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Volumn 1254, Issue , 2015, Pages

Neuronal cell death: An overview of its different forms in central and peripheral neurons

Author keywords

Apoptosis; Autophagy; Necrosis; Oncosis; Pyroptosis

Indexed keywords

ANIMAL CELL; ANIMAL EXPERIMENT; APOPTOSIS; ARTICLE; AUTOPHAGOSOME; BRAIN CELL CULTURE; CELL DIFFERENTIATION; CELL MEMBRANE PERMEABILITY; CELL NUCLEUS MEMBRANE; CENTRAL NERVOUS SYSTEM; CHROMATIN CONDENSATION; CONTROLLED STUDY; EUKARYOTIC CELL; LYSOSOME; MACROAUTOPHAGY; MITOCHONDRIAL RESPIRATION; NERVE CELL; NERVE CELL NECROSIS; NONHUMAN; PERIPHERAL NERVOUS SYSTEM; PRIORITY JOURNAL; PYROPTOSIS; AUTOPHAGY; CELL DEATH; CYTOLOGY; GENETICS; GLIA; MOLECULAR BIOLOGY; NECROSIS; NERVOUS SYSTEM DEVELOPMENT; PROCEDURES;

EID: 84954602494     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-2152-2_1     Document Type: Article
Times cited : (14)

References (90)
  • 3
    • 84872469150 scopus 로고    scopus 로고
    • Nineteenth century research on cell death
    • Clarke PG, Clarke S (2012) Nineteenth century research on cell death. Exp Oncol 34: 139–145
    • (2012) Exp Oncol , vol.34 , pp. 139-145
    • Clarke, P.G.1    Clarke, S.2
  • 5
    • 0002710249 scopus 로고
    • Ber die Bildung von Richtungsfi guren in Säugethiereiern beim Untergang Graaf'scher Follikel
    • Flemming W (1885) Über die Bildung von Richtungsfi guren in Säugethiereiern beim Untergang Graaf'scher Follikel. Arch Anat Entwickl:221–244
    • (1885) Arch Anat Entwickl , pp. 221-244
    • Flemming, W.1
  • 6
    • 34250615757 scopus 로고    scopus 로고
    • IVth edn. Kluwer Academic/Plenum Publishers, New York, Boston, Dordrecht, London, Moscow
    • Rao MS, Jacobson M (2005) Developmental neurobiology, IVth edn. Kluwer Academic/Plenum Publishers, New York, Boston, Dordrecht, London, Moscow
    • (2005) Developmental neurobiology
    • Rao, M.S.1    Jacobson, M.2
  • 7
    • 1542588577 scopus 로고
    • On the early development of Lepidosteus osseus—preliminary notice
    • Beard J (1889) On the early development of Lepidosteus osseus—preliminary notice. Proc Roy Soc Lond 46:108–118
    • (1889) Proc Roy Soc Lond , vol.46 , pp. 108-118
    • Beard, J.1
  • 8
    • 1542798809 scopus 로고
    • The transient ganglion cells and their nerves in Raja batis
    • Beard J (1892) The transient ganglion cells and their nerves in Raja batis. Anat Anz 7: 191–206
    • (1892) Anat Anz , vol.7 , pp. 191-206
    • Beard, J.1
  • 9
    • 1542484003 scopus 로고
    • Histolyse de certains neuroblastes au cours du développement du tube nerveux chez le poulet
    • Collin R (1906) Histolyse de certains neuroblastes au cours du développement du tube nerveux chez le poulet. C R Soc Biol 60: 1080–1081
    • (1906) C R Soc Biol , vol.60 , pp. 1080-1081
    • Collin, R.1
  • 10
    • 0000608944 scopus 로고
    • Ber Untergang von Zellen während der normalen Entwicklung bei Wirbeltieren
    • Ernst M (1926) Über Untergang von Zellen während der normalen Entwicklung bei Wirbeltieren. Z Anat Entwicklungsgesch 79: 228–262
    • (1926) Z Anat Entwicklungsgesch , vol.79 , pp. 228-262
    • Ernst, M.1
  • 11
    • 84915943405 scopus 로고
    • Cell deaths in normal vertebrate ontogeny
    • Glücksmann PD (1951) Cell deaths in normal vertebrate ontogeny. Biol Rev 26:59–86
    • (1951) Biol Rev , vol.26 , pp. 59-86
    • Glücksmann, P.D.1
  • 12
    • 84892109705 scopus 로고
    • Effects of the extract of the mouse submaxillary salivary glands on the sympathetic system of mammals
    • Levi-Montalcini R, Cohen S (1960) Effects of the extract of the mouse submaxillary salivary glands on the sympathetic system of mammals. Ann N Y Acad Sci 85:324–341
    • (1960) Ann N Y Acad Sci , vol.85 , pp. 324-341
