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Volumn 10, Issue 3, 1998, Pages 181-192

Amyloid β-peptide(1-40)-mediated oxidative stress in cultured hippocampal neurons: Protein carbonyl formation, CK BB expression, and the level of Cu, Zn, and Mn SOD mRNA

Author keywords

Amyloid peptide; CK BB; Oxidative stress; Protein carbonyls; SOD

Indexed keywords

AMYLOID BETA PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; CREATINE KINASE BB; MESSENGER RNA;

EID: 0031753798     PISSN: 08958696     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02761773     Document Type: Article
Times cited : (43)

References (57)
  • 1
    • 0030657456 scopus 로고    scopus 로고
    • Oxidative modification of glutamine synthetase by amyloid beta peptide
    • Aksenov M. Y., Aksenova M. V., Carney J. M., and Butterfield D. A. (1997a) Oxidative modification of glutamine synthetase by amyloid beta peptide. Free Radical Res, 27, 267-281.
    • (1997) Free Radical Res , vol.27 , pp. 267-281
    • Aksenov, M.Y.1    Aksenova, M.V.2    Carney, J.M.3    Butterfield, D.A.4
  • 2
    • 0031213840 scopus 로고    scopus 로고
    • The expression of creatine kinase isoenzymes in neocortex of patients with neurodegenerative disorders: Alzheimer's and Pick's disease
    • Aksenov M. Y., Aksenova M. V., Payne R. M., Smith C. D., Markesbery W. R., and Carney J. (1997b) The expression of creatine kinase isoenzymes in neocortex of patients with neurodegenerative disorders: Alzheimer's and Pick's disease. Exp. Neurol. 146, 458-465.
    • (1997) Exp. Neurol. , vol.146 , pp. 458-465
    • Aksenov, M.Y.1    Aksenova, M.V.2    Payne, R.M.3    Smith, C.D.4    Markesbery, W.R.5    Carney, J.6
  • 3
    • 0026045294 scopus 로고
    • Oxygen metabolite effects on creatine kinase and cardiac energetics after reperfusion
    • Banerjee A., Grosso M. A., Brown J. M., Rogers K. B., and Whitman G. J. R. (1991) Oxygen metabolite effects on creatine kinase and cardiac energetics after reperfusion. Am. J. Physiol. 261, H590-H597.
    • (1991) Am. J. Physiol. , vol.261
    • Banerjee, A.1    Grosso, M.A.2    Brown, J.M.3    Rogers, K.B.4    Whitman, G.J.R.5
  • 4
    • 0030612205 scopus 로고    scopus 로고
    • Mechanism of amyloid beta protein induced neuronal cell death: Current concepts and future perspectives
    • Behl C. and Sagara Y. (1997) Mechanism of amyloid beta protein induced neuronal cell death: current concepts and future perspectives. J. Neural Trans. Suppl. 49, 125-134.
    • (1997) J. Neural Trans. Suppl. , vol.49 , pp. 125-134
    • Behl, C.1    Sagara, Y.2
  • 5
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shutle
    • Bessman S. P. (1985) The creatine-creatine phosphate energy shutle. Annu. Rev. Biochem. 54, 831.
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 831
    • Bessman, S.P.1
  • 6
    • 0028936986 scopus 로고
    • Bioenergetic and oxidative stress in neurodegenerative diseases
    • Bowling A. C. and Beal M. F. (1995) Bioenergetic and oxidative stress in neurodegenerative diseases. Life Sci. 56, 1151-1171.
    • (1995) Life Sci. , vol.56 , pp. 1151-1171
    • Bowling, A.C.1    Beal, M.F.2
  • 7
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented neurobasal, a new serum-free medium combination
    • Brewer G. J., Torricelli J. R., Evege E. K., and Price P. J. (1993) Optimized survival of hippocampal neurons in B27-supplemented neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35, 567-576.
    • (1993) J. Neurosci. Res. , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 8
    • 0026577487 scopus 로고
    • Decreased level of creatine kinase BB in the frontal cortex of Alzheimer patients
    • Burbaeva G. S., Aksenova M. V., Makarenko I. G. (1992) Decreased level of creatine kinase BB in the frontal cortex of Alzheimer patients. Dementia 3, 91-94.
