메뉴 건너뛰기




Volumn 14, Issue 3, 2010, Pages 564-577

Tau dephosphorylation and microfilaments disruption are upstream events of the anti-proliferative effects of DADS in SH-SY5Y cells

Author keywords

Diallyl disulphide; Garlic; Microfilaments; Microtubules; Tau

Indexed keywords

ALLYL COMPOUND; COPPER ZINC SUPEROXIDE DISMUTASE; DIALLYL DISULFIDE; DISULFIDE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; SUPEROXIDE DISMUTASE; TAU PROTEIN;

EID: 77953512362     PISSN: 15821838     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1582-4934.2008.00588.x     Document Type: Article
Times cited : (21)

References (65)
  • 1
    • 33846931878 scopus 로고    scopus 로고
    • Cancer chemoprevention with garlic and its constituents
    • Shukla Y, Kalra N. Cancer chemoprevention with garlic and its constituents. Cancer Lett. 2007, 247:167-81.
    • (2007) Cancer Lett. , vol.247 , pp. 167-181
    • Shukla, Y.1    Kalra, N.2
  • 2
    • 33644843461 scopus 로고    scopus 로고
    • Garlic and cardiovascular disease: a critical review
    • Rahman K, Lowe GM. Garlic and cardiovascular disease: a critical review. J Nutr. 2006, 136:736S-40S.
    • (2006) J Nutr. , vol.136
    • Rahman, K.1    Lowe, G.M.2
  • 3
    • 0022039421 scopus 로고
    • The chemistry of garlic and onions
    • Block E. The chemistry of garlic and onions. Sci Am. 1985, 252:114-9.
    • (1985) Sci Am. , vol.252 , pp. 114-119
    • Block, E.1
  • 4
    • 34548408192 scopus 로고    scopus 로고
    • Molecular targets of cancer chemoprevention by garlic-derived organosulfides
    • Herman-Antosiewicz A, Powolny AA, Singh SV. Molecular targets of cancer chemoprevention by garlic-derived organosulfides. Acta Pharmacol Sin. 2007, 28:1355-64.
    • (2007) Acta Pharmacol Sin. , vol.28 , pp. 1355-1364
    • Herman-Antosiewicz, A.1    Powolny, A.A.2    Singh, S.V.3
  • 5
    • 0141842655 scopus 로고    scopus 로고
    • Reactive oxygen species-dependent c-Jun NH2-terminal kinase/c-Jun signaling cascade mediates neuroblastoma cell death induced by diallyl disulfide
    • Filomeni G, Aquilano K, Rotilio G. Reactive oxygen species-dependent c-Jun NH2-terminal kinase/c-Jun signaling cascade mediates neuroblastoma cell death induced by diallyl disulfide. Cancer Res. 2003, 63:5940-9.
    • (2003) Cancer Res. , vol.63 , pp. 5940-5949
    • Filomeni, G.1    Aquilano, K.2    Rotilio, G.3    et al4
  • 6
    • 34248167167 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase protects neuroblastoma cells from oxidative stress mediated by garlic derivatives
    • Aquilano K, Filomeni G, Baldelli S. Neuronal nitric oxide synthase protects neuroblastoma cells from oxidative stress mediated by garlic derivatives. J Neurochem. 2007, 101:1327-37.
    • (2007) J Neurochem. , vol.101 , pp. 1327-1337
    • Aquilano, K.1    Filomeni, G.2    Baldelli, S.3
  • 7
    • 29244489231 scopus 로고    scopus 로고
    • Glutathione-related systems and modulation of extracellular signal-regulated kinases are involved in the resistance of AGS adenocarcinoma gastric cells to diallyl disulfide-induced apoptosis
    • Filomeni G, Aquilano K, Rotilio G. Glutathione-related systems and modulation of extracellular signal-regulated kinases are involved in the resistance of AGS adenocarcinoma gastric cells to diallyl disulfide-induced apoptosis. Cancer Res. 2005, 65:11735-42.
