메뉴 건너뛰기




Volumn 87, Issue 6, 2003, Pages 1456-1470

Selective prion protein binding to synaptic components is modulated by oxidative and nitrosative changes induced by copper(II) and peroxynitrite in cholinergic synaptosomes, unveiling a role for calcineurin B and thioredoxin

Author keywords

Calcineurin; Cu2+; Peroxynitrite; Prion; Synaptosomes; Thioredoxin

Indexed keywords

CALCINEURIN; CHOLINE; CHOLINE ACETYLTRANSFERASE; COPPER; COPPER SULFATE; GLUTATHIONE; PEROXYNITRITE; PRION PROTEIN; RECOMBINANT PROTEIN; THIOREDOXIN;

EID: 0347064330     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.02111.x     Document Type: Article
Times cited : (6)

References (83)
  • 1
    • 0037363599 scopus 로고    scopus 로고
    • Involvement of calcineurin in the neurotoxic effects induced by amyloid-beta and prion peptides
    • Agostinho P. and Oliveira C. R. (2003) Involvement of calcineurin in the neurotoxic effects induced by amyloid-beta and prion peptides. Eur. J. Neurosci. 17, 1189-1196.
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 1189-1196
    • Agostinho, P.1    Oliveira, C.R.2
  • 5
    • 0029805172 scopus 로고    scopus 로고
    • Nitric oxide, superoxide and peroxynitrite: The good, the bad, and the ugly
    • Beckman J. S. and Koppenol W. H. (1996) Nitric oxide, superoxide and peroxynitrite: the good, the bad, and the ugly. Am. J. Physiol. 271, C1424-C1437.
    • (1996) Am. J. Physiol. , vol.271
    • Beckman, J.S.1    Koppenol, W.H.2
  • 6
    • 0034062098 scopus 로고    scopus 로고
    • Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide: Evidence for a dithiodisulfide equilibrium and implications for redox regulation
    • Bogumyl R., Namgaladze D., Schaarschmidt D., Schachtel T., Hellstern S., Mutzel R. and Ullrich V. (2000) Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide: evidence for a dithiodisulfide equilibrium and implications for redox regulation. Eur. J. Biochem. 267, 1407-1415.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1407-1415
    • Bogumyl, R.1    Namgaladze, D.2    Schaarschmidt, D.3    Schachtel, T.4    Hellstern, S.5    Mutzel, R.6    Ullrich, V.7
  • 8
    • 0032080434 scopus 로고    scopus 로고
    • Prion protein fragment interacts with PrP-deficient cells
    • Brown D. R., Schmidt B. and Kretzschmar H. A. (1998) Prion protein fragment interacts with PrP-deficient cells. J. Neurosci. Res. 52, 260-267.
    • (1998) J. Neurosci. Res. , vol.52 , pp. 260-267
    • Brown, D.R.1    Schmidt, B.2    Kretzschmar, H.A.3
  • 9
    • 0021922503 scopus 로고
    • Identification of a transmembrane glycoprotein specific for secretory vesicles of neurons and endocrine cells
    • Buckley K. M. and Kelly R. B. (1985) Identification of a transmembrane glycoprotein specific for secretory vesicles of neurons and endocrine cells. J. Cell. Biol. 100, 1284-1294.
    • (1985) J. Cell. Biol. , vol.100 , pp. 1284-1294
    • Buckley, K.M.1    Kelly, R.B.2
  • 10
    • 0034035616 scopus 로고    scopus 로고
    • Metals and neuroscience
    • Bush A. I. (2000) Metals and neuroscience. Curr. Opin. Chem. Biol. 4, 184-191.
    • (2000) Curr. Opin. Chem. Biol. , vol.4 , pp. 184-191
    • Bush, A.I.1
  • 13
    • 0037415754 scopus 로고    scopus 로고
    • Scrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells
    • Cohen E. and Taraboulos A. (2003) Scrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells. EMBO J. 22, 404-417.