    • Levi-Montalcini, R.1    Cohen, S.2
  • 13
    • 70449239593 scopus 로고
    • Regression versus peripheral control of differentiation in motor hypoplasia
    • Hamburger V (1958) Regression versus peripheral control of differentiation in motor hypoplasia. Am J Anat 102:365–409
    • (1958) Am J Anat , vol.102 , pp. 365-409
    • Hamburger, V.1
  • 14
    • 0001620448 scopus 로고
    • Cell degeneration in the larval ventral horn of Xenopus laevis (Daudin)
    • Hughes A (1961) Cell degeneration in the larval ventral horn of Xenopus laevis (Daudin). J Embryol Exp Morphol 9:269–284
    • (1961) J Embryol Exp Morphol , vol.9 , pp. 269-284
    • Hughes, A.1
  • 15
    • 36949089633 scopus 로고
    • Effect of limb ablation on neurones in Xenopus larvae
    • Hughes AF, Lewis PR (1961) Effect of limb ablation on neurones in Xenopus larvae. Nature 189:333–334
    • (1961) Nature , vol.189 , pp. 333-334
    • Hughes, A.F.1    Lewis, P.R.2
  • 16
    • 0011805498 scopus 로고
    • Cell turnover in the spinal ganglia of Xenopus laevis tadpoles
    • Prestige MC (1965) Cell turnover in the spinal ganglia of Xenopus laevis tadpoles. J Embryol Exp Morphol 13:63–72
    • (1965) J Embryol Exp Morphol , vol.13 , pp. 63-72
    • Prestige, M.C.1
  • 17
    • 0038012640 scopus 로고    scopus 로고
    • In vivo cellular and molecular mechanisms of neuronal apoptosis in the mammalian CNS
    • Lossi L, Merighi A (2003) In vivo cellular and molecular mechanisms of neuronal apoptosis in the mammalian CNS. Prog Neurobiol 69: 287–312
    • (2003) Prog Neurobiol , vol.69 , pp. 287-312
    • Lossi, L.1    Merighi, A.2
  • 19
    • 0015880897 scopus 로고
    • The morphology of various types of cell death in prenatal tissues
    • Schweichel JU, Merker HJ (1973) The morphology of various types of cell death in prenatal tissues. Teratology 7:253–266
    • (1973) Teratology , vol.7 , pp. 253-266
    • Schweichel, J.U.1    Merker, H.J.2
  • 20
    • 0025283961 scopus 로고
    • Developmental cell death: Morphological diversity and multiple mechanisms
    • Clarke PGH (1990) Developmental cell death: Morphological diversity and multiple mechanisms. Anat Embryol 181:195–213
    • (1990) Anat Embryol , vol.181 , pp. 195-213
    • Clarke, P.G.H.1
  • 21
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR (1972) Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26:239–257
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 22
    • 0037025034 scopus 로고    scopus 로고
    • Synapseindependent and synapse-dependent apoptosis of cerebellar granule cells in postnatal rabbits occur at two subsequent but partly overlapping developmental stages
    • Lossi L, Mioletti S, Merighi A (2002) Synapseindependent and synapse-dependent apoptosis of cerebellar granule cells in postnatal rabbits occur at two subsequent but partly overlapping developmental stages. Neuroscience 112: 509–523
    • (2002) Neuroscience , vol.112 , pp. 509-523
    • Lossi, L.1    Mioletti, S.2    Merighi, A.3
  • 25
    • 84857700077 scopus 로고    scopus 로고
    • Cell death pathways and autophagy in the central nervous system and its involvement in neurodegeneration, immunity and central nervous system infection: To die or not to die—that is the question
    • Rosello A, Warnes G, Meier UC (2012) Cell death pathways and autophagy in the central nervous system and its involvement in neurodegeneration, immunity and central nervous system infection: to die or not to die—that is the question. Clin Exp Immunol 168:52–57
    • (2012) Clin Exp Immunol , vol.168 , pp. 52-57
    • Rosello, A.1    Warnes, G.2    Meier, U.C.3
  • 26
    • 34548188741 scopus 로고    scopus 로고
    • Self-eating and self-killing: Crosstalk between autophagy and apoptosis
