메뉴 건너뛰기




Volumn 6, Issue SUPPL. 2, 2006, Pages

Involvement of apoptosis and cholinergic dysfunction in Alzheimer's disease

Author keywords

Alzheimer's disease; Amyloid beta peptides; Amyloid beta peptides oligomers; Amyloid beta peptides toxicity; Apoptosis; Central cholinergic neurons; Neurofibrillary tangles; Nicotinic receptor

Indexed keywords

AMYLOID BETA PROTEIN; APOPTOSIS INHIBITOR; BH4 PROTEIN; CASPASE; CASPASE INHIBITOR; CYSTEINE PROTEINASE; FAS ANTIGEN; TAU PROTEIN; UNCLASSIFIED DRUG;

EID: 33749599696     PISSN: 13463500     EISSN: 14798301     Source Type: Journal    
DOI: 10.1111/j.1479-8301.2006.00172.x     Document Type: Article
Times cited : (5)

References (53)
  • 2
    • 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
  • 3
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis. Science 1997; 275: 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 4
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K etal. Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked. Science 1997; 275: 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 5
    • 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
  • 6
    • 0030916417 scopus 로고    scopus 로고
    • DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis
    • Liu X, Zou H, Slaughter C, Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 1997; 89: 175-184.
    • (1997) Cell , vol.89 , pp. 175-184
    • Liu, X.1    Zou, H.2    Slaughter, C.3    Wang, X.4
  • 7
    • 0033596980 scopus 로고    scopus 로고
    • An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9
    • Zou H, Li Y, Liu X, Wang X. An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9. J Biol Chem 1999; 274: 11549-11556.
    • (1999) J Biol Chem , vol.274 , pp. 11549-11556
    • Zou, H.1    Li, Y.2    Liu, X.3    Wang, X.4
  • 8
    • 0037401562 scopus 로고    scopus 로고
    • Cell death regulation by the Bcl-2 protein family in the mitochondria
    • Tsujimoto Y. Cell death regulation by the Bcl-2 protein family in the mitochondria. J Cell Physiol 2003; 195: 158-167.
    • (2003) J Cell Physiol , vol.195 , pp. 158-167
    • Tsujimoto, Y.1
  • 9
    • 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
  • 10
    • 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, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102: 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 11
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen AM, Ekert PG, Pakusch M et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 2000; 102: 43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3
  • 12
  • 13
    • 0032910169 scopus 로고    scopus 로고
    • Apoptosis control by death and decoy receptors
    • Ashkenazi A, Dixit VM. Apoptosis control by death and decoy receptors. Curr Opin Cell Biol 1999; 11: 255-260.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 255-260
    • Ashkenazi, A.1    Dixit, V.M.2
  • 14
    • 0032555716 scopus 로고    scopus 로고
    • Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors
    • Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 1998; 94: 481-490.
    • (1998) Cell , vol.94 , pp. 481-490
    • Luo, X.1    Budihardjo, I.2    Zou, H.3    Slaughter, C.4    Wang, X.5
  • 15
    • 0035978485 scopus 로고    scopus 로고
    • The unfolded protein response and Alzheimer's disease
    • Imaizumi K, Miyoshi K, Katayama T etal. The unfolded protein response and Alzheimer's disease. Biochim Biophys Acta 2001; 1536: 85-96.
    • (2001) Biochim Biophys Acta , vol.1536 , pp. 85-96
    • Imaizumi, K.1    Miyoshi, K.2    Katayama, T.3
  • 16
    • 0031755020 scopus 로고    scopus 로고
    • Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control
    • Shi Y, Vattem KM, Sood R et al. Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control. Mol Cell Biol 1998; 18: 7499-7509.
    • (1998) Mol Cell Biol , vol.18 , pp. 7499-7509
    • Shi, Y.1    Vattem, K.M.2    Sood, R.3
  • 17
    • 0032525990 scopus 로고    scopus 로고
    • A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells
    • Tirasophon W, Welihinda AA, Kaufman RJ. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev 1998; 12: 1812-1824.
    • (1998) Genes Dev , vol.12 , pp. 1812-1824
    • Tirasophon, W.1    Welihinda, A.A.2    Kaufman, R.J.3
  • 18
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 1999; 10: 3787-3799.