    • (2005) Cancer Res. , vol.65 , pp. 11735-11742
    • Filomeni, G.1    Aquilano, K.2    Rotilio, G.3    et al4
  • 8
    • 0035893961 scopus 로고    scopus 로고
    • The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself
    • Dalle-Donne I, Rossi R, Milzani A. The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself. Free Radic Biol Med. 2001, 31:1624-32.
    • (2001) Free Radic Biol Med. , vol.31 , pp. 1624-1632
    • Dalle-Donne, I.1    Rossi, R.2    Milzani, A.3    et al4
  • 9
    • 0036569808 scopus 로고    scopus 로고
    • Methionine oxidation as a major cause of the functional impairment of oxidized actin
    • Dalle-Donne I, Rossi R, Giustarini D. Methionine oxidation as a major cause of the functional impairment of oxidized actin. Free Radic Biol Med. 2002, 32:927-37.
    • (2002) Free Radic Biol Med. , vol.32 , pp. 927-937
    • Dalle-Donne, I.1    Rossi, R.2    Giustarini, D.3    et al4
  • 10
    • 28844469924 scopus 로고    scopus 로고
    • Molecular mechanism of nrf2 activation by oxidative stress
    • Kang KW, Lee SJ, Kim SG. Molecular mechanism of nrf2 activation by oxidative stress. Antioxid Redox Signal. 2005, 7:1664-73.
    • (2005) Antioxid Redox Signal. , vol.7 , pp. 1664-1673
    • Kang, K.W.1    Lee, S.J.2    Kim, S.G.3
  • 11
    • 33746492421 scopus 로고    scopus 로고
    • Selectively increased oxidative modifications mapped to detergent-insoluble forms of Abeta and beta-III tubulin in Alzheimer's disease
    • Boutte AM, Woltjer RL, Zimmerman LJ. Selectively increased oxidative modifications mapped to detergent-insoluble forms of Abeta and beta-III tubulin in Alzheimer's disease. FASEB J. 2006, 20:1473-83.
    • (2006) FASEB J. , vol.20 , pp. 1473-1483
    • Boutte, A.M.1    Woltjer, R.L.2    Zimmerman, L.J.3    et al4
  • 12
    • 0023790206 scopus 로고
    • Alterations of surface morphology caused by the metabolism of menadione in mammalian cells are associated with the oxidation of critical sulfhydryl groups in cytoskeletal proteins
    • Mirabelli F, Salis A, Perotti M. Alterations of surface morphology caused by the metabolism of menadione in mammalian cells are associated with the oxidation of critical sulfhydryl groups in cytoskeletal proteins. Biochem Pharmacol. 1988, 37:3423-7.
    • (1988) Biochem Pharmacol. , vol.37 , pp. 3423-3427
    • Mirabelli, F.1    Salis, A.2    Perotti, M.3    et al4
  • 13
    • 0028215274 scopus 로고
    • Oxidative stress induces S-thiolation of specific proteins in cultured gastric mucosal cells
    • Rokutan K, Johnston RB, Kawai K. Oxidative stress induces S-thiolation of specific proteins in cultured gastric mucosal cells. Am J Physiol. 1994, 266:G247-54.
    • (1994) Am J Physiol. , vol.266
    • Rokutan, K.1    Johnston, R.B.2    Kawai, K.3
  • 14
    • 0028939386 scopus 로고
    • Junctional sites of erythrocyte skeletal proteins are specific targets of tert-butylhydroperoxide oxidative damage
    • Caprari P, Bozzi A, Malorni W. Junctional sites of erythrocyte skeletal proteins are specific targets of tert-butylhydroperoxide oxidative damage. Chem Biol Interact. 1995, 94:243-58.
