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Volumn 22, Issue 5-6, 2000, Pages 348-358

Role of mitochondria in neuronal apoptosis

Author keywords

Apoptosis; Caspase; Cytochrome c; Hypoxia; Mitochondria

Indexed keywords

ADENOSINE TRIPHOSPHATE; APOPTOSIS INDUCING FACTOR; CALCIUM ION; CASPASE; CELL PROTEIN; CYTOCHROME C; NEUROTOXIN;

EID: 0033667521     PISSN: 03785866     EISSN: None     Source Type: Journal    
DOI: 10.1159/000017460     Document Type: Article
Times cited : (78)

References (118)
  • 1
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G, Dallaporta B, Resche-Rigon M: The mitochondrial death/life regulator in apoptosis and necrosis. Annu Rev Physiol 1998;60: 619-642.
    • (1998) Annu Rev Physiol , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 4
    • 0032416062 scopus 로고    scopus 로고
    • Death by a thousand cuts: An ever increasing list of caspase substrates
    • Stroh C, Schulze-Osthoff K: Death by a thousand cuts: An ever increasing list of caspase substrates. Cell Death Differ 1998;5:997-1000.
    • (1998) Cell Death Differ , vol.5 , pp. 997-1000
    • Stroh, C.1    Schulze-Osthoff, K.2
  • 6
    • 0032544268 scopus 로고    scopus 로고
    • Apoptotic pathways: The roads to ruin
    • Green DR: Apoptotic pathways: The roads to ruin. Cell 1998;94:695-698.
    • (1998) Cell , vol.94 , pp. 695-698
    • Green, D.R.1
  • 7
    • 0027990778 scopus 로고
    • Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β-converting enzyme
    • Kumar S, Kinoshita M, Noda M, Copeland NG, Jenkins NA: Induction of apoptosis by the mouse Nedd2 gene, which encodes a protein similar to the product of the Caenorhabditis elegans cell death gene ced-3 and the mammalian IL-1β-converting enzyme. Genes Dev 1994; 8:1613-1626.
    • (1994) Genes Dev , vol.8 , pp. 1613-1626
    • Kumar, S.1    Kinoshita, M.2    Noda, M.3    Copeland, N.G.4    Jenkins, N.A.5
  • 12
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • Darmon AJ, Nicholson DW, Bleackley RC: Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature 1995;377:446-448.
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 13
    • 0033568430 scopus 로고    scopus 로고
    • Implication of calpain in caspase activation during B cell clonal deletion
    • Ruiz-Vela A, Gonzalez de Buitrago G, Martinez-A C: Implication of calpain in caspase activation during B cell clonal deletion. EMBO J 1999;18:4988-4998.
    • (1999) EMBO J , vol.18 , pp. 4988-4998
    • Ruiz-Vela, A.1    Gonzalez De Buitrago, G.2    Martinez-A, C.3
  • 16
    • 0031823035 scopus 로고    scopus 로고
    • Neurotrophins: The biological paradox of survival factors eliciting apoptosis
    • Casaccia-Bonnefil P, Kong H, Chao MV: Neurotrophins: The biological paradox of survival factors eliciting apoptosis. Cell Death Differ 1998;5:357-564.
    • (1998) Cell Death Differ , vol.5 , pp. 357-564
    • Casaccia-Bonnefil, P.1    Kong, H.2    Chao, M.V.3
  • 17
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, Wang X: Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997;91:479-489.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 18
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • Zou H, Henzel WJ, Liu X, Lutschg A, Wang X: Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 1997; 90:405-413.
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 19
    • 0033580926 scopus 로고    scopus 로고
    • Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation
    • Saleh A, Srinivasula SM, Acharya S, Fishel R, Alnemri ES: Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation. J Biol Chem 1999;274:17941-17945.
    • (1999) J Biol Chem , vol.274 , pp. 17941-17945
    • Saleh, A.1    Srinivasula, S.M.2    Acharya, S.3    Fishel, R.4    Alnemri, E.S.5
  • 20
    • 0033597923 scopus 로고    scopus 로고
    • Regulation of apoptotic protease activating factor-1 oligomerization and apoptosis by the WD-40 repeat region
    • Adrain C, Slee EA, Harte MT, Martin SJ: Regulation of apoptotic protease activating factor-1 oligomerization and apoptosis by the WD-40 repeat region. J Biol Chem 1999;274:20855-20860.