    • (2003) EMBO J. , vol.22 , pp. 404-417
    • Cohen, E.1    Taraboulos, A.2
  • 14
    • 0037162538 scopus 로고    scopus 로고
    • Redox systems of the cell: Possible links and implications
    • Das K. C. and White C. W. (2002) Redox systems of the cell: possible links and implications. Proc. Natl Acad. Sci. USA 99, 9617-9618.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9617-9618
    • Das, K.C.1    White, C.W.2
  • 15
    • 0032584141 scopus 로고    scopus 로고
    • Diffusion of peroxynitrite across erythrocyte membranes
    • Denicola A., De Souza J. M. and Radi R. (1998) Diffusion of peroxynitrite across erythrocyte membranes. Proc. Natl Acad. Sci. USA 95, 3566-3571.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3566-3571
    • Denicola, A.1    De Souza, J.M.2    Radi, R.3
  • 16
    • 0036069281 scopus 로고    scopus 로고
    • Peroxynitrite affects exocytosis and SNARE complex formation and induces tyrosine nitration of synaptic proteins
    • Di Stasi A. M., Mallozzi C., Macchia G., Maura G., Petrucci T. C. and Minetti M. (2002) Peroxynitrite affects exocytosis and SNARE complex formation and induces tyrosine nitration of synaptic proteins. J. Neurochem. 82, 420-429.
    • (2002) J. Neurochem. , vol.82 , pp. 420-429
    • Di Stasi, A.M.1    Mallozzi, C.2    Macchia, G.3    Maura, G.4    Petrucci, T.C.5    Minetti, M.6
  • 18
    • 0032992466 scopus 로고    scopus 로고
    • Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: A nitric oxide-dependent mechanism of cellular injury
    • Eiserich J. P., Estevez A. G., Bamberg T. V., Ye Y.-Z., Chumley P. H., Beckman J. S. and Freeman B. A. (1999) Microtubule dysfunction by posttranslational nitrotyrosination of alpha-tubulin: a nitric oxide-dependent mechanism of cellular injury. Proc. Natl Acad. Sci. USA 96, 6365-6370.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6365-6370
    • Eiserich, J.P.1    Estevez, A.G.2    Bamberg, T.V.3    Ye, Y.-Z.4    Chumley, P.H.5    Beckman, J.S.6    Freeman, B.A.7
  • 19
    • 0035979163 scopus 로고    scopus 로고
    • 2+ binding site 2 in calcineurin-B modulates calmodulin-dependent calcineurin phosphatase activity
    • 2+ binding site 2 in calcineurin-B modulates calmodulin-dependent calcineurin phosphatase activity. Biochem. 40, 8808-8814.
    • (2001) Biochem. , vol.40 , pp. 8808-8814
    • Feng, B.1    Stemmer, P.M.2
  • 20
    • 0033400532 scopus 로고    scopus 로고
    • Copper treatment alters the permeability of tight junctions in cultured human intestinal Caco-2 cells
    • Ferruzza S., Scarino M.-L., Rotilio G., Ciriolo M. R., Santaroni P. and Muda A. O. (1999) Copper treatment alters the permeability of tight junctions in cultured human intestinal Caco-2 cells. Am. J. Physiol. 277, G1138-G1148.
    • (1999) Am. J. Physiol. , vol.277
    • Ferruzza, S.1    Scarino, M.-L.2    Rotilio, G.3    Ciriolo, M.R.4    Santaroni, P.5    Muda, A.O.6
  • 21
    • 0036732661 scopus 로고    scopus 로고
    • Potential involvement of copper and thiol-disulphide interchange in prion protein's conformational conversion
    • Feughelman M. and Willis B. K. (2002) Potential involvement of copper and thiol-disulphide interchange in prion protein's conformational conversion. Med. Hypothesis 59, 321-324.
    • (2002) Med. Hypothesis , vol.59 , pp. 321-324
    • Feughelman, M.1    Willis, B.K.2
  • 22
    • 0028050923 scopus 로고
    • Peptidylprolyl cis-trans isomerases and their effectors
    • Fischer G. (1993) Peptidylprolyl cis-trans isomerases and their effectors. Angew. Chem. Int. Ed. Engl. 33, 1415-1436.
