메뉴 건너뛰기




Volumn 73, Issue 3, 1999, Pages 1288-1292

Cysteine 144 is a key residue in the copper reduction by the β-amyloid precursor protein

Author keywords

Amyloid precursor protein; Alzheimer's disease; Copper reduction

Indexed keywords

AMYLOID PRECURSOR PROTEIN; COPPER; CYSTEINE; SYNTHETIC PEPTIDE;

EID: 0345035452     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0731288.x     Document Type: Article
Times cited : (50)

References (19)
  • 1
    • 0030061861 scopus 로고    scopus 로고
    • Extracellular matrix regulates the amount of the β-amyloid precursor protein and its amyloidogenic fragments
    • Bronfman F. C., Soto C., Tapia L., Tapia V., and Inestrosa N. C. (1996) Extracellular matrix regulates the amount of the β-amyloid precursor protein and its amyloidogenic fragments. J. Cell Physiol. 166, 360-369.
    • (1996) J. Cell Physiol. , vol.166 , pp. 360-369
    • Bronfman, F.C.1    Soto, C.2    Tapia, L.3    Tapia, V.4    Inestrosa, N.C.5
  • 2
    • 0029832894 scopus 로고    scopus 로고
    • Application of compartmental modeling to determination of trace element requirements in humans
    • Buckley W. T. (1996) Application of compartmental modeling to determination of trace element requirements in humans. J. Nutr. 126, 2312S-2319S.
    • (1996) J. Nutr. , vol.126
    • Buckley, W.T.1
  • 3
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals. II. Modification of amino acids
    • Davies K. J. A., Delsignore M. A., and Lin S. W. (1987) Protein damage and degradation by oxygen radicals. II. Modification of amino acids. J. Biol. Chem. 262, 9902-9907.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9902-9907
    • Davies, K.J.A.1    Delsignore, M.A.2    Lin, S.W.3
  • 4
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell B. and Gutteridge J. M. C. (1984) Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219, 1-14.
    • (1984) Biochem. J. , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 5
    • 0028799741 scopus 로고
    • Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae
    • Hassett R. and Kosman D. J. (1995) Evidence for Cu(II) reduction as a component of copper uptake by Saccharomyces cerevisiae. J. Biol. Chem. 270, 128-134.
    • (1995) J. Biol. Chem. , vol.270 , pp. 128-134
    • Hassett, R.1    Kosman, D.J.2
  • 6
    • 0028177269 scopus 로고
    • The βA4 amyloid precursor protein binding to copper
    • Hesse L., Beher D., Masters C. L., and Multhaup G. (1994) The βA4 amyloid precursor protein binding to copper. FEBS Lett. 349, 109-116.
    • (1994) FEBS Lett. , vol.349 , pp. 109-116
    • Hesse, L.1    Beher, D.2    Masters, C.L.3    Multhaup, G.4
  • 7
    • 0023219731 scopus 로고
    • Acetylcholinesterase from bovine caudate nucleus is attached to membranes by novel subunit distinct from those of acetylcholinesterase in other tissues
    • Inestrosa N. C., Roberts W. L., Marshall T. L., and Rosenberry T. L. (1987) Acetylcholinesterase from bovine caudate nucleus is attached to membranes by novel subunit distinct from those of acetylcholinesterase in other tissues. J. Biol. Chem. 262, 4441-4444.
    • (1987) J. Biol. Chem. , vol.262 , pp. 4441-4444
    • Inestrosa, N.C.1    Roberts, W.L.2    Marshall, T.L.3    Rosenberry, T.L.4
  • 8
    • 0029863697 scopus 로고    scopus 로고
    • Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's amyloid fibrils: Possible role of the peripheral binding site of the enzyme
    • Inestrosa N. C., Alvarez A., Pérez C., Moreno R., Vicente M., Lincker C., Soto C., and Garrido J. (1996) Acetylcholinesterase accelerates assembly of amyloid-β-peptides into Alzheimer's amyloid fibrils: possible role of the peripheral binding site of the enzyme. Neuron 16, 881-891.
    • (1996) Neuron , vol.16 , pp. 881-891
    • Inestrosa, N.C.1    Alvarez, A.2    Pérez, C.3    Moreno, R.4    Vicente, M.5    Lincker, C.6    Soto, C.7    Garrido, J.8
  • 9
    • 0030839796 scopus 로고    scopus 로고