    • (1995) Chem Biol Interact. , vol.94 , pp. 243-258
    • Caprari, P.1    Bozzi, A.2    Malorni, W.3
  • 15
    • 0034069867 scopus 로고    scopus 로고
    • Carbonylation and disassembly of the F-actin cytoskeleton in oxidant induced barrier dysfunction and its prevention by epidermal growth factor and transforming growth factor alpha in a human colonic cell line
    • Banan A, Zhang Y, Losurdo J. Carbonylation and disassembly of the F-actin cytoskeleton in oxidant induced barrier dysfunction and its prevention by epidermal growth factor and transforming growth factor alpha in a human colonic cell line. Gut. 2000, 46:830-7.
    • (2000) Gut. , vol.46 , pp. 830-837
    • Banan, A.1    Zhang, Y.2    Losurdo, J.3    et al4
  • 16
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin N, Bhatt AK, Dutt P. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J Biol Chem. 2001, 276:48382-8.
    • (2001) J Biol Chem. , vol.276 , pp. 48382-48388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3
  • 17
  • 18
    • 34250021123 scopus 로고    scopus 로고
    • The apoptotic microtubule network preserves plasma membrane integrity during the execution phase of apoptosis
    • Sanchez-Alcazar JA, Rodriguez-Hernandez A, Cordero MD. The apoptotic microtubule network preserves plasma membrane integrity during the execution phase of apoptosis. Apoptosis. 2007, 12:1195-208.
    • (2007) Apoptosis. , vol.12 , pp. 1195-1208
    • Sanchez-Alcazar, J.A.1    Rodriguez-Hernandez, A.2    Cordero, M.D.3    et al4
  • 19
    • 0030957458 scopus 로고    scopus 로고
    • Actin is cleaved during constitutive apoptosis
    • Brown SB, Bailey K, Savill J. Actin is cleaved during constitutive apoptosis. Biochem J. 1997, 323:233-7.
    • (1997) Biochem J. , vol.323 , pp. 233-237
    • Brown, S.B.1    Bailey, K.2    Savill, J.3
  • 20
    • 0033561495 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of cytoskeletal actin plays a positive role in the process of morphological apoptosis
    • Mashima T, Naito M, Tsuruo T. Caspase-mediated cleavage of cytoskeletal actin plays a positive role in the process of morphological apoptosis. Oncogene. 1999, 18:2423-30.
    • (1999) Oncogene. , vol.18 , pp. 2423-2430
    • Mashima, T.1    Naito, M.2    Tsuruo, T.3
  • 21
    • 34249690230 scopus 로고    scopus 로고
    • Dual roles of intermediate filaments in apoptosis
    • Marceau N, Schutte B, Gilbert S. Dual roles of intermediate filaments in apoptosis. Exp Cell Res. 2007, 313:2265-81.
    • (2007) Exp Cell Res. , vol.313 , pp. 2265-2281
    • Marceau, N.1    Schutte, B.2    Gilbert, S.3
  • 22
    • 0037418238 scopus 로고    scopus 로고
    • JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis
    • Lei K, Davis RJ. JNK phosphorylation of Bim-related members of the Bcl2 family induces Bax-dependent apoptosis. Proc Natl Acad Sci USA. 2003, 100:2432-7.
    • (2003) Proc Natl Acad Sci USA. , vol.100 , pp. 2432-2437
    • Lei, K.1    Davis, R.J.2
  • 23
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway
    • Kensler TW, Wakabayashi N, Biswal S. Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu Rev Pharmacol Toxicol. 2007, 47:89-116.
    • (2007) Annu Rev Pharmacol Toxicol. , vol.47 , pp. 89-116
    • Kensler, T.W.1    Wakabayashi, N.2    Biswal, S.3
  • 24
    • 0038445642 scopus 로고    scopus 로고
    • Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases
    • Woodring PJ, Hunter T, Wang JY. Regulation of F-actin-dependent processes by the Abl family of tyrosine kinases. J Cell Sci. 2003, 116:2613-26.
