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Volumn 20, Issue 1, 2015, Pages 92-109

RIP1-dependent Bid cleavage mediates TNFα-induced but Caspase-3-independent cell death in L929 fibroblastoma cells

Author keywords

Bid cleavage; L929 fibroblastoma cells; L929 fibrosarcoma cells; Necrosis; RIP1; RIP3; TNF

Indexed keywords

BENZYLOXYCARBONYLASPARTYLGLUTAMYLVALYLASPARTYL FLUOROMETHYL KETONE; CASPASE 3; CASPASE 8; CELL PROTEIN; NECROSTATIN 1; PROTEIN BID; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; RIP1 PROTEIN; RIP3 PROTEIN; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; BENZYLOXYCARBONYLVALYL-ALANYL-ASPARTYL FLUOROMETHYL KETONE; BID PROTEIN, MOUSE; CASPASE INHIBITOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PEPTIDE CHLOROMETHYL KETONE; RALBP1 PROTEIN, MOUSE; RECEPTOR INTERACTING PROTEIN SERINE THREONINE KINASE; RIPK3 PROTEIN, MOUSE; TUMOR NECROSIS FACTOR;

EID: 84922076378     PISSN: 13608185     EISSN: 1573675X     Source Type: Journal    
DOI: 10.1007/s10495-014-1058-0     Document Type: Article
Times cited : (28)

References (66)
  • 1
    • 77952236200 scopus 로고    scopus 로고
    • Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features
    • Berghe TV et al (2009) Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features. Cell Death Differ 17(6):922-930
    • (2009) Cell Death Differ , vol.17 , Issue.6 , pp. 922-930
    • Berghe, T.V.1
  • 2
    • 57649149333 scopus 로고    scopus 로고
    • Classification of cell death: Recommendations of the Nomenclature Committee on Cell Death 2009
    • 2744427 18846107 10.1038/cdd.2008.150
    • Kroemer G et al (2008) Classification of cell death: recommendations of the Nomenclature Committee on Cell Death 2009. Cell Death Differ 16(1):3-11
    • (2008) Cell Death Differ , vol.16 , Issue.1 , pp. 3-11
    • Kroemer, G.1
  • 3
    • 77951251430 scopus 로고    scopus 로고
    • Necroptosis as an alternative form of programmed cell death
    • 1:CAS:528:DC%2BC3cXks1Sru7c%3D 2854308 20045303
    • Christofferson DE, Yuan J (2010) Necroptosis as an alternative form of programmed cell death. Curr Opin Cell Biol 22(2):263-268
    • (2010) Curr Opin Cell Biol , vol.22 , Issue.2 , pp. 263-268
    • Christofferson, D.E.1    Yuan, J.2
  • 4
    • 81255195542 scopus 로고    scopus 로고
    • Programmed necrosis: Backup to and competitor with apoptosis in the immune system
    • 1:CAS:528:DC%2BC3MXhsVOisbjN 22089220
    • Han J, Zhong C-Q, Zhang D-W (2011) Programmed necrosis: backup to and competitor with apoptosis in the immune system. Nat Immunol 12(12):1143-1149
    • (2011) Nat Immunol , vol.12 , Issue.12 , pp. 1143-1149
    • Han, J.1    Zhong, C.-Q.2    Zhang, D.-W.3
  • 5
    • 84861653411 scopus 로고    scopus 로고
    • The 'complexities' of life and death: Death receptor signalling platforms
    • 1:CAS:528:DC%2BC38Xnsl2rt7w%3D 22542855
    • Dickens LS et al (2012) The 'complexities' of life and death: death receptor signalling platforms. Exp Cell Res 318(11):1269-1277
    • (2012) Exp Cell Res , vol.318 , Issue.11 , pp. 1269-1277
    • Dickens, L.S.1
  • 6
    • 33847051539 scopus 로고    scopus 로고
    • RIP1, a kinase on the crossroads of a cell's decision to live or die
    • 1:CAS:528:DC%2BD2sXhslWht7k%3D 17301840
    • Festjens N et al (2007) RIP1, a kinase on the crossroads of a cell's decision to live or die. Cell Death Differ 14(3):400-410
    • (2007) Cell Death Differ , vol.14 , Issue.3 , pp. 400-410
    • Festjens, N.1
  • 7