    • (1992) Dementia , vol.3 , pp. 91-94
    • Burbaeva, G.S.1    Aksenova, M.V.2    Makarenko, I.G.3
  • 9
    • 0030928406 scopus 로고    scopus 로고
    • β-Amyloid-associated free radical oxidative stress and neurotoxicity: Implications for Alzheimer's disease
    • Butterfield D. A. (1997) β-Amyloid-associated free radical oxidative stress and neurotoxicity: implications for Alzheimer's disease. Chem. Res. Toxicol. 10, 495-506.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 495-506
    • Butterfield, D.A.1
  • 10
    • 0028178837 scopus 로고
    • β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: Implications to Alzheimer's disease
    • Butterfield D. A., Hensley K., Harris M., Mattson M., and Carney J. (1994) β-Amyloid peptide free radical fragments initiate synaptosomal lipoperoxidation in a sequence-specific fashion: implications to Alzheimer's disease. Biochem. Biophys. Res. Commun. 200, 710-715.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 710-715
    • Butterfield, D.A.1    Hensley, K.2    Harris, M.3    Mattson, M.4    Carney, J.5
  • 11
    • 0342761759 scopus 로고    scopus 로고
    • Beta-amyloid-derived free radical oxidation: A fundamental process in Alzheimer's disease
    • Tanzi R. E. and Wasco W., eds., Humana, Totowa, NJ
    • Butterfield D. A., Hensley K., Hall N., Subramaniam R., Howard B. J., Cole P., et al. (1996) Beta-amyloid-derived free radical oxidation: a fundamental process in Alzheimer's disease, in Molecular Models of Dementia (Tanzi R. E. and Wasco W., eds.), Humana, Totowa, NJ, pp. 145-167.
    • (1996) Molecular Models of Dementia , pp. 145-167
    • Butterfield, D.A.1    Hensley, K.2    Hall, N.3    Subramaniam, R.4    Howard, B.J.5    Cole, P.6
  • 12
    • 0030071207 scopus 로고    scopus 로고
    • Oxidative stress after acute and chronic application of β-amyloid fragment 25-35 in cortical ciltures
    • Cafe C., Torri C., Bertorelli L., Angeretti N., Lucca E., Forloni G., and Marzatico F. (1996) Oxidative stress after acute and chronic application of β-amyloid fragment 25-35 in cortical ciltures. Neurosci. Lett. 203, 61-65.
    • (1996) Neurosci. Lett. , vol.203 , pp. 61-65
    • Cafe, C.1    Torri, C.2    Bertorelli, L.3    Angeretti, N.4    Lucca, E.5    Forloni, G.6    Marzatico, F.7
  • 13
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinum thiocyanate-phenol-chloroform extraction
    • Chromczynski P. and Sacchi N. (1987) Single-step method of RNA isolation by acid guanidinum thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chromczynski, P.1    Sacchi, N.2
  • 14
    • 0030513849 scopus 로고    scopus 로고
    • Oxidative mechanisms in beta-amyloid cytotoxicity
    • Davis J. B. (1996) Oxidative mechanisms in beta-amyloid cytotoxicity. Neurodegeneration 5, 441-144.
    • (1996) Neurodegeneration , vol.5 , pp. 441-1144
    • Davis, J.B.1
  • 15
    • 0028983336 scopus 로고
    • Amyloid beta-protein induces its own production in cultured degenerating cerebrovascular smooth muscle cells
    • Davis-Salinas J., Saporito-Irwin S. M., Cotman C. W., and Van Nostrand W. E. (1995) Amyloid beta-protein induces its own production in cultured degenerating cerebrovascular smooth muscle cells. J. Neurochem. 65, 931-934.
    • (1995) J. Neurochem. , vol.65 , pp. 931-934
    • Davis-Salinas, J.1    Saporito-Irwin, S.M.2    Cotman, C.W.3    Van Nostrand, W.E.4
  • 16
    • 0030808462 scopus 로고    scopus 로고
    • Aggregated amyloid-β protein induces cortical neuronal apoptosis and concominant "apoptotic" pattern of gene induction
    • Estus S., Tucker H. M., van Rooyen C., Wright S., Brigham E., Wogulis M., et al. (1997) Aggregated amyloid-β protein induces cortical neuronal apoptosis and concominant "apoptotic" pattern of gene induction. J. Neurosci. 17, 7736-7745.
