메뉴 건너뛰기




Volumn 116, Issue 11, 2015, Pages 1800-1809

Regulated necrotic cell death: The passive aggressive side of bax and bak

Author keywords

apoptosis; calcium; mitochondria; necrosis

Indexed keywords

ADENOSINE TRIPHOSPHATE; CASPASE; MITOCHONDRIAL PERMEABILITY TRANSITION PORE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NUCLEASE; PROTEIN BAK; PROTEIN BAX; REACTIVE OXYGEN METABOLITE; BAK1 PROTEIN, HUMAN; BAX PROTEIN, HUMAN; CARRIER PROTEIN; MITOCHONDRIAL PROTEIN;

EID: 84936815629     PISSN: 00097330     EISSN: 15244571     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.116.305421     Document Type: Review
Times cited : (130)

References (105)
  • 1
    • 0030031099 scopus 로고    scopus 로고
    • Nineteenth century research on naturally occurring cell death and related phenomena
    • Clarke PG, Clarke S., Nineteenth century research on naturally occurring cell death and related phenomena. Anat Embryol (Berl) 1996; 193: 81-99.
    • (1996) Anat Embryol (Berl) , vol.193 , pp. 81-99
    • Clarke, P.G.1    Clarke, S.2
  • 2
    • 0028891783 scopus 로고
    • Apoptosis, oncosis, and necrosis. An overview of cell death
    • Majno G, Joris I., Apoptosis, oncosis, and necrosis. An overview of cell death. Am J Pathol 1995; 146: 3-15.
    • (1995) Am J Pathol , vol.146 , pp. 3-15
    • Majno, G.1    Joris, I.2
  • 3
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR., Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972; 26: 239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 4
    • 0020557883 scopus 로고
    • Mutations affecting programmed cell deaths in The nematode Caenorhabditis elegans
    • Hedgecock EM, Sulston JE, Thomson JN., Mutations affecting programmed cell deaths in The nematode Caenorhabditis elegans. Science 1983; 220: 1277-1279.
    • (1983) Science , vol.220 , pp. 1277-1279
    • Hedgecock, E.M.1    Sulston, J.E.2    Thomson, J.N.3
  • 5
    • 0017618537 scopus 로고
    • Post-embryonic cell lineages of The nematode, Caenorhabditis elegans
    • Sulston JE, Horvitz HR., Post-embryonic cell lineages of The nematode, Caenorhabditis elegans. Dev Biol 1977; 56: 110-156.
    • (1977) Dev Biol , vol.56 , pp. 110-156
    • Sulston, J.E.1    Horvitz, H.R.2
  • 6
    • 0022546957 scopus 로고
    • Analysis of The structure, transcripts, and protein products of bcl-2, The gene involved in human follicular lymphoma
    • Tsujimoto Y, Croce CM., Analysis of The structure, transcripts, and protein products of bcl-2, The gene involved in human follicular lymphoma. Proc Natl Acad Sci U S A 1986; 83: 5214-5218.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 5214-5218
    • Tsujimoto, Y.1    Croce, C.M.2
  • 7
    • 0027050145 scopus 로고
    • Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2
    • Vaux DL, Weissman IL, Kim SK., Prevention of programmed cell death in Caenorhabditis elegans by human bcl-2. Science 1992; 258: 1955-1957.
    • (1992) Science , vol.258 , pp. 1955-1957
    • Vaux, D.L.1    Weissman, I.L.2    Kim, S.K.3
  • 9
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Oltvai ZN, Milliman CL, Korsmeyer SJ., Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. Cell 1993; 74: 609-619.
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 11
    • 0027449187 scopus 로고
    • Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of The C. Elegans cell death gene ced-3
