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Volumn 39, Issue 3, 2004, Pages 243-250

The role of protein p53 in neurodegenerative processes throughout the 25 years of its history;La proteína p53 en procesos neurodegenerativos en sus 25 años de historia

Author keywords

Apoptosis; Cancer; Cell cycle; Genome; Mitochondria; Neurodegeneration; P53; Transcription factors

Indexed keywords

PROTEIN P53; VIRUS LARGE T ANTIGEN;

EID: 4744372189     PISSN: 02100010     EISSN: None     Source Type: Journal    
DOI: 10.33588/rn.3903.2004355     Document Type: Review
Times cited : (3)

References (126)
  • 1
    • 0018778606 scopus 로고
    • Identification and partial characterization of new antigens from simian virus 40-transformed mouse cells
    • Chang C, Simmons DT, Martin MA, Mora PT. Identification and partial characterization of new antigens from simian virus 40-transformed mouse cells. J Virol 1979; 31: 463-71.
    • (1979) J Virol , vol.31 , pp. 463-471
    • Chang, C.1    Simmons, D.T.2    Martin, M.A.3    Mora, P.T.4
  • 2
    • 0018769971 scopus 로고
    • Simian Virus 40-transformed cells express new species of proteins precipitable by anti-simian virus 40 serum
    • Kress M, May E, Cassingena R, May P. Simian Virus 40-transformed cells express new species of proteins precipitable by anti-simian virus 40 serum. J Virol 1979; 31: 472-83.
    • (1979) J Virol , vol.31 , pp. 472-483
    • Kress, M.1    May, E.2    Cassingena, R.3    May, P.4
  • 3
    • 0018348655 scopus 로고
    • T antigen is bound to a host protein in SV40-transformed cells
    • Lane DP, Crawford LV. T antigen is bound to a host protein in SV40-transformed cells. Nature 1979; 278: 261-3.
    • (1979) Nature , vol.278 , pp. 261-263
    • Lane, D.P.1    Crawford, L.V.2
  • 4
    • 0018760324 scopus 로고
    • Characterization of a 54 kDa cellular SV40 tumor antigen present in SV40-transformed cells and in unfected embryonal carcinoma cells
    • Linzer DIH, Levine AJ. Characterization of a 54 kDa cellular SV40 tumor antigen present in SV40-transformed cells and in unfected embryonal carcinoma cells. Cell 1979; 1: 43-52.
    • (1979) Cell , vol.1 , pp. 43-52
    • Linzer, D.I.H.1    Levine, A.J.2
  • 5
    • 0018348936 scopus 로고
    • Identification of new polypeptide species (48-55K) immunoprecipitable by antiserum to purified large T antigen and present in simian virus 40-infected and transformed cells
    • Melero JA, Stitt DT, Mangel WF, Carroll RB. Identification of new polypeptide species (48-55K) immunoprecipitable by antiserum to purified large T antigen and present in simian virus 40-infected and transformed cells. J Virol 1979; 93: 466-80.
    • (1979) J Virol , vol.93 , pp. 466-480
    • Melero, J.A.1    Stitt, D.T.2    Mangel, W.F.3    Carroll, R.B.4
  • 6
    • 0018743916 scopus 로고
    • Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse
    • De Leo AB, Jay G, Appella E, Dubois GC, Law LW, Old LJ. Detection of a transformation-related antigen in chemically induced sarcomas and other transformed cells of the mouse. Proc Natl Acad Sci 1979; 76: 2420-4.
    • (1979) Proc Natl Acad Sci , vol.76 , pp. 2420-2424
    • De Leo, A.B.1    Jay, G.2    Appella, E.3    Dubois, G.C.4    Law, L.W.5    Old, L.J.6
  • 7
    • 0018965514 scopus 로고
    • Abelson murine leukemia virus-induced tumors elicit antibodies against a host cell protein, p50
    • Rotter V, Witte ON, Coffman R, Baltimore D. Abelson murine leukemia virus-induced tumors elicit antibodies against a host cell protein, p50. J Virol 1980; 36: 547-55.
    • (1980) J Virol , vol.36 , pp. 547-555
    • Rotter, V.1    Witte, O.N.2    Coffman, R.3    Baltimore, D.4
  • 8
    • 0019898801 scopus 로고
    • Detection of antibodies against the cellular protein p53 in sera from patients with breast cancer
    • Crawford LV, Pim DC, Bulbrook RD. Detection of antibodies against the cellular protein p53 in sera from patients with breast cancer. Int J Cancer 1982; 30: 403-8.
    • (1982) Int J Cancer , vol.30 , pp. 403-408
    • Crawford, L.V.1    Pim, D.C.2    Bulbrook, R.D.3
  • 9
    • 0023153055 scopus 로고
    • Presence of circulating antibodies against cellular protein p53 in a notable proportion of children with B-cell lymphoma
    • Caron de Fromentel C, May-Levin F, Mouriesse H, Lemerle J, Chandrasekaran K, May P. Presence of circulating antibodies against cellular protein p53 in a notable proportion of children with B-cell lymphoma. Int J Cancer 1987; 39: 185-9.
    • (1987) Int J Cancer , vol.39 , pp. 185-189
    • Caron De Fromentel, C.1    May-Levin, F.2    Mouriesse, H.3    Lemerle, J.4    Chandrasekaran, K.5    May, P.6
  • 10
    • 0024382760 scopus 로고
    • The p53 proto-oncogene can act as a suppressor of transformation
    • Finlay CA, Hinds PW, Levine AJ. The p53 proto-oncogene can act as a suppressor of transformation. Cell 1989; 57: 1083-93.
    • (1989) Cell , vol.57 , pp. 1083-1093
    • Finlay, C.A.1    Hinds, P.W.2    Levine, A.J.3
  • 11
    • 0027109075 scopus 로고
    • Cancer. p53, guardian of the genome
    • Lane DP. Cancer. p53, guardian of the genome. Nature 1992; 358: 15-6.
    • (1992) Nature , vol.358 , pp. 15-16
    • Lane, D.P.1
  • 13
    • 0030812331 scopus 로고    scopus 로고
    • Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers
    • Kaghad M, Bonnet H, Yang A, Creancier L, Biscan JC, Valent A, et al. Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers. Cell 1997; 90: 809-19.
    • (1997) Cell , vol.90 , pp. 809-819
    • Kaghad, M.1    Bonnet, H.2    Yang, A.3    Creancier, L.4    Biscan, J.C.5    Valent, A.6
  • 14
    • 0032161624 scopus 로고    scopus 로고
    • p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing, and dominant-negative activities
    • Yang A, Kaghad M, Wang Y, Gillet E, Fleming MD, Dotsch V, et al. p63, a p53 homolog at 3q27-29, encodes multiple products with transactivating, death-inducing, and dominant-negative activities. Mol Cell 1998; 2: 305-16.