    • (1993) Angew. Chem. Int. Ed. Engl. , vol.33 , pp. 1415-1436
    • Fischer, G.1
  • 23
    • 0033597885 scopus 로고    scopus 로고
    • Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase
    • Fischer A. B., Dodia C., Manevich Y., Chen J.-W. and Feinstein S. I. (1999) Phospholipid hydroperoxides are substrates for non-selenium glutathione peroxidase. J. Biol. Chem. 274, 21326-21334.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21326-21334
    • Fischer, A.B.1    Dodia, C.2    Manevich, Y.3    Chen, J.-W.4    Feinstein, S.I.5
  • 27
    • 0034811593 scopus 로고    scopus 로고
    • Inhibition of acetylcholine synthesis and tyrosine nitration induced by peroxynitrite are differentially prevented by antioxidants
    • Guermonprez L., Ducrocq C. and Morot-Gaudry-Talarmain Y. (2001) Inhibition of acetylcholine synthesis and tyrosine nitration induced by peroxynitrite are differentially prevented by antioxidants. Mol. Pharmacol. 60, 838-846.
    • (2001) Mol. Pharmacol. , vol.60 , pp. 838-846
    • Guermonprez, L.1    Ducrocq, C.2    Morot-Gaudry-Talarmain, Y.3
  • 28
    • 0036677889 scopus 로고    scopus 로고
    • The neuronal choline transporter CHT1 is regulated by immunosuppressor-sensitive pathways
    • Guermonprez L., O'Regan S., Meunier F. M. and Morot-Gaudry-Talarmain Y. (2002) The neuronal choline transporter CHT1 is regulated by immunosuppressor-sensitive pathways. J. Neurochem. 82, 874-884.
    • (2002) J. Neurochem. , vol.82 , pp. 874-884
    • Guermonprez, L.1    O'Regan, S.2    Meunier, F.M.3    Morot-Gaudry-Talarmain, Y.4
  • 30
    • 0036174890 scopus 로고    scopus 로고
    • The biochemistry and physiology of S-nitrosothiols
    • Hogg N. (2002) The biochemistry and physiology of S-nitrosothiols. Annu. Rev. Pharmacol. Toxicol. 42, 585-600.
    • (2002) Annu. Rev. Pharmacol. Toxicol. , vol.42 , pp. 585-600
    • Hogg, N.1
  • 31
    • 0028844207 scopus 로고
    • Copper binding to the N-terminal repeat region of mammalian and avian prion protein: Structural studies using synthetic peptides
    • Hornshaw M. P., McDermott J. R., Candy J. M. and Lakey J. H. (1995) Copper binding to the N-terminal repeat region of mammalian and avian prion protein: structural studies using synthetic peptides. Biochem. Biophys. Res. Commun. 214, 993-999.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 993-999
    • Hornshaw, M.P.1    McDermott, J.R.2    Candy, J.M.3    Lakey, J.H.4
  • 33
    • 0037222168 scopus 로고    scopus 로고
    • Activation of microsomal glutathione S-transferase by peroxynitrite
    • Ji Y. and Bennett B. M. (2003) Activation of microsomal glutathione S-transferase by peroxynitrite. Mol. Pharmacol. 63, 136-146.
    • (2003) Mol. Pharmacol. , vol.63 , pp. 136-146
    • Ji, Y.1    Bennett, B.M.2
  • 34
    • 0024362166 scopus 로고
    • Nerve endings from rat brain tissue release copper upon depolarization: A possible role in regulating neuronal excitability
    • Kardos J., Kovacs I., Hajos F., Kalman M. and Simonyi M. (1989) Nerve endings from rat brain tissue release copper upon depolarization: a possible role in regulating neuronal excitability. Neurosci. Lett. 103, 139-144.