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 19
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T, Zhu H, Morishima N et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000; 403: 98-103.
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3
  • 21
    • 11344265672 scopus 로고    scopus 로고
    • Interactions between beta-amyloid and central cholinergic neurons: Implications for Alzheimer's disease
    • Kar S, Slowikowski SP, Westaway D, Mount HT. Interactions between beta-amyloid and central cholinergic neurons: Implications for Alzheimer's disease. J Psychiatry Neurosci 2004; 29: 427-441.
    • (2004) J Psychiatry Neurosci , vol.29 , pp. 427-441
    • Kar, S.1    Slowikowski, S.P.2    Westaway, D.3    Mount, H.T.4
  • 22
    • 0032525799 scopus 로고    scopus 로고
    • Amyloid beta neurotoxicity in the cholinergic but not in the serotonergic phenotype of RN46A cells
    • Olesen OF, Dago L, Mikkelsen JD. Amyloid beta neurotoxicity in the cholinergic but not in the serotonergic phenotype of RN46A cells. Brain Res Mol Brain Res 1998; 57: 266-274.
    • (1998) Brain Res Mol Brain Res , vol.57 , pp. 266-274
    • Olesen, O.F.1    Dago, L.2    Mikkelsen, J.D.3
  • 23
    • 0027302886 scopus 로고
    • Cultured GABA-immunoreactive neurons are resistant to toxicity induced by beta-amyloid
    • Pike CJ, Cotman CW. Cultured GABA-immunoreactive neurons are resistant to toxicity induced by beta-amyloid. Neuroscience 1993; 56: 269-274.
    • (1993) Neuroscience , vol.56 , pp. 269-274
    • Pike, C.J.1    Cotman, C.W.2
  • 24
    • 0035251752 scopus 로고    scopus 로고
    • Nicotinic receptor-mediated protection against beta-amyloid neurotoxicity
    • Shimohama S, Kihara T. Nicotinic receptor-mediated protection against beta-amyloid neurotoxicity. Biol Psychiatry 2001; 49: 233-239.
    • (2001) Biol Psychiatry , vol.49 , pp. 233-239
    • Shimohama, S.1    Kihara, T.2
  • 25
    • 0035836747 scopus 로고    scopus 로고
    • Beta-amyloid peptide blocks the response of alpha 7-containing nicotinic receptors on hippocampal neurons
    • Liu Q, Kawai H, Berg DK. Beta-amyloid peptide blocks the response of alpha 7-containing nicotinic receptors on hippocampal neurons. Proc Natl Acad Sci USA 2001; 98: 4734-4739.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4734-4739
    • Liu, Q.1    Kawai, H.2    Berg, D.K.3
  • 26
    • 0036534870 scopus 로고    scopus 로고
    • Role of p75 neurotrophin receptor in the neurotoxicity by beta-amyloid peptides and synergistic effect of inflammatory cytokines
    • Perini G, Della-Bianca V, Politi V et al. Role of p75 neurotrophin receptor in the neurotoxicity by beta-amyloid peptides and synergistic effect of inflammatory cytokines. J Exp Med 2002; 195: 907-918.
    • (2002) J Exp Med , vol.195 , pp. 907-918
    • Perini, G.1    Della-Bianca, V.2    Politi, V.3
  • 27
    • 0028985574 scopus 로고
    • Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein
    • Games D, Adams D, Alessandrini R etal. Alzheimer-type neuropathology in transgenic mice overexpressing V717F beta-amyloid precursor protein. Nature 1995; 373: 523-527.
    • (1995) Nature , vol.373 , pp. 523-527
    • Games, D.1    Adams, D.2    Alessandrini, R.3
  • 28
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice
    • Hsiao K, Chapman P, Nilsen S et al. Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice. Science 1996; 274: 99-102.
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3
  • 29
    • 0034426011 scopus 로고    scopus 로고
    • Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein
    • Lewis J, McGowan E, Rockwood J et al. Neurofibrillary tangles, amyotrophy and progressive motor disturbance in mice expressing mutant (P301L) tau protein. Nat Genet 2000; 25: 402-405.
    • (2000) Nat Genet , vol.25 , pp. 402-405
    • Lewis, J.1    McGowan, E.2    Rockwood, J.3
  • 30
    • 17944382037 scopus 로고    scopus 로고
    • Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
    • Lewis J, Dickson DW, Lin WL etal. Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP. Science 2001; 293: 1487-1491.
    • (2001) Science , vol.293 , pp. 1487-1491
    • Lewis, J.1    Dickson, D.W.2    Lin, W.L.3
  • 31
    • 0035943436 scopus 로고    scopus 로고
    • Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils
    • Gotz J, Chen F, van Dorpe J, Nitsch RM. Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils. Science 2001; 293: 1491-1495.
    • (2001) Science , vol.293 , pp. 1491-1495
    • Gotz, J.1    Chen, F.2    van Dorpe, J.3    Nitsch, R.M.4
  • 32
    • 0026487365 scopus 로고
    • Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase
    • Hanger DP, Hughes K, Woodgett JR, Brion JP, Anderton BH. Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase. Neurosci Lett 1992; 147: 58-62.
    • (1992) Neurosci Lett , vol.147 , pp. 58-62
    • Hanger, D.P.1    Hughes, K.2    Woodgett, J.R.3    Brion, J.P.4    Anderton, B.H.5
  • 33
    • 0029994754 scopus 로고    scopus 로고
    • Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: The effects on the organization and stability of microtubules
    • Lovestone S, Hartley CL, Pearce J, Anderton BH. Phosphorylation of tau by glycogen synthase kinase-3 beta in intact mammalian cells: The effects on the organization and stability of microtubules. Neuroscience 1996; 73: 1145-1157.
    • (1996) Neuroscience , vol.73 , pp. 1145-1157
    • Lovestone, S.1    Hartley, C.L.2    Pearce, J.3    Anderton, B.H.4
  • 34
    • 0037836969 scopus 로고    scopus 로고
    • Significance of intracellular A beta in Alzheimer's disease
    • Tabira T. [Significance of intracellular A beta in Alzheimer's disease]. Nihon Shinkei Seishin Yakurigaku Zasshi 2002; 22: 175-180.
    • (2002) Nihon Shinkei Seishin Yakurigaku Zasshi , vol.22 , pp. 175-180
    • Tabira, T.1
  • 35
    • 7244236841 scopus 로고    scopus 로고
    • A modified beta-amyloid hypothesis: Intraneuronal accumulation of the beta-amyloid peptide-the first step of a fatal cascade
    • Wirths O, Multhaup G, Bayer TA. A modified beta-amyloid hypothesis: intraneuronal accumulation of the beta-amyloid peptide-the first step of a fatal cascade. J Neurochem 2004; 91: 513-520.
    • (2004) J Neurochem , vol.91 , pp. 513-520
    • Wirths, O.1    Multhaup, G.2    Bayer, T.A.3
  • 36
    • 0036272650 scopus 로고    scopus 로고
    • Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities
    • Casley CS, Canevari L, Land JM, Clark JB, Sharpe MA. Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J Neurochem 2002; 80: 91-100.
    • (2002) J Neurochem , vol.80 , pp. 91-100
    • Casley, C.S.1    Canevari, L.2    Land, J.M.3    Clark, J.B.4    Sharpe, M.A.5
  • 37
    • 11144353586 scopus 로고    scopus 로고
    • ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease
    • Lustbader JW, Cirilli M, Lin C et al. ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science 2004; 304: 448-452.
    • (2004) Science , vol.304 , pp. 448-452
    • Lustbader, J.W.1    Cirilli, M.2    Lin, C.3
  • 38
    • 20144388830 scopus 로고    scopus 로고
    • ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction
    • Takuma K, Yao J, Huang J et al. ABAD enhances Abeta-induced cell stress via mitochondrial dysfunction. Faseb J 2005; 19: 597-598.
    • (2005) Faseb J , vol.19 , pp. 597-598
    • Takuma, K.1    Yao, J.2    Huang, J.3
  • 39
    • 0025987048 scopus 로고
    • Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment
    • Terry RD, Masliah E, Salmon DP et al. Physical basis of cognitive alterations in Alzheimer's disease: Synapse loss is the major correlate of cognitive impairment. Ann Neurol 1991; 30: 572-580.
    • (1991) Ann Neurol , vol.30 , pp. 572-580
    • Terry, R.D.1    Masliah, E.2    Salmon, D.P.3
  • 40
    • 0035830408 scopus 로고    scopus 로고
    • Altered expression of synaptic proteins occurs early during progression of Alzheimer's disease
    • Masliah E, Mallory M, Alford M et al. Altered expression of synaptic proteins occurs early during progression of Alzheimer's disease. Neurology 2001; 56: 127-129.
    • (2001) Neurology , vol.56 , pp. 127-129
    • Masliah, E.1    Mallory, M.2    Alford, M.3
  • 41
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy J, Selkoe DJ. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002; 297: 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 42
    • 0032539975 scopus 로고    scopus 로고
    • Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red
    • Podlisny MB, Walsh DM, Amarante P et al. Oligomerization of endogenous and synthetic amyloid beta-protein at nanomolar levels in cell culture and stabilization of monomer by Congo red. Biochemistry 1998; 37: 3602-3611.