    • (2003) J Cell Sci. , vol.116 , pp. 2613-2626
    • Woodring, P.J.1    Hunter, T.2    Wang, J.Y.3
  • 26
    • 0032006059 scopus 로고    scopus 로고
    • Microtubules and actin filaments: dynamic targets for cancer chemotherapy
    • Jordan MA, Wilson L. Microtubules and actin filaments: dynamic targets for cancer chemotherapy. Curr Opin Cell Biol. 1998, 10:123-30.
    • (1998) Curr Opin Cell Biol. , vol.10 , pp. 123-130
    • Jordan, M.A.1    Wilson, L.2
  • 28
    • 33646773191 scopus 로고    scopus 로고
    • Specialisation of the tropomyosin composition of actin filaments provides new potential targets for chemotherapy
    • Stehn JR, Schevzov G, O'Neill GM. Specialisation of the tropomyosin composition of actin filaments provides new potential targets for chemotherapy. Curr Cancer Drug Targets. 2006, 6:245-56.
    • (2006) Curr Cancer Drug Targets. , vol.6 , pp. 245-256
    • Stehn, J.R.1    Schevzov, G.2    O'Neill, G.M.3    et al4
  • 29
    • 33749679855 scopus 로고    scopus 로고
    • Effects of water garlic extracts on cell cycle and viability of HepG2 hepatoma cells
    • De Martino A, Filomeni G, Aquilano K. Effects of water garlic extracts on cell cycle and viability of HepG2 hepatoma cells. J Nutr Biochem. 2006, 17:742-9.
    • (2006) J Nutr Biochem. , vol.17 , pp. 742-749
    • De Martino, A.1    Filomeni, G.2    Aquilano, K.3    et al4
  • 30
    • 0142188703 scopus 로고    scopus 로고
    • Induction of apoptosis by the garlic-derived compound S-allylmercaptocysteine (SAMC) is associated with microtubule depolymerization and c-Jun NH-terminal kinase 1 activation
    • Xiao D, Pinto JT, Soh JW. Induction of apoptosis by the garlic-derived compound S-allylmercaptocysteine (SAMC) is associated with microtubule depolymerization and c-Jun NH-terminal kinase 1 activation. Cancer Res. 2003, 63:6825-37.
    • (2003) Cancer Res. , vol.63 , pp. 6825-6837
    • Xiao, D.1    Pinto, J.T.2    Soh, J.W.3    et al4
  • 31
    • 33644666598 scopus 로고    scopus 로고
    • Effects of a series of organosulfur compounds on mitotic arrest and induction of apoptosis in colon cancer cells
    • Xiao D, Pinto JT, Gundersen GG. Effects of a series of organosulfur compounds on mitotic arrest and induction of apoptosis in colon cancer cells. Mol Cancer Ther. 2005, 4:1388-98.
    • (2005) Mol Cancer Ther. , vol.4 , pp. 1388-1398
    • Xiao, D.1    Pinto, J.T.2    Gundersen, G.G.3    et al4
  • 32
    • 29244484434 scopus 로고    scopus 로고
    • Diallyl trisulfide suppresses the proliferation and induces apoptosis of human colon cancer cells through oxidative modification of beta-tubulin
    • Hosono T, Fukao T, Ogihara J. Diallyl trisulfide suppresses the proliferation and induces apoptosis of human colon cancer cells through oxidative modification of beta-tubulin. J Biol Chem. 2005, 280:41487-93.
    • (2005) J Biol Chem. , vol.280 , pp. 41487-41493
    • Hosono, T.1    Fukao, T.2    Ogihara, J.3
  • 33
    • 34247210874 scopus 로고    scopus 로고
    • Allicin inhibits cell polarization, migration and division via its direct effect on microtubules
    • Prager-Khoutorsky M, Goncharov I, Rabinkov A. Allicin inhibits cell polarization, migration and division via its direct effect on microtubules. Cell Motil Cytoskeleton. 2007, 64:321-37.