    • (1989) Neurosci. Lett. , vol.103 , pp. 139-144
    • Kardos, J.1    Kovacs, I.2    Hajos, F.3    Kalman, M.4    Simonyi, M.5
  • 35
    • 0033012137 scopus 로고    scopus 로고
    • Scrapie-infected mice and PrP knockout mice share abnormal localization and activity of neuronal nitric oxide synthase
    • Keshet G. I., Ovadia H., Taraboulos A. and Gabizon R. (1999) Scrapie-infected mice and PrP knockout mice share abnormal localization and activity of neuronal nitric oxide synthase. J. Neurochem. 72, 1224-1231.
    • (1999) J. Neurochem. , vol.72 , pp. 1224-1231
    • Keshet, G.I.1    Ovadia, H.2    Taraboulos, A.3    Gabizon, R.4
  • 36
    • 0033793094 scopus 로고    scopus 로고
    • The cellular prion protein colocalizes with the dystroglycan complex in the brain
    • Keshet G. I., Bar-Peled O., Yaffe D., Nudel U. and Gabizon R. (2000) The cellular prion protein colocalizes with the dystroglycan complex in the brain. J. Neurochem. 75, 1889-1897.
    • (2000) J. Neurochem. , vol.75 , pp. 1889-1897
    • Keshet, G.I.1    Bar-Peled, O.2    Yaffe, D.3    Nudel, U.4    Gabizon, R.5
  • 37
    • 0025959264 scopus 로고
    • Possible regulation of the in vitro assembly of bovine brain tubulin by the thioredoxin system
    • Khan I. A. and Ludueña R. F. (1991) Possible regulation of the in vitro assembly of bovine brain tubulin by the thioredoxin system. Biochim. Biophys. Acta 1076, 289-297.
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 289-297
    • Khan, I.A.1    Ludueña, R.F.2
  • 38
    • 0001018554 scopus 로고
    • Calcineurin: A calcium and calmodulin-binding protein of the nervous system
    • Klee C. B., Crouch M. H. and Krinks M. H. (1979) Calcineurin: a calcium and calmodulin-binding protein of the nervous system. Proc. Natl Acad. Sci. USA 76, 6270-6273.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 6270-6273
    • Klee, C.B.1    Crouch, M.H.2    Krinks, M.H.3
  • 39
    • 0032577483 scopus 로고    scopus 로고
    • Regulation of the calmodulin-stimulated protein phosphatase, calcineurin
    • Klee C. B., Ren H. and Wang X. (1998) Regulation of the calmodulin-stimulated protein phosphatase, calcineurin. J. Biol. Chem. 273, 13367-13370.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13367-13370
    • Klee, C.B.1    Ren, H.2    Wang, X.3
  • 40
    • 0033043959 scopus 로고    scopus 로고
    • In vivo modulation of rodent glutathione and its role in peroxynitrite-induced neocortical synaptosomal membrane protein damage
    • Koppal T., Drake J. and Butterfield D. A. (1999a) In vivo modulation of rodent glutathione and its role in peroxynitrite-induced neocortical synaptosomal membrane protein damage. Biochim. Biophys. Acta 1453, 407-411.
    • (1999) Biochim. Biophys. Acta , vol.1453 , pp. 407-411
    • Koppal, T.1    Drake, J.2    Butterfield, D.A.3
  • 41
    • 0032948006 scopus 로고    scopus 로고
    • Peroxynitrite-induced alterations in synaptosomal membrane proteins: Insight into oxidative stress in Alzheimer's disease
    • Koppal T., Drake J., Yatin S., Jordan B., Varadarajan S., Bettenhausen L. and Butterfield D. A. (1999b) Peroxynitrite-induced alterations in synaptosomal membrane proteins: insight into oxidative stress in Alzheimer's disease. J. Neurochem. 72, 310-317.
    • (1999) J. Neurochem. , vol.72 , pp. 310-317
    • Koppal, T.1    Drake, J.2    Yatin, S.3    Jordan, B.4    Varadarajan, S.5    Bettenhausen, L.6    Butterfield, D.A.7
  • 43
    • 1242318787 scopus 로고    scopus 로고
    • Identification of two calcineurin B-binding proteins: Tubulin and heat shock protein 60
    • Li W. and Handschumacher R. E. (2002) Identification of two calcineurin B-binding proteins: tubulin and heat shock protein 60. Biochim. Biophys. Acta 1599, 72-81.