    • Miura M, Zhu H, Rotello R, Hartwieg EA, Yuan J., Induction of apoptosis in fibroblasts by IL-1 beta-converting enzyme, a mammalian homolog of The C. Elegans cell death gene ced-3. Cell 1993; 75: 653-660.
    • (1993) Cell , vol.75 , pp. 653-660
    • Miura, M.1    Zhu, H.2    Rotello, R.3    Hartwieg, E.A.4    Yuan, J.5
  • 12
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen G., Caspases: The executioners of apoptosis. Biochem J 1997; 326: 1-16.
    • (1997) Biochem J , vol.326 , pp. 1-16
    • Cohen, G.1
  • 13
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X, Kim CN, Yang J, Jemmerson R, Wang X., Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 1996; 86: 147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 14
    • 0025204548 scopus 로고
    • Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
    • Hockenbery D, Nuñez G, Milliman C, Schreiber RD, Korsmeyer SJ., Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 1990; 348: 334-336. doi: 10.1038/348334a0.
    • (1990) Nature , vol.348 , pp. 334-336
    • Hockenbery, D.1    Nuñez, G.2    Milliman, C.3    Schreiber, R.D.4    Korsmeyer, S.J.5
  • 15
    • 0028809209 scopus 로고
    • Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death
    • Yang E, Zha J, Jockel J, Boise LH, Thompson CB, Korsmeyer SJ., Bad, a heterodimeric partner for Bcl-XL and Bcl-2, displaces Bax and promotes cell death. Cell 1995; 80: 285-291.
    • (1995) Cell , vol.80 , pp. 285-291
    • Yang, E.1    Zha, J.2    Jockel, J.3    Boise, L.H.4    Thompson, C.B.5    Korsmeyer, S.J.6
  • 16
    • 0029990550 scopus 로고    scopus 로고
    • Immunohistochemical analysis of in vivo patterns of Bak expression, a proapoptotic member of The Bcl-2 protein family
    • Krajewski S, Krajewska M, Reed JC., Immunohistochemical analysis of in vivo patterns of Bak expression, a proapoptotic member of The Bcl-2 protein family. Cancer Res 1996; 56: 2849-2855.
    • (1996) Cancer Res , vol.56 , pp. 2849-2855
    • Krajewski, S.1    Krajewska, M.2    Reed, J.C.3
  • 17
    • 0031953601 scopus 로고    scopus 로고
    • Calcium in ischemic cell death
    • Kristián T, Siesjö BK., Calcium in ischemic cell death. Stroke 1998; 29: 705-718.
    • (1998) Stroke , vol.29 , pp. 705-718
    • Kristián, T.1    Siesjö, B.K.2
  • 18
    • 0017706049 scopus 로고
    • Myocardial contracture and accumulation of mitochondrial calcium in ischemic rabbit heart
    • Henry PD, Schuchleib R, Davis J, Weiss ES, Sobel BE., Myocardial contracture and accumulation of mitochondrial calcium in ischemic rabbit heart. Am J Physiol 1977 233 H677 H684
    • (1977) Am J Physiol , vol.233 , pp. H677-H684
    • Henry, P.D.1    Schuchleib, R.2    Davis, J.3    Weiss, E.S.4    Sobel, B.E.5
  • 19
    • 84960993949 scopus 로고
    • Swelling of isolated mitochondria of The liver and their susceptibility to physicochemical influences
    • Raaflaub J., Swelling of isolated mitochondria of The liver and their susceptibility to physicochemical influences. Helv Physiol Pharmacol Acta 1953; 11: 142-156.
    • (1953) Helv Physiol Pharmacol Acta , vol.11 , pp. 142-156
    • Raaflaub, J.1
  • 20
    • 0343123179 scopus 로고
    • Inactivation of oxidative and phosphorylative systems in mitochondria by preincubation with phosphate and other ions
    • Hunter FE Jr, Ford L., Inactivation of oxidative and phosphorylative systems in mitochondria by preincubation with phosphate and other ions. J Biol Chem 1955; 216: 357-369.