    • Maiuri MC, Zalckvar E, Kimchi A et al (2007) Self-eating and self-killing: Crosstalk between autophagy and apoptosis. Nat Rev Mol Cell Biol 8:741–752
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 741-752
    • Maiuri, M.C.1    Zalckvar, E.2    Kimchi, A.3
  • 27
    • 34250753161 scopus 로고    scopus 로고
    • Cell death modalities: Classifi cation and pathophysiological implications
    • Galluzzi L, Maiuri MC, Vitale I et al (2007) Cell death modalities: Classifi cation and pathophysiological implications. Cell Death Differ 14:1237–1243
    • (2007) Cell Death Differ , vol.14 , pp. 1237-1243
    • Galluzzi, L.1    Maiuri, M.C.2    Vitale, I.3
  • 30
    • 0028984948 scopus 로고
    • Mice defi cient in IL-1 beta converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxin shock
    • Li P, Allen H, Banerjee SK et al (1995) Mice defi cient in IL-1 beta converting enzyme are defective in production of mature IL-1 beta and resistant to endotoxin shock. Cell 80: 401–411
    • (1995) Cell , vol.80 , pp. 401-411
    • Li, P.1    Allen, H.2    Banerjee, S.K.3
  • 31
    • 0028920863 scopus 로고
    • Altered cytokine export and apoptosis in mice defi cient in interleukine-1-beta converting enzyme
    • Kuida K, Lippke JA, Ku G et al (1995) Altered cytokine export and apoptosis in mice defi cient in interleukine-1-beta converting enzyme. Science 267:2000–2003
    • (1995) Science , vol.267 , pp. 2000-2003
    • Kuida, K.1    Lippke, J.A.2    Ku, G.3
  • 32
    • 0346103651 scopus 로고    scopus 로고
    • Fundamental role of the Rip2/caspase- 1 pathway in hypoxia and ischemia-induced neuronal cell death
    • Zhang WH, Wang X, Narayanan M et al (2003) Fundamental role of the Rip2/caspase- 1 pathway in hypoxia and ischemia-induced neuronal cell death. Proc Natl Acad Sci U S A 100:16012–16017
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 16012-16017
    • Zhang, W.H.1    Wang, X.2    Narayanan, M.3
  • 34
    • 8044252166 scopus 로고    scopus 로고
    • Expression of a dominant negative mutant of interleukin-1 beta converting enzyme in transgenic mice prevents neuronal cell death induced by trophic factor withdrawal and ischemic brain injury
    • Friedlander RM, Gagliardini V, Hara H et al (1997) Expression of a dominant negative mutant of interleukin-1 beta converting enzyme in transgenic mice prevents neuronal cell death induced by trophic factor withdrawal and ischemic brain injury. J Exp Med 185: 933–940
    • (1997) J Exp Med , vol.185 , pp. 933-940
    • Friedlander, R.M.1    Gagliardini, V.2    Hara, H.3
  • 35
    • 23444435250 scopus 로고
    • Prevention of vertebrate neuronal death by the crmA gene
    • Gagliardini V, Fernandez PA, Lee RK et al (1994) Prevention of vertebrate neuronal death by the crmA gene. Science 263: 826–828
    • (1994) Science , vol.263 , pp. 826-828
    • Gagliardini, V.1    Fernandez, P.A.2    Lee, R.K.3
  • 36
    • 84870702650 scopus 로고    scopus 로고
    • Oncosis: An important non-apoptotic mode of cell death
    • Weerasinghe P, Buja LM (2012) Oncosis: An important non-apoptotic mode of cell death. Exp Mol Pathol 93:302–308
    • (2012) Exp Mol Pathol , vol.93 , pp. 302-308
    • Weerasinghe, P.1    Buja, L.M.2
  • 37
    • 0028891783 scopus 로고
    • Apoptosis, oncosis, and necrosis. An overview of cell death
    • Majno G, Joris I (1995) Apoptosis, oncosis, and necrosis. An overview of cell death. Am J Pathol 146:3–15
    • (1995) Am J Pathol , vol.146 , pp. 3-15
    • Majno, G.1    Joris, I.2
  • 38
    • 0031047146 scopus 로고    scopus 로고
    • The pathways of cell death: Oncosis, apoptosis, and necrosis
    • Trump BF, Berezesky IK, Chang SH et al (1997) The pathways of cell death: Oncosis, apoptosis, and necrosis. Toxicol Pathol 25: 82–88