    • 33847251527 scopus 로고    scopus 로고
    • Ubiquitination of RIP1 regulates an NF-κB-independent cell-death switch in TNF signaling
    • 1868513 17306544 10.1016/j.cub.2007.01.027
    • O'Donnell MA et al (2007) Ubiquitination of RIP1 regulates an NF-κB-independent cell-death switch in TNF signaling. Curr Biol 17(5):418-424
    • (2007) Curr Biol , vol.17 , Issue.5 , pp. 418-424
    • O'Donnell, M.A.1
  • 8
    • 43049152912 scopus 로고    scopus 로고
    • TNF-α induces two distinct Caspase-8 activation pathways
    • 1:CAS:528:DC%2BD1cXmsVOru78%3D 18485876
    • Wang L, Du F, Wang X (2008) TNF-α induces two distinct Caspase-8 activation pathways. Cell 133(4):693-703
    • (2008) Cell , vol.133 , Issue.4 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 9
    • 83155192804 scopus 로고    scopus 로고
    • TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex i and II members
    • 1:STN:280:DC%2BC38%2FgsFeisg%3D%3D 3223695 22089168 10.1038/cddis.2011.111
    • Vanlangenakker N et al (2011) TNF-induced necroptosis in L929 cells is tightly regulated by multiple TNFR1 complex I and II members. Cell Death Dis 2(11):e230
    • (2011) Cell Death Dis , vol.2 , Issue.11 , pp. 230
    • Vanlangenakker, N.1
  • 10
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • 1:CAS:528:DC%2BD3sXlvFCgu7Y%3D 12887920
    • Micheau O, Tschopp J (2003) Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 114(2):181-190
    • (2003) Cell , vol.114 , Issue.2 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 11
    • 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
    • 1:CAS:528:DyaK1cXlslOrsbw%3D 9727491
    • Luo X et al (1998) Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94(4):481-490
    • (1998) Cell , vol.94 , Issue.4 , pp. 481-490
    • Luo, X.1
  • 12
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • 1:CAS:528:DyaK1cXlslOrsbY%3D 9727492
    • Li H et al (1998) Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94(4):491-501
    • (1998) Cell , vol.94 , Issue.4 , pp. 491-501
    • Li, H.1
  • 13
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced Inflammation
    • 1:CAS:528:DC%2BD1MXps1eiu7o%3D 2727676 19524513
    • Cho Y et al (2009) Phosphorylation-Driven Assembly of the RIP1-RIP3 Complex Regulates Programmed Necrosis and Virus-Induced Inflammation. Cell 137(6):1112-1123
    • (2009) Cell , vol.137 , Issue.6 , pp. 1112-1123
    • Cho, Y.1
  • 14
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α
    • 1:CAS:528:DC%2BD1MXps1eiu70%3D 19524512
    • He S et al (2009) Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α. Cell 137(6):1100-1111
    • (2009) Cell , vol.137 , Issue.6 , pp. 1100-1111
    • He, S.1
  • 15
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • 1:CAS:528:DC%2BD1MXos1Sqt7Y%3D 19498109
    • Zhang DW et al (2009) RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 325(5938):332-336
    • (2009) Science , vol.325 , Issue.5938 , pp. 332-336
    • Zhang, D.W.1
  • 16
    • 84856160569 scopus 로고    scopus 로고
    • Caspase 8 inhibits programmed necrosis by processing CYLD
    • 3229661 22037414 10.1038/ncb2362
    • O'Donnell MA et al (2011) Caspase 8 inhibits programmed necrosis by processing CYLD. Nat Cell Biol 13(12):1437-1442
    • (2011) Nat Cell Biol , vol.13 , Issue.12 , pp. 1437-1442
    • O'Donnell, M.A.1
  • 17
    • 84856759660 scopus 로고    scopus 로고
    • Many stimuli pull the necrotic trigger, an overview
    • 3252835 22075985 10.1038/cdd.2011.164