    • (1999) J Biol Chem , vol.274 , pp. 20855-20860
    • Adrain, C.1    Slee, E.A.2    Harte, M.T.3    Martin, S.J.4
  • 21
    • 0030782177 scopus 로고    scopus 로고
    • Cytochrome c: Can't live with it - Can't live without it
    • Reed JC: Cytochrome c: Can't live with it - Can't live without it. Cell 1997;91:559-562.
    • (1997) Cell , vol.91 , pp. 559-562
    • Reed, J.C.1
  • 22
    • 0032502866 scopus 로고    scopus 로고
    • Disruption of the outer mitochondrial membrane as a result of large amplitude swelling: The impact of irreversible permeability transition
    • Petit PX, Goubern M, Diolez P, Susin SA, Zamzami N, Kroemer G: Disruption of the outer mitochondrial membrane as a result of large amplitude swelling: The impact of irreversible permeability transition. FEBS Lett 1998;426:111-116.
    • (1998) FEBS Lett , vol.426 , pp. 111-116
    • Petit, P.X.1    Goubern, M.2    Diolez, P.3    Susin, S.A.4    Zamzami, N.5    Kroemer, G.6
  • 24
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC: Mitochondria and apoptosis. Science 1998;281:1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 25
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M, Szabo I: The mitochondrial permeability transition. Biochim Biophys Acta 1995; 1241:139-176.
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 26
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S, Narita M, Tsujimoto Y: Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 1999;399:483-487.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 30
    • 0032541132 scopus 로고    scopus 로고
    • Detection of pro-caspase-3 in cytosol and mitochondria of various tissues
    • Samali A, Zhivotovsky B, Jones DP, Orrenius S: Detection of pro-caspase-3 in cytosol and mitochondria of various tissues. FEBS Lett 1998;431:167-169.
    • (1998) FEBS Lett , vol.431 , pp. 167-169
    • Samali, A.1    Zhivotovsky, B.2    Jones, D.P.3    Orrenius, S.4
  • 31
    • 0033561295 scopus 로고    scopus 로고
    • Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells
    • Samali A, Cai J, Zhivotovsky B, Jones DP, Orrenius S: Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 and Hsp10 in the mitochondrial fraction of Jurkat cells. EMBO J 1999;18:2040-2048.
    • (1999) EMBO J , vol.18 , pp. 2040-2048
    • Samali, A.1    Cai, J.2    Zhivotovsky, B.3    Jones, D.P.4    Orrenius, S.5
  • 33
    • 0032799633 scopus 로고    scopus 로고
    • Caspases: Their intracellular localization and translocation during apoptosis
    • Zhivotovsky B, Samali A, Gahm A, Orrenius S: Caspases: Their intracellular localization and translocation during apoptosis. Cell Death Differ 1999;6:644-651.
    • (1999) Cell Death Differ , vol.6 , pp. 644-651
    • Zhivotovsky, B.1    Samali, A.2    Gahm, A.3    Orrenius, S.4
  • 36
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A, McDonnell JM, Korsmeyer SJ: BCL-2 family members and the mitochondria in apoptosis. Genes Dev 1999;13:1899-1911.
    • (1999) Genes Dev , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 42
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M, Shimizu S, Ito T, Chittenden T, Lutz RJ, Matsuda H, Tsujimoto Y: Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci USA 1998;95:14681-14686.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 45
    • 0027362667 scopus 로고
    • Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes
    • Krajewski S, Tanaka S, Takayama S, Schibler MJ, Fenton W, Reed JC: Investigation of the subcellular distribution of the bcl-2 oncoprotein: Residence in the nuclear envelope, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res 1993;53:4701-4714.
    • (1993) Cancer Res , vol.53 , pp. 4701-4714
    • Krajewski, S.1    Tanaka, S.2    Takayama, S.3    Schibler, M.J.4    Fenton, W.5    Reed, J.C.6
  • 46
    • 0027977928 scopus 로고
    • The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane
    • Lithgow T, van Driel R, Bertram JF, Strasser A: The protein product of the oncogene bcl-2 is a component of the nuclear envelope, the endoplasmic reticulum, and the outer mitochondrial membrane. Cell Growth Differ 1994;5: 411-417.