    • (2007) Cell Motil Cytoskeleton. , vol.64 , pp. 321-337
    • Prager-Khoutorsky, M.1    Goncharov, I.2    Rabinkov, A.3
  • 34
    • 49349109009 scopus 로고    scopus 로고
    • Alkenyl group is responsible for the disruption of microtubule network formation in human colon cancer cell line HT-29 cells
    • Hosono T, Hosono-Fukao T, Inada K. Alkenyl group is responsible for the disruption of microtubule network formation in human colon cancer cell line HT-29 cells. Carcinogenesis. 2008, 29:1400-6.
    • (2008) Carcinogenesis. , vol.29 , pp. 1400-1406
    • Hosono, T.1    Hosono-Fukao, T.2    Inada, K.3
  • 35
    • 11144356349 scopus 로고    scopus 로고
    • Allicin inhibits SDF-1alpha-induced T cell interactions with fibronectin and endothelial cells by down-regulating cytoskeleton rearrangement, Pyk-2 phosphorylation and VLA-4 expression
    • Sela U, Ganor S, Hecht I. Allicin inhibits SDF-1alpha-induced T cell interactions with fibronectin and endothelial cells by down-regulating cytoskeleton rearrangement, Pyk-2 phosphorylation and VLA-4 expression. Immunology. 2004, 111:391-9.
    • (2004) Immunology. , vol.111 , pp. 391-399
    • Sela, U.1    Ganor, S.2    Hecht, I.3
  • 36
    • 0022365608 scopus 로고
    • The distribution of tau in the mammalian central nervous system
    • Binder LI, Frankfurter A, Rebhun LI. The distribution of tau in the mammalian central nervous system. J Cell Biol. 1985, 101:1371-8.
    • (1985) J Cell Biol. , vol.101 , pp. 1371-1378
    • Binder, L.I.1    Frankfurter, A.2    Rebhun, L.I.3
  • 37
    • 33947286683 scopus 로고    scopus 로고
    • Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
    • Fulga TA, Elson-Schwab I, Khurana V. Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat Cell Biol. 2007, 9:139-48.
    • (2007) Nat Cell Biol. , vol.9 , pp. 139-148
    • Fulga, T.A.1    Elson-Schwab, I.2    Khurana, V.3
  • 38
    • 17344365975 scopus 로고    scopus 로고
    • Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis
    • Canu N, Dus L, Barbato C. Tau cleavage and dephosphorylation in cerebellar granule neurons undergoing apoptosis. J Neurosci. 1998, 18:7061-74.
    • (1998) J Neurosci. , vol.18 , pp. 7061-7074
    • Canu, N.1    Dus, L.2    Barbato, C.3
  • 39
    • 11144227267 scopus 로고    scopus 로고
    • Linking alterations in tau phosphorylation and cleavage during neuronal apoptosis
    • Rametti A, Esclaire F, Yardin C. Linking alterations in tau phosphorylation and cleavage during neuronal apoptosis. J Biol Chem. 2004, 279:54518-28.
    • (2004) J Biol Chem. , vol.279 , pp. 54518-54528
    • Rametti, A.1    Esclaire, F.2    Yardin, C.3
  • 40
    • 0029669963 scopus 로고    scopus 로고
    • Site-specific dephosphorylation of tau protein at Ser202/Thr205 in response to microtubule depolymerization in cultured human neurons involves protein phosphatase 2A
    • Merrick SE, Demoise DC, Lee VM. Site-specific dephosphorylation of tau protein at Ser202/Thr205 in response to microtubule depolymerization in cultured human neurons involves protein phosphatase 2A. J Biol Chem. 1996, 271:5589-94.