    • (2002) Biochim. Biophys. Acta , vol.1599 , pp. 72-81
    • Li, W.1    Handschumacher, R.E.2
  • 44
    • 0018261210 scopus 로고
    • Reduced choline acetyltransferase activity in scrapie mouse brain
    • McDermott J. R., Fraser H. and Dickinson A. G. (1978) Reduced choline acetyltransferase activity in scrapie mouse brain. Lancet 2, 318-319.
    • (1978) Lancet , vol.2 , pp. 318-319
    • McDermott, J.R.1    Fraser, H.2    Dickinson, A.G.3
  • 45
    • 0020743519 scopus 로고
    • Asymmetry of lipid organization in cholinergic synaptic vesicle membranes
    • Michaelson D. M., Barkai G. and Barrenholz Y. (1983) Asymmetry of lipid organization in cholinergic synaptic vesicle membranes. Biochem. J. 211, 155-162.
    • (1983) Biochem. J. , vol.211 , pp. 155-162
    • Michaelson, D.M.1    Barkai, G.2    Barrenholz, Y.3
  • 46
    • 0036124813 scopus 로고    scopus 로고
    • Oxidative stress and the prion protein in transmissible spongiform encephalopathies
    • Milhavet O. and Lehmann S. (2002) Oxidative stress and the prion protein in transmissible spongiform encephalopathies. Brain Res. Rev. 38, 328-339.
    • (2002) Brain Res. Rev. , vol.38 , pp. 328-339
    • Milhavet, O.1    Lehmann, S.2
  • 47
    • 0017659283 scopus 로고
    • Isolation of pure cholinergic nerve endings from Torpedo electric organ: Evaluation of their metabolic properties
    • Morel N., Israël M., Manaranche R. and Mastour-Frachon P. (1977) Isolation of pure cholinergic nerve endings from Torpedo electric organ: evaluation of their metabolic properties. J. Cell Biol. 75, 43-55.
    • (1977) J. Cell Biol. , vol.75 , pp. 43-55
    • Morel, N.1    Israël, M.2    Manaranche, R.3    Mastour-Frachon, P.4
  • 48
    • 0029764601 scopus 로고    scopus 로고
    • S-Nitrosogluthathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide
    • Nikitovic D. and Holmgren A. (1996) S-Nitrosogluthathione is cleaved by the thioredoxin system with liberation of glutathione and redox regulating nitric oxide. J. Biol. Chem. 271, 19180-19185.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19180-19185
    • Nikitovic, D.1    Holmgren, A.2
  • 50
    • 0034682776 scopus 로고    scopus 로고
    • Metallochaperones, an intracellular shuttle service for metal ions
    • O'Halloran T. V. and Culotta C. V. (2000) Metallochaperones, an intracellular shuttle service for metal ions. J. Biol. Chem. 275, 25057-25060.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25057-25060
    • O'Halloran, T.V.1    Culotta, C.V.2
  • 51
    • 0037434837 scopus 로고    scopus 로고
    • Identification of cDNA from Japanese pufferfish (Fugu rubripes) and Atlantic salmon (Salmo salar) coding for homologues to tetrapod prion proteins
    • Oidtmann B., Simon D., Holtkamp N., Hoffmann R. and Baier M. (2003) Identification of cDNA from Japanese pufferfish (Fugu rubripes) and Atlantic salmon (Salmo salar) coding for homologues to tetrapod prion proteins. FEBS Lett. 538, 96-100.
    • (2003) FEBS Lett. , vol.538 , pp. 96-100
    • Oidtmann, B.1    Simon, D.2    Holtkamp, N.3    Hoffmann, R.4    Baier, M.5
  • 53
    • 0034660568 scopus 로고    scopus 로고
    • Metal-catalyzed oxidation of alpha-synuclein in the presence of copper(II) and hydrogen peroxide
    • Paik S. R., Shin H. J. and Lee J. H. (2000) Metal-catalyzed oxidation of alpha-synuclein in the presence of copper(II) and hydrogen peroxide. Arch. Biochem. Biophys. 378, 269-277.