    • (1997) Toxicol Pathol , vol.25 , pp. 82-88
    • Trump, B.F.1    Berezesky, I.K.2    Chang, S.H.3
  • 39
    • 15944423619 scopus 로고    scopus 로고
    • Apoptosis and oncosis in acute coronary syndromes: Assessment and implications
    • Jugdutt BI, Idikio HA (2005) Apoptosis and oncosis in acute coronary syndromes: Assessment and implications. Mol Cell Biochem 270:177–200
    • (2005) Mol Cell Biochem , vol.270 , pp. 177-200
    • Jugdutt, B.I.1    Idikio, H.A.2
  • 40
    • 0027724039 scopus 로고
    • Apoptosis and necrosis. Basic types and mechanisms of cell death
    • Buja LM, Eigenbrodt ML, Eigenbrodt EH (1993) Apoptosis and necrosis. Basic types and mechanisms of cell death. Arch Pathol Lab Med 117:1208–1214
    • (1993) Arch Pathol Lab Med , vol.117 , pp. 1208-1214
    • Buja, L.M.1    Eigenbrodt, M.L.2    Eigenbrodt, E.H.3
  • 41
    • 22144467314 scopus 로고    scopus 로고
    • Myocardial ischemia and reperfusion injury
    • Buja LM (2005) Myocardial ischemia and reperfusion injury. Cardiovasc Pathol 14: 170–175
    • (2005) Cardiovasc Pathol , vol.14 , pp. 170-175
    • Buja, L.M.1
  • 42
    • 0030996827 scopus 로고    scopus 로고
    • Discrimination of late apoptotic/ necrotic cells (type III) by fl ow cytometry in solid tumors
    • O’Brien MC, Healy SF Jr, Raney SR et al (1997) Discrimination of late apoptotic/ necrotic cells (type III) by fl ow cytometry in solid tumors. Cytometry 28:81–89
    • (1997) Cytometry , vol.28 , pp. 81-89
    • O’brien, M.C.1    Healy, S.F.2    Raney, S.R.3
  • 43
    • 77953912521 scopus 로고    scopus 로고
    • Persistent oxygen-glucose deprivation induces astrocytic death through two different pathways and calpain- mediated proteolysis of cytoskeletal proteins during astrocytic oncosis
    • Cao X, Zhang Y, Zou L et al (2010) Persistent oxygen-glucose deprivation induces astrocytic death through two different pathways and calpain- mediated proteolysis of cytoskeletal proteins during astrocytic oncosis. Neurosci Lett 479:118–122
    • (2010) Neurosci Lett , vol.479 , pp. 118-122
    • Cao, X.1    Zhang, Y.2    Zou, L.3
  • 44
    • 34247520570 scopus 로고    scopus 로고
    • Oncosis, the possible cell death pathway in astrocytes after focal cerebral ischemia
    • Chu X, Fu X, Zou L et al (2007) Oncosis, the possible cell death pathway in astrocytes after focal cerebral ischemia. Brain Res 1149: 157–164
    • (2007) Brain Res , vol.1149 , pp. 157-164
    • Chu, X.1    Fu, X.2    Zou, L.3
  • 45
    • 0034930391 scopus 로고    scopus 로고
    • Signaling pathways and effector mechanisms pre-programmed cell death
    • Blatt NB, Glick GD (2001) Signaling pathways and effector mechanisms pre-programmed cell death. Bioorg Med Chem 9:1371–1384
    • (2001) Bioorg Med Chem , vol.9 , pp. 1371-1384
    • Blatt, N.B.1    Glick, G.D.2
  • 46
    • 0036899079 scopus 로고    scopus 로고
    • Apoptosomes: Engines for caspase activation
    • Adams JM, Cory S (2002) Apoptosomes: Engines for caspase activation. Curr Opin Cell Biol 14:715–720
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 715-720
    • Adams, J.M.1    Cory, S.2
  • 47
    • 0023159034 scopus 로고
    • Induction and activation of tissue transglutaminase during programmed cell death
    • Fesus L, Nemes Z, Piredda L et al (1987) Induction and activation of tissue transglutaminase during programmed cell death. FEBS Lett 224:104–108
    • (1987) FEBS Lett , vol.224 , pp. 104-108
    • Fesus, L.1    Nemes, Z.2    Piredda, L.3
  • 49
    • 0026508561 scopus 로고
    • Exposure of phosphatidylserine on the surface of apoptotic lypmphocytes triggers specifi c recognition and removal by macrophages