    • Vanlangenakker N, Vanden Berghe T, Vandenabeele P (2011) Many stimuli pull the necrotic trigger, an overview. Cell Death Differ 19(1):75-86
    • (2011) Cell Death Differ , vol.19 , Issue.1 , pp. 75-86
    • Vanlangenakker, N.1    Vanden Berghe, T.2    Vandenabeele, P.3
  • 18
    • 79960922705 scopus 로고    scopus 로고
    • CIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms
    • 1:CAS:528:DC%2BC3MXpvFSqtrY%3D 3163271 21737330
    • Feoktistova M et al (2011) cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol Cell 43(3):449-463
    • (2011) Mol Cell , vol.43 , Issue.3 , pp. 449-463
    • Feoktistova, M.1
  • 19
    • 79960921946 scopus 로고    scopus 로고
    • The ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs
    • 1:CAS:528:DC%2BC3MXpvFSqtrs%3D 21737329
    • Tenev T et al (2011) The ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol Cell 43(3):432-448
    • (2011) Mol Cell , vol.43 , Issue.3 , pp. 432-448
    • Tenev, T.1
  • 20
    • 0032871139 scopus 로고    scopus 로고
    • Modes of L929 cell death induced by TNF-alpha and other cytotoxic agents
    • 1:CAS:528:DyaK1MXms1Crtr4%3D 10525316
    • Humphreys DT, Wilson MR (1999) Modes of L929 cell death induced by TNF-alpha and other cytotoxic agents. Cytokine 11(10):773-782
    • (1999) Cytokine , vol.11 , Issue.10 , pp. 773-782
    • Humphreys, D.T.1    Wilson, M.R.2
  • 21
    • 0028951326 scopus 로고
    • Atypical apoptotic cell death induced in L929 targets by exposure to tumor necrosis factor
    • 1:CAS:528:DyaK2MXjsFeqsLY%3D 7648436
    • Fady C et al (1995) Atypical apoptotic cell death induced in L929 targets by exposure to tumor necrosis factor. J Interferon Cytokine Res 15(1):71-80
    • (1995) J Interferon Cytokine Res , vol.15 , Issue.1 , pp. 71-80
    • Fady, C.1
  • 22
    • 0030249771 scopus 로고    scopus 로고
    • Cytolytic processes induced by TNF in L929 and K562 differ in DNA fragmentation mechanisms
    • 1:CAS:528:DyaK28XlvFGhtb0%3D 8905404
    • Mirkina II et al (1996) Cytolytic processes induced by TNF in L929 and K562 differ in DNA fragmentation mechanisms. Immunol Lett 52(2-3):105-108
    • (1996) Immunol Lett , vol.52 , Issue.2-3 , pp. 105-108
    • Mirkina, I.I.1
  • 23
    • 76749126360 scopus 로고    scopus 로고
    • Selective unresponsiveness to the inhibition of p38 MAPK activation by cAMP helps L929 fibroblastoma cells escape TNF-alpha-induced cell death
    • 1:CAS:528:DC%2BC3cXktF2mtbo%3D 2818697 20070884
    • Wang J et al (2010) Selective unresponsiveness to the inhibition of p38 MAPK activation by cAMP helps L929 fibroblastoma cells escape TNF-alpha-induced cell death. Mol Cancer 9:6
    • (2010) Mol Cancer , vol.9 , pp. 6
    • Wang, J.1
  • 24
    • 0032494143 scopus 로고    scopus 로고
    • Dual signaling of the Fas receptor: Initiation of both apoptotic and necrotic cell death pathways
    • 1:CAS:528:DyaK1cXmtVagtLw%3D 2213397 9730893
    • Vercammen D et al (1998) Dual signaling of the Fas receptor: initiation of both apoptotic and necrotic cell death pathways. J Exp Med 188(5):919-930
    • (1998) J Exp Med , vol.188 , Issue.5 , pp. 919-930
    • Vercammen, D.1
  • 25
    • 0031282499 scopus 로고    scopus 로고
    • Tumour necrosis factor-induced necrosis versus anti-Fas-induced apoptosis in L929 cells
    • 1:CAS:528:DyaK2sXnslCjtro%3D 9367540
    • Vercammen D et al (1997) Tumour necrosis factor-induced necrosis versus anti-Fas-induced apoptosis in L929 cells. Cytokine 9(11):801-808
    • (1997) Cytokine , vol.9 , Issue.11 , pp. 801-808