    • (1998) Mol Cell , vol.2 , pp. 305-316
    • Yang, A.1    Kaghad, M.2    Wang, Y.3    Gillet, E.4    Fleming, M.D.5    Dotsch, V.6
  • 15
    • 0035082243 scopus 로고    scopus 로고
    • Role of the newer p53 family proteins in malignancy
    • Irwin MS, Kaelin WG Jr. Role of the newer p53 family proteins in malignancy. Apoptosis 2001; 6: 17-29.
    • (2001) Apoptosis , vol.6 , pp. 17-29
    • Irwin, M.S.1    Kaelin Jr., W.G.2
  • 16
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho Y, Gorina S, Jeffrey PD, Pavletich NP. Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations. Science 1994; 265: 345-55.
    • (1994) Science , vol.265 , pp. 345-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 17
    • 0019830333 scopus 로고
    • Post-translational regulation of the 54K cellular tumor antigen in normal and transformed cells
    • Oren M, Maltzman W, Levine AJ. Post-translational regulation of the 54K cellular tumor antigen in normal and transformed cells. Mol Cell Biol 1981; 1: 101-10.
    • (1981) Mol Cell Biol , vol.1 , pp. 101-110
    • Oren, M.1    Maltzman, W.2    Levine, A.J.3
  • 18
    • 0022390692 scopus 로고
    • p53 cellular tumor antigen: Analysis of mRNA levels in normal adult tissues, embryos, and tumors
    • Rogel A, Popliker M, Webb CG, Oren M. p53 cellular tumor antigen: analysis of mRNA levels in normal adult tissues, embryos, and tumors. Mol Cell Biol 1985; 5: 2851-5.
    • (1985) Mol Cell Biol , vol.5 , pp. 2851-2855
    • Rogel, A.1    Popliker, M.2    Webb, C.G.3    Oren, M.4
  • 23
    • 0030722533 scopus 로고    scopus 로고
    • Intracellular localization of p53 tumor suppressor protein in gamma-irradiated cells in cell cycle regulated and determined by the nucleus
    • Komarova EA, Zelnick CR, Chin D, Zeremski M, Gleiberman AS, Bacus SS, et al. Intracellular localization of p53 tumor suppressor protein in gamma-irradiated cells in cell cycle regulated and determined by the nucleus. Cancer Res 1997; 57: 5217-20.
    • (1997) Cancer Res , vol.57 , pp. 5217-5220
    • Komarova, E.A.1    Zelnick, C.R.2    Chin, D.3    Zeremski, M.4    Gleiberman, A.S.5    Bacus, S.S.6
  • 25
    • 0029964158 scopus 로고    scopus 로고
    • A reversible, p53-dependent G0/G1 cell cycle arrest induced by ribonucleotide depletion in the absence of detectable DNA damage
    • Linke SP, Clarkin KC, Di Leonardo A, Tsou A, Wahl GM. A reversible, p53-dependent G0/G1 cell cycle arrest induced by ribonucleotide depletion in the absence of detectable DNA damage. Genes Dev 1996; 10: 934-47.
    • (1996) Genes Dev , vol.10 , pp. 934-947
    • Linke, S.P.1    Clarkin, K.C.2    Di Leonardo, A.3    Tsou, A.4    Wahl, G.M.5
  • 26
    • 0030025773 scopus 로고    scopus 로고
    • Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours
    • Graeber TG, Osmanian C, Jacks T, Housman DE, Koch CJ, Lowe SW, et al. Hypoxia-mediated selection of cells with diminished apoptotic potential in solid tumours. Nature 1996; 379: 88-91.
    • (1996) Nature , vol.379 , pp. 88-91
    • Graeber, T.G.1    Osmanian, C.2    Jacks, T.3    Housman, D.E.4    Koch, C.J.5    Lowe, S.W.6
  • 27
    • 15844364884 scopus 로고    scopus 로고
    • p53-dependent induction of WAF1 by heat treatment in human glioblastoma cells
    • Ohnishi T, Wang X, Ohnishi K, Matsumoto H, Takahashi A. p53-dependent induction of WAF1 by heat treatment in human glioblastoma cells. J Biol Chem 1996; 271: 14510-3.
    • (1996) J Biol Chem , vol.271 , pp. 14510-14513
    • Ohnishi, T.1    Wang, X.2    Ohnishi, K.3    Matsumoto, H.4    Takahashi, A.5
  • 28
    • 9244232804 scopus 로고    scopus 로고
    • Nitric oxide-induced p53 accumulation and regulation of inducible nitric oxide synthase expression by wild-type p53
    • Forrester K, Ambs S, Lupold SE, Kapust RB, Spillare EA, Weinberg WC, et al. Nitric oxide-induced p53 accumulation and regulation of inducible nitric oxide synthase expression by wild-type p53. Proc Natl Acad Sci 1996; 93: 2442-7.
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 2442-2447
    • Forrester, K.1    Ambs, S.2    Lupold, S.E.3    Kapust, R.B.4    Spillare, E.A.5    Weinberg, W.C.6
  • 30
    • 0027749169 scopus 로고
    • A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein
    • Bargonetti J, Manfredi JJ, Chen X, Marshak DR, Prives C. A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein. Genes Dev 1993; 7: 2565-74.
    • (1993) Genes Dev , vol.7 , pp. 2565-2574
    • Bargonetti, J.1    Manfredi, J.J.2    Chen, X.3    Marshak, D.R.4    Prives, C.5
  • 31
    • 0027406042 scopus 로고
    • Isolation and characterization of DNA sequences that are specifically bound by wild-type p53 protein
    • Foord O, Navot N, Rotter V. Isolation and characterization of DNA sequences that are specifically bound by wild-type p53 protein. Mol Cell Biol 1993; 13: 1378-84.
    • (1993) Mol Cell Biol , vol.13 , pp. 1378-1384
    • Foord, O.1    Navot, N.2    Rotter, V.3
  • 32
    • 0037038699 scopus 로고    scopus 로고
    • Groups of p53 target genes involved in specific p53 downstream effects cluster into different classes of DNA binding sites
    • Qian H, Wang T, Naumovski L, López CD, Brachmann RK. Groups of p53 target genes involved in specific p53 downstream effects cluster into different classes of DNA binding sites. Oncogene 2002; 21: 7901-11.
    • (2002) Oncogene , vol.21 , pp. 7901-7911
    • Qian, H.1    Wang, T.2    Naumovski, L.3    López, C.D.4    Brachmann, R.K.5
  • 33
    • 0031840253 scopus 로고    scopus 로고
    • ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins
    • Waterman MJ, Stavridi ES, Waterman JL, Halazonetis TD. ATM-dependent activation of p53 involves dephosphorylation and association with 14-3-3 proteins. Nat Genet 1998; 19: 175-8.