    • Fadok VA, Voelker D, Campbell PA et al (1992) Exposure of phosphatidylserine on the surface of apoptotic lypmphocytes triggers specifi c recognition and removal by macrophages. J Immunol 148:2207–2216
    • (1992) J Immunol , vol.148 , pp. 2207-2216
    • Fadok, V.A.1    Voelker, D.2    Campbell, P.A.3
  • 50
    • 0031985647 scopus 로고    scopus 로고
    • Annexin V-affi nity assay: A review on an apoptosis detection system based on phosphatidylserine exposure
    • van Engeland M, Nieland LJ, Ramaekers FC et al (1998) Annexin V-affi nity assay: A review on an apoptosis detection system based on phosphatidylserine exposure. Cytometry 31:1–9
    • (1998) Cytometry , vol.31 , pp. 1-9
    • Van Engeland, M.1    Nieland, L.J.2    Ramaekers, F.C.3
  • 51
    • 0037390598 scopus 로고    scopus 로고
    • Annexin I is an endogenous ligand that mediates apoptotic cell engulfment
    • Arur S, Uche UE, Rezaul K et al (2003) Annexin I is an endogenous ligand that mediates apoptotic cell engulfment. Dev Cell 4: 587–598
    • (2003) Dev Cell , vol.4 , pp. 587-598
    • Arur, S.1    Uche, U.E.2    Rezaul, K.3
  • 52
    • 78049514583 scopus 로고    scopus 로고
    • Surface-exposed calreticulin in the interaction between dying cells and phagocytes
    • Martins I, Kepp O, Galluzzi L et al (2010) Surface-exposed calreticulin in the interaction between dying cells and phagocytes. Ann N Y Acad Sci 1209:77–82
    • (2010) Ann N Y Acad Sci , vol.1209 , pp. 77-82
    • Martins, I.1    Kepp, O.2    Galluzzi, L.3
  • 53
    • 78650666213 scopus 로고    scopus 로고
    • Annexin A1: A central player in the anti- infl ammatory and neuroprotective role of microglia
    • McArthur S, Cristante E, Paterno M et al (2010) Annexin A1: A central player in the anti- infl ammatory and neuroprotective role of microglia. J Immunol 185:6317–6328
    • (2010) J Immunol , vol.185 , pp. 6317-6328
    • Mc Arthur, S.1    Cristante, E.2    Paterno, M.3
  • 54
    • 0033985183 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Sastry PS, Rao K (2000) Apoptosis in the nervous system. J Neurochem 74:1–20
    • (2000) J Neurochem , vol.74 , pp. 1-20
    • Sastry, P.S.1    Rao, K.2
  • 55
    • 2342471409 scopus 로고    scopus 로고
    • Toxic proteins released from mitochondria in cell death
    • Saelens X, Festjens N, Vande WL et al (2004) Toxic proteins released from mitochondria in cell death. Oncogene 23:2861–2874
    • (2004) Oncogene , vol.23 , pp. 2861-2874
    • Saelens, X.1    Festjens, N.2    Vande, W.L.3
  • 56
    • 0032504574 scopus 로고    scopus 로고
    • Mitochondrial control of apoptosis: The role of cytochrome c
    • Cai J, Yang J, Jones DP (1998) Mitochondrial control of apoptosis: The role of cytochrome c. Biochim Biophys Acta 1366:139–149
    • (1998) Biochim Biophys Acta , vol.1366 , pp. 139-149
    • Cai, J.1    Yang, J.2    Jones, D.P.3
  • 57
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y et al (2000) Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102:33–42
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3
  • 58
    • 18244386261 scopus 로고    scopus 로고
    • The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity
    • van Loo G, van Gurp M, Depuydt B et al (2002) The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity. Cell Death Differ 9:20–26
    • (2002) Cell Death Differ , vol.9 , pp. 20-26
    • Van Loo, G.1    Van Gurp, M.2    Depuydt, B.3
  • 59
    • 0036792475 scopus 로고    scopus 로고
    • The role of mitochondrial factors in apoptosis: A Russian roulette with more than one bullet
    • van Loo G, Saelens X, van Gurp M et al (2002) The role of mitochondrial factors in apoptosis: A Russian roulette with more than one bullet. Cell Death Differ 9:1031–1042
    • (2002) Cell Death Differ , vol.9 , pp. 1031-1042
    • Van Loo, G.1    Saelens, X.2    Van Gurp, M.3