    • (1994) Cell Growth Differ , vol.5 , pp. 411-417
    • Lithgow, T.1    Van Driel, R.2    Bertram, J.F.3    Strasser, A.4
  • 47
    • 0028274733 scopus 로고
    • Multiple subcellular localization of bcl-2: Detection in nuclear outer membrane, endoplasmic reticulum membrane, and mitochondrial membranes
    • Akao Y, Otsuki Y, Kataoka S, Ito Y, Tsujimoto Y: Multiple subcellular localization of bcl-2: Detection in nuclear outer membrane, endoplasmic reticulum membrane, and mitochondrial membranes. Cancer Res 1994;54:2468-2471.
    • (1994) Cancer Res , vol.54 , pp. 2468-2471
    • Akao, Y.1    Otsuki, Y.2    Kataoka, S.3    Ito, Y.4    Tsujimoto, Y.5
  • 49
    • 0029318670 scopus 로고
    • Apoptosis. A sticky business
    • Hacker G, Vaux DL: Apoptosis. A sticky business. Curr Biol 1995;5:622-624.
    • (1995) Curr Biol , vol.5 , pp. 622-624
    • Hacker, G.1    Vaux, D.L.2
  • 52
    • 0030917601 scopus 로고    scopus 로고
    • Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid beta-peptide: Involvement of calcium and oxyradicals
    • Guo Q, Sopher BL, Furukawa K, Pham DG, Robinson N, Martin GM, Mattson MP: Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid beta-peptide: Involvement of calcium and oxyradicals. J Neurosci 1997;17:4212-4222.
    • (1997) J Neurosci , vol.17 , pp. 4212-4222
    • Guo, Q.1    Sopher, B.L.2    Furukawa, K.3    Pham, D.G.4    Robinson, N.5    Martin, G.M.6    Mattson, M.P.7
  • 54
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel E, Newmeyer DD, Green DR: Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. EMBO J 1998; 17:37-49.
    • (1998) EMBO J , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 55
    • 0343267405 scopus 로고    scopus 로고
    • Energy supply and the shape of death in neurons and lymphoid cells
    • Nicotera P, Leist M: Energy supply and the shape of death in neurons and lymphoid cells. Cell Death Differ 1997;4:435-442.
    • (1997) Cell Death Differ , vol.4 , pp. 435-442
    • Nicotera, P.1    Leist, M.2
  • 56
    • 0000322764 scopus 로고    scopus 로고
    • Apoptosis and necrosis: Intracellular ATP level as a determinant for cell death modes
    • Tsujimoto Y: Apoptosis and necrosis: Intracellular ATP level as a determinant for cell death modes Cell Death Differ 1997;4:429-434.
    • (1997) Cell Death Differ , vol.4 , pp. 429-434
    • Tsujimoto, Y.1
  • 58
    • 0030900980 scopus 로고    scopus 로고
    • Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis
    • Leist M, Single B, Castoldi AF, Kuhnle S, Nicotera P: Intracellular adenosine triphosphate (ATP) concentration: A switch in the decision between apoptosis and necrosis. J Exp Med 1997;185:1481-1486.
    • (1997) J Exp Med , vol.185 , pp. 1481-1486
    • Leist, M.1    Single, B.2    Castoldi, A.F.3    Kuhnle, S.4    Nicotera, P.5
  • 59
    • 0031027794 scopus 로고    scopus 로고
    • Role of peroxide and superoxide anion during tumour cell apoptosis
    • Gorman A, McGowan A, Cotter TG: Role of peroxide and superoxide anion during tumour cell apoptosis. FEBS Lett 1997;404:27-33.
    • (1997) FEBS Lett , vol.404 , pp. 27-33
    • Gorman, A.1    McGowan, A.2    Cotter, T.G.3
  • 60
    • 0032496143 scopus 로고    scopus 로고
    • Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss
    • Cai J, Jones DP: Superoxide in apoptosis. Mitochondrial generation triggered by cytochrome c loss. J Biol Chem 1998;273:11401-11404.
    • (1998) J Biol Chem , vol.273 , pp. 11401-11404
    • Cai, J.1    Jones, D.P.2
  • 61
    • 0028837221 scopus 로고
    • The early intracellular production of a reactive oxygen intermediate mediates apoptosis in dexamethasone-treated thymocytes
    • Torres-Roca JF, Lecoeur H, Amatore C, Gougeon M-L: The early intracellular production of a reactive oxygen intermediate mediates apoptosis in dexamethasone-treated thymocytes. Cell Death Differ 1995;2:309-319.