    • (1998) Nat Genet , vol.19 , pp. 175-178
    • Waterman, M.J.1    Stavridi, E.S.2    Waterman, J.L.3    Halazonetis, T.D.4
  • 34
    • 0021616838 scopus 로고
    • UV irradiation stimulates levels of p53 cellular tumor antigen in nontransformed mouse cells
    • Maltzman W, Czyzyk L. UV irradiation stimulates levels of p53 cellular tumor antigen in nontransformed mouse cells. Mol Cell Biol 1984; 4: 1689-94.
    • (1984) Mol Cell Biol , vol.4 , pp. 1689-1694
    • Maltzman, W.1    Czyzyk, L.2
  • 35
    • 0030610565 scopus 로고    scopus 로고
    • The CDK7-cycH-p36 complex of transcription factor IIH phosphorylates p53, enhancing its sequence-specific DNA binding activity in vitro
    • Lu H, Fisher RP, Bailey P, Levine AJ. The CDK7-cycH-p36 complex of transcription factor IIH phosphorylates p53, enhancing its sequence-specific DNA binding activity in vitro. Mol Cell Biol 1997; 17: 5923-34.
    • (1997) Mol Cell Biol , vol.17 , pp. 5923-5934
    • Lu, H.1    Fisher, R.P.2    Bailey, P.3    Levine, A.J.4
  • 36
    • 0029993161 scopus 로고    scopus 로고
    • Murine p53 is phosphorylated within the PAb421 epitope by protein kinase C in vitro, but not in vivo, even after stimulation with the phorbol ester o-tetradecanoylphorbol 13-acetate
    • Milne DM, McKendrick L, Jardine LJ, Deacon E, Lord JM, Meek DW. Murine p53 is phosphorylated within the PAb421 epitope by protein kinase C in vitro, but not in vivo, even after stimulation with the phorbol ester o-tetradecanoylphorbol 13-acetate. Oncogene 1996; 13: 205-11.
    • (1996) Oncogene , vol.13 , pp. 205-211
    • Milne, D.M.1    McKendrick, L.2    Jardine, L.J.3    Deacon, E.4    Lord, J.M.5    Meek, D.W.6
  • 37
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53(1)
    • Maki CG, Huibregtse JM, Howley PM. In vivo ubiquitination and proteasome-mediated degradation of p53(1). Cancer Res 1996; 56: 2649-54.
    • (1996) Cancer Res , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 38
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat MH, Vousden KH. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol Cell Biol 1997; 17: 460-8.
    • (1997) Mol Cell Biol , vol.17 , pp. 460-468
    • Kubbutat, M.H.1    Vousden, K.H.2
  • 39
    • 0035794541 scopus 로고    scopus 로고
    • COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system
    • Bech-Otschir D, Kraft R, Huang X, Henklein P, Kapelari B, Pollmann C, et al. COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system. EMBO J 2001; 20: 1630-9.
    • (2001) EMBO J , vol.20 , pp. 1630-1639
    • Bech-Otschir, D.1    Kraft, R.2    Huang, X.3    Henklein, P.4    Kapelari, B.5    Pollmann, C.6
  • 40
    • 0029985647 scopus 로고    scopus 로고
    • Cell type-specific inhibition of p53-mediated apoptosis by mdm2
    • Haupt Y, Barak Y, Oren M. Cell type-specific inhibition of p53-mediated apoptosis by mdm2. EMBO J 1996; 15: 1596-606.
    • (1996) EMBO J , vol.15 , pp. 1596-1606
    • Haupt, Y.1    Barak, Y.2    Oren, M.3
  • 41
  • 42
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao W, Levine AJ. Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc Natl Acad Sci USA 1999; 96: 3077-80.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 43
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R, Tanaka H, Yasuda H. Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53, FEBS Lett 1997; 420: 25-7.
    • (1997) FEBS Lett , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 44
    • 0027459198 scopus 로고
    • mdm2 expression is induced by wild type p53 activity
    • Barak Y, Juven T, Haffner R, Oren M. mdm2 expression is induced by wild type p53 activity. EMBO J 1993; 12: 461-8.
    • (1993) EMBO J , vol.12 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 45
    • 0033579412 scopus 로고    scopus 로고
    • Regulation of the p53 tumor suppressor protein
    • Oren M. Regulation of the p53 tumor suppressor protein. J Biol Chem 1999; 274: 36031-4.
    • (1999) J Biol Chem , vol.274 , pp. 36031-36034
    • Oren, M.1
  • 46
    • 0030881590 scopus 로고    scopus 로고
    • Differential regulation of the p21/WAF-1 and mdm2 genes after high-dose UV irradiation: p53-dependent and p53-independent regulation of the mdm2 gene
    • Wu L, Levine AJ. Differential regulation of the p21/WAF-1 and mdm2 genes after high-dose UV irradiation: p53-dependent and p53-independent regulation of the mdm2 gene. Mol Med 1997; 3: 441-51.
    • (1997) Mol Med , vol.3 , pp. 441-451
    • Wu, L.1    Levine, A.J.2
  • 47
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN, Roe AE, Donehower LA, Bradley A. Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 1995; 378: 206-8.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 49
    • 1542358136 scopus 로고    scopus 로고
    • Inhibition of p53 degradation by Mdm2 acetylation
    • Wang X, Taplick J, Geva N, Oren M. Inhibition of p53 degradation by Mdm2 acetylation. FEBS Lett 2004; 561: 195-201.
    • (2004) FEBS Lett , vol.561 , pp. 195-201
    • Wang, X.1    Taplick, J.2    Geva, N.3    Oren, M.4
  • 50
    • 0027155885 scopus 로고
    • Mutation of the serine 15 phosphorylation site of human p53 reduces the ability of p53 to inhibit cell cycle progression
    • Fiscella M, Ullrich SJ, Zambrano N, Shields MT, Lin D, Lees-Miller SP, et al. Mutation of the serine 15 phosphorylation site of human p53 reduces the ability of p53 to inhibit cell cycle progression. Oncogene 1993; 8: 1519-28.
    • (1993) Oncogene , vol.8 , pp. 1519-1528
    • Fiscella, M.1    Ullrich, S.J.2    Zambrano, N.3    Shields, M.T.4    Lin, D.5    Lees-Miller, S.P.6
  • 51
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh SY, Ikeda M, Taya Y, Prives C. DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 1997; 91: 325-34.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 53
    • 1242294418 scopus 로고    scopus 로고
    • Decreased p21 levels are required for efficient restart of DNA synthesis after S phase block
    • Gottifredi V, McKinney K, Poyurovsky MV, Prives C. Decreased p21 levels are required for efficient restart of DNA synthesis after S phase block. J Biol Chem 2004; 279: 5802-10.
    • (2004) J Biol Chem , vol.279 , pp. 5802-5810
    • Gottifredi, V.1    McKinney, K.2    Poyurovsky, M.V.3    Prives, C.4
  • 54
    • 0029980043 scopus 로고    scopus 로고
    • p53 in growth control and neoplasia
    • Gottlieb TM, Oren M. p53 in growth control and neoplasia. Biochem Biophys Acta 1996; 1287: 77-102.