    • (1955) J Biol Chem , vol.216 , pp. 357-369
    • Hunter, F.E.1    Ford, L.2
  • 21
    • 1642610686 scopus 로고
    • The effect of thyroxine and other substances on The swelling of isolated rat liver mitochondria
    • Tapley DF., The effect of thyroxine and other substances on The swelling of isolated rat liver mitochondria. J Biol Chem 1956; 222: 325-339.
    • (1956) J Biol Chem , vol.222 , pp. 325-339
    • Tapley, D.F.1
  • 22
    • 0018865922 scopus 로고
    • Improvement of mitochondrial energy production in ischemic myocardium by in vivo infusion of ruthenium red
    • Peng CF, Kane JJ, Straub KD, Murphy ML., Improvement of mitochondrial energy production in ischemic myocardium by in vivo infusion of ruthenium red. J Cardiovasc Pharmacol 1980; 2: 45-54.
    • (1980) J Cardiovasc Pharmacol , vol.2 , pp. 45-54
    • Peng, C.F.1    Kane, J.J.2    Straub, K.D.3    Murphy, M.L.4
  • 23
    • 0023263612 scopus 로고
    • Action of cyclosporine on mitochondrial calcium fluxes
    • Fournier N, Ducet G, Crevat A., Action of cyclosporine on mitochondrial calcium fluxes. J Bioenerg Biomembr 1987; 19: 297-303.
    • (1987) J Bioenerg Biomembr , vol.19 , pp. 297-303
    • Fournier, N.1    Ducet, G.2    Crevat, A.3
  • 24
    • 0023821864 scopus 로고
    • Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress
    • Crompton M, Ellinger H, Costi A., Inhibition by cyclosporin A of a Ca2+-dependent pore in heart mitochondria activated by inorganic phosphate and oxidative stress. Biochem J 1988; 255: 357-360.
    • (1988) Biochem J , vol.255 , pp. 357-360
    • Crompton, M.1    Ellinger, H.2    Costi, A.3
  • 25
    • 0024360271 scopus 로고
    • Cyclosporin A is a potent inhibitor of The inner membrane permeability transition in liver mitochondria
    • Broekemeier KM, Dempsey ME, Pfeiffer DR., Cyclosporin A is a potent inhibitor of The inner membrane permeability transition in liver mitochondria. J Biol Chem 1989; 264: 7826-7830.
    • (1989) J Biol Chem , vol.264 , pp. 7826-7830
    • Broekemeier, K.M.1    Dempsey, M.E.2    Pfeiffer, D.R.3
  • 27
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with The permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M, Shimizu S, Ito T, Chittenden T, Lutz RJ, Matsuda H, Tsujimoto Y., Bax interacts with The permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci U S A 1998; 95: 14681-14686.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 29
    • 0032571294 scopus 로고    scopus 로고
    • The overexpression of Bax produces cell death upon induction of The mitochondrial permeability transition
    • Pastorino JG, Chen ST, Tafani M, Snyder JW, Farber JL., The overexpression of Bax produces cell death upon induction of The mitochondrial permeability transition. J Biol Chem 1998; 273: 7770-7775.
    • (1998) J Biol Chem , vol.273 , pp. 7770-7775
    • Pastorino, J.G.1    Chen, S.T.2    Tafani, M.3    Snyder, J.W.4    Farber, J.L.5
  • 31
    • 84904608695 scopus 로고    scopus 로고
    • Identifying The components of The elusive mitochondrial permeability transition pore
    • Karch J, Molkentin JD., Identifying The components of The elusive mitochondrial permeability transition pore. Proc Natl Acad Sci U S A 2014; 111: 10396-10397. doi: 10.1073/pnas.1410104111.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 10396-10397
    • Karch, J.1    Molkentin, J.D.2
  • 32
    • 33749178260 scopus 로고    scopus 로고