  • 60
    • 0036848165 scopus 로고    scopus 로고
    • Caspases are not localized in mitochondria during life or death
    • van Loo G, Saelens X, Matthijssens F et al (2002) Caspases are not localized in mitochondria during life or death. Cell Death Differ 9:1207–1211
    • (2002) Cell Death Differ , vol.9 , pp. 1207-1211
    • Van Loo, G.1    Saelens, X.2    Matthijssens, F.3
  • 61
    • 0035967169 scopus 로고    scopus 로고
    • Essential role of the mitochondrial apoptosisinducing factor in programmed cell death
    • Joza N, Susin SA, Daugas E et al (2001) Essential role of the mitochondrial apoptosisinducing factor in programmed cell death. Nature 410:549–554
    • (2001) Nature , vol.410 , pp. 549-554
    • Joza, N.1    Susin, S.A.2    Daugas, E.3
  • 62
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin SA, Lorenzo HK, Zamzami N et al (1999) Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 397:441–446
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3
  • 63
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li LY, Luo X, Wang X (2001) Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412:95–99
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 64
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H et al (1998) A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391:43–50
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3
  • 65
    • 0034698733 scopus 로고    scopus 로고
    • Two distinct pathways leading to nuclear apoptosis
    • Susin SA, Daugas E, Ravagnan L et al (2000) Two distinct pathways leading to nuclear apoptosis. J Exp Med 192:571–580
    • (2000) J Exp Med , vol.192 , pp. 571-580
    • Susin, S.A.1    Daugas, E.2    Ravagnan, L.3
  • 66
    • 0032575688 scopus 로고    scopus 로고
    • The Bcl-2 protein family: Arbiters of cell survival
    • Adams JM, Cory S (1998) The Bcl-2 protein family: Arbiters of cell survival. Science 281:1322–1326
    • (1998) Science , vol.281 , pp. 1322-1326
    • Adams, J.M.1    Cory, S.2
  • 67
    • 0035146929 scopus 로고    scopus 로고
    • Life-or-death decisions by the Bcl-2 protein family
    • Adams JM, Cory S (2001) Life-or-death decisions by the Bcl-2 protein family. Trends Biochem Sci 26:61–66
    • (2001) Trends Biochem Sci , vol.26 , pp. 61-66
    • Adams, J.M.1    Cory, S.2
  • 68
    • 70350247717 scopus 로고    scopus 로고
    • Posttranslational regulation of BCL2 levels in cerebellar granule cells: A mechanism of neuronal survival
    • Lossi L, Gambino G, Ferrini F et al (2009) Posttranslational regulation of BCL2 levels in cerebellar granule cells: A mechanism of neuronal survival. Dev Neurobiol 69:855–870
    • (2009) Dev Neurobiol , vol.69 , pp. 855-870
    • Lossi, L.1    Gambino, G.2    Ferrini, F.3
  • 69
    • 77953419932 scopus 로고    scopus 로고
    • Autophagy regulates the post-translational cleavage of BCL-2 and promotes neuronal survival
    • Lossi L, Gambino G, Salio C et al (2010) Autophagy regulates the post-translational cleavage of BCL-2 and promotes neuronal survival. Scientifi cWorldJournal 10:924–929
    • (2010) Scientifi cWorldJournal , vol.10 , pp. 924-929
    • Lossi, L.1    Gambino, G.2    Salio, C.3
  • 70
    • 43149090064 scopus 로고    scopus 로고
    • FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells
    • Hara T, Takamura A, Kishi C et al (2008) FIP200, a ULK-interacting protein, is required for autophagosome formation in mammalian cells. J Cell Biol 181:497–510
    • (2008) J Cell Biol , vol.181 , pp. 497-510
    • Hara, T.1    Takamura, A.2    Kishi, C.3
  • 71
    • 65249176304 scopus 로고    scopus 로고
    • ULKAtg13- FIP200 complexes mediate mTOR signaling to the autophagy machinery