    • (1996) Biochem Biophys Acta , vol.1287 , pp. 77-102
    • Gottlieb, T.M.1    Oren, M.2
  • 55
    • 0034594978 scopus 로고    scopus 로고
    • A ribonucleotide reductase gene involved in a p53.dependent cell-cycle checkpoint for DNA damage
    • Tanaka H, Arakawa H, Yamaguchi T, Shiraishi K, Fukuda S, Matsui K, et al. A ribonucleotide reductase gene involved in a p53.dependent cell-cycle checkpoint for DNA damage. Nature 2000; 404: 42-9.
    • (2000) Nature , vol.404 , pp. 42-49
    • Tanaka, H.1    Arakawa, H.2    Yamaguchi, T.3    Shiraishi, K.4    Fukuda, S.5    Matsui, K.6
  • 56
    • 0033812557 scopus 로고    scopus 로고
    • Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis
    • Lin Y, Ma W, Benchimol S. Pidd, a new death-domain-containing protein, is induced by p53 and promotes apoptosis. Nat Genet 2000; 26: 122-7.
    • (2000) Nat Genet , vol.26 , pp. 122-127
    • Lin, Y.1    Ma, W.2    Benchimol, S.3
  • 57
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A, Dixit VM. Death receptors: signaling and modulation. Science 1998; 281: 1305-8.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 58
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai ZN, Milliman CL, Korsmeyer SJ. Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 1993; 74: 609-19.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 59
    • 0033120591 scopus 로고    scopus 로고
    • Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase
    • Harada H, Becknell B, Wilm M, Mann M, Huang LJ, Taylor SS, et al. Phosphorylation and inactivation of BAD by mitochondria-anchored protein kinase. A Mol Cell 1999; 3: 413-22.
    • (1999) A Mol Cell , vol.3 , pp. 413-422
    • Harada, H.1    Becknell, B.2    Wilm, M.3    Mann, M.4    Huang, L.J.5    Taylor, S.S.6
  • 60
    • 0035496905 scopus 로고    scopus 로고
    • Interleukin-5 inhibits translocation of Bax to the mitochondria, cytochrome c release, and activation of caspases in human eosinophils
    • Dewson G, Cohen GM, Wardlaw AJ. Interleukin-5 inhibits translocation of Bax to the mitochondria, cytochrome c release, and activation of caspases in human eosinophils. Blood 2001; 98: 2239-47.
    • (2001) Blood , vol.98 , pp. 2239-2247
    • Dewson, G.1    Cohen, G.M.2    Wardlaw, A.J.3
  • 61
    • 0035833337 scopus 로고    scopus 로고
    • Bax translocation is crucial for the sensitivity of leukaemic cells to etoposide-induced apoptosis
    • Jia L, Patwari Y, Srinivasula SM, Newland AC, Fernandes-Alnemri T, Alnemri ES, et al. Bax translocation is crucial for the sensitivity of leukaemic cells to etoposide-induced apoptosis. Oncogene 2001; 20: 4817-26.
    • (2001) Oncogene , vol.20 , pp. 4817-4826
    • Jia, L.1    Patwari, Y.2    Srinivasula, S.M.3    Newland, A.C.4    Fernandes-Alnemri, T.5    Alnemri, E.S.6
  • 62
    • 0033713002 scopus 로고    scopus 로고
    • Structure of Bax: Coregulation of dimer formation and intracellular localization
    • Suzuki M, Youle RJ, Tjandra N. Structure of Bax: coregulation of dimer formation and intracellular localization. Cell 2000; 103: 645-54.
    • (2000) Cell , vol.103 , pp. 645-654
    • Suzuki, M.1    Youle, R.J.2    Tjandra, N.3
  • 63
    • 0035844867 scopus 로고    scopus 로고
    • Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis
    • Nechushtan A, Smith CL, Lamensdoff I, Yoon SH, Youle RJ. Bax and Bak coalesce into novel mitochondria-associated clusters during apoptosis. J Cell Biol 2001; 153: 1265-76.
    • (2001) J Cell Biol , vol.153 , pp. 1265-1276
    • Nechushtan, A.1    Smith, C.L.2    Lamensdoff, I.3    Yoon, S.H.4    Youle, R.J.5
  • 64
    • 0034710940 scopus 로고    scopus 로고
    • Peg3/Pw1 promotes p53-mediated apoptosis by inducing Bax translocation from cytosol to mitochondria
    • Deng Y, Wu X. Peg3/Pw1 promotes p53-mediated apoptosis by inducing Bax translocation from cytosol to mitochondria. Proc Natl Acad Sci 2000; 97: 12050-5.
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 12050-12055
    • Deng, Y.1    Wu, X.2
  • 65
    • 0029976253 scopus 로고    scopus 로고
    • DNA damage and apoptosis in Alzheimer's disease: Colocalization with c-Jun immunoreactivity, relationship to brain area and effect of post mortem delay
    • Anderson AJ, Su JH, Cotman CW. DNA damage and apoptosis in Alzheimer's disease: colocalization with c-Jun immunoreactivity, relationship to brain area and effect of post mortem delay. J Neurosci 1996; 16: 1710-9.
    • (1996) J Neurosci , vol.16 , pp. 1710-1719
    • Anderson, A.J.1    Su, J.H.2    Cotman, C.W.3
  • 66
    • 0030831489 scopus 로고    scopus 로고
    • Corretates of p53- and Fas (CD95)-mediated apoptosis in Alzheimer's disease
    • De la Monte SM, Sohn YK, Wands JR. Corretates of p53- and Fas (CD95)-mediated apoptosis in Alzheimer's disease. J Neurol Sci 1997; 152: 73-83.
    • (1997) J Neurol Sci , vol.152 , pp. 73-83
    • De La Monte, S.M.1    Sohn, Y.K.2    Wands, J.R.3
  • 67
    • 0030638139 scopus 로고    scopus 로고
    • Bax protein expression is increased in Alzheimers brain: Correlations with DNA damage, Bcl-2 expression, and brain pathology
    • Su JH, Deng GM, Cotman CW. Bax protein expression is increased in Alzheimers brain: correlations with DNA damage, Bcl-2 expression, and brain pathology. J Neuropathol. Exp. Neurol 1997; 56: 86-93.
    • (1997) J Neuropathol Exp Neurol , vol.56 , pp. 86-93
    • Su, J.H.1    Deng, G.M.2    Cotman, C.W.3
  • 68
    • 2642620565 scopus 로고    scopus 로고
    • Bcl-2 and Bax protein expression in Alzheimer's disease
    • Tortosa A, López W, Ferrer I. Bcl-2 and Bax protein expression in Alzheimer's disease. Acta Neuropathol 1998; 95: 407-12.