    • (1997) J. Neurosci. , vol.17 , pp. 7736-7745
    • Estus, S.1    Tucker, H.M.2    Van Rooyen, C.3    Wright, S.4    Brigham, E.5    Wogulis, M.6
  • 17
    • 0028216311 scopus 로고
    • Compartmentation of brain-type creatine kinase and ubiquitous mitochondrial creatine kinase in neurons: Evidence for a creatine phosphate energy shuttle in adult rat brain
    • Friedman D. L. and Roberts R. (1994) Compartmentation of brain-type creatine kinase and ubiquitous mitochondrial creatine kinase in neurons: evidence for a creatine phosphate energy shuttle in adult rat brain. J. Comp. Neurol. 343, 500-511.
    • (1994) J. Comp. Neurol. , vol.343 , pp. 500-511
    • Friedman, D.L.1    Roberts, R.2
  • 18
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
    • Games D., Adams D., Alessandrini R., Barbour R., Berthelette P., Blackwell C., et al. (1995) Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein. Nature 373, 523-527.
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3    Barbour, R.4    Berthelette, P.5    Blackwell, C.6
  • 20
    • 0022764985 scopus 로고
    • Antibody probing on Western blots have been stained with india ink
    • Glenney J. R. (1986) Antibody probing on Western blots have been stained with india ink. Anal. Biochem. 156, 315-318.
    • (1986) Anal. Biochem. , vol.156 , pp. 315-318
    • Glenney, J.R.1
  • 21
    • 0028908516 scopus 로고
    • Direct evidence of oxidative injury by the Alzheimer's amyloid β-peptide in cultured hippocampal neurons
    • Harris M. E., Hensley K., Butterfield D. A., Leedle R. E., and Carney J. M. (1995) Direct evidence of oxidative injury by the Alzheimer's amyloid β-peptide in cultured hippocampal neurons. Exp. Neurol. 131, 193-202.
    • (1995) Exp. Neurol. , vol.131 , pp. 193-202
    • Harris, M.E.1    Hensley, K.2    Butterfield, D.A.3    Leedle, R.E.4    Carney, J.M.5
  • 22
    • 0027724925 scopus 로고
    • Functional aspects of creatine kinase in brain
    • Hemmer W. and Walliman T. (1993) Functional aspects of creatine kinase in brain. Dev. Neurosci. 15, 249-260.
    • (1993) Dev. Neurosci. , vol.15 , pp. 249-260
    • Hemmer, W.1    Walliman, T.2
  • 23
    • 0028180518 scopus 로고
    • A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: Relevance to Alzheimer's disease
    • Hensley K., Carney J. M., Mattson M. P., Aksenova M. V., Harris M. E., Wu J. F., et al. (1994) A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer's disease. Proc. Natl. Acad. Sci. USA 91, 3270-3274.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3270-3274
    • Hensley, K.1    Carney, J.M.2    Mattson, M.P.3    Aksenova, M.V.4    Harris, M.E.5    Wu, J.F.6
  • 24
    • 0028985210 scopus 로고
    • Amyloid β-peptide spin trapping I: Peptide enzyme toxicity is related to free radical spin trap reactivity
    • Hensley K., Aksenova M., Carney J. M., Harris M., and Butterfield D. A. (1995) Amyloid β-peptide spin trapping I: peptide enzyme toxicity is related to free radical spin trap reactivity. Neuroreport 6, 489-492.
    • (1995) Neuroreport , vol.6 , pp. 489-492
    • Hensley, K.1    Aksenova, M.2    Carney, J.M.3    Harris, M.4    Butterfield, D.A.5
  • 25
    • 0030090426 scopus 로고    scopus 로고
    • Changes in gene transcription during a beta-mediated cell death
    • Iwasaki K., Sunderland T., Kusiak J. W., and Wolozin B. (1996) Changes in gene transcription during a beta-mediated cell death. Mol. Psych. 1, 65-71.