    • (1995) Cell Death Differ , vol.2 , pp. 309-319
    • Torres-Roca, J.F.1    Lecoeur, H.2    Amatore, C.3    Gougeon, M.-L.4
  • 62
    • 0029125857 scopus 로고
    • Aging, energy, and oxidative stress in neurodegenerative diseases
    • Beal MF: Aging, energy, and oxidative stress in neurodegenerative diseases. Ann Neurol 1995; 38:357-366.
    • (1995) Ann Neurol , vol.38 , pp. 357-366
    • Beal, M.F.1
  • 63
  • 64
    • 0028815621 scopus 로고
    • Dithiocarbamates induce apoptosis in thymocytes by raising the intracellular level of redox-active copper
    • Nobel CI, Kimland M, Lind B, Orrenius S, Slater AF: Dithiocarbamates induce apoptosis in thymocytes by raising the intracellular level of redox-active copper. J Biol Chem 1995;270: 26202-26208.
    • (1995) J Biol Chem , vol.270 , pp. 26202-26208
    • Nobel, C.I.1    Kimland, M.2    Lind, B.3    Orrenius, S.4    Slater, A.F.5
  • 65
    • 0029670976 scopus 로고    scopus 로고
    • 1,10-Phenanthroline stimulates internucleosomal DNA fragmentation in isolated rat-liver nuclei by promoting the redox activity of endogenous copper ions
    • Burkitt MJ, Milne L, Nicotera P, Orrenius S: 1,10-Phenanthroline stimulates internucleosomal DNA fragmentation in isolated rat-liver nuclei by promoting the redox activity of endogenous copper ions. Biochem J 1996;313: 163-169.
    • (1996) Biochem J , vol.313 , pp. 163-169
    • Burkitt, M.J.1    Milne, L.2    Nicotera, P.3    Orrenius, S.4
  • 66
    • 0031813589 scopus 로고    scopus 로고
    • Oxidative stress induces a form of programmed cell death with characteristics of both apoptosis and necrosis in neuronal cells
    • Tan S, Wood M, Maher P: Oxidative stress induces a form of programmed cell death with characteristics of both apoptosis and necrosis in neuronal cells. J Neurochem 1998;71:95-105.
    • (1998) J Neurochem , vol.71 , pp. 95-105
    • Tan, S.1    Wood, M.2    Maher, P.3
  • 70
    • 0031016799 scopus 로고    scopus 로고
    • 2+ following intense glutamate stimulation of cultured rat forebrain neurones
    • 2+ following intense glutamate stimulation of cultured rat forebrain neurones. J Physiol 1997;498:31-47.
    • (1997) J Physiol , vol.498 , pp. 31-47
    • White, R.J.1    Reynolds, I.J.2
  • 71
    • 0029827804 scopus 로고    scopus 로고
    • Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells
    • Budd SL, Nicholls DG: Mitochondria, calcium regulation, and acute glutamate excitotoxicity in cultured cerebellar granule cells. J Neurochem 1996;67:2282-2291.
    • (1996) J Neurochem , vol.67 , pp. 2282-2291
    • Budd, S.L.1    Nicholls, D.G.2
  • 72
    • 0029788243 scopus 로고    scopus 로고
    • Mitochondrial depolarization in glutamate-stimulated neurons: An early signal specific to excitotoxin exposure
    • White RJ, Reynolds IJ: Mitochondrial depolarization in glutamate-stimulated neurons: An early signal specific to excitotoxin exposure. J Neurosci 1996;16:5688-5697.
    • (1996) J Neurosci , vol.16 , pp. 5688-5697
    • White, R.J.1    Reynolds, I.J.2
  • 73
    • 0029810095 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is a primary event in glutamate neurotoxicity
    • Schinder AF, Olson EC, Spitzer NC, Montal M: Mitochondrial dysfunction is a primary event in glutamate neurotoxicity. J Neurosci 1996;16:6125-6133.
    • (1996) J Neurosci , vol.16 , pp. 6125-6133
    • Schinder, A.F.1    Olson, E.C.2    Spitzer, N.C.3    Montal, M.4
  • 74
    • 0030800033 scopus 로고    scopus 로고
    • Mitochondrial permeability transition in the central nervous system: Induction by calcium cycling-dependent and -independent pathways
    • Kristal BS, Dubinsky JM: Mitochondrial permeability transition in the central nervous system: Induction by calcium cycling-dependent and -independent pathways. J Neurochem 1997;69:524-538.