    • (1998) Acta Neuropathol , vol.95 , pp. 407-412
    • Tortosa, A.1    López, W.2    Ferrer, I.3
  • 69
    • 0032509773 scopus 로고    scopus 로고
    • Alteration of proteins regulating apoptosis, Bcl-2, Bcl-x, Bax, Bad, ICH-1 and CPP32, in Alzheimer's disease
    • Kitamura Y, Shimohama S, Kamoshima W, Ota T, Matsuoka ¿¿INICIAL??, Nomura Y, et al. Alteration of proteins regulating apoptosis, Bcl-2, Bcl-x, Bax, Bad, ICH-1 and CPP32, in Alzheimer's disease. Brain Res 1998; 780: 260-9.
    • (1998) Brain Res , vol.780 , pp. 260-269
    • Kitamura, Y.1    Shimohama, S.2    Kamoshima, W.3    Ota, T.4    Matsuoka5    Nomura, Y.6
  • 70
    • 0032993576 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative diseases: The role of mithocondria
    • Tatton WG, Olanow CW. Apoptosis in neurodegenerative diseases: the role of mithocondria. Biochem Biophys Acta 1999; 1410: 195-214.
    • (1999) Biochem Biophys Acta , vol.1410 , pp. 195-214
    • Tatton, W.G.1    Olanow, C.W.2
  • 71
    • 0031668930 scopus 로고    scopus 로고
    • Programmed cell death: Does it playa role in Parkinson's disease?
    • Burke RE, Kholodilov NG. Programmed cell death: does it playa role in Parkinson's disease? Ann Neurol 1998; 44: 126-33.
    • (1998) Ann Neurol , vol.44 , pp. 126-133
    • Burke, R.E.1    Kholodilov, N.G.2
  • 73
    • 0031013141 scopus 로고    scopus 로고
    • Apoptotic-like changes in Lewy-body-associated disorders and normal aging in substantia nigral neurons
    • Tompkins MM, Basgall EJ, Zamrini E, Hill WD. Apoptotic-like changes in Lewy-body-associated disorders and normal aging in substantia nigral neurons. Am J Pathol 1997; 150: 119-31.
    • (1997) Am J Pathol , vol.150 , pp. 119-131
    • Tompkins, M.M.1    Basgall, E.J.2    Zamrini, E.3    Hill, W.D.4
  • 74
    • 0029040355 scopus 로고
    • In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes
    • Dragunow M, Faull RL, Lawlor P, Beilharz EJ, Singleton K, Walker EB, et al. In situ evidence for DNA fragmentation in Huntington's disease striatum and Alzheimer's disease temporal lobes. Neuroreport 1995; 6: 1053-7.
    • (1995) Neuroreport , vol.6 , pp. 1053-1057
    • Dragunow, M.1    Faull, R.L.2    Lawlor, P.3    Beilharz, E.J.4    Singleton, K.5    Walker, E.B.6
  • 75
    • 0032581167 scopus 로고    scopus 로고
    • Trinucleotide (CAG) repeat length is positively correlated with the degree of DNA fragmentation in Huntington's disease striatum
    • Butterworth NJ, Williams L, Bullock JY, Love DR, Faull RL, Dragunow M. Trinucleotide (CAG) repeat length is positively correlated with the degree of DNA fragmentation in Huntington's disease striatum. Neuroscience 1998; 87: 49-53.
    • (1998) Neuroscience , vol.87 , pp. 49-53
    • Butterworth, N.J.1    Williams, L.2    Bullock, J.Y.3    Love, D.R.4    Faull, R.L.5    Dragunow, M.6
  • 76
    • 0036260697 scopus 로고    scopus 로고
    • Cellular response to oxidative stress: Signaling for suicide and survival
    • Martindale JL, Holbrook NJ. Cellular response to oxidative stress: signaling for suicide and survival. J Cell Physiol 2002; 192: 1-15.
    • (2002) J Cell Physiol , vol.192 , pp. 1-15
    • Martindale, J.L.1    Holbrook, N.J.2
  • 77
    • 0035003439 scopus 로고    scopus 로고
    • Chemistry and biochemistry of oxidative stress in neurodegenerative disease
    • Sayre LM, Smith MA, Perry G. Chemistry and biochemistry of oxidative stress in neurodegenerative disease. Curr Med Chem 2001; 8: 721-38.
    • (2001) Curr Med Chem , vol.8 , pp. 721-738
    • Sayre, L.M.1    Smith, M.A.2    Perry, G.3
  • 78
    • 0030884358 scopus 로고    scopus 로고
    • Apoptosis and protein expression after focal cerebral ischemia in rat
    • Li Y, Chopp M, Powers C, Jiang N. Apoptosis and protein expression after focal cerebral ischemia in rat. Brain Res 1997; 765: 301-12.
    • (1997) Brain Res , vol.765 , pp. 301-312
    • Li, Y.1    Chopp, M.2    Powers, C.3    Jiang, N.4
  • 79
    • 0036498286 scopus 로고    scopus 로고
    • Inmunohistochemical study of p53-associated proteins in rat brain following lithium-pilocarpine status epilepticus
    • Tan Z, Sankar R, Shin D, Sun N, Liu H, Wasterlain CG, et al. Inmunohistochemical study of p53-associated proteins in rat brain following lithium-pilocarpine status epilepticus. Brain Res 2002; 929: 129-38.
    • (2002) Brain Res , vol.929 , pp. 129-138
    • Tan, Z.1    Sankar, R.2    Shin, D.3    Sun, N.4    Liu, H.5    Wasterlain, C.G.6
  • 81
    • 0033059025 scopus 로고    scopus 로고
    • The tumor-suppressor gene, p53, is induced in injured brain regions following experimental traumatic brain injury
    • Napieralski JA, Raghupathi R, McIntosh TK. The tumor-suppressor gene, p53, is induced in injured brain regions following experimental traumatic brain injury. Brain Res Mol Brain Res 1999; 71: 78-86.
    • (1999) Brain Res Mol Brain Res , vol.71 , pp. 78-86
    • Napieralski, J.A.1    Raghupathi, R.2    McIntosh, T.K.3
  • 82
    • 0043180531 scopus 로고    scopus 로고
    • Excitotoxic and excitoprotective mechanisms: Abundant targets for the prevention and treatment of neurodegenerative disorders
    • Mattson MP. Excitotoxic and excitoprotective mechanisms: abundant targets for the prevention and treatment of neurodegenerative disorders. Neuromolecular Med 2003; 3: 65-94.
    • (2003) Neuromolecular Med , vol.3 , pp. 65-94
    • Mattson, M.P.1
  • 83
    • 0037418596 scopus 로고    scopus 로고
    • Involvement of DNA damage and repair systems in neurodegenerative process
    • Uberti D, Ferrari-Toninelli G, Memo M. Involvement of DNA damage and repair systems in neurodegenerative process. Toxicol Lett 2003; 139: 99-105.