    • (2000) Arch. Biochem. Biophys. , vol.378 , pp. 269-277
    • Paik, S.R.1    Shin, H.J.2    Lee, J.H.3
  • 54
    • 0035029131 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxin
    • Powis G. and Montfort W. R. (2001) Properties and biological activities of thioredoxin. Ann. Rev. Pharmacol. Toxicol. 41, 261-295.
    • (2001) Ann. Rev. Pharmacol. Toxicol. , vol.41 , pp. 261-295
    • Powis, G.1    Montfort, W.R.2
  • 55
    • 0034718162 scopus 로고    scopus 로고
    • Detection of thiol modification following generation of reactive species: Analysis of synaptic vesicle proteins
    • Prior I. A. and Clague M. J. (2000) Detection of thiol modification following generation of reactive species: analysis of synaptic vesicle proteins. Biochim. Biophys. Acta 1475, 281-286.
    • (2000) Biochim. Biophys. Acta , vol.1475 , pp. 281-286
    • Prior, I.A.1    Clague, M.J.2
  • 58
    • 0037715143 scopus 로고    scopus 로고
    • Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery
    • Rachidi W., Vilette D., Guiraud P., Arlotto M., Riondel J., Laude H., Lehmann S. and Favier A. (2003) Expression of prion protein increases cellular copper binding and antioxidant enzyme activities but not copper delivery. J. Biol. Chem. 278, 9064-9072.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9064-9072
    • Rachidi, W.1    Vilette, D.2    Guiraud, P.3    Arlotto, M.4    Riondel, J.5    Laude, H.6    Lehmann, S.7    Favier, A.8
  • 60
    • 0035863115 scopus 로고    scopus 로고
    • Thioredoxin converts the Syrian hamster (29-231) recombinant prion protein to an insoluble form
    • Requena J. R. and Levine R. L. (2001) Thioredoxin converts the Syrian hamster (29-231) recombinant prion protein to an insoluble form. Free Radic. Biol. Med. 30, 141-147.
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 141-147
    • Requena, J.R.1    Levine, R.L.2
  • 62
    • 0034127890 scopus 로고    scopus 로고
    • High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility
    • Rezaei H., Marc D., Choiset Y., Takahashi M., Hui Bon Hoa G., Haertle T., Grosclaude J. and Debey P. (2000) High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility. Eur. J. Biochem. 267, 2833-2839.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2833-2839
    • Rezaei, H.1    Marc, D.2    Choiset, Y.3    Takahashi, M.4    Hui Bon Hoa, G.5    Haertle, T.6    Grosclaude, J.7    Debey, P.8
  • 63
    • 0037301562 scopus 로고    scopus 로고
    • An evolutionary basis for scrapie disease: Identification of a fish prion mRNA
    • Rivera-Milla E., Stuermer C. A. O. and Malaga-Trillo E. (2003) An evolutionary basis for scrapie disease: identification of a fish prion mRNA. Trends Genet. 19, 72-75.
    • (2003) Trends Genet. , vol.19 , pp. 72-75
    • Rivera-Milla, E.1    Stuermer, C.A.O.2    Malaga-Trillo, E.3
  • 64
    • 0348104554 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman J. E. (1994) Mechanisms of intracellular protein transport. Nature 393, 14-15.
    • (1994) Nature , vol.393 , pp. 14-15
    • Rothman, J.E.1
  • 65
    • 0034456918 scopus 로고    scopus 로고
    • Copper-dependent oxidative stress and neurodegeneration
    • Rotilio G., Carri M. T., Rossi L. and Cirilio M. R. (2000) Copper-dependent oxidative stress and neurodegeneration. IUBMB Life 50, 309-314.