    • (1996) Mol. Psych. , vol.1 , pp. 65-71
    • Iwasaki, K.1    Sunderland, T.2    Kusiak, J.W.3    Wolozin, B.4
  • 26
    • 0028850087 scopus 로고
    • Suppression of mitochondrial succinate dehydrogenase, a primary target of β-amyloid, and its derivative racemized at Ser residue
    • Kaneko I., Yamada N., Sakuraba Y., Kamenosomo M., and Tutumi S. (1995) Suppression of mitochondrial succinate dehydrogenase, a primary target of β-amyloid, and its derivative racemized at Ser residue. J. Neurochem. 65, 2585-2593.
    • (1995) J. Neurochem. , vol.65 , pp. 2585-2593
    • Kaneko, I.1    Yamada, N.2    Sakuraba, Y.3    Kamenosomo, M.4    Tutumi, S.5
  • 27
    • 0029900084 scopus 로고    scopus 로고
    • Amyloid β-peptide disrupts carbachol-induced muscarinic cholinergic signal transduction in cortical neurons: Involvement of free radicals
    • Kelly J., Furukawa K., Barger S. W., Mark R. J., Rengen M. R., Roth G., and Mattson M. P. (1996) Amyloid β-peptide disrupts carbachol-induced muscarinic cholinergic signal transduction in cortical neurons: involvement of free radicals. Proc. Natl. Acad. Sci. USA 93, 6753-6758.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 6753-6758
    • Kelly, J.1    Furukawa, K.2    Barger, S.W.3    Mark, R.J.4    Rengen, M.R.5    Roth, G.6    Mattson, M.P.7
  • 29
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine R. L., Williams J. A., Stadtman E. R., and Shacter E. (1994) Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 233, 346-357.
    • (1994) Methods Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 31
    • 0028971093 scopus 로고
    • β-Amyloid-induced toxicity in rat hippocampal cells: In vitro evidence for the involvement of free radicals
    • Manelli A. M. and Puttfarcken P. S. (1995) β-Amyloid-induced toxicity in rat hippocampal cells: in vitro evidence for the involvement of free radicals. Brain Res. Bull. 38, 569-576.
    • (1995) Brain Res. Bull. , vol.38 , pp. 569-576
    • Manelli, A.M.1    Puttfarcken, P.S.2
  • 33
    • 0030155860 scopus 로고    scopus 로고
    • Amyloid beta-peptide and oxidative cellular injury in Alzheimer's disease
    • Mark R. J., Blanc E. M., and Mattson M. P. (1996) Amyloid beta-peptide and oxidative cellular injury in Alzheimer's disease. Mol. Neurobiol. 12, 211-224.
    • (1996) Mol. Neurobiol. , vol.12 , pp. 211-224
    • Mark, R.J.1    Blanc, E.M.2    Mattson, M.P.3
  • 34
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • Markesbery W. R. (1997) Oxidative stress hypothesis in Alzheimer's disease. Free Radical Biol. Med. 23, 134-147.
    • (1997) Free Radical Biol. Med. , vol.23 , pp. 134-147
    • Markesbery, W.R.1
  • 36
    • 0027297138 scopus 로고
    • Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF
    • Mattson M. P., Tomaselli K. J., and Rydel R. E. (1993) Calcium-destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF. Brain Res. 621, 35-49.
    • (1993) Brain Res. , vol.621 , pp. 35-49
    • Mattson, M.P.1    Tomaselli, K.J.2    Rydel, R.E.3
  • 37
    • 0030611750 scopus 로고    scopus 로고
    • Activation of NF-kappaB protects hippocampal neurons against oxidative stress-induced apoptosis: Evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration
    • Mattson M. P., Goodman Y., Luo H., Fu W., and Furukawa K. (1997) Activation of NF-kappaB protects hippocampal neurons against oxidative stress-induced apoptosis: evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration. J. Neurosci. Res. 49, 681-697.
    • (1997) J. Neurosci. Res. , vol.49 , pp. 681-697
    • Mattson, M.P.1    Goodman, Y.2    Luo, H.3    Fu, W.4    Furukawa, K.5
  • 39
    • 0028048610 scopus 로고
    • Developmental expression of sarcomeric and ubiquitous mitochondrial creatine kinase is tissue-specific
    • Payne R. M. and Strauss A. W. (1994) Developmental expression of sarcomeric and ubiquitous mitochondrial creatine kinase is tissue-specific. Biochim. Biophys. Acta. 1219, 33-38.