    • (2003) Toxicol Lett , vol.139 , pp. 99-105
    • Uberti, D.1    Ferrari-Toninelli, G.2    Memo, M.3
  • 85
    • 0031842231 scopus 로고    scopus 로고
    • Induction of tumour-suppressor phosphoprotein p53 in the apoptosis of cultured rat cerebellar neurones triggered by excitatory amino acids
    • Uberti D, Belloni M, Grilli M, Spano P, Memo M. Induction of tumour-suppressor phosphoprotein p53 in the apoptosis of cultured rat cerebellar neurones triggered by excitatory amino acids. Eur J Neurosci 1998; 10: 246-54.
    • (1998) Eur J Neurosci , vol.10 , pp. 246-254
    • Uberti, D.1    Belloni, M.2    Grilli, M.3    Spano, P.4    Memo, M.5
  • 86
    • 0034214879 scopus 로고    scopus 로고
    • Contribution of NF-kappaB and p53 in the glutamate-induced apoptosis
    • Uberti D, Grilli M, Memo M. Contribution of NF-kappaB and p53 in the glutamate-induced apoptosis. Int J Dev Neurosci 2000; 18: 447-54.
    • (2000) Int J Dev Neurosci , vol.18 , pp. 447-454
    • Uberti, D.1    Grilli, M.2    Memo, M.3
  • 87
    • 0033525538 scopus 로고    scopus 로고
    • Long term lithium treatment suppresses p53 and Bax expression but increases Bcl-2 expression. A prominent role in neuroprotection against excitotoxicity
    • Chen RW, Chuang DM. Long term lithium treatment suppresses p53 and Bax expression but increases Bcl-2 expression. A prominent role in neuroprotection against excitotoxicity. J Biol Chem 1999; 274: 6039-42.
    • (1999) J Biol Chem , vol.274 , pp. 6039-6042
    • Chen, R.W.1    Chuang, D.M.2
  • 88
    • 0033593608 scopus 로고    scopus 로고
    • Free radical scavenger OPC-14117 attenuates quinolinic acid-induced NF-kappaB activation and apoptosis in rat striatum
    • Nakai M, Qin ZH, Wang Y, Chase TN. Free radical scavenger OPC-14117 attenuates quinolinic acid-induced NF-kappaB activation and apoptosis in rat striatum. Brain Res Mol Brain Res 1999; 64: 59-68.
    • (1999) Brain Res Mol Brain Res , vol.64 , pp. 59-68
    • Nakai, M.1    Qin, Z.H.2    Wang, Y.3    Chase, T.N.4
  • 89
    • 0028577208 scopus 로고
    • Immunohistochemical evidence for apoptosis in Alzheimer's disease
    • Su JH, Anderson AJ, Cummings BJ, Cotman CW. Immunohistochemical evidence for apoptosis in Alzheimer's disease. Neuroreport 1994; 5: 2529-33.
    • (1994) Neuroreport , vol.5 , pp. 2529-2533
    • Su, J.H.1    Anderson, A.J.2    Cummings, B.J.3    Cotman, C.W.4
  • 91
    • 0036728812 scopus 로고    scopus 로고
    • Abeta [25-35] peptide and iron promote apoptosis in lymphocytes by an oxidative stress mechanism: Involvement of H2O2, caspase-3, NF-kappaB, p53 and c-Jun
    • Vélez-Pardo C, Ospina GG, Jiménez-Del Río M. Abeta [25-35] peptide and iron promote apoptosis in lymphocytes by an oxidative stress mechanism: involvement of H2O2, caspase-3, NF-kappaB, p53 and c-Jun. Neurotoxicology 2002; 23: 351-65.
    • (2002) Neurotoxicology , vol.23 , pp. 351-365
    • Vélez-Pardo, C.1    Ospina, G.G.2    Jiménez-Del Río, M.3
  • 92
    • 0041304626 scopus 로고    scopus 로고
    • El daño neuronal se correlaciona con la detección in situ de los factores de transcripción c-Jun, factor nuclear kB, p53 y Par-4 y en la entermedad de Alzheimer
    • García-Ospina GP, Jiménez-Del Río M, Lopera F, Vélez-Pardo C. El daño neuronal se correlaciona con la detección in situ de los factores de transcripción c-Jun, factor nuclear kB, p53 y Par-4 y en la entermedad de Alzheimer. Rev Neurol 2003; 36: 1004-10.
    • (2003) Rev Neurol , vol.36 , pp. 1004-1010
    • García-Ospina, G.P.1    Jiménez-Del Río, M.2    Lopera, F.3    Vélez-Pardo, C.4
  • 93
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 1994; 77: 817-27.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 94
    • 9044243405 scopus 로고    scopus 로고
    • Protective effect of transforming growth factor-beta 1 on beta-amyloid neurotoxicity in rat hippocampal neurons
    • Prehn JH, Bindokas VP, Jordan J, Galindo MF, Ghadge GD, et al. Protective effect of transforming growth factor-beta 1 on beta-amyloid neurotoxicity in rat hippocampal neurons. Mol Pharmacol 1996; 49: 319-28.
    • (1996) Mol Pharmacol , vol.49 , pp. 319-328
    • Prehn, J.H.1    Bindokas, V.P.2    Jordan, J.3    Galindo, M.F.4    Ghadge, G.D.5
  • 95
    • 0031857269 scopus 로고    scopus 로고
    • Microwave irradiation lowers immunohistological detection thresholds for p53 protein in squamous epithelium from non-neoplastic oesophagus
    • Darnton SJ, Jenner K. Microwave irradiation lowers immunohistological detection thresholds for p53 protein in squamous epithelium from non-neoplastic oesophagus. J Pathol 1998; 185: 334-5.
    • (1998) J Pathol , vol.185 , pp. 334-335
    • Darnton, S.J.1    Jenner, K.2
  • 96
    • 0027973861 scopus 로고
    • Expression of p53 protein in oesophageal carcinoma: Clinicopathological correlation and prognostic significance
    • Vijeyasingam R, Darnton SJ, Jenner K, Allen CA, Billingham C, Matthews HR. Expression of p53 protein in oesophageal carcinoma: clinicopathological correlation and prognostic significance. Br J Surg 1994; 81: 1623-6.
    • (1994) Br J Surg , vol.81 , pp. 1623-1626
    • Vijeyasingam, R.1    Darnton, S.J.2    Jenner, K.3    Allen, C.A.4    Billingham, C.5    Matthews, H.R.6
  • 97
    • 0028528280 scopus 로고
    • p53 and PCNA expression in malignant melanomas of the head and neck
    • Girod SC, Groth W, Junk M, Gerlach KL. p53 and PCNA expression in malignant melanomas of the head and neck. Pigment Cell Res 1994; 7: 354-7.
    • (1994) Pigment Cell Res , vol.7 , pp. 354-357
    • Girod, S.C.1    Groth, W.2    Junk, M.3    Gerlach, K.L.4
  • 99
    • 0028982274 scopus 로고
    • p21ras as a common signaling target of reactive free radicals and cellular redox stress
    • Lander HM, Ogiste JS, Teng KK, Novogrodsky A, p21ras as a common signaling target of reactive free radicals and cellular redox stress. J Biol Chem 1995; 270: 21195-8.