    • Jung CH, Jun CB, Ro SH et al (2009) ULKAtg13- FIP200 complexes mediate mTOR signaling to the autophagy machinery. Mol Biol Cell 20:1992–2003
    • (2009) Mol Biol Cell , vol.20 , pp. 1992-2003
    • Jung, C.H.1    Jun, C.B.2    Ro, S.H.3
  • 72
    • 59249089394 scopus 로고    scopus 로고
    • Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG
    • Itakura E, Kishi C, Inoue K et al (2008) Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG. Mol Biol Cell 19:5360–5372
    • (2008) Mol Biol Cell , vol.19 , pp. 5360-5372
    • Itakura, E.1    Kishi, C.2    Inoue, K.3
  • 73
    • 58049192897 scopus 로고    scopus 로고
    • Identifi cation of Barkor as a mammalian autophagy-specifi c factor for Beclin 1 and class III phosphatidylinositol 3-kinase
    • Sun Q, Fan W, Chen K et al (2008) Identifi cation of Barkor as a mammalian autophagy-specifi c factor for Beclin 1 and class III phosphatidylinositol 3-kinase. Proc Natl Acad Sci U S A 105:19211–19216
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19211-19216
    • Sun, Q.1    Fan, W.2    Chen, K.3
  • 74
    • 58149473473 scopus 로고    scopus 로고
    • Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13- independent mechanism
    • Chan EY, Longatti A, McKnight NC et al (2009) Kinase-inactivated ULK proteins inhibit autophagy via their conserved C-terminal domains using an Atg13- independent mechanism. Mol Cell Biol 29: 157–171
    • (2009) Mol Cell Biol , vol.29 , pp. 157-171
    • Chan, E.Y.1    Longatti, A.2    Mc Knight, N.C.3
  • 75
    • 33750366092 scopus 로고    scopus 로고
    • Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes
    • Young AR, Chan EY, Hu XW et al (2006) Starvation and ULK1-dependent cycling of mammalian Atg9 between the TGN and endosomes. J Cell Sci 119:3888–3900
    • (2006) J Cell Sci , vol.119 , pp. 3888-3900
    • Young, A.R.1    Chan, E.Y.2    Hu, X.W.3
  • 76
    • 19244384656 scopus 로고    scopus 로고
    • Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-defi cient mice
    • Tanaka Y, Guhde G, Suter A et al (2000) Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-defi cient mice. Nature 406:902–906
    • (2000) Nature , vol.406 , pp. 902-906
    • Tanaka, Y.1    Guhde, G.2    Suter, A.3
  • 77
    • 7244255989 scopus 로고    scopus 로고
    • Role for Rab7 in maturation of late autophagic vacuoles
    • Jager S, Bucci C, Tanida I et al (2004) Role for Rab7 in maturation of late autophagic vacuoles. J Cell Sci 117:4837–4848
    • (2004) J Cell Sci , vol.117 , pp. 4837-4848
    • Jager, S.1    Bucci, C.2    Tanida, I.3
  • 78
    • 33746108329 scopus 로고    scopus 로고
    • Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy
    • Tanida I, Minematsu-Ikeguchi N, Ueno T et al (2005) Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy. Autophagy 1:84–91
    • (2005) Autophagy , vol.1 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3
  • 79
    • 33847048316 scopus 로고    scopus 로고
    • Regulation of autophagy by extracellular signalregulated protein kinases during 1-methyl-4- phenylpyridinium-induced cell death
    • Zhu JH, Horbinski C, Guo F et al (2007) Regulation of autophagy by extracellular signalregulated protein kinases during 1-methyl-4- phenylpyridinium-induced cell death. Am J Pathol 170:75–86
    • (2007) Am J Pathol , vol.170 , pp. 75-86
    • Zhu, J.H.1    Horbinski, C.2    Guo, F.3
  • 80
    • 16244362671 scopus 로고    scopus 로고
    • Apoptosis, pyroptosis, and necrosis: Mechanistic description of dead and dying eukaryotic cells
    • Fink SL, Cookson BT (2005) Apoptosis, pyroptosis, and necrosis: mechanistic description of dead and dying eukaryotic cells. Infect Immun 73:1907–1916
    • (2005) Infect Immun , vol.73 , pp. 1907-1916
    • Fink, S.L.1    Cookson, B.T.2
  • 81
    • 33749576792 scopus 로고    scopus 로고