    • (1997) J Neurochem , vol.69 , pp. 524-538
    • Kristal, B.S.1    Dubinsky, J.M.2
  • 75
    • 0032032943 scopus 로고    scopus 로고
    • Mitochondria - The Kraken wakes!
    • Miller RJ: Mitochondria - The Kraken wakes! Trends Neurosci 1998;21:95-97.
    • (1998) Trends Neurosci , vol.21 , pp. 95-97
    • Miller, R.J.1
  • 76
    • 0030724539 scopus 로고    scopus 로고
    • Release of apoptogenic proteins from the mitochondrial intermembrane space during the mitochondrial permeability transition
    • Scarlett JL, Murphy MP: Release of apoptogenic proteins from the mitochondrial intermembrane space during the mitochondrial permeability transition. FEBS Lett 1997;418:282-286.
    • (1997) FEBS Lett , vol.418 , pp. 282-286
    • Scarlett, J.L.1    Murphy, M.P.2
  • 77
    • 0030951890 scopus 로고    scopus 로고
    • Amelioration by cyclosporin A of brain damage following 5 or 10 min of ischemia in rats subjected to preischemic hyperglycemia
    • Li PA, Uchino H, Elmer E, Siesjo BK: Amelioration by cyclosporin A of brain damage following 5 or 10 min of ischemia in rats subjected to preischemic hyperglycemia. Brain Res 1997; 753:133-140.
    • (1997) Brain Res , vol.753 , pp. 133-140
    • Li, P.A.1    Uchino, H.2    Elmer, E.3    Siesjo, B.K.4
  • 78
    • 0032561733 scopus 로고    scopus 로고
    • Amelioration by cyclosporin A of brain damage in transient forebrain ischemia in the rat
    • Uchino H, Elmer E, Uchino K, Li PA, He QP, Smith ML, Siesjo BK: Amelioration by cyclosporin A of brain damage in transient forebrain ischemia in the rat. Brain Res 1998;812:216-226.
    • (1998) Brain Res , vol.812 , pp. 216-226
    • Uchino, H.1    Elmer, E.2    Uchino, K.3    Li, P.A.4    He, Q.P.5    Smith, M.L.6    Siesjo, B.K.7
  • 79
    • 0032528154 scopus 로고    scopus 로고
    • Cyclosporin A, but not FK 506, protects mitochondria and neurons against hypoglycemic damage and implicates the mitochondrial permeability transition in cell death
    • Friberg H, Ferrand-Drake M, Bengtsson F, Halestrap AP, Wieloch T: Cyclosporin A, but not FK 506, protects mitochondria and neurons against hypoglycemic damage and implicates the mitochondrial permeability transition in cell death. J Neurosci 1998;18:5151-5159.
    • (1998) J Neurosci , vol.18 , pp. 5151-5159
    • Friberg, H.1    Ferrand-Drake, M.2    Bengtsson, F.3    Halestrap, A.P.4    Wieloch, T.5
  • 80
    • 0032906990 scopus 로고    scopus 로고
    • Mitochondrial permeability transition induced DNA-fragmentation in the rat hippocampus following hypoglycemia
    • Ferrand-Drake M, Friberg H, Wieloch T: Mitochondrial permeability transition induced DNA-fragmentation in the rat hippocampus following hypoglycemia. Neuroscience 1999; 90:1325-1338.
    • (1999) Neuroscience , vol.90 , pp. 1325-1338
    • Ferrand-Drake, M.1    Friberg, H.2    Wieloch, T.3
  • 81
    • 0032602932 scopus 로고    scopus 로고
    • Calcineurin: Structure, function, and inhibition
    • Hemenway CS, Heitman J: Calcineurin: Structure, function, and inhibition. Cell Biochem Biophys 1999;30:115-151.
    • (1999) Cell Biochem Biophys , vol.30 , pp. 115-151
    • Hemenway, C.S.1    Heitman, J.2
  • 83
    • 0017797670 scopus 로고
    • Structure-activity relations for the neurotoxicity of kainic acid derivatives and glutamate analogues
    • Schwarcz R, Scholz D, Coyle JT: Structure-activity relations for the neurotoxicity of kainic acid derivatives and glutamate analogues. Neuropharmacology 1978;17:145-151.