    • (1995) J Biol Chem , vol.270 , pp. 21195-21198
    • Lander, H.M.1    Ogiste, J.S.2    Teng, K.K.3    Novogrodsky, A.4
  • 100
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso OA, Chiariello M, Yu JC, Teramoto H, Crespo P, Xu N, et al. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 1995; 81: 1137-46.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6
  • 101
    • 0028934827 scopus 로고
    • Transforming G protein-coupled receptors potently activate JNK (SAPK). Evidence for a divergence from the tyrosine kinase signaling pathway
    • Coso OA, Chiariello M, Kalinec G, Kyriakis JM, Woodgett J, Gutkind JS. Transforming G protein-coupled receptors potently activate JNK (SAPK). Evidence for a divergence from the tyrosine kinase signaling pathway. J Biol Chem 1995; 270: 5620-4.
    • (1995) J Biol Chem , vol.270 , pp. 5620-5624
    • Coso, O.A.1    Chiariello, M.2    Kalinec, G.3    Kyriakis, J.M.4    Woodgett, J.5    Gutkind, J.S.6
  • 102
    • 0028167599 scopus 로고
    • NF-kappa B activation of p53. A potential mechanism for suppressing cell growth in response to stress
    • Wu H, Lozano G. NF-kappa B activation of p53. A potential mechanism for suppressing cell growth in response to stress. J Biol Chem 1994; 9: 20067-74.
    • (1994) J Biol Chem , vol.9 , pp. 20067-20074
    • Wu, H.1    Lozano, G.2
  • 104
    • 85047697335 scopus 로고    scopus 로고
    • A conserved intronic response element mediates direct p53-dependent transcriptional activation of both the human and murine bax genes
    • Thornborrow EC, Patel S, Mastropietro AE, Schwartzfarb EM, Manfredi JJ. A conserved intronic response element mediates direct p53-dependent transcriptional activation of both the human and murine bax genes. Oncogene 2002; 21: 990-9.
    • (2002) Oncogene , vol.21 , pp. 990-999
    • Thornborrow, E.C.1    Patel, S.2    Mastropietro, A.E.3    Schwartzfarb, E.M.4    Manfredi, J.J.5
  • 105
    • 0036829557 scopus 로고    scopus 로고
    • p53 inhibitors preserve dopamine neurons and motor function in experimental parkinsonism
    • Duan W, Zhu X, Ladenheim B, Yu QS, Guo Z, Oyler J, et al. p53 inhibitors preserve dopamine neurons and motor function in experimental parkinsonism. Ann Neurol 2002; 52: 597-606.
    • (2002) Ann Neurol , vol.52 , pp. 597-606
    • Duan, W.1    Zhu, X.2    Ladenheim, B.3    Yu, Q.S.4    Guo, Z.5    Oyler, J.6
  • 106
    • 0035845532 scopus 로고    scopus 로고
    • An AAV-derived Apaf-1 dominant negative inhibitor prevents MPTP toxicity as antiapoptotic gene therapy for Parkinson's disease
    • Mochizuki H, Hayakawa H, Migita M, Shibata M, Tanaka R, Suzuki A, et al. An AAV-derived Apaf-1 dominant negative inhibitor prevents MPTP toxicity as antiapoptotic gene therapy for Parkinson's disease. Proc Natl Acad Sci 2001; 98: 10918-23.
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 10918-10923
    • Mochizuki, H.1    Hayakawa, H.2    Migita, M.3    Shibata, M.4    Tanaka, R.5    Suzuki, A.6
  • 107
    • 0030249597 scopus 로고    scopus 로고
    • Dopamine neurons from transgenic mice with a knockout of the p53 gene resist MPTP neurotoxicity
    • Trimmer PA, Smith TS, Jung AB, Bennett JP Jr. Dopamine neurons from transgenic mice with a knockout of the p53 gene resist MPTP neurotoxicity. Neurodegeneration 1996; 5: 233-9.
    • (1996) Neurodegeneration , vol.5 , pp. 233-239
    • Trimmer, P.A.1    Smith, T.S.2    Jung, A.B.3    Bennett Jr., J.P.4
  • 108
    • 0037096193 scopus 로고    scopus 로고
    • The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's diseases
    • Giasson BI, Ischiropoulos H, Lee VM, Trojanowski JQ. The relationship between oxidative/nitrative stress and pathological inclusions in Alzheimer's and Parkinson's diseases. Free Radic Biol Med 2002; 32: 1264-75.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1264-1275
    • Giasson, B.I.1    Ischiropoulos, H.2    Lee, V.M.3    Trojanowski, J.Q.4
  • 109
    • 0037185004 scopus 로고    scopus 로고
    • Alpha-synuclein lowers p53-dependent apoptotic response of neuronal cells. Abolishment by 6-hydroxydopamine and implication for Parkinson's disease
    • Da Costa CA, Paitel E, Vincent B, Checler F. Alpha-synuclein lowers p53-dependent apoptotic response of neuronal cells. Abolishment by 6-hydroxydopamine and implication for Parkinson's disease. J Biol Chem 2002; 277: 50980-4.
    • (2002) J Biol Chem , vol.277 , pp. 50980-50984
    • Da Costa, C.A.1    Paitel, E.2    Vincent, B.3    Checler, F.4
  • 110
    • 0141844595 scopus 로고    scopus 로고
    • Beta-synuclein displays an antiapoptotic p53-dependent phenotype and protects neurons from 6-hydroxydopamine-induced caspase 3 activation: Cross-talk with alpha-synuclein and implication for Parkinson's disease
    • Da Costa CA, Masliah E, Checler F. Beta-synuclein displays an antiapoptotic p53-dependent phenotype and protects neurons from 6-hydroxydopamine-induced caspase 3 activation: cross-talk with alpha-synuclein and implication for Parkinson's disease. J Biol Chem 2003; 278: 37330-5.
    • (2003) J Biol Chem , vol.278 , pp. 37330-37335
    • Da Costa, C.A.1    Masliah, E.2    Checler, F.3
  • 111
    • 0018824851 scopus 로고
    • Long-term effects of repeated methylsamphetamine administration on dopamine and serotonin neurons in the rat brain: Regional study
    • Ricaurte GA, Schister CR, Seiden LS. Long-term effects of repeated methylsamphetamine administration on dopamine and serotonin neurons in the rat brain: regional study. Brain Res 1980; 193: 153-63.
    • (1980) Brain Res , vol.193 , pp. 153-163
    • Ricaurte, G.A.1    Schister, C.R.2    Seiden, L.S.3
  • 112
    • 0030840777 scopus 로고    scopus 로고
    • P53-knockout mice are protected against the long-term effects of metahamphetamine on dopaminergic terminals and cell bodies
    • Hirata H, Cadet JL. P53-knockout mice are protected against the long-term effects of metahamphetamine on dopaminergic terminals and cell bodies. J Neurochem 1997; 69: 780-90.
