesias, R., Pajares, M. A., Ocal, C., Carlos, E. J., Oesch, B. and Gasset, M. (2002) Prion protein interaction with glycosaminoglycan occurs with the formation of oligomeric complexes stabilized by Cu(II) bridges. J. Mol. Biol. 319, 527-540
    • (2002) J. Mol. Biol. , vol.319 , pp. 527-540
    • Gonzalez-Iglesias, R.1    Pajares, M.A.2    Ocal, C.3    Carlos, E.J.4    Oesch, B.5    Gasset, M.6
  • 27
    • 0037018914 scopus 로고    scopus 로고
    • Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner
    • Ellis, V., Daniels, M., Misra, R. and Brown, D. R. (2002) Plasminogen activation is stimulated by prion protein and regulated in a copper-dependent manner. Biochemistry 41, 6891-6896
    • (2002) Biochemistry , vol.41 , pp. 6891-6896
    • Ellis, V.1    Daniels, M.2    Misra, R.3    Brown, D.R.4
  • 28
    • 0034764599 scopus 로고    scopus 로고
    • Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities
    • Wong, B. S., Brown, D. R., Pan, T., Whiteman, M., Liu, T., Bu, X., Li, R., Gambetti, P., Olesik, J., Rubenstein, R. and Sy, M. S. (2001) Oxidative impairment in scrapie-infected mice is associated with brain metals perturbations and altered antioxidant activities. J. Neurochem. 79, 689-698
    • (2001) J. Neurochem. , vol.79 , pp. 689-698
    • Wong, B.S.1    Brown, D.R.2    Pan, T.3    Whiteman, M.4    Liu, T.5    Bu, X.6    Li, R.7    Gambetti, P.8    Olesik, J.9    Rubenstein, R.10    Sy, M.S.11
  • 29
    • 0141717118 scopus 로고    scopus 로고
    • No superoxide dismutase activity of cellular prion protein in vivo
    • Hutter, G., Heppner, F. L. and Aguzzi, A. (2003) No superoxide dismutase activity of cellular prion protein in vivo. Biol. Chem. 384, 1279-1285
    • (2003) Biol. Chem. , vol.384 , pp. 1279-1285
    • Hutter, G.1    Heppner, F.L.2    Aguzzi, A.3
  • 32
    • 0027368497 scopus 로고
    • Spectrophotometric assay of superoxide dismutase activity based on the activated autoxidation of a tetracyclic catechol
    • Nebot, C., Moutet, M., Huet, P., Xu, J. Z., Yadan, J. C. and Chaudiere, J. (1993) Spectrophotometric assay of superoxide dismutase activity based on the activated autoxidation of a tetracyclic catechol. Anal. Biochem. 214, 442-451
    • (1993) Anal. Biochem. , vol.214 , pp. 442-451
    • Nebot, C.1    Moutet, M.2    Huet, P.3    Xu, J.Z.4    Yadan, J.C.5    Chaudiere, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.