    • (1994) Biochim. Biophys. Acta , vol.1219 , pp. 33-38
    • Payne, R.M.1    Strauss, A.W.2
  • 40
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike C. J., Burdick D., Walencewicz A. J., Glabe C. G., and Cotman C. W. (1993) Neurodegeneration induced by β-amyloid peptides in vitro: the role of peptide assembly state. J. Neurosci. 13, 1676-1687
    • (1993) J. Neurosci. , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 41
    • 0030924506 scopus 로고    scopus 로고
    • β-Amyloid neurotoxicity in vitro: Evidence of oxidative stress but not protection by antioxidants
    • Pike C. J., Ramezan-Arab N., and Cotman C. W. (1997) β-Amyloid neurotoxicity in vitro: evidence of oxidative stress but not protection by antioxidants. J. Neurochem. 69, 1601-1611.
    • (1997) J. Neurochem. , vol.69 , pp. 1601-1611
    • Pike, C.J.1    Ramezan-Arab, N.2    Cotman, C.W.3
  • 42
    • 0029670228 scopus 로고    scopus 로고
    • Inhibition of age-induced β-amyloid neurotoxicity in rat hippocampal cells
    • Puttfarcken P. S., Manelli A. M., Neilly J., and Frail D. E. (1996) Inhibition of age-induced β-amyloid neurotoxicity in rat hippocampal cells. Exp. Neurol. 138, 73-81.
    • (1996) Exp. Neurol. , vol.138 , pp. 73-81
    • Puttfarcken, P.S.1    Manelli, A.M.2    Neilly, J.3    Frail, D.E.4
  • 43
    • 0027491355 scopus 로고
    • Morphological and biochemical analyses of amyloid plague core proteins purified from Alzheimer disease tissue
    • Roher A. E., Palmer K. C., Yurewicz E. C., Ball M. J., and Greenberg B. D. (1993) Morphological and biochemical analyses of amyloid plague core proteins purified from Alzheimer disease tissue. J. Neurochem. 61, 1916-1926.
    • (1993) J. Neurochem. , vol.61 , pp. 1916-1926
    • Roher, A.E.1    Palmer, K.C.2    Yurewicz, E.C.3    Ball, M.J.4    Greenberg, B.D.5
  • 44
    • 0030030030 scopus 로고    scopus 로고
    • Increased antioxidant enzyme activity in amyloid beta protein-resistant cells
    • Sagara Y., Dargusch R., Klier F. G., Schubert D., and Behl C. (1996) Increased antioxidant enzyme activity in amyloid beta protein-resistant cells. J. Neurosci. 16, 497-505.
    • (1996) J. Neurosci. , vol.16 , pp. 497-505
    • Sagara, Y.1    Dargusch, R.2    Klier, F.G.3    Schubert, D.4    Behl, C.5
  • 46
    • 0029784838 scopus 로고    scopus 로고
    • Amyloid β-protein and the genetics of Alzheimer's disease
    • Selkoe D. J. (1996) Amyloid β-protein and the genetics of Alzheimer's disease. J. Biol. Chem. 271, 18,295-18,298.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18295-18298
    • Selkoe, D.J.1
  • 47
    • 0028118846 scopus 로고
    • Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death
    • Shearman M. S., Ragan C. I., and Iversen L. L. (1994) Inhibition of PC12 cell redox activity is a specific, early indicator of the mechanism of β-amyloid-mediated cell death. Proc. Natl. Acad. Sci. USA 91, 1470-1474.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1470-1474
    • Shearman, M.S.1    Ragan, C.I.2    Iversen, L.L.3
  • 48
    • 0029040824 scopus 로고
    • The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by beta-amyloid peptides
    • Shearman M. S., Hawtin S. R., and Tailor V. J. (1995) The intracellular component of cellular 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) reduction is specifically inhibited by beta-amyloid peptides. J. Neurochem. 65, 218-227.