    • (1997) J Neurochem , vol.69 , pp. 780-790
    • Hirata, H.1    Cadet, J.L.2
  • 113
    • 0027411564 scopus 로고
    • Striatal dopamine release in vivo following neurotoxic doses of methamphetamine and effect of the neuroprotective drugs, chlormethiazole and dizocilpine
    • Bakdwin HA, Colado MI, Murry TK, De Souza RJ, Green AR. Striatal dopamine release in vivo following neurotoxic doses of methamphetamine and effect of the neuroprotective drugs, chlormethiazole and dizocilpine. Br J Pharmacol 1993; 108: 590-6.
    • (1993) Br J Pharmacol , vol.108 , pp. 590-596
    • Bakdwin, H.A.1    Colado, M.I.2    Murry, T.K.3    De Souza, R.J.4    Green, A.R.5
  • 115
    • 0016378870 scopus 로고
    • The generation of hydrogen peroxide, superoxide radical and hydroxyl radical by hydroxydopamine, dialuric acid, and related cytotoxic agents
    • Cohen G, Heikkila RE. The generation of hydrogen peroxide, superoxide radical and hydroxyl radical by hydroxydopamine, dialuric acid, and related cytotoxic agents. J Biol Chem 1974; 249: 2447-52.
    • (1974) J Biol Chem , vol.249 , pp. 2447-2452
    • Cohen, G.1    Heikkila, R.E.2
  • 116
    • 0003026298 scopus 로고
    • A unifying hypothesis of movement and madness: Involvement of free radicals in disorders of the isodendritic core
    • Cadet JL. A unifying hypothesis of movement and madness: involvement of free radicals in disorders of the isodendritic core. Med Hypotheses 1988; 27: 87-94.
    • (1988) Med Hypotheses , vol.27 , pp. 87-94
    • Cadet, J.L.1
  • 117
    • 0031200869 scopus 로고    scopus 로고
    • Free radicals and the pathobiology of brain dopamine systems
    • Cadet JL, Brannock C. Free radicals and the pathobiology of brain dopamine systems. Neurochem Int 1998; 32: 117-31.
    • (1998) Neurochem Int , vol.32 , pp. 117-131
    • Cadet, J.L.1    Brannock, C.2
  • 118
    • 0021914474 scopus 로고
    • Pretreatment with ascorbic acid attenuates the neurotoxic effects of methamphetamine in rats
    • Wagner GC, Carelli RM, Jarvis MF. Pretreatment with ascorbic acid attenuates the neurotoxic effects of methamphetamine in rats. Res Commun Chem Pathol Pharmacol 1985; 47: 221-8.
    • (1985) Res Commun Chem Pathol Pharmacol , vol.47 , pp. 221-228
    • Wagner, G.C.1    Carelli, R.M.2    Jarvis, M.F.3
  • 119
    • 0028329215 scopus 로고
    • Methamphetamine neurotoxicity involves vacuolation of endocytic organelles and dopamine-dependent intracellular oxidative stress
    • Cubells JF, Rayport S, Rajndron G, Sulzer D. Methamphetamine neurotoxicity involves vacuolation of endocytic organelles and dopamine-dependent intracellular oxidative stress. J Neurosci 1994; 14: 2260-71.
    • (1994) J Neurosci , vol.14 , pp. 2260-2271
    • Cubells, J.F.1    Rayport, S.2    Rajndron, G.3    Sulzer, D.4
  • 120
    • 0026696841 scopus 로고
    • Methamphetamine neurotoxicity and striatal glutamate release: Comparison to 3,4-methylenedioxymetahmphetamine
    • Nash JF, Yamamoto BK. Methamphetamine neurotoxicity and striatal glutamate release: comparison to 3,4-methylenedioxymetahmphetamine. Brain Res 1992; 581: 237-43.
    • (1992) Brain Res , vol.581 , pp. 237-243
    • Nash, J.F.1    Yamamoto, B.K.2
  • 121
    • 0348048797 scopus 로고    scopus 로고
    • Hypoxia-induced apoptosis of dorsal root ganglion neurons is associated with DNA damage recognition and cell cycle disruption in rats
    • Honma H, Gross L, Windebank AJ. Hypoxia-induced apoptosis of dorsal root ganglion neurons is associated with DNA damage recognition and cell cycle disruption in rats. Neurosci Lett 2004; 354: 95-8.
    • (2004) Neurosci Lett , vol.354 , pp. 95-98
    • Honma, H.1    Gross, L.2    Windebank, A.J.3
  • 122
    • 0242401920 scopus 로고    scopus 로고
    • Role and regulation of p53 in depolarization-induced neuronal death
    • Jordan J, Galindo MF, González-García C, Cena V. Role and regulation of p53 in depolarization-induced neuronal death. Neuroscience 2003; 122: 707-15.
    • (2003) Neuroscience , vol.122 , pp. 707-715
    • Jordan, J.1    Galindo, M.F.2    González-García, C.3    Cena, V.4
  • 123
    • 0033052291 scopus 로고    scopus 로고
    • Necrosis and apoptosis after retinal ischemia: Involvement of NMDA-mediated excitotoxicity and p53
    • Joo CK, Choi JS, Ko HW, Park KY, Sohn S, Chun MH, et al. Necrosis and apoptosis after retinal ischemia: involvement of NMDA-mediated excitotoxicity and p53. Invest Ophthalmol Vis Sci 1999; 40: 713-20.
    • (1999) Invest Ophthalmol Vis Sci , vol.40 , pp. 713-720
    • Joo, C.K.1    Choi, J.S.2    Ko, H.W.3    Park, K.Y.4    Sohn, S.5    Chun, M.H.6
  • 125
    • 0034517935 scopus 로고    scopus 로고
    • p53 is abnormally elevated and active in the CNS of patients with amyotrophic lateral sclerosis
    • Martin LJ. p53 is abnormally elevated and active in the CNS of patients with amyotrophic lateral sclerosis. Neurobiol Dis 2000; 7: 613-22.
    • (2000) Neurobiol Dis , vol.7 , pp. 613-622
    • Martin, L.J.1
  • 126
    • 0033826143 scopus 로고    scopus 로고
    • Alteration of the Bcl-x/Bax ratio in a transgenic mouse model of amyotrophic lateral sclerosis: Evidence for the implication of the p53 signaling pathway
    • González de Aguilar JL, Gordon JW, Rene F, De Tapia M, Lutz-Bucher B, Gaiddon C, et al. Alteration of the Bcl-x/Bax ratio in a transgenic mouse model of amyotrophic lateral sclerosis: evidence for the implication of the p53 signaling pathway. Neurobiol Dis 2000; 7: 406-15.
    • (2000) Neurobiol Dis , vol.7 , pp. 406-415
    • González De Aguilar, J.L.1    Gordon, J.W.2    Rene, F.3    De Tapia, M.4    Lutz-Bucher, B.5    Gaiddon, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.