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Volumn 170, Issue 1, 2007, Pages 75-86

Regulation of autophagy by extracellular signal-regulated protein kinases during 1-methyl-4-phenylpyridinium-induced cell death

Author keywords

[No Author keywords available]

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; MITOGEN ACTIVATED PROTEIN KINASE; NEUROTOXIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE; APOPTOSIS REGULATORY PROTEIN; BECN1 PROTEIN, HUMAN; BECN1 PROTEIN, MOUSE; MEMBRANE PROTEIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 33847048316     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.2353/ajpath.2007.060524     Document Type: Article
Times cited : (403)

References (80)
  • 1
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross CA, Poirier MA: Protein aggregation and neurodegenerative disease. Nat Med 2004, 10(Suppl):S10-S17
    • (2004) Nat Med , vol.10 , Issue.SUPPL.
    • Ross, C.A.1    Poirier, M.A.2
  • 2
    • 0034004683 scopus 로고    scopus 로고
    • Ubiquitin immunochemistry as a diagnostic aid for community pathologists evaluating patients who have dementia
    • Chu CT, Caruso JL, Cummings TJ, Ervin J, Rosenberg C, Hulette CM: Ubiquitin immunochemistry as a diagnostic aid for community pathologists evaluating patients who have dementia. Mod Pathol 2000, 13:420-426
    • (2000) Mod Pathol , vol.13 , pp. 420-426
    • Chu, C.T.1    Caruso, J.L.2    Cummings, T.J.3    Ervin, J.4    Rosenberg, C.5    Hulette, C.M.6
  • 5
    • 0037109770 scopus 로고    scopus 로고
    • Methamphetamine-induced degeneration of dopaminergic neurons involves autophagy and upregulation of dopamine synthesis
    • Larsen KE, Fon EA, Hastings TG, Edwards RH, Sulzer D: Methamphetamine-induced degeneration of dopaminergic neurons involves autophagy and upregulation of dopamine synthesis. J Neurosci 2002, 22:8951-8960
    • (2002) J Neurosci , vol.22 , pp. 8951-8960
    • Larsen, K.E.1    Fon, E.A.2    Hastings, T.G.3    Edwards, R.H.4    Sulzer, D.5
  • 6
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo AM, Stefanis L, Fredenburg R, Lansbury PT, Sulzer D: Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 2004, 305:1292-1295
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 7
    • 0043173825 scopus 로고    scopus 로고
    • Dopamine induces autophagic cell death and alpha-synuclein increase in human neuroblastoma SH-SY5Y cells
    • Gómez-Santos C, Ferrer I, Santidrian AF, Barrachina M, Gil J, Ambrosio S: Dopamine induces autophagic cell death and alpha-synuclein increase in human neuroblastoma SH-SY5Y cells. J Neurosci Res 2003, 73:341-350
    • (2003) J Neurosci Res , vol.73 , pp. 341-350
    • Gómez-Santos, C.1    Ferrer, I.2    Santidrian, A.F.3    Barrachina, M.4    Gil, J.5    Ambrosio, S.6
  • 8
    • 0242499488 scopus 로고    scopus 로고
    • Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases
    • Zhu J-H, Guo F, Shelburne J, Watkins S, Chu CT: Localization of phosphorylated ERK/MAP kinases to mitochondria and autophagosomes in Lewy body diseases. Brain Pathol 2003, 13:473-481
    • (2003) Brain Pathol , vol.13 , pp. 473-481
    • Zhu, J.-H.1    Guo, F.2    Shelburne, J.3    Watkins, S.4    Chu, C.T.5
  • 12
    • 0035364748 scopus 로고    scopus 로고
    • Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration
    • Petersén A, Larsen KE, Behr GG, Romero N, Przedborski S, Brundin P, Sulzer D: Expanded CAG repeats in exon 1 of the Huntington's disease gene stimulate dopamine-mediated striatal neuron autophagy and degeneration. Hum Mol Genet 2001, 10:1243-1254
    • (2001) Hum Mol Genet , vol.10 , pp. 1243-1254
    • Petersén, A.1    Larsen, K.E.2    Behr, G.G.3    Romero, N.4    Przedborski, S.5    Brundin, P.6    Sulzer, D.7
  • 14