    • (1978) Neuropharmacology , vol.17 , pp. 145-151
    • Schwarcz, R.1    Scholz, D.2    Coyle, J.T.3
  • 84
    • 0029053638 scopus 로고
    • Excitatory amino acid-induced cytotoxicity in primary cultures of mouse cerebellar granule cells correlates with elevated, sustained c-fos proto-oncogene expression
    • Gorman AM, Scott MP, Rumsby PC, Meredith C, Griffiths R: Excitatory amino acid-induced cytotoxicity in primary cultures of mouse cerebellar granule cells correlates with elevated, sustained c-fos proto-oncogene expression. Neurosci Lett 1995;191:116-120.
    • (1995) Neurosci Lett , vol.191 , pp. 116-120
    • Gorman, A.M.1    Scott, M.P.2    Rumsby, P.C.3    Meredith, C.4    Griffiths, R.5
  • 86
    • 0029072217 scopus 로고
    • Colchicine induces apoptosis in cerebellar granule cells
    • Bonfoco E, Ceccatelli S, Manzo L, Nicotera P: Colchicine induces apoptosis in cerebellar granule cells. Exp Cell Res 1995;218:189-200.
    • (1995) Exp Cell Res , vol.218 , pp. 189-200
    • Bonfoco, E.1    Ceccatelli, S.2    Manzo, L.3    Nicotera, P.4
  • 87
    • 0033006449 scopus 로고    scopus 로고
    • Cytochrome c release and caspase-3 activation during colchicine-induced apoptosis of cerebellar granule cells
    • Gorman AM, Bonfoco E, Zhivotovsky B, Orrenius S, Ceccatelli S: Cytochrome c release and caspase-3 activation during colchicine-induced apoptosis of cerebellar granule cells. Eur J Neurosci 1999;11:1067-1072.
    • (1999) Eur J Neurosci , vol.11 , pp. 1067-1072
    • Gorman, A.M.1    Bonfoco, E.2    Zhivotovsky, B.3    Orrenius, S.4    Ceccatelli, S.5
  • 88
    • 0030995802 scopus 로고    scopus 로고
    • Programmed cell death in neurons: Focus on the pathway of nerve growth factor deprivation-induced death of sympathetic neurons
    • Deshmukh M, Johnson EM: Programmed cell death in neurons: Focus on the pathway of nerve growth factor deprivation-induced death of sympathetic neurons. Mol Pharmacol 1997; 51:897-906.
    • (1997) Mol Pharmacol , vol.51 , pp. 897-906
    • Deshmukh, M.1    Johnson, E.M.2
  • 89
    • 0030984429 scopus 로고    scopus 로고
    • Involvement of a caspase-3-like cysteine protease in 1-methyl-4-phenylpyridinium-mediated apoptosis of cultured cerebellar granule neurons
    • Du Y, Dodel RC, Bales KR, Jemmerson R, Hamilton-Byrd E, Paul SM: Involvement of a caspase-3-like cysteine protease in 1-methyl-4-phenylpyridinium-mediated apoptosis of cultured cerebellar granule neurons. J Neurochem 1997;69:1382-1388.
    • (1997) J Neurochem , vol.69 , pp. 1382-1388
    • Du, Y.1    Dodel, R.C.2    Bales, K.R.3    Jemmerson, R.4    Hamilton-Byrd, E.5    Paul, S.M.6
  • 90
    • 0032192529 scopus 로고    scopus 로고
    • Evidence of a novel event during neuronal death: Development of a competence-to-die in response to cytoplasmic cytochrome c
    • Deshmukh M, Johnson EM: Evidence of a novel event during neuronal death: Development of a competence-to-die in response to cytoplasmic cytochrome c. Neuron 1998;21:695-705.
    • (1998) Neuron , vol.21 , pp. 695-705
    • Deshmukh, M.1    Johnson, E.M.2
  • 91
    • 0033535345 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event
    • Martinou I, Desagher S, Eskes R, Antonsson B, Andre E, Fakan S, Martinou JC: The release of cytochrome c from mitochondria during apoptosis of NGF-deprived sympathetic neurons is a reversible event. J Cell Biol 1999;144:883-889.
    • (1999) J Cell Biol , vol.144 , pp. 883-889
    • Martinou, I.1    Desagher, S.2    Eskes, R.3    Antonsson, B.4    Andre, E.5    Fakan, S.6    Martinou, J.C.7
  • 92
    • 0032555934 scopus 로고    scopus 로고
    • Blocking cytochrome c activity within intact neurons inhibits apoptosis
    • Neame SJ, Rubin LL, Philpott KL: Blocking cytochrome c activity within intact neurons inhibits apoptosis. J Cell Biol 1998;142: 1583-1593.
