메뉴 건너뛰기




Volumn 581, Issue 23, 2007, Pages 4544-4548

The whole hexapeptide repeats domain from avian PrP displays untypical hallmarks in aspect of the Cu2+ complexes formation

Author keywords

Avian prion protein; Cu2+ complexes; SOD activity

Indexed keywords

COPPER COMPLEX; COPPER ION; COPPER ZINC SUPEROXIDE DISMUTASE; HEXAPEPTIDE; PRION PROTEIN; SUPEROXIDE DISMUTASE;

EID: 34548454441     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.08.043     Document Type: Article
Times cited : (21)

References (32)
  • 3
    • 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. Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity. Exp. Neurol. 146 (1997) 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
  • 4
    • 0032169565 scopus 로고    scopus 로고
    • Prion protein expression and superoxide dismutase activity
    • Brown D.R., and Besinger A. Prion protein expression and superoxide dismutase activity. Biochem. J. 334 (1998) 423-429
    • (1998) Biochem. J. , vol.334 , pp. 423-429
    • Brown, D.R.1    Besinger, A.2
  • 6
    • 0035158321 scopus 로고    scopus 로고
    • Antioxidant activity related to copper binding of native prion protein
    • Brown D.R., Clive C., and Haswell S.J. Antioxidant activity related to copper binding of native prion protein. J. Neurochem. 76 (2001) 69-76
    • (2001) J. Neurochem. , vol.76 , pp. 69-76
    • Brown, D.R.1    Clive, C.2    Haswell, S.J.3
  • 7
    • 0032509499 scopus 로고    scopus 로고
    • Copper stimulates endocytosis of the prion protein
    • Pauly P.C., and Harris D.A. Copper stimulates endocytosis of the prion protein. J. Biol. Chem. 273 (1998) 33107-33110
    • (1998) J. Biol. Chem. , vol.273 , pp. 33107-33110
    • Pauly, P.C.1    Harris, D.A.2
  • 8
    • 27944486535 scopus 로고    scopus 로고
    • Assigning functions to distinct regions of the N-terminus of the prion protein that are involved in its copper-stimulated endocytosis
    • Taylor D.R., Watt N.T., Perera W.S., and Hooper N.M. Assigning functions to distinct regions of the N-terminus of the prion protein that are involved in its copper-stimulated endocytosis. J. Cell Sci. 118 (2005) 5141-5153
    • (2005) J. Cell Sci. , vol.118 , pp. 5141-5153
    • Taylor, D.R.1    Watt, N.T.2    Perera, W.S.3    Hooper, N.M.4
  • 10
    • 1242316297 scopus 로고    scopus 로고
    • Copper binding in the prion protein
    • Millhauser G.L. Copper binding in the prion protein. Acc. Chem. Res. 37 (2004) 79-85
    • (2004) Acc. Chem. Res. , vol.37 , pp. 79-85
    • Millhauser, G.L.1
  • 11
    • 0041302374 scopus 로고    scopus 로고
    • Cellular prion protein function in copper homeostasis and redox signalling at the synapse
    • Vassallo N., and Herms J. Cellular prion protein function in copper homeostasis and redox signalling at the synapse. J. Neurochem. 86 (2003) 538-544
    • (2003) J. Neurochem. , vol.86 , pp. 538-544
    • Vassallo, N.1    Herms, J.2
  • 12
    • 20544450600 scopus 로고    scopus 로고
    • Copper reduction by the octapeptide repeat region of prion protein: pH dependence and implications in cellular copper uptake
    • Miura T., Sasaki S., Toyama A., and Takeuchi H. Copper reduction by the octapeptide repeat region of prion protein: pH dependence and implications in cellular copper uptake. Biochemistry 44 (2005) 8712-8720
    • (2005) Biochemistry , vol.44 , pp. 8712-8720
    • Miura, T.1    Sasaki, S.2    Toyama, A.3    Takeuchi, H.4
  • 18
    • 33751430514 scopus 로고    scopus 로고