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine B, Klionsky DJ: Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev Cell 2004, 6:463-477
    • (2004) Dev Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 16
    • 4344660368 scopus 로고    scopus 로고
    • The role of macroautophagy in the ageing process, anti-ageing intervention and age-associated diseases
    • Bergamini E, Cavallini G, Donati A, Gori Z: The role of macroautophagy in the ageing process, anti-ageing intervention and age-associated diseases. Int J Biochem Cell Biol 2004, 36:2392-2404
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2392-2404
    • Bergamini, E.1    Cavallini, G.2    Donati, A.3    Gori, Z.4
  • 17
    • 4544385218 scopus 로고    scopus 로고
    • Autophagy: Many paths to the same end
    • Cuervo AM: Autophagy: many paths to the same end. Mol Cell Biochem 2004, 263:55-72
    • (2004) Mol Cell Biochem , vol.263 , pp. 55-72
    • Cuervo, A.M.1
  • 18
    • 0032747486 scopus 로고    scopus 로고
    • Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease: Evidence for apoptotic cell death
    • Stadelmann C, Deckwerth TL, Srinivasan A, Bancher C, Bruck W, Jellinger K, Lassmann H: Activation of caspase-3 in single neurons and autophagic granules of granulovacuolar degeneration in Alzheimer's disease: evidence for apoptotic cell death. Am J Pathol 1999, 155:1459-1466
    • (1999) Am J Pathol , vol.155 , pp. 1459-1466
    • Stadelmann, C.1    Deckwerth, T.L.2    Srinivasan, A.3    Bancher, C.4    Bruck, W.5    Jellinger, K.6    Lassmann, H.7
  • 19
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system
    • Cataldo AM, Barnett JL, Berman SA, Li J, Quarless S, Bursztajn S, Lippa C, Nixon RA: Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: evidence for early up-regulation of the endosomal-lysosomal system. Neuron 1995, 14:671-680
    • (1995) Neuron , vol.14 , pp. 671-680
    • Cataldo, A.M.1    Barnett, J.L.2    Berman, S.A.3    Li, J.4    Quarless, S.5    Bursztajn, S.6    Lippa, C.7    Nixon, R.A.8
  • 22
    • 0037193474 scopus 로고    scopus 로고
    • DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
    • Inbal B, Bialik S, Sabanay I, Shani G, Kimchi A: DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death. J Cell Biol 2002, 157:455-468
    • (2002) J Cell Biol , vol.157 , pp. 455-468
    • Inbal, B.1    Bialik, S.2    Sabanay, I.3    Shani, G.4    Kimchi, A.5
  • 23
    • 0032870475 scopus 로고    scopus 로고
    • Autophagy is activated by apoptotic signalling in sympathetic neurons: An alternative mechanism of death execution
    • Xue L, Fletcher GC, Tolkovsky AM: Autophagy is activated by apoptotic signalling in sympathetic neurons: an alternative mechanism of death execution. Mol Cell Neurosci 1999, 14:180-198
    • (1999) Mol Cell Neurosci , vol.14 , pp. 180-198
    • Xue, L.1    Fletcher, G.C.2    Tolkovsky, A.M.3
  • 25
    • 0034849783 scopus 로고    scopus 로고
    • Autophagic cell death and its execution by lysosomal cathepsins
    • Uchiyama Y: Autophagic cell death and its execution by lysosomal cathepsins. Arch Histol Cytol 2001, 64:233-246
    • (2001) Arch Histol Cytol , vol.64 , pp. 233-246
    • Uchiyama, Y.1
  • 28
    • 0041411115 scopus 로고    scopus 로고
    • Autophagic programmed cell death in Drosophila
    • Baehrecke EH: Autophagic programmed cell death in Drosophila. Cell Death Differ 2003, 10:940-945
    • (2003) Cell Death Differ , vol.10 , pp. 940-945
    • Baehrecke, E.H.1
  • 31
    • 0034001444 scopus 로고    scopus 로고
    • Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation
    • Doh-Ura K, Iwaki T, Caughey B: Lysosomotropic agents and cysteine protease inhibitors inhibit scrapie-associated prion protein accumulation. J Virol 2000, 74:4894-4897
    • (2000) J Virol , vol.74 , pp. 4894-4897
    • Doh-Ura, K.1    Iwaki, T.2    Caughey, B.3
  • 32