    • N-terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes' disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat
    • Lutsenko S., Petrukhin K., Cooper M. J., Gillian C. T., and Kaplan J. H. (1997) N-Terminal domains of human copper-transporting adenosine triphosphatases (the Wilson's and Menkes' disease proteins) bind copper selectively in vivo and in vitro with stoichiometry of one copper per metal-binding repeat. J. Biol. Chem. 272, 18939-18944.
    • (1997) J. Biol. Chem. , vol.272 , pp. 18939-18944
    • Lutsenko, S.1    Petrukhin, K.2    Cooper, M.J.3    Gillian, C.T.4    Kaplan, J.H.5
  • 10
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper (II) to copper (I)
    • Multhaup G., Schlicksupp A., Hess L., Beher D., Ruppert T., Masters C. L., and Beyreuther K. (1996) The amyloid precursor protein of Alzheimer's disease in the reduction of copper (II) to copper (I). Science 271, 1406-1409.
    • (1996) Science , vol.271 , pp. 1406-1409
    • Multhaup, G.1    Schlicksupp, A.2    Hess, L.3    Beher, D.4    Ruppert, T.5    Masters, C.L.6    Beyreuther, K.7
  • 11
    • 0032546577 scopus 로고    scopus 로고
    • Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide
    • Multhaup G., Ruppert T., Schlicksupp A., Hess L., Bill E., Pipkorn R., Masters C. L., and Beyreuther K. (1998) Copper-binding amyloid precursor protein undergoes a site-specific fragmentation in the reduction of hydrogen peroxide. Biochemistry 37, 7224-7230.
    • (1998) Biochemistry , vol.37 , pp. 7224-7230
    • Multhaup, G.1    Ruppert, T.2    Schlicksupp, A.3    Hess, L.4    Bill, E.5    Pipkorn, R.6    Masters, C.L.7    Beyreuther, K.8
  • 12
    • 0031891944 scopus 로고    scopus 로고
    • Crosslinking of amyloid-ß peptide to brain acetylcholinesterase
    • Opazo C. and Inestrosa N. C. (1998) Crosslinking of amyloid-ß peptide to brain acetylcholinesterase. Mol. Chem. Neuropathol. 33, 39-49.
    • (1998) Mol. Chem. Neuropathol. , vol.33 , pp. 39-49
    • Opazo, C.1    Inestrosa, N.C.2
  • 15
    • 0032211830 scopus 로고    scopus 로고
    • The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease
    • Selkoe D. J. (1998) The cell biology of β-amyloid precursor protein and presenilin in Alzheimer's disease. Trends Cell Biol. 8, 447-453.
    • (1998) Trends Cell Biol. , vol.8 , pp. 447-453
    • Selkoe, D.J.1
  • 16
    • 0028031486 scopus 로고
    • Structural determinants of the Alzheimer's amyloid β-peptide
    • Soto C., Brañes M. C., Alvarez J., and Inestrosa N. C. (1994) Structural determinants of the Alzheimer's amyloid β-peptide. J. Neurochem. 63, 1191-1198.
    • (1994) J. Neurochem. , vol.63 , pp. 1191-1198
    • Soto, C.1    Brañes, M.C.2    Alvarez, J.3    Inestrosa, N.C.4
  • 17
    • 0030467256 scopus 로고    scopus 로고
    • Biochemical characterization and intracellular localization of the Menkes disease protein
    • Yamaguchi Y., Heiny M. E., Suzuki M., and Gitlin J. (1996) Biochemical characterization and intracellular localization of the Menkes disease protein. Proc. Natl. Acad. Sci. USA 93, 14030-14035.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 14030-14035
    • Yamaguchi, Y.1    Heiny, M.E.2    Suzuki, M.3    Gitlin, J.4
  • 18
    • 0029896354 scopus 로고    scopus 로고
    • Mechanisms of neuronal degeneration in Alzheimer's disease
    • Yankner B. A. (1996) Mechanisms of neuronal degeneration in Alzheimer's disease. Neuron 16, 921-932.
    • (1996) Neuron , vol.16 , pp. 921-932
    • Yankner, B.A.1
  • 19
    • 0030844529 scopus 로고    scopus 로고
    • hCTR1: A human gene for copper uptake identified by complementation in yeast
    • Zhou B. and Gitschier J. (1997) hCTR1: a human gene for copper uptake identified by complementation in yeast. Proc. Natl. Acad. Sci. USA 94, 7481-7486.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7481-7486
    • Zhou, B.1    Gitschier, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.