    • (2000) IUBMB Life , vol.50 , pp. 309-314
    • Rotilio, G.1    Carri, M.T.2    Rossi, L.3    Cirilio, M.R.4
  • 66
    • 0025896969 scopus 로고
    • Alterations in neurotransmitter-related enzyme activity in scrapie-infected PC12 cells
    • Rubenstein R., Deng H., Scalici C. L. and Papini M. C. (1991) Alterations in neurotransmitter-related enzyme activity in scrapie-infected PC12 cells. J. Gen. Virol. 72, 1279-1285.
    • (1991) J. Gen. Virol. , vol.72 , pp. 1279-1285
    • Rubenstein, R.1    Deng, H.2    Scalici, C.L.3    Papini, M.C.4
  • 68
    • 0027278599 scopus 로고
    • The SV2 protein of synaptic vesicles is a keratan sulfate proteoglycan
    • Scranton T. W., Iwata M. and Carlson S. S. (1993) The SV2 protein of synaptic vesicles is a keratan sulfate proteoglycan. J. Neurochem. 61, 29-44.
    • (1993) J. Neurochem. , vol.61 , pp. 29-44
    • Scranton, T.W.1    Iwata, M.2    Carlson, S.S.3
  • 69
    • 0031006845 scopus 로고    scopus 로고
    • Association of syntaxin with SNAP-25 and VAMP (synaptobrevin) during axonal transport
    • Shiff G. and Morel N. (1997) Association of syntaxin with SNAP-25 and VAMP (synaptobrevin) during axonal transport. J. Neurosc. Res. 48, 313-323.
    • (1997) J. Neurosc. Res. , vol.48 , pp. 313-323
    • Shiff, G.1    Morel, N.2
  • 71
    • 0025243737 scopus 로고
    • Immunolocalisation of heparan sulfate proteoglycan to the prion amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie
    • Snow A. D., Wight T. N., Nochlin D., Koike Y., Kimata K., DeArmond S. J. and Prusiner S. B. (1990) Immunolocalisation of heparan sulfate proteoglycan to the prion amyloid plaques of Gerstmann-Straussler syndrome, Creutzfeldt-Jakob disease and scrapie. Laboratory Invest. 63, 601-611.
    • (1990) Laboratory Invest , vol.63 , pp. 601-611
    • Snow, A.D.1    Wight, T.N.2    Nochlin, D.3    Koike, Y.4    Kimata, K.5    DeArmond, S.J.6    Prusiner, S.B.7
  • 72
    • 0035977053 scopus 로고    scopus 로고
    • c directly interacts with proteins involved in signaling pathways
    • c directly interacts with proteins involved in signaling pathways. J. Biol. Chem. 276, 44604-44612.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44604-44612
    • Spielhaupter, C.1    Schätzl, H.M.2
  • 73
    • 0020338573 scopus 로고
    • Identification of a heparan sulfate-containing proteoglycan as a specific core component of cholinergic synaptic vesicles from Torpedo marmorata
    • Stadler H. and Dowe G. H. C. (1982) Identification of a heparan sulfate-containing proteoglycan as a specific core component of cholinergic synaptic vesicles from Torpedo marmorata. EMBO J. 1, 1381-1384.
    • (1982) EMBO J. , vol.1 , pp. 1381-1384
    • Stadler, H.1    Dowe, G.H.C.2
  • 74
    • 0022407571 scopus 로고
    • Axoplasmic transport of thioredoxin and thioredoxin reductase in rat sciatic nerve
    • Stemme S., Hansson H. A., Holmgren A. and Rozell B. (1985) Axoplasmic transport of thioredoxin and thioredoxin reductase in rat sciatic nerve. Brain Res. 359, 140-146.