    • Vercammen, D.1
  • 26
    • 0027858222 scopus 로고
    • Cell membrane permeabilization and cellular collapse, followed by loss of dehydrogenase activity: Early events in tumour necrosis factor-induced cytotoxicity
    • 1:CAS:528:DyaK2cXitFCqsb0%3D 8186366
    • Grooten J et al (1993) Cell membrane permeabilization and cellular collapse, followed by loss of dehydrogenase activity: early events in tumour necrosis factor-induced cytotoxicity. Cytokine 5(6):546-555
    • (1993) Cytokine , vol.5 , Issue.6 , pp. 546-555
    • Grooten, J.1
  • 27
    • 80051481307 scopus 로고    scopus 로고
    • RIP1-dependent and independent effects of necrostatin-1 in necrosis and T cell activation
    • 1:CAS:528:DC%2BC3MXhtFCjsLnI 3154273 21853090
    • Cho Y et al (2011) RIP1-dependent and independent effects of necrostatin-1 in necrosis and T cell activation. PLoS One 6(8):e23209
    • (2011) PLoS One , vol.6 , Issue.8 , pp. 23209
    • Cho, Y.1
  • 28
    • 81455149975 scopus 로고    scopus 로고
    • TNFalpha-induced necroptosis and autophagy via supression of the p38-NF-kappaB survival pathway in L929 cells
    • 1:CAS:528:DC%2BC3MXhsFygs7rP 22027097
    • Ye YC et al (2011) TNFalpha-induced necroptosis and autophagy via supression of the p38-NF-kappaB survival pathway in L929 cells. J Pharmacol Sci 117(3):160-169
    • (2011) J Pharmacol Sci , vol.117 , Issue.3 , pp. 160-169
    • Ye, Y.C.1
  • 29
    • 43949085388 scopus 로고    scopus 로고
    • Autophagy plays a protective role during zVAD-induced necrotic cell death
    • 1:CAS:528:DC%2BD1cXntFynur4%3D 18253089
    • Wu YT et al (2008) Autophagy plays a protective role during zVAD-induced necrotic cell death. Autophagy 4(4):457-466
    • (2008) Autophagy , vol.4 , Issue.4 , pp. 457-466
    • Wu, Y.T.1
  • 30
    • 0032482169 scopus 로고    scopus 로고
    • Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor
    • 1:CAS:528:DyaK1cXivVGjur8%3D 2212268 9565639
    • Vercammen D et al (1998) Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor. J Exp Med 187(9):1477-1485
    • (1998) J Exp Med , vol.187 , Issue.9 , pp. 1477-1485
    • Vercammen, D.1
  • 31
    • 78650175369 scopus 로고    scopus 로고
    • ZVAD-induced necroptosis in L929 cells depends on autocrine production of TNFα mediated by the PKC-MAPKs-AP-1 pathway
    • 1:CAS:528:DC%2BC3cXmvFKgtrY%3D 3131876 20539307
    • Wu YT et al (2010) zVAD-induced necroptosis in L929 cells depends on autocrine production of TNFα mediated by the PKC-MAPKs-AP-1 pathway. Cell Death Differ 18(1):26-37
    • (2010) Cell Death Differ , vol.18 , Issue.1 , pp. 26-37
    • Wu, Y.T.1
  • 32
    • 84897088275 scopus 로고    scopus 로고
    • Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis
    • 1:CAS:528:DC%2BC2cXktl2gs7g%3D 24557836
    • Newton K et al (2014) Activity of protein kinase RIPK3 determines whether cells die by necroptosis or apoptosis. Science 343(6177):1357-1360
    • (2014) Science , vol.343 , Issue.6177 , pp. 1357-1360
    • Newton, K.1
  • 33
    • 0034123026 scopus 로고    scopus 로고
    • Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: A potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release
    • 1:CAS:528:DC%2BD3cXktFCltLk%3D 10822279
    • Slee EA, Keogh SA, Martin SJ (2000) Cleavage of BID during cytotoxic drug and UV radiation-induced apoptosis occurs downstream of the point of Bcl-2 action and is catalysed by caspase-3: a potential feedback loop for amplification of apoptosis-associated mitochondrial cytochrome c release. Cell Death Differ 7(6):556-565