    • (1998) Biochemistry , vol.37 , pp. 3602-3611
    • Podlisny, M.B.1    Walsh, D.M.2    Amarante, P.3
  • 43
    • 0032590054 scopus 로고    scopus 로고
    • Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease
    • McLean CA, Cherny RA, Fraser FW et al. Soluble pool of Abeta amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease. Ann Neurol 1999; 46: 860-866.
    • (1999) Ann Neurol , vol.46 , pp. 860-866
    • McLean, C.A.1    Cherny, R.A.2    Fraser, F.W.3
  • 44
    • 0037041426 scopus 로고    scopus 로고
    • Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo
    • Walsh DM, Klyubin I, Fadeeva JV et al. Naturally secreted oligomers of amyloid beta protein potently inhibit hippocampal long-term potentiation in vivo. Nature 2002; 416: 535-539.
    • (2002) Nature , vol.416 , pp. 535-539
    • Walsh, D.M.1    Klyubin, I.2    Fadeeva, J.V.3
  • 45
    • 8744220663 scopus 로고    scopus 로고
    • Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases
    • Kayed R, Sokolov Y, Edmonds B et al. Permeabilization of lipid bilayers is a common conformation-dependent activity of soluble amyloid oligomers in protein misfolding diseases. J Biol Chem 2004; 279: 46363-46366.
    • (2004) J Biol Chem , vol.279 , pp. 46363-46366
    • Kayed, R.1    Sokolov, Y.2    Edmonds, B.3
  • 46
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 2003; 300: 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3
  • 47
    • 0034098993 scopus 로고    scopus 로고
    • Subcellular localization of presenilins: Association with a unique membrane pool in cultured cells
    • Kim SH, Lah JJ, Thinakaran G, Levey A, Sisodia SS. Subcellular localization of presenilins: Association with a unique membrane pool in cultured cells. Neurobiol Dis 2000; 7: 99-117.
    • (2000) Neurobiol Dis , vol.7 , pp. 99-117
    • Kim, S.H.1    Lah, J.J.2    Thinakaran, G.3    Levey, A.4    Sisodia, S.S.5
  • 48
    • 0033258544 scopus 로고    scopus 로고
    • Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response
    • Katayama T, Imaizumi K, Sato N et al. Presenilin-1 mutations downregulate the signalling pathway of the unfolded-protein response. Nat Cell Biol 1999; 1: 479-485.
    • (1999) Nat Cell Biol , vol.1 , pp. 479-485
    • Katayama, T.1    Imaizumi, K.2    Sato, N.3
  • 49
    • 0033671650 scopus 로고    scopus 로고
    • Upregulation of BiP and CHOP by the unfolded-protein response is independent of presenilin expression
    • Sato N, Urano F, Yoon Leem J et al. Upregulation of BiP and CHOP by the unfolded-protein response is independent of presenilin expression. Nat Cell Biol 2000; 2: 863-870.
    • (2000) Nat Cell Biol , vol.2 , pp. 863-870
    • Sato, N.1    Urano, F.2    Yoon Leem, J.3
  • 50
    • 2442432416 scopus 로고    scopus 로고
    • Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death
    • Hitomi J, Katayama T, Eguchi Y et al. Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Abeta-induced cell death. J Cell Biol 2004; 165: 347-356.
    • (2004) J Cell Biol , vol.165 , pp. 347-356
    • Hitomi, J.1    Katayama, T.2    Eguchi, Y.3
  • 51
    • 23844481790 scopus 로고    scopus 로고
    • Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis
    • Obeng EA, Boise LH. Caspase-12 and caspase-4 are not required for caspase-dependent endoplasmic reticulum stress-induced apoptosis. J Biol Chem 2005; 280: 29578-29587.
    • (2005) J Biol Chem , vol.280 , pp. 29578-29587
    • Obeng, E.A.1    Boise, L.H.2
  • 52
    • 0346753589 scopus 로고    scopus 로고
    • BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo
    • Sugioka R, Shimizu S, Funatsu T et al. BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo. Oncogene 2003; 22: 8432-8440.
    • (2003) Oncogene , vol.22 , pp. 8432-8440
    • Sugioka, R.1    Shimizu, S.2    Funatsu, T.3
  • 53
    • 10344262564 scopus 로고    scopus 로고
    • Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes
    • Shimizu S, Kanaseki T, Mizushima N et al. Role of Bcl-2 family proteins in a non-apoptotic programmed cell death dependent on autophagy genes. Nat Cell Biol 2004; 6: 1221-1228.
    • (2004) Nat Cell Biol , vol.6 , pp. 1221-1228
    • Shimizu, S.1    Kanaseki, T.2    Mizushima, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.