    • 4344689871 scopus 로고    scopus 로고
    • Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: Implications for beta-amyloid peptide over-production and localization in Alzheimer's disease
    • Yu WH, Kumar A, Peterhoff C, Shapiro Kulnane L, Uchiyama Y, Lamb BT, Cuervo AM, Nixon RA: Autophagic vacuoles are enriched in amyloid precursor protein-secretase activities: implications for beta-amyloid peptide over-production and localization in Alzheimer's disease. Int J Biochem Cell Biol 2004, 36:2531-2540
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2531-2540
    • Yu, W.H.1    Kumar, A.2    Peterhoff, C.3    Shapiro Kulnane, L.4    Uchiyama, Y.5    Lamb, B.T.6    Cuervo, A.M.7    Nixon, R.A.8
  • 34
    • 0347986620 scopus 로고    scopus 로고
    • Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes
    • Tassa A, Roux MP, Attaix D, Bechet DM: Class III phosphoinositide 3-kinase-Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes. Biochem J 2003, 376:577-586
    • (2003) Biochem J , vol.376 , pp. 577-586
    • Tassa, A.1    Roux, M.P.2    Attaix, D.3    Bechet, D.M.4
  • 37
    • 0033104442 scopus 로고    scopus 로고
    • Characterization and time course of MPP+-induced apoptosis in human SH-SY5Y neuroblastoma cells
    • Fall CP, Bennett JP Jr: Characterization and time course of MPP+-induced apoptosis in human SH-SY5Y neuroblastoma cells. J Neurosci Res 1999, 55:620-628
    • (1999) J Neurosci Res , vol.55 , pp. 620-628
    • Fall, C.P.1    Bennett Jr, J.P.2
  • 38
    • 25444469905 scopus 로고    scopus 로고
    • Investigating the receptor-independent neuroprotective mechanisms of nicotine in mitochondria
    • Xie YX, Bezard E, Zhao BL: Investigating the receptor-independent neuroprotective mechanisms of nicotine in mitochondria. J Biol Chem 2005, 280:32405-32412
    • (2005) J Biol Chem , vol.280 , pp. 32405-32412
    • Xie, Y.X.1    Bezard, E.2    Zhao, B.L.3
  • 39
    • 0035018119 scopus 로고    scopus 로고
    • Sustained extracellular signal-regulated kinase activation by 6-hydroxydopamine: Implications for Parkinson's disease
    • Kulich SM, Chu CT: Sustained extracellular signal-regulated kinase activation by 6-hydroxydopamine: implications for Parkinson's disease. J Neurochem 2001, 77:1058-1066
    • (2001) J Neurochem , vol.77 , pp. 1058-1066
    • Kulich, S.M.1    Chu, C.T.2
  • 41
    • 0030787340 scopus 로고    scopus 로고
    • Receptor dimerization is not a factor in the signalling activity of a transforming variant epidermal growth factor receptor (EGFRvIII)
    • Chu CT, Everiss KD, Batra S, Wikstrand CJ, Kung H-J, Bigner DD: Receptor dimerization is not a factor in the signalling activity of a transforming variant epidermal growth factor receptor (EGFRvIII). Biochem J 1997, 324:855-861
    • (1997) Biochem J , vol.324 , pp. 855-861
    • Chu, C.T.1    Everiss, K.D.2    Batra, S.3    Wikstrand, C.J.4    Kung, H.-J.5    Bigner, D.D.6
  • 42
    • 0037332108 scopus 로고    scopus 로고
    • Role of reactive oxygen species in ERK phosphorylation and 6-hydroxydopamine cytotoxicity
    • Kulich SM, Chu CT: Role of reactive oxygen species in ERK phosphorylation and 6-hydroxydopamine cytotoxicity. J Biosci 2003, 28:83-89
    • (2003) J Biosci , vol.28 , pp. 83-89
    • Kulich, S.M.1    Chu, C.T.2
  • 43
    • 24044455008 scopus 로고    scopus 로고
    • Manganese superoxide dismutase protects against 6-hydroxydopamine injury in mouse brains
    • Callio J, Oury TD, Chu CT: Manganese superoxide dismutase protects against 6-hydroxydopamine injury in mouse brains. J Biol Chem 2005, 280:18536-18542
    • (2005) J Biol Chem , vol.280 , pp. 18536-18542
    • Callio, J.1    Oury, T.D.2    Chu, C.T.3
  • 44
    • 0034757896 scopus 로고    scopus 로고
    • A novel assay to study autophagy: Regulation of autophagosome vacuole size by amino acid deprivation