    • Caspase-1- dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages
    • Fink SL, Cookson BT (2006) Caspase-1- dependent pore formation during pyroptosis leads to osmotic lysis of infected host macrophages. Cell Microbiol 8:1812–1825
    • (2006) Cell Microbiol , vol.8 , pp. 1812-1825
    • Fink, S.L.1    Cookson, B.T.2
  • 82
    • 0033815330 scopus 로고    scopus 로고
    • Salmonella induces macrophage death by caspase-1- dependent necrosis
    • Brennan MA, Cookson BT (2000) Salmonella induces macrophage death by caspase-1- dependent necrosis. Mol Microbiol 38:31–40
    • (2000) Mol Microbiol , vol.38 , pp. 31-40
    • Brennan, M.A.1    Cookson, B.T.2
  • 83
    • 0034596826 scopus 로고    scopus 로고
    • Salmonella-induced caspase-2 activation in macrophages: A novel mechanism in pathogenmediated apoptosis
    • Jesenberger V, Procyk KJ, Yuan J et al (2000) Salmonella-induced caspase-2 activation in macrophages: a novel mechanism in pathogenmediated apoptosis. J Exp Med 192: 1035–1046
    • (2000) J Exp Med , vol.192 , pp. 1035-1046
    • Jesenberger, V.1    Procyk, K.J.2    Yuan, J.3
  • 84
    • 0035859894 scopus 로고    scopus 로고
    • Molecular cloning of Porimin, a novel cell surface receptor mediating oncotic cell death
    • Ma F, Zhang C, Prasad KV et al (2001) Molecular cloning of Porimin, a novel cell surface receptor mediating oncotic cell death. Proc Natl Acad Sci U S A 98:9778–9783
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9778-9783
    • Ma, F.1    Zhang, C.2    Prasad, K.V.3
  • 85
    • 0030915587 scopus 로고    scopus 로고
    • Intracellular ATP levels determine cell death fate by apoptosis or necrosis
    • Eguchi Y, Shimizu S, Tsujimoto Y (1997) Intracellular ATP levels determine cell death fate by apoptosis or necrosis. Cancer Res 57:1835–1840
    • (1997) Cancer Res , vol.57 , pp. 1835-1840
    • Eguchi, Y.1    Shimizu, S.2    Tsujimoto, Y.3
  • 86
    • 84876516775 scopus 로고    scopus 로고
    • Cell death pathways in astrocytes with a modifi ed model of oxygen-glucose deprivation
    • Huang Q, Zhang R, Zou L et al (2013) Cell death pathways in astrocytes with a modifi ed model of oxygen-glucose deprivation. PLoS One 8:61345
    • (2013) PLoS One , vol.8 , pp. 61345
    • Huang, Q.1    Zhang, R.2    Zou, L.3
  • 87
    • 0030916669 scopus 로고    scopus 로고
    • The proto-oncogene Bcl-2 and its role in regulating apoptosis
    • Kroemer G (1997) The proto-oncogene Bcl-2 and its role in regulating apoptosis. Nat Med 3:614–620
    • (1997) Nat Med , vol.3 , pp. 614-620
    • Kroemer, G.1
  • 88
    • 21444445692 scopus 로고    scopus 로고
    • Apoptosis in the mammalian CNS: Lessons from animal models
    • Lossi L, Cantile C, Tamagno I et al (2005) Apoptosis in the mammalian CNS: lessons from animal models. Vet J 170:52–66
    • (2005) Vet J , vol.170 , pp. 52-66
    • Lossi, L.1    Cantile, C.2    Tamagno, I.3
  • 89
    • 16644379682 scopus 로고    scopus 로고
    • Molecular morphology of neuronal apoptosis: Activation of caspase 3 during postnatal development of mouse cerebellar cortex
    • Lossi L, Tamagno I, Merighi A (2004) Molecular morphology of neuronal apoptosis: Activation of caspase 3 during postnatal development of mouse cerebellar cortex. J Mol Histol 35:621–629
    • (2004) J Mol Histol , vol.35 , pp. 621-629
    • Lossi, L.1    Tamagno, I.2    Merighi, A.3
  • 90
    • 34247523696 scopus 로고    scopus 로고
    • Pathological apoptosis in the developing brain
    • Blomgren K, Leist M, Groc L (2007) Pathological apoptosis in the developing brain. Apoptosis 12:993–1010
    • (2007) Apoptosis , vol.12 , pp. 993-1010
    • Blomgren, K.1    Leist, M.2    Groc, L.3


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