    • (1998) J Cell Biol , vol.142 , pp. 1583-1593
    • Neame, S.J.1    Rubin, L.L.2    Philpott, K.L.3
  • 93
    • 0033042778 scopus 로고    scopus 로고
    • Glutamate neurotoxicity in rat cerebellar granule cells involves cytochrome c release from mitochondria and mitochondrial shuttle impairment
    • Atlante A, Gagliardi S, Marra E, Calissano P, Passarella S: Glutamate neurotoxicity in rat cerebellar granule cells involves cytochrome c release from mitochondria and mitochondrial shuttle impairment. J Neurochem 1999;73: 237-246.
    • (1999) J Neurochem , vol.73 , pp. 237-246
    • Atlante, A.1    Gagliardi, S.2    Marra, E.3    Calissano, P.4    Passarella, S.5
  • 94
    • 0031820341 scopus 로고    scopus 로고
    • Potassium deprivation-induced apoptosis of cerebellar granule neurons: Cytochrome c release in the absence of altered expression of Bcl-2 family proteins
    • Gleichmann M, Beinroth S, Reed JC, Krajewski S, Schulz JB, Wullner U, Klockgether T, Weller M: Potassium deprivation-induced apoptosis of cerebellar granule neurons: Cytochrome c release in the absence of altered expression of Bcl-2 family proteins. Cell Physiol Biochem 1998;8:194-201.
    • (1998) Cell Physiol Biochem , vol.8 , pp. 194-201
    • Gleichmann, M.1    Beinroth, S.2    Reed, J.C.3    Krajewski, S.4    Schulz, J.B.5    Wullner, U.6    Klockgether, T.7    Weller, M.8
  • 96
    • 0028110234 scopus 로고
    • Cortical cytochrome oxidase activity is reduced in Alzheimer's disease
    • Mutisya EM, Bowling AC, Beal MF: Cortical cytochrome oxidase activity is reduced in Alzheimer's disease. J Neurochem 1994;63: 2179-2184.
    • (1994) J Neurochem , vol.63 , pp. 2179-2184
    • Mutisya, E.M.1    Bowling, A.C.2    Beal, M.F.3
  • 97
    • 0021883670 scopus 로고
    • Regional mitochondrial respiratory activity in Huntington's disease brain
    • Brennan WA Jr, Bird ED, Aprille JR: Regional mitochondrial respiratory activity in Huntington's disease brain. J Neurochem 1985; 44:1948-1950.
    • (1985) J Neurochem , vol.44 , pp. 1948-1950
    • Brennan Jr., W.A.1    Bird, E.D.2    Aprille, J.R.3
  • 98
    • 0033510014 scopus 로고    scopus 로고
    • Mitochondria in neurodegeneration: Acute ischemia and chronic neurodegenerative diseases
    • Fiskum G, Murphy AN, Beal MF: Mitochondria in neurodegeneration: Acute ischemia and chronic neurodegenerative diseases. J Cereb Blood Flow Metab 1999;19:351-369.
    • (1999) J Cereb Blood Flow Metab , vol.19 , pp. 351-369
    • Fiskum, G.1    Murphy, A.N.2    Beal, M.F.3
  • 99
  • 100
    • 0032515191 scopus 로고    scopus 로고
    • Hypoxia induces apoptosis in human neuroblastoma SK-N-MC cells by caspase activation accompanying cytochrome c release from mitochondria
    • Araya R, Uehara T, Nomura Y: Hypoxia induces apoptosis in human neuroblastoma SK-N-MC cells by caspase activation accompanying cytochrome c release from mitochondria. FEBS Lett 1998;439:168-172.
    • (1998) FEBS Lett , vol.439 , pp. 168-172
    • Araya, R.1    Uehara, T.2    Nomura, Y.3
  • 103
    • 0033573708 scopus 로고    scopus 로고
    • Exogenous creatine delays anoxic depolarization and protects from hypoxic damage: Dose-effect relationship
    • Balestrino M, Rebaudo R, Lunardi G: Exogenous creatine delays anoxic depolarization and protects from hypoxic damage: Dose-effect relationship. Brain Res 1999;816:124-130.
    • (1999) Brain Res , vol.816 , pp. 124-130
    • Balestrino, M.1    Rebaudo, R.2    Lunardi, G.3
  • 104
    • 0030641754 scopus 로고    scopus 로고
    • Understanding Parkinson's disease
    • Youdim MB, Riederer P : Understanding Parkinson's disease. Sci Am 1997;276:52-59.