    • Munafó DB, Colombo MI: A novel assay to study autophagy: regulation of autophagosome vacuole size by amino acid deprivation. J Cell Sci 2001, 114:3619-3629
    • (2001) J Cell Sci , vol.114 , pp. 3619-3629
    • Munafó, D.B.1    Colombo, M.I.2
  • 45
    • 24944576007 scopus 로고    scopus 로고
    • Apoptosis inducing factor mediates caspase-independent 1-methyl-4-phenylpyridinium toxicity in dopaminergic cells
    • Chu CT, Zhu JH, Cao G, Signore A, Wang S, Chen J: Apoptosis inducing factor mediates caspase-independent 1-methyl-4-phenylpyridinium toxicity in dopaminergic cells. J Neurochem 2005, 94:1685-1695
    • (2005) J Neurochem , vol.94 , pp. 1685-1695
    • Chu, C.T.1    Zhu, J.H.2    Cao, G.3    Signore, A.4    Wang, S.5    Chen, J.6
  • 46
    • 0028836002 scopus 로고
    • Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles
    • Biederbick A, Kern HF, Elsasser HP: Monodansylcadaverine (MDC) is a specific in vivo marker for autophagic vacuoles. Eur J Cell Biol 1995, 66:3-14
    • (1995) Eur J Cell Biol , vol.66 , pp. 3-14
    • Biederbick, A.1    Kern, H.F.2    Elsasser, H.P.3
  • 47
    • 0033997045 scopus 로고    scopus 로고
    • The lysosomotropic agent monodansylcadaverine also acts as a solvent polarity probe
    • Niemann A, Takatsuki A, Elsasser HP: The lysosomotropic agent monodansylcadaverine also acts as a solvent polarity probe. J Histochem Cytochem 2000, 48:251-258
    • (2000) J Histochem Cytochem , vol.48 , pp. 251-258
    • Niemann, A.1    Takatsuki, A.2    Elsasser, H.P.3
  • 48
    • 33645652024 scopus 로고    scopus 로고
    • Phosphatidylserine in addition to phosphatidylethanolamine is an in vitro target of the mammalian Atg8 modifiers, LC3, GABARAP, and GATE-16
    • Sou YS, Tanida I, Komatsu M, Ueno T, Kominami E: Phosphatidylserine in addition to phosphatidylethanolamine is an in vitro target of the mammalian Atg8 modifiers, LC3, GABARAP, and GATE-16. J Biol Chem 2006, 281:3017-3024
    • (2006) J Biol Chem , vol.281 , pp. 3017-3024
    • Sou, Y.S.1    Tanida, I.2    Komatsu, M.3    Ueno, T.4    Kominami, E.5
  • 49
    • 0038718698 scopus 로고    scopus 로고
    • MAP-LC3, a promising autophagosomal marker, is processed during the differentiation and recovery of podocytes from PAN nephrosis
    • Asanuma K, Tanida I, Shirato I, Ueno T, Takahara H, Nishitani T, Kominami E, Tomino Y: MAP-LC3, a promising autophagosomal marker, is processed during the differentiation and recovery of podocytes from PAN nephrosis. FASEB J 2003, 17:1165-1167
    • (2003) FASEB J , vol.17 , pp. 1165-1167
    • Asanuma, K.1    Tanida, I.2    Shirato, I.3    Ueno, T.4    Takahara, H.5    Nishitani, T.6    Kominami, E.7    Tomino, Y.8
  • 51
    • 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, Kominami E: Lysosomal turnover, but not a cellular level, of endogenous LC3 is a marker for autophagy. Autophagy 2005, 1:84-91
    • (2005) Autophagy , vol.1 , pp. 84-91
    • Tanida, I.1    Minematsu-Ikeguchi, N.2    Ueno, T.3    Kominami, E.4
  • 52
    • 0031593675 scopus 로고    scopus 로고
    • Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells
    • Yamamoto A, Tagawa Y, Yoshimori T, Moriyama Y, Masaki R, Tashiro Y: Bafilomycin A1 prevents maturation of autophagic vacuoles by inhibiting fusion between autophagosomes and lysosomes in rat hepatoma cell line, H-4-II-E cells. Cell Struct Funct 1998, 23:33-42
    • (1998) Cell Struct Funct , vol.23 , pp. 33-42
    • Yamamoto, A.1    Tagawa, Y.2    Yoshimori, T.3    Moriyama, Y.4    Masaki, R.5    Tashiro, Y.6
  • 54
    • 0031769654 scopus 로고    scopus 로고
    • The 2G2 antibody recognizes an acidic 110-kDa human mitochondrial protein
    • Paulin-Levasseur M, Chen G, Lariviere C: The 2G2 antibody recognizes an acidic 110-kDa human mitochondrial protein. Histochem J 1998, 30:617-625