    • Can chicken and human PrPs possess SOD-like activity after beta-cleavage?
    • Stańczak P., and Kozłowski H. Can chicken and human PrPs possess SOD-like activity after beta-cleavage?. Biochem. Biophys. Res. Commun. 352 (2007) 198-202
    • (2007) Biochem. Biophys. Res. Commun. , vol.352 , pp. 198-202
    • Stańczak, P.1    Kozłowski, H.2
  • 20
    • 0025232814 scopus 로고
    • Solid-phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields G.B., and Noble R.L. Solid-phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int. J. Pept. Protein Res. 35 (1990) 161-214
    • (1990) Int. J. Pept. Protein Res. , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 21
    • 0000307259 scopus 로고
    • Determination of the equivalent point in potentiometric titrations
    • Gran G. Determination of the equivalent point in potentiometric titrations. Acta Chem. Scand. 4 (1950) 559-577
    • (1950) Acta Chem. Scand. , vol.4 , pp. 559-577
    • Gran, G.1
  • 23
    • 0013566107 scopus 로고
    • SUPERQUAD: an improved general program for computation of formation constants from potentiometric data
    • Gans P., Sabatini A., and Vacca A. SUPERQUAD: an improved general program for computation of formation constants from potentiometric data. J. Chem. Soc., Dalton Trans. (1985) 1195-1200
    • (1985) J. Chem. Soc., Dalton Trans. , pp. 1195-1200
    • Gans, P.1    Sabatini, A.2    Vacca, A.3
  • 24
    • 0030272334 scopus 로고    scopus 로고
    • Investigation of equilibria in solution. Determination of equilibrium constants with the HYPERQUAD suite of programs
    • Gans P., Sabatini A., and Vacca A. Investigation of equilibria in solution. Determination of equilibrium constants with the HYPERQUAD suite of programs. Talanta 43 (1996) 1739-1753
    • (1996) Talanta , vol.43 , pp. 1739-1753
    • Gans, P.1    Sabatini, A.2    Vacca, A.3
  • 25
    • 0015153416 scopus 로고
    • Superoxide dismutase: improved assays and an assay applicable to acrylamide gels
    • Beauchamp C., and Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 44 (1971) 276-287
    • (1971) Anal. Biochem. , vol.44 , pp. 276-287
    • Beauchamp, C.1    Fridovich, I.2
  • 29
    • 32444433270 scopus 로고    scopus 로고
    • Cu, Zn Superoxide dismutase: distorted active site binds substrate without significant energetic cost
    • Branco R.J.F., Fernandes P.A., and Ramos M.J. Cu, Zn Superoxide dismutase: distorted active site binds substrate without significant energetic cost. Theor. Chem. Acc. 115 (2006) 27-31
    • (2006) Theor. Chem. Acc. , vol.115 , pp. 27-31
    • Branco, R.J.F.1    Fernandes, P.A.2    Ramos, M.J.3
  • 30
    • 37049109773 scopus 로고
    • Specific binding of the tyrosine residue in copper (II) complexes of Tyr-Pro-Gly-Tyr and Tyr-Gly-Pro-Tyr
    • Pettit L.D., Steel I., Kowalik T., Kozlowski H., and Bataille M. Specific binding of the tyrosine residue in copper (II) complexes of Tyr-Pro-Gly-Tyr and Tyr-Gly-Pro-Tyr. J. Chem. Soc., Dalton Trans. (1985) 1201-1205
    • (1985) J. Chem. Soc., Dalton Trans. , pp. 1201-1205
    • Pettit, L.D.1    Steel, I.2    Kowalik, T.3    Kozlowski, H.4    Bataille, M.5
  • 31
    • 24744456323 scopus 로고    scopus 로고
    • Chattopadhyay, M., Walter, E.D., Newell, D.J., Jackson, P.J., Aronoff-Spencer, E., Peisach, J., Gerfen, G.J., Bennett, B., Antholine, W.E., and Millhauser, G.L., (2005) The octarepeat domain of the prion protein binds Cu(II) with three distinct coordination modes at pH 7.4. 127, 12647-12656.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.