    • (1996) J Biol Chem. , vol.271 , pp. 5589-5594
    • Merrick, S.E.1    Demoise, D.C.2    Lee, V.M.3
  • 41
    • 0029123294 scopus 로고
    • The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and beta-amyloid in primary rat cortical neuronal cultures
    • Davis DR, Brion JP, Couck AM. The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and beta-amyloid in primary rat cortical neuronal cultures. Biochem J. 1995, 309:941-9.
    • (1995) Biochem J. , vol.309 , pp. 941-949
    • Davis, D.R.1    Brion, J.P.2    Couck, A.M.3
  • 42
    • 0026650367 scopus 로고
    • Effects of microtubule stabilization and destabilization on tau immunoreactivity in cultured hippocampal neurons
    • Mattson MP. Effects of microtubule stabilization and destabilization on tau immunoreactivity in cultured hippocampal neurons. Brain Res. 1992, 582:107-18.
    • (1992) Brain Res. , vol.582 , pp. 107-118
    • Mattson, M.P.1
  • 43
    • 0031559896 scopus 로고    scopus 로고
    • Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH-SY5Y cells
    • Carri MT, Ferri A, Battistoni A. Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca2+ concentration in transfected neuroblastoma SH-SY5Y cells. FEBS Lett. 1997, 414:365-8.
    • (1997) FEBS Lett. , vol.414 , pp. 365-368
    • Carri, M.T.1    Ferri, A.2    Battistoni, A.3
  • 44
    • 0037565274 scopus 로고    scopus 로고
    • Proteasome activation and nNOS down-regulation in neuroblastoma cells expressing a Cu,Zn superoxide dismutase mutant involved in familial ALS
    • Aquilano K, Rotilio G, Ciriolo MR. Proteasome activation and nNOS down-regulation in neuroblastoma cells expressing a Cu,Zn superoxide dismutase mutant involved in familial ALS. J Neurochem. 2003, 85:1324-35.
    • (2003) J Neurochem. , vol.85 , pp. 1324-1335
    • Aquilano, K.1    Rotilio, G.2    Ciriolo, M.R.3
  • 45
    • 43249095971 scopus 로고    scopus 로고
    • Transient cytoskeletal alterations after SOD1 depletion in neuroblastoma cells
    • Vigilanza P, Aquilano K, Rotilio G. Transient cytoskeletal alterations after SOD1 depletion in neuroblastoma cells. Cell Mol Life Sci. 2008, 65:991-1004.
    • (2008) Cell Mol Life Sci. , vol.65 , pp. 991-1004
    • Vigilanza, P.1    Aquilano, K.2    Rotilio, G.3
  • 46
    • 71849104860 scopus 로고
    • Protein measurement with the Folin phenol reagent
    • Lowry OH, Rosebrough NJ, Farr AL. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951, 193:265-75.
    • (1951) J Biol Chem. , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3
  • 47
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • Gamblin TC, Chen F, Zambrano A. Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc Natl Acad Sci USA. 2003, 100:10032-7.
    • (2003) Proc Natl Acad Sci USA. , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1    Chen, F.2    Zambrano, A.3
  • 48
    • 0033874144 scopus 로고    scopus 로고
    • Misdirected vimentin messenger RNA alters cell morphology and motility
    • Morris EJ, Evason K, Wiand C. Misdirected vimentin messenger RNA alters cell morphology and motility. J Cell Sci. 2000, 113:2433-43.
    • (2000) J Cell Sci. , vol.113 , pp. 2433-2443
    • Morris, E.J.1    Evason, K.2    Wiand, C.3
  • 49
    • 0025726216 scopus 로고
    • A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry
    • Nicoletti I, Migliorati G, Pagliacci MC. A rapid and simple method for measuring thymocyte apoptosis by propidium iodide staining and flow cytometry. J Immunol Methods. 1991, 139:271-9.