    • (1998) Histochem J , vol.30 , pp. 617-625
    • Paulin-Levasseur, M.1    Chen, G.2    Lariviere, C.3
  • 56
    • 8044257699 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes
    • Blommaart EF, Krause U, Schellens JP, Vreeling-Sindelarova H, Meijer AJ: The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes. Eur J Biochem 1997, 243:240-246
    • (1997) Eur J Biochem , vol.243 , pp. 240-246
    • Blommaart, E.F.1    Krause, U.2    Schellens, J.P.3    Vreeling-Sindelarova, H.4    Meijer, A.J.5
  • 57
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells
    • Petiot A, Ogier-Denis E, Blommaart EF, Meijer AJ, Codogno P: Distinct classes of phosphatidylinositol 3′-kinases are involved in signaling pathways that control macroautophagy in HT-29 cells. J Biol Chem 2000, 275:992-998
    • (2000) J Biol Chem , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.3    Meijer, A.J.4    Codogno, P.5
  • 58
    • 0038269032 scopus 로고    scopus 로고
    • Amino acids interfere with the ERK1/2-dependent control of macroautophagy by controlling the activation of Raf-1 in human colon cancer HT-29 cells
    • Pattingre S, Bauvy C, Codogno P: Amino acids interfere with the ERK1/2-dependent control of macroautophagy by controlling the activation of Raf-1 in human colon cancer HT-29 cells. J Biol Chem 2003, 278:16667-16674
    • (2003) J Biol Chem , vol.278 , pp. 16667-16674
    • Pattingre, S.1    Bauvy, C.2    Codogno, P.3
  • 59
    • 0037052633 scopus 로고    scopus 로고
    • MPP+ increases alpha-synuclein expression and ERK/MAP-kinase phosphorylation in human neuroblastoma SH-SY5Y cells
    • Gómez-Santos C, Ferrer I, Reiriz J, Vinals F, Barrachina M, Ambrosio S: MPP+ increases alpha-synuclein expression and ERK/MAP-kinase phosphorylation in human neuroblastoma SH-SY5Y cells. Brain Res 2002, 935:32-39
    • (2002) Brain Res , vol.935 , pp. 32-39
    • Gómez-Santos, C.1    Ferrer, I.2    Reiriz, J.3    Vinals, F.4    Barrachina, M.5    Ambrosio, S.6
  • 60
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y: In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 2004, 15:1101-1111
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 62
    • 0345166111 scopus 로고    scopus 로고
    • Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor
    • Yue Z, Jin S, Yang C, Levine AJ, Heintz N: Beclin 1, an autophagy gene essential for early embryonic development, is a haploinsufficient tumor suppressor. Proc Natl Acad Sci USA 2003, 100:15077-15082
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 15077-15082
    • Yue, Z.1    Jin, S.2    Yang, C.3    Levine, A.J.4    Heintz, N.5
  • 63
    • 4444293342 scopus 로고    scopus 로고
    • Peroxisome turnover by micropexophagy: An autophagy-related process
    • Farre JC, Subramani S: Peroxisome turnover by micropexophagy: an autophagy-related process. Trends Cell Biol 2004, 14:515-523
    • (2004) Trends Cell Biol , vol.14 , pp. 515-523
    • Farre, J.C.1    Subramani, S.2
  • 64
    • 0242570685 scopus 로고    scopus 로고
    • Peroxisome homeostasis in Hansenula polymorpha
    • Leão AN, Kiel JA: Peroxisome homeostasis in Hansenula polymorpha. FEMS Yeast Res 2003, 4:131-139
    • (2003) FEMS Yeast Res , vol.4 , pp. 131-139
    • Leão, A.N.1    Kiel, J.A.2
  • 65
    • 29644435706 scopus 로고    scopus 로고
    • Molecular mechanisms and regulation of specific and nonspecific autophagy pathways in yeast
    • Nair U, Klionsky DJ: Molecular mechanisms and regulation of specific and nonspecific autophagy pathways in yeast. J Biol Chem 2005, 280:41785-41788
    • (2005) J Biol Chem , vol.280 , pp. 41785-41788
    • Nair, U.1    Klionsky, D.J.2
  • 66
    • 0036479052 scopus 로고    scopus 로고
    • Mitochondrial disappearance from cells: A clue to the role of autophagy in programmed cell death and disease?