    • (2000) Cell Death Differ , vol.7 , Issue.6 , pp. 556-565
    • Slee, E.A.1    Keogh, S.A.2    Martin, S.J.3
  • 34
    • 0141953270 scopus 로고    scopus 로고
    • A JNK-dependent pathway is required for TNFalpha-induced apoptosis
    • 1:CAS:528:DC%2BD3sXotFSltLY%3D 14532003
    • Deng Y et al (2003) A JNK-dependent pathway is required for TNFalpha-induced apoptosis. Cell 115(1):61-70
    • (2003) Cell , vol.115 , Issue.1 , pp. 61-70
    • Deng, Y.1
  • 35
    • 0042525938 scopus 로고    scopus 로고
    • NF-kappaB inhibits TNF-induced accumulation of ROS that mediate prolonged MAPK activation and necrotic cell death
    • 1:CAS:528:DC%2BD3sXlsl2ks7k%3D 169052 12881424
    • Sakon S et al (2003) NF-kappaB inhibits TNF-induced accumulation of ROS that mediate prolonged MAPK activation and necrotic cell death. EMBO J 22(15):3898-3909
    • (2003) EMBO J , vol.22 , Issue.15 , pp. 3898-3909
    • Sakon, S.1
  • 36
    • 14844327760 scopus 로고    scopus 로고
    • Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases
    • 1:CAS:528:DC%2BD2MXis1yhsbg%3D 15766528
    • Kamata H et al (2005) Reactive oxygen species promote TNFα-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Cell 120(5):649-661
    • (2005) Cell , vol.120 , Issue.5 , pp. 649-661
    • Kamata, H.1
  • 37
    • 84855714255 scopus 로고    scopus 로고
    • BID regulates AIF-mediated caspase-independent necroptosis by promoting BAX activation
    • 3263500 21738214 10.1038/cdd.2011.91
    • Cabon L et al (2011) BID regulates AIF-mediated caspase-independent necroptosis by promoting BAX activation. Cell Death Differ 19(2):245-256
    • (2011) Cell Death Differ , vol.19 , Issue.2 , pp. 245-256
    • Cabon, L.1
  • 38
    • 49649123891 scopus 로고    scopus 로고
    • Cysteine cathepsins trigger caspase-dependent cell death through cleavage of bid and antiapoptotic Bcl-2 homologues
    • 1:CAS:528:DC%2BD1cXnvVSjs78%3D 18469004
    • Droga-Mazovec G et al (2008) Cysteine cathepsins trigger caspase-dependent cell death through cleavage of bid and antiapoptotic Bcl-2 homologues. J Biol Chem 283(27):19140-19150
    • (2008) J Biol Chem , vol.283 , Issue.27 , pp. 19140-19150
    • Droga-Mazovec, G.1
  • 39
    • 43749102922 scopus 로고    scopus 로고
    • Chymotrypsin B cached in rat liver lysosomes and involved in apoptotic regulation through a mitochondrial pathway
    • 1:CAS:528:DC%2BD1cXjsFCgsr0%3D 18211899
    • Miao Q et al (2008) Chymotrypsin B cached in rat liver lysosomes and involved in apoptotic regulation through a mitochondrial pathway. J Biol Chem 283(13):8218-8228
    • (2008) J Biol Chem , vol.283 , Issue.13 , pp. 8218-8228
    • Miao, Q.1
  • 40
    • 48849108199 scopus 로고    scopus 로고
    • The mitochondrial gateway to cell death
    • 1:CAS:528:DC%2BD1cXhtlKnu7vM 18425780
    • Smith DJ et al (2008) The mitochondrial gateway to cell death. IUBMB Life 60(6):383-389
    • (2008) IUBMB Life , vol.60 , Issue.6 , pp. 383-389
    • Smith, D.J.1
  • 41
    • 68949099606 scopus 로고    scopus 로고
    • Mitochondrial outer-membrane permeabilization and remodelling in apoptosis
    • 1:CAS:528:DC%2BD1MXhtVentbvF 19439192
    • Jourdain A, Martinou J-C (2009) Mitochondrial outer-membrane permeabilization and remodelling in apoptosis. Int J Biochem Cell Biol 41(10):1884-1889
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.10 , pp. 1884-1889
    • Jourdain, A.1    Martinou, J.-C.2
  • 42