    • (1995) J. Neurochem. , vol.65 , pp. 218-227
    • Shearman, M.S.1    Hawtin, S.R.2    Tailor, V.J.3
  • 49
    • 0028892186 scopus 로고
    • Amyloid beta prptide induces cytoplasmic accumulation of amyloid protein precursor via tau protein kinase 1/glycogen synthase kinase-3 beta in rat hippocampal neurons
    • Takashima A., Yamaguchi H., Noguchi K., Michel G., Ishiguro K., Sato K., et al. (1995) Amyloid beta prptide induces cytoplasmic accumulation of amyloid protein precursor via tau protein kinase 1/glycogen synthase kinase-3 beta in rat hippocampal neurons. Neurosci. Lett. 198, 83-86.
    • (1995) Neurosci. Lett. , vol.198 , pp. 83-86
    • Takashima, A.1    Yamaguchi, H.2    Noguchi, K.3    Michel, G.4    Ishiguro, K.5    Sato, K.6
  • 50
    • 0028000309 scopus 로고
    • Free radical inactivation of rabbit muscle creatine kinase: Catalysis by physiological and hydrolyzed ICRF-187 (ICRF-198) iron chelates
    • Thomas C., Carr A. C., and Winterbourn C. C. (1994) Free radical inactivation of rabbit muscle creatine kinase: catalysis by physiological and hydrolyzed ICRF-187 (ICRF-198) iron chelates. Free Radical Res. 21, 387-397.
    • (1994) Free Radical Res. , vol.21 , pp. 387-397
    • Thomas, C.1    Carr, A.C.2    Winterbourn, C.C.3
  • 52
    • 0021351106 scopus 로고
    • Function of M-line-bound creatine kinase as intramyofibrillar ATP regenerator and the receiving end of the phosphorylcreatine shuttle in muscle
    • Wallimann T., Schlosser T., and Eppenberger H. M. (1984) Function of M-line-bound creatine kinase as intramyofibrillar ATP regenerator and the receiving end of the phosphorylcreatine shuttle in muscle. J. Biol. Chem. 259, 5238-5246.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5238-5246
    • Wallimann, T.1    Schlosser, T.2    Eppenberger, H.M.3
  • 53
    • 85012314876 scopus 로고
    • Subcellular localization of creatine kinase in Torpedo electrocytes: Association with acetylcholine receptor-rich membranes
    • Wallimann T., Walzthony D., Wegmann G., Moser H., Eppenberger H. M., and Barrantes F. J. (1985) Subcellular localization of creatine kinase in Torpedo electrocytes: association with acetylcholine receptor-rich membranes. J. Cell. Biol. 100, 1063-1072.
    • (1985) J. Cell. Biol. , vol.100 , pp. 1063-1072
    • Wallimann, T.1    Walzthony, D.2    Wegmann, G.3    Moser, H.4    Eppenberger, H.M.5    Barrantes, F.J.6
  • 54
    • 0029670992 scopus 로고    scopus 로고
    • Deposits of Aβ fibrils are not toxic to cortical and hippocampal neurons in vitro
    • Wujek J. R., Dority M. D., Frederickson R. C. A., and Brunden K. R. (1996) Deposits of Aβ fibrils are not toxic to cortical and hippocampal neurons in vitro. Neurobiol. Aging 17, 107-113.
    • (1996) Neurobiol. Aging , vol.17 , pp. 107-113
    • Wujek, J.R.1    Dority, M.D.2    Frederickson, R.C.A.3    Brunden, K.R.4
  • 55
    • 0013615899 scopus 로고    scopus 로고
    • RAGE and amylois-β peptide neurotoxicity in Alzheimer's disease
    • Yan S. D., Chen X., Fu J., Chen M., Zhu H., Roher A., et al. (1996) RAGE and amylois-β peptide neurotoxicity in Alzheimer's disease. Nature 382, 685-691.
    • (1996) Nature , vol.382 , pp. 685-691
    • Yan, S.D.1    Chen, X.2    Fu, J.3    Chen, M.4    Zhu, H.5    Roher, A.6
  • 56
    • 0024990330 scopus 로고
    • Neurotrophic and neurotoxic effects of amyloid β protein: Reversal by tachykinin neuropeptides
    • Yankner B. A., Duffy L. K., and Kirschner D. A. (1990) Neurotrophic and neurotoxic effects of amyloid β protein: reversal by tachykinin neuropeptides. Science 250, 279.
    • (1990) Science , vol.250 , pp. 279
    • Yankner, B.A.1    Duffy, L.K.2    Kirschner, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.