    • (1991) J Immunol Methods. , vol.139 , pp. 271-279
    • Nicoletti, I.1    Migliorati, G.2    Pagliacci, M.C.3
  • 50
    • 0031671581 scopus 로고    scopus 로고
    • Microtubule-damaging drugs triggered bcl2 phosphorylation-requirement of phosphorylation on both serine-70 and serine-87 residues of bcl2 protein
    • Basu A, Haldar S. Microtubule-damaging drugs triggered bcl2 phosphorylation-requirement of phosphorylation on both serine-70 and serine-87 residues of bcl2 protein. Int J Oncol. 1998, 13:659-64.
    • (1998) Int J Oncol. , vol.13 , pp. 659-664
    • Basu, A.1    Haldar, S.2
  • 51
    • 0035524625 scopus 로고    scopus 로고
    • Microtubule-targeting drugs induce bcl-2 phosphorylation and association with Pin1
    • Pathan N, Aime-Sempe C, Kitada S. Microtubule-targeting drugs induce bcl-2 phosphorylation and association with Pin1. Neoplasia. 2001, 3:550-9.
    • (2001) Neoplasia. , vol.3 , pp. 550-559
    • Pathan, N.1    Aime-Sempe, C.2    Kitada, S.3
  • 52
    • 33747401659 scopus 로고    scopus 로고
    • Tau phosphorylation and proteolysis: insights and perspectives
    • Johnson GV. Tau phosphorylation and proteolysis: insights and perspectives. J Alzheimers Dis. 2006, 9:243-50.
    • (2006) J Alzheimers Dis. , vol.9 , pp. 243-250
    • Johnson, G.V.1
  • 53
    • 0032540459 scopus 로고    scopus 로고
    • The regulation of phosphorylation of tau in SY5Y neuroblastoma cells: the role of protein phosphatases
    • Tanaka T, Zhong J, Iqbal K. The regulation of phosphorylation of tau in SY5Y neuroblastoma cells: the role of protein phosphatases. FEBS Lett. 1998, 426:248-54.
    • (1998) FEBS Lett. , vol.426 , pp. 248-254
    • Tanaka, T.1    Zhong, J.2    Iqbal, K.3
  • 54
    • 0036769791 scopus 로고    scopus 로고
    • Role of serine/threonine protein phosphatase in Alzheimer's disease
    • Tian Q, Wang J. Role of serine/threonine protein phosphatase in Alzheimer's disease. Neurosignals. 2002, 11:262-9.
    • (2002) Neurosignals. , vol.11 , pp. 262-269
    • Tian, Q.1    Wang, J.2
  • 55
    • 0030998758 scopus 로고    scopus 로고
    • Oxidative stress induces dephosphorylation of tau in rat brain primary neuronal cultures
    • Davis DR, Anderton BH, Brion JP. Oxidative stress induces dephosphorylation of tau in rat brain primary neuronal cultures. J Neurochem. 1997, 68:1590-7.
    • (1997) J Neurochem. , vol.68 , pp. 1590-1597
    • Davis, D.R.1    Anderton, B.H.2    Brion, J.P.3
  • 56
    • 33745819942 scopus 로고    scopus 로고
    • The peptidylprolyl cis/trans-isomerase Pin1 modulates stress-induced dephosphorylation of Tau in neurons. Implication in a pathological mechanism related to Alzheimer disease
    • Galas MC, Dourlen P, Begard S. The peptidylprolyl cis/trans-isomerase Pin1 modulates stress-induced dephosphorylation of Tau in neurons. Implication in a pathological mechanism related to Alzheimer disease. J Biol Chem. 2006, 281:19296-304.
    • (2006) J Biol Chem. , vol.281 , pp. 19296-19304
    • Galas, M.C.1    Dourlen, P.2    Begard, S.3
  • 57
    • 2342466091 scopus 로고    scopus 로고
    • Oxidative stress promotes tau dephosphorylation in neuronal cells: the roles of cdk5 and PP1
    • Zambrano CA, Egana JT, Nunez MT. Oxidative stress promotes tau dephosphorylation in neuronal cells: the roles of cdk5 and PP1. Free Radic Biol Med. 2004, 36:1393-402.