    • 79551570336 scopus 로고    scopus 로고
    • ZVAD-induced autophagic cell death requires c-Src-dependent ERK and JNK activation and reactive oxygen species generation
    • 1:CAS:528:DC%2BC3MXivVSmu7c%3D 3039770 21127402
    • Chen SY et al (2011) zVAD-induced autophagic cell death requires c-Src-dependent ERK and JNK activation and reactive oxygen species generation. Autophagy 7(2):217-228
    • (2011) Autophagy , vol.7 , Issue.2 , pp. 217-228
    • Chen, S.Y.1
  • 43
    • 84868100171 scopus 로고    scopus 로고
    • Necrosis-like death can engage multiple pro-apoptotic Bcl-2 protein family members
    • 1:CAS:528:DC%2BC38XhsVOnsb7K 22971741
    • Tischner D et al (2012) Necrosis-like death can engage multiple pro-apoptotic Bcl-2 protein family members. Apoptosis 17(11):1197-1209
    • (2012) Apoptosis , vol.17 , Issue.11 , pp. 1197-1209
    • Tischner, D.1
  • 44
    • 33749551653 scopus 로고    scopus 로고
    • Loss of caspase-9 provides genetic evidence for the type I/II concept of CD95-mediated apoptosis
    • 1:CAS:528:DC%2BD28XhtVahsb7I 16895904
    • Samraj AK et al (2006) Loss of caspase-9 provides genetic evidence for the type I/II concept of CD95-mediated apoptosis. J Biol Chem 281(40):29652-29659
    • (2006) J Biol Chem , vol.281 , Issue.40 , pp. 29652-29659
    • Samraj, A.K.1
  • 45
    • 84857207839 scopus 로고    scopus 로고
    • Pick your poison: The Ripoptosome, a cell death platform regulating apoptosis and necroptosis
    • 1:CAS:528:DC%2BC38Xjs1Krt7w%3D 22274400
    • Feoktistova M et al (2012) Pick your poison: the Ripoptosome, a cell death platform regulating apoptosis and necroptosis. Cell Cycle 11(3):460-467
    • (2012) Cell Cycle , vol.11 , Issue.3 , pp. 460-467
    • Feoktistova, M.1
  • 46
    • 84868236208 scopus 로고    scopus 로고
    • RIP1-mediated mitochondrial dysfunction and ROS production contributed to tumor necrosis factor alpha-induced L929 cell necroptosis and autophagy
    • Ye YC et al (2012) RIP1-mediated mitochondrial dysfunction and ROS production contributed to tumor necrosis factor alpha-induced L929 cell necroptosis and autophagy. Int Immunopharmacol 14(4):674-682
    • (2012) Int Immunopharmacol , vol.14 , Issue.4 , pp. 674-682
    • Ye, Y.C.1
  • 47
    • 78650361485 scopus 로고    scopus 로고
    • Bid stands at the crossroad of stress-response pathways
    • 1:CAS:528:DC%2BC3cXhtFSktLfF 20482490
    • Song G et al (2010) Bid stands at the crossroad of stress-response pathways. Curr Cancer Drug Targets 10(6):584-592
    • (2010) Curr Cancer Drug Targets , vol.10 , Issue.6 , pp. 584-592
    • Song, G.1
  • 48
    • 21244502158 scopus 로고    scopus 로고
    • Caspase-10 triggers Bid cleavage and caspase cascade activation in FasL-induced apoptosis
    • 1:CAS:528:DC%2BD2MXktFyls7c%3D 15772077
    • Milhas D et al (2005) Caspase-10 triggers Bid cleavage and caspase cascade activation in FasL-induced apoptosis. J Biol Chem 280(20):19836-19842
    • (2005) J Biol Chem , vol.280 , Issue.20 , pp. 19836-19842
    • Milhas, D.1
  • 49
    • 44949233264 scopus 로고    scopus 로고
    • Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress
    • 1:CAS:528:DC%2BD1cXntFanurg%3D 2423129 18426910
    • Upton JP et al (2008) Caspase-2 cleavage of BID is a critical apoptotic signal downstream of endoplasmic reticulum stress. Mol Cell Biol 28(12):3943-3951
    • (2008) Mol Cell Biol , vol.28 , Issue.12 , pp. 3943-3951
    • Upton, J.P.1
  • 50
    • 4544274785 scopus 로고    scopus 로고
    • Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway
    • 1:CAS:528:DC%2BD2cXmvFemt7w%3D 15173176
    • Wagner KW, Engels IH, Deveraux QL (2004) Caspase-2 can function upstream of bid cleavage in the TRAIL apoptosis pathway. J Biol Chem 279(33):35047-35052
    • (2004) J Biol Chem , vol.279 , Issue.33 , pp. 35047-35052
    • Wagner, K.W.1    Engels, I.H.2    Deveraux, Q.L.3
  • 51
    • 22344435528 scopus 로고    scopus 로고
    • Bid is upstream of lysosome-mediated caspase 2 activation in tumor necrosis factor alpha-induced hepatocyte apoptosis
    • 1:CAS:528:DC%2BD2MXntVGrsbY%3D 16012953
    • Guicciardi ME et al (2005) Bid is upstream of lysosome-mediated caspase 2 activation in tumor necrosis factor alpha-induced hepatocyte apoptosis. Gastroenterology 129(1):269-284
    • (2005) Gastroenterology , vol.129 , Issue.1 , pp. 269-284
    • Guicciardi, M.E.1
  • 52
    • 0036236471 scopus 로고    scopus 로고
    • Calpain-mediated Bid cleavage and calpain-independent Bak modulation: Two separate pathways in cisplatin-induced apoptosis
    • 1:CAS:528:DC%2BD38XivFylsbo%3D 133754 11940658
    • Mandic A et al (2002) Calpain-mediated Bid cleavage and calpain-independent Bak modulation: two separate pathways in cisplatin-induced apoptosis. Mol Cell Biol 22(9):3003-3013
    • (2002) Mol Cell Biol , vol.22 , Issue.9 , pp. 3003-3013
    • Mandic, A.1
  • 53
    • 0034694091 scopus 로고    scopus 로고
    • Initiation of apoptosis by granzyme B requires direct cleavage of bid, but not direct granzyme B-mediated caspase activation
    • 1:CAS:528:DC%2BD3cXotlaisr0%3D 2193191 11085743
    • Sutton VR et al (2000) Initiation of apoptosis by granzyme B requires direct cleavage of bid, but not direct granzyme B-mediated caspase activation. J Exp Med 192(10):1403-1414
    • (2000) J Exp Med , vol.192 , Issue.10 , pp. 1403-1414
    • Sutton, V.R.1
  • 54
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route
    • 1:CAS:528:DC%2BD3MXhtFWjtbs%3D 11073962
    • Stoka V et al (2001) Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J Biol Chem 276(5):3149-3157
    • (2001) J Biol Chem , vol.276 , Issue.5 , pp. 3149-3157
    • Stoka, V.1
  • 55
    • 33644657517 scopus 로고    scopus 로고
    • Bid, a BH3-only multi-functional molecule, is at the cross road of life and death
    • 1:CAS:528:DC%2BD28XhvF2nurs%3D 16446060
    • Yin XM (2006) Bid, a BH3-only multi-functional molecule, is at the cross road of life and death. Gene 369:7-19
    • (2006) Gene , vol.369 , pp. 7-19
    • Yin, X.M.1
  • 56
    • 33645001095 scopus 로고    scopus 로고
    • Butylated hydroxyanisole is more than a reactive oxygen species scavenger
    • Festjens N et al (2005) Butylated hydroxyanisole is more than a reactive oxygen species scavenger. Cell Death Differ 13(1):166-169
    • (2005) Cell Death Differ , vol.13 , Issue.1 , pp. 166-169
    • Festjens, N.1
  • 57
    • 0035890085 scopus 로고    scopus 로고
    • The expanding role of mitochondria in apoptosis
    • 1:CAS:528:DC%2BD3MXovVOrtbs%3D 11711427
    • Wang X (2001) The expanding role of mitochondria in apoptosis. Genes Dev 15(22):2922-2933
    • (2001) Genes Dev , vol.15 , Issue.22 , pp. 2922-2933
    • Wang, X.1
  • 58
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • 1:CAS:528:DC%2BC3MXms1SisLg%3D 3103342 21454557
    • Yoshii SR et al (2011) Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J Biol Chem 286(22):19630-19640
    • (2011) J Biol Chem , vol.286 , Issue.22 , pp. 19630-19640
    • Yoshii, S.R.1
  • 59