    • (1985) Brain Res. , vol.359 , pp. 140-146
    • Stemme, S.1    Hansson, H.A.2    Holmgren, A.3    Rozell, B.4
  • 75
    • 0033214985 scopus 로고    scopus 로고
    • Mechanism of S-nitrosothiol formation and degradation mediated by copper ions
    • Stubauer G., Giuffrè A. and Sarti P. (1999) Mechanism of S-nitrosothiol formation and degradation mediated by copper ions. J. Biol. Chem. 274, 28128-28133.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28128-28133
    • Stubauer, G.1    Giuffrè, A.2    Sarti, P.3
  • 76
    • 0036298793 scopus 로고    scopus 로고
    • cDNA sequence and tissue expression of Fugu rubripes prion protein-like: A candidate for the teleost orthologue of tetrapod PrPs
    • Suzuki T., Kurokawa T., Hashimoto H. and Sugiyama M. (2002) cDNA sequence and tissue expression of Fugu rubripes prion protein-like: a candidate for the teleost orthologue of tetrapod PrPs. Bioc. Biop. Res. Com. 294, 912-917.
    • (2002) Bioc. Biop. Res. Com. , vol.294 , pp. 912-917
    • Suzuki, T.1    Kurokawa, T.2    Hashimoto, H.3    Sugiyama, M.4
  • 77
    • 0033065593 scopus 로고    scopus 로고
    • Thiol oxidation of actin produces dimers that enhance the elasticity of the F-actin-network
    • Tang J. X., Janmey P. A., Stossel T. P. and Ito T. (1999) Thiol oxidation of actin produces dimers that enhance the elasticity of the F-actin-network. Biophys. J. 76, 2208-2215.
    • (1999) Biophys. J. , vol.76 , pp. 2208-2215
    • Tang, J.X.1    Janmey, P.A.2    Stossel, T.P.3    Ito, T.4
  • 78
    • 0018270913 scopus 로고
    • Chemical composition of cholinergic synaptic vesicles from Torpedo marmorata based on improved purification
    • Tashiro T. and Stadler H. (1978) Chemical composition of cholinergic synaptic vesicles from Torpedo marmorata based on improved purification. Eur. J. Biochem. 90, 479-487.
    • (1978) Eur. J. Biochem. , vol.90 , pp. 479-487
    • Tashiro, T.1    Stadler, H.2
  • 79
    • 0025060737 scopus 로고
    • Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation
    • Thomas J. P., Maiorino M., Ursini F. and Girotti A. W. (1990) Protective action of phospholipid hydroperoxide glutathione peroxidase against membrane-damaging lipid peroxidation. J. Biol. Chem. 265, 454-461.
    • (1990) J. Biol. Chem. , vol.265 , pp. 454-461
    • Thomas, J.P.1    Maiorino, M.2    Ursini, F.3    Girotti, A.W.4
  • 80
    • 0029991419 scopus 로고    scopus 로고
    • Synthesis of peroxynitrite in a two-phase system using isoamyl nitrite and hydrogen peroxide
    • Uppu R. M. and Pryor W. A. (1996) Synthesis of peroxynitrite in a two-phase system using isoamyl nitrite and hydrogen peroxide. Anal. Biochem. 236, 242-249.
    • (1996) Anal. Biochem. , vol.236 , pp. 242-249
    • Uppu, R.M.1    Pryor, W.A.2
  • 81
    • 0343580474 scopus 로고    scopus 로고
    • Peroxynitrite-mediated decarboxylation of pyruvate to both carbon dioxide and carbon dioxide radical anion
    • Vasquez-Vivar J., Denicola A., Radi R. and Augusto O. (1997) Peroxynitrite-mediated decarboxylation of pyruvate to both carbon dioxide and carbon dioxide radical anion. Chem. Res. Toxicol. 10, 786-794.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 786-794
    • Vasquez-Vivar, J.1    Denicola, A.2    Radi, R.3    Augusto, O.4
  • 83
    • 0037121618 scopus 로고    scopus 로고
    • Overexpressed protein disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease
    • Yoo B. C., Krapfenbauer K., Caims N., Belay G., Bajo M. and Lubec G. (2002) Overexpressed protein disulfide isomerase in brains of patients with sporadic Creutzfeldt-Jakob disease. Neurosci. Lett. 334, 196-200.
    • (2002) Neurosci. Lett. , vol.334 , pp. 196-200
    • Yoo, B.C.1    Krapfenbauer, K.2    Caims, N.3    Belay, G.4    Bajo, M.5    Lubec, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.