    • (2004) Free Radic Biol Med. , vol.36 , pp. 1393-1402
    • Zambrano, C.A.1    Egana, J.T.2    Nunez, M.T.3
  • 58
    • 0037102481 scopus 로고    scopus 로고
    • Differential susceptibilities of serine/threonine phosphatases to oxidative and nitrosative stress
    • Sommer D, Coleman S, Swanson SA. Differential susceptibilities of serine/threonine phosphatases to oxidative and nitrosative stress. Arch Biochem Biophys. 2002, 404:271-8.
    • (2002) Arch Biochem Biophys. , vol.404 , pp. 271-278
    • Sommer, D.1    Coleman, S.2    Swanson, S.A.3
  • 60
    • 0035968240 scopus 로고    scopus 로고
    • Neuronal Cdc2-like protein kinase (Cdk5/p25) is associated with protein phosphatase 1 and phosphorylates inhibitor-2
    • Agarwal-Mawal A, Paudel HK. Neuronal Cdc2-like protein kinase (Cdk5/p25) is associated with protein phosphatase 1 and phosphorylates inhibitor-2. J Biol Chem. 2001, 276:23712-8.
    • (2001) J Biol Chem. , vol.276 , pp. 23712-23718
    • Agarwal-Mawal, A.1    Paudel, H.K.2
  • 61
    • 0036257468 scopus 로고    scopus 로고
    • Antitumor activity of Z-ajoene, a natural compound purified from garlic: antimitotic and microtubule-interaction properties
    • Li M, Ciu JR, Ye Y. Antitumor activity of Z-ajoene, a natural compound purified from garlic: antimitotic and microtubule-interaction properties. Carcinogenesis. 2002, 23:573-9.
    • (2002) Carcinogenesis. , vol.23 , pp. 573-579
    • Li, M.1    Ciu, J.R.2    Ye, Y.3
  • 62
    • 0035500775 scopus 로고    scopus 로고
    • Actin carbonylation: from a simple marker of protein oxidation to relevant signs of severe functional impairment
    • Dalle-Donne I, Rossi R, Giustarini D. Actin carbonylation: from a simple marker of protein oxidation to relevant signs of severe functional impairment. Free Radic Biol Med. 2001, 31:1075-83.
    • (2001) Free Radic Biol Med. , vol.31 , pp. 1075-1083
    • Dalle-Donne, I.1    Rossi, R.2    Giustarini, D.3
  • 63
    • 0033302335 scopus 로고    scopus 로고
    • Tau protein in normal and Alzheimer's disease brain
    • Johnson GV, Jenkins SM. Tau protein in normal and Alzheimer's disease brain. J Alzheimers Dis. 1999, 1:307-28.
    • (1999) J Alzheimers Dis. , vol.1 , pp. 307-328
    • Johnson, G.V.1    Jenkins, S.M.2
  • 64
    • 1642289188 scopus 로고    scopus 로고
    • Role of tau protein in both physiological and pathological conditions
    • Avila J, Lucas JJ, Perez M. Role of tau protein in both physiological and pathological conditions. Physiol Rev. 2004, 84:361-84.
    • (2004) Physiol Rev. , vol.84 , pp. 361-384
    • Avila, J.1    Lucas, J.J.2    Perez, M.3
  • 65
    • 0031913730 scopus 로고    scopus 로고
    • Activation of a PP2A-like phosphatase and dephosphorylation of tau protein characterize onset of the execution phase of apoptosis
    • Mills JC, Lee VM, Pittman RN. Activation of a PP2A-like phosphatase and dephosphorylation of tau protein characterize onset of the execution phase of apoptosis. J Cell Sci. 1998, 111:625-36.
    • (1998) J Cell Sci. , vol.111 , pp. 625-636
    • Mills, J.C.1    Lee, V.M.2    Pittman, R.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.