    • 75949130828 scopus 로고    scopus 로고
    • PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1
    • 1:CAS:528:DC%2BC3cXhtlCqtbs%3D 20098416
    • Geisler S et al (2010) PINK1/Parkin-mediated mitophagy is dependent on VDAC1 and p62/SQSTM1. Nat Cell Biol 12(2):119-131
    • (2010) Nat Cell Biol , vol.12 , Issue.2 , pp. 119-131
    • Geisler, S.1
  • 60
    • 84860180832 scopus 로고    scopus 로고
    • Bax regulates primary necrosis through mitochondrial dynamics
    • 1:CAS:528:DC%2BC38Xmslyjtbo%3D 3340068 22493254
    • Whelan RS et al (2012) Bax regulates primary necrosis through mitochondrial dynamics. Proc Natl Acad Sci USA 109(17):6566-6571
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.17 , pp. 6566-6571
    • Whelan, R.S.1
  • 61
    • 78651468702 scopus 로고    scopus 로고
    • The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes
    • 1:CAS:528:DC%2BC3MXhtVWqtbg%3D 3072068 21255726
    • Hoppins S et al (2011) The soluble form of Bax regulates mitochondrial fusion via MFN2 homotypic complexes. Mol Cell 41(2):150-160
    • (2011) Mol Cell , vol.41 , Issue.2 , pp. 150-160
    • Hoppins, S.1
  • 62
    • 78649679754 scopus 로고    scopus 로고
    • Bax is essential for Drp1-mediated mitochondrial fission but not for mitochondrial outer membrane permeabilization caused by photodynamic therapy
    • 1:CAS:528:DC%2BC3cXhsVOkt7nL 20683914
    • Wu S et al (2011) Bax is essential for Drp1-mediated mitochondrial fission but not for mitochondrial outer membrane permeabilization caused by photodynamic therapy. J Cell Physiol 226(2):530-541
    • (2011) J Cell Physiol , vol.226 , Issue.2 , pp. 530-541
    • Wu, S.1
  • 63
    • 49349105966 scopus 로고    scopus 로고
    • Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome C release
    • 1:CAS:528:DC%2BD1cXhtVyksbnN 18722181
    • Sheridan C et al (2008) Bax- or Bak-induced mitochondrial fission can be uncoupled from cytochrome C release. Mol Cell 31(4):570-585
    • (2008) Mol Cell , vol.31 , Issue.4 , pp. 570-585
    • Sheridan, C.1
  • 64
    • 0037164813 scopus 로고    scopus 로고
    • Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis
    • 1:CAS:528:DC%2BD3sXjt1ai 2173996 12499352
    • Karbowski M et al (2002) Spatial and temporal association of Bax with mitochondrial fission sites, Drp1, and Mfn2 during apoptosis. J Cell Biol 159(6):931-938
    • (2002) J Cell Biol , vol.159 , Issue.6 , pp. 931-938
    • Karbowski, M.1
  • 65
    • 28444487509 scopus 로고    scopus 로고
    • Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death
    • 1:CAS:528:DC%2BD2MXhtlSiurfL 16332536
    • Arnoult D et al (2005) Bax/Bak-dependent release of DDP/TIMM8a promotes Drp1-mediated mitochondrial fission and mitoptosis during programmed cell death. Curr Biol 15(23):2112-2118
    • (2005) Curr Biol , vol.15 , Issue.23 , pp. 2112-2118
    • Arnoult, D.1
  • 66
    • 46349099816 scopus 로고    scopus 로고
    • Novel mechanism of elimination of malfunctioning mitochondria (mitoptosis): Formation of mitoptotic bodies and extrusion of mitochondrial material from the cell
    • 1:CAS:528:DC%2BD1cXnsFCmtLw%3D 18433711
    • Lyamzaev KG et al (2008) Novel mechanism of elimination of malfunctioning mitochondria (mitoptosis): formation of mitoptotic bodies and extrusion of mitochondrial material from the cell. Biochim Biophys Acta 1777(7-8):817-825
    • (2008) Biochim Biophys Acta , vol.1777 , Issue.7-8 , pp. 817-825
    • Lyamzaev, K.G.1


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