    • (1997) Sci Am , vol.276 , pp. 52-59
    • Youdim, M.B.1    Riederer, P.2
  • 106
    • 0025047351 scopus 로고
    • Normal mitochondrial genome in brain from patients with Parkinson's disease and complex I defect
    • Lestienne P, Nelson J, Riederer P, Jellinger K, Reichmann H: Normal mitochondrial genome in brain from patients with Parkinson's disease and complex I defect. J Neurochem 1990;55:1810-1812.
    • (1990) J Neurochem , vol.55 , pp. 1810-1812
    • Lestienne, P.1    Nelson, J.2    Riederer, P.3    Jellinger, K.4    Reichmann, H.5
  • 108
    • 0026408618 scopus 로고
    • Abnormalities of glucose metabolism in Alzheimer's disease
    • Hoyer S: Abnormalities of glucose metabolism in Alzheimer's disease. Ann N Y Acad Sci 1991;640:53-58.
    • (1991) Ann N Y Acad Sci , vol.640 , pp. 53-58
    • Hoyer, S.1
  • 109
    • 0029145084 scopus 로고
    • Are reactive oxygen species involved in Alzheimer's disease?
    • Benzi G, Moretti A: Are reactive oxygen species involved in Alzheimer's disease? Neurobiol Aging 1995;16:661-674.
    • (1995) Neurobiol Aging , vol.16 , pp. 661-674
    • Benzi, G.1    Moretti, A.2
  • 110
    • 0028200649 scopus 로고
    • Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative
    • Gabuzda D, Busciglio J, Chen LB, Matsudaira P, Yankner BA: Inhibition of energy metabolism alters the processing of amyloid precursor protein and induces a potentially amyloidogenic derivative. J Biol Chem 1994;269: 13623-13628.
    • (1994) J Biol Chem , vol.269 , pp. 13623-13628
    • Gabuzda, D.1    Busciglio, J.2    Chen, L.B.3    Matsudaira, P.4    Yankner, B.A.5
  • 111
    • 0026730350 scopus 로고
    • Amyloidogenicity of beta A4 and beta A4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation
    • Dyrks T, Dyrks E, Hartmann T, Masters C, Beyreuther K: Amyloidogenicity of beta A4 and beta A4-bearing amyloid protein precursor fragments by metal-catalyzed oxidation. J Biol Chem 1992;267:18210-18217.
    • (1992) J Biol Chem , vol.267 , pp. 18210-18217
    • Dyrks, T.1    Dyrks, E.2    Hartmann, T.3    Masters, C.4    Beyreuther, K.5
  • 112
    • 0029910952 scopus 로고    scopus 로고
    • Programmed cell death in the developing nervous system
    • Burek MJ, Oppenheim RW: Programmed cell death in the developing nervous system. Brain Pathol 1996;6:427-446.
    • (1996) Brain Pathol , vol.6 , pp. 427-446
    • Burek, M.J.1    Oppenheim, R.W.2
  • 113
    • 0028784940 scopus 로고
    • Apoptosis in the developing CNS
    • Naruse I, Keino H: Apoptosis in the developing CNS. Prog Neurobiol 1995;47:135-155.
    • (1995) Prog Neurobiol , vol.47 , pp. 135-155
    • Naruse, I.1    Keino, H.2
  • 114
    • 0026058318 scopus 로고
    • Cell death during development of the nervous system
    • Oppenheim RW: Cell death during development of the nervous system. Annu Rev Neurosci 1991;14:453-501.
    • (1991) Annu Rev Neurosci , vol.14 , pp. 453-501
    • Oppenheim, R.W.1
  • 115
    • 0023736226 scopus 로고
    • Trophic regulation of nerve cell morphology and innervation in the autonomic nervous system
    • Purves D, Snider WD, Voyvodic JT: Trophic regulation of nerve cell morphology and innervation in the autonomic nervous system. Nature 1988;336:123-128.
    • (1988) Nature , vol.336 , pp. 123-128
    • Purves, D.1    Snider, W.D.2    Voyvodic, J.T.3
  • 116
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi F, Alvarez-Bolado G, Meyer BI, Roth KA, Grass P: Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell 1998;94:727-737.
    • (1998) Cell , vol.94 , pp. 727-737
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Grass, P.5


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