    • Tolkovsky AM, Xue L, Fletcher GC, Borutaite V: Mitochondrial disappearance from cells: a clue to the role of autophagy in programmed cell death and disease? Biochimie 2002, 84:233-240
    • (2002) Biochimie , vol.84 , pp. 233-240
    • Tolkovsky, A.M.1    Xue, L.2    Fletcher, G.C.3    Borutaite, V.4
  • 67
    • 10344242925 scopus 로고    scopus 로고
    • Kinase signaling cascades in the mitochondrion: A matter of life or death
    • Horbinski C, Chu CT: Kinase signaling cascades in the mitochondrion: a matter of life or death. Free Radic Biol Med 2005, 38:2-11
    • (2005) Free Radic Biol Med , vol.38 , pp. 2-11
    • Horbinski, C.1    Chu, C.T.2
  • 69
    • 0036899278 scopus 로고    scopus 로고
    • Cytoplasmic aggregates of phosphorylated extracellular signal-regulated kinase in Lewy body diseases
    • Zhu J-H, Kulich SM, Oury TD, Chu CT: Cytoplasmic aggregates of phosphorylated extracellular signal-regulated kinase in Lewy body diseases. Am J Pathol 2002, 161:2087-2098
    • (2002) Am J Pathol , vol.161 , pp. 2087-2098
    • Zhu, J.-H.1    Kulich, S.M.2    Oury, T.D.3    Chu, C.T.4
  • 70
    • 31544461235 scopus 로고    scopus 로고
    • Inhibition of Akt signaling and enhanced ERK1/2 activity are involved in induction of macroautophagy by triterpenoid B-group soyasaponins in colon cancer cells
    • Ellington AA, Berhow MA, Singletary KW: Inhibition of Akt signaling and enhanced ERK1/2 activity are involved in induction of macroautophagy by triterpenoid B-group soyasaponins in colon cancer cells. Carcinogenesis 2006, 27:298-306
    • (2006) Carcinogenesis , vol.27 , pp. 298-306
    • Ellington, A.A.1    Berhow, M.A.2    Singletary, K.W.3
  • 72
    • 25144506835 scopus 로고    scopus 로고
    • Autophagy in cell death: An innocent convict?
    • Levine B, Yuan J: Autophagy in cell death: an innocent convict? J Clin Invest 2005, 115:2679-2688
    • (2005) J Clin Invest , vol.115 , pp. 2679-2688
    • Levine, B.1    Yuan, J.2
  • 74
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signaling: Their role in cell survival and cell death
    • Codogno P, Meijer AJ: Autophagy and signaling: their role in cell survival and cell death. Cell Death Differ 2005, 12(Suppl 2):1509-1518
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 2 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 75
    • 33745866310 scopus 로고    scopus 로고
    • Autophagic stress in neuronal injury and disease
    • Chu CT: Autophagic stress in neuronal injury and disease. J Neuropathol Exp Neurol 2006, 65:423-432
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 423-432
    • Chu, C.T.1
  • 76
    • 0037818296 scopus 로고    scopus 로고
    • HSpin1, a transmembrane protein interacting with Bcl-2/Bcl-xL, induces a caspase-independent autophagic cell death
    • Yanagisawa H, Miyashita T, Nakano Y, Yamamoto D: HSpin1, a transmembrane protein interacting with Bcl-2/Bcl-xL, induces a caspase-independent autophagic cell death. Cell Death Differ 2003, 10:798-807
    • (2003) Cell Death Differ , vol.10 , pp. 798-807
    • Yanagisawa, H.1    Miyashita, T.2    Nakano, Y.3    Yamamoto, D.4
  • 77
    • 1642280930 scopus 로고    scopus 로고
    • Coronavirus replication complex formation utilizes components of cellular autophagy
    • Prentice E, Jerome WG, Yoshimori T, Mizushima N, Denison MR: Coronavirus replication complex formation utilizes components of cellular autophagy. J Biol Chem 2004, 279:10136-10141
    • (2004) J Biol Chem , vol.279 , pp. 10136-10141
    • Prentice, E.1    Jerome, W.G.2    Yoshimori, T.3    Mizushima, N.4    Denison, M.R.5
  • 79
    • 0036236006 scopus 로고    scopus 로고
    • The mitochondrial-lysosomal axis theory of aging: Accumulation of damaged mitochondria as a result of imperfect autophagocytosis
    • Brunk UT, Terman A: The mitochondrial-lysosomal axis theory of aging: accumulation of damaged mitochondria as a result of imperfect autophagocytosis. Eur J Biochem 2002, 269:1996-2002
    • (2002) Eur J Biochem , vol.269 , pp. 1996-2002
    • Brunk, U.T.1    Terman, A.2


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