    • Necrosis, a well-orchestrated form of cell demise: Signalling cascades, important mediators and concomitant immune response
    • Festjens N, Vanden Berghe T, Vandenabeele P., Necrosis, a well-orchestrated form of cell demise: signalling cascades, important mediators and concomitant immune response. Biochim Biophys Acta 2006; 1757: 1371-1387. doi: 10.1016/j.bbabio.2006.06.014.
    • (2006) Biochim Biophys Acta , vol.1757 , pp. 1371-1387
    • Festjens, N.1    Vanden Berghe, T.2    Vandenabeele, P.3
  • 33
    • 33646389796 scopus 로고    scopus 로고
    • Bioenergetic aspects of apoptosis, necrosis and mitoptosis
    • Skulachev VP., Bioenergetic aspects of apoptosis, necrosis and mitoptosis. Apoptosis 2006; 11: 473-485. doi: 10.1007/s10495-006-5881-9.
    • (2006) Apoptosis , vol.11 , pp. 473-485
    • Skulachev, V.P.1
  • 34
    • 0026336737 scopus 로고
    • Inhibition of anoxia-induced injury in heart myocytes by cyclosporin A
    • Nazareth W, Yafei N, Crompton M., Inhibition of anoxia-induced injury in heart myocytes by cyclosporin A. J Mol Cell Cardiol 1991; 23: 1351-1354.
    • (1991) J Mol Cell Cardiol , vol.23 , pp. 1351-1354
    • Nazareth, W.1    Yafei, N.2    Crompton, M.3
  • 35
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M., The mitochondrial permeability transition pore and its role in cell death. Biochem J 1999 341 Pt 2 233 249
    • (1999) Biochem J , vol.341 , Issue.PT 2 , pp. 233-249
    • Crompton, M.1
  • 36
    • 33745950626 scopus 로고    scopus 로고
    • Mitochondrial outer membrane permeabilization during apoptosis: The innocent bystander scenario
    • Chipuk JE, Bouchier-Hayes L, Green DR., Mitochondrial outer membrane permeabilization during apoptosis: The innocent bystander scenario. Cell Death Differ 2006; 13: 1396-1402. doi: 10.1038/sj.cdd.4401963.
    • (2006) Cell Death Differ , vol.13 , pp. 1396-1402
    • Chipuk, J.E.1    Bouchier-Hayes, L.2    Green, D.R.3
  • 40
    • 0036716281 scopus 로고    scopus 로고
    • The Bcl2 family: Regulators of The cellular life-or-death switch
    • Cory S, Adams JM., The Bcl2 family: regulators of The cellular life-or-death switch. Nat Rev Cancer 2002; 2: 647-656. doi: 10.1038/nrc883.
    • (2002) Nat Rev Cancer , vol.2 , pp. 647-656
    • Cory, S.1    Adams, J.M.2
  • 43
    • 37549048249 scopus 로고    scopus 로고
    • The BCL-2 protein family: Opposing activities that mediate cell death
    • Youle RJ, Strasser A., The BCL-2 protein family: opposing activities that mediate cell death. Nat Rev Mol Cell Biol 2008; 9: 47-59. doi: 10.1038/nrm2308.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 47-59
    • Youle, R.J.1    Strasser, A.2
  • 44
    • 70350025502 scopus 로고    scopus 로고
    • Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis
    • Dewson G, Kluck RM., Mechanisms by which Bak and Bax permeabilise mitochondria during apoptosis. J Cell Sci 2009; 122: 2801-2808.
    • (2009) J Cell Sci , vol.122 , pp. 2801-2808
    • Dewson, G.1    Kluck, R.M.2
  • 46
    • 0032481346 scopus 로고    scopus 로고
    • The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4
    • Huang DC, Adams JM, Cory S., The conserved N-terminal BH4 domain of Bcl-2 homologues is essential for inhibition of apoptosis and interaction with CED-4. EMBO J 1998; 17: 1029-1039. doi: 10.1093/emboj/17.4.1029.
    • (1998) EMBO J , vol.17 , pp. 1029-1039
    • Huang, D.C.1    Adams, J.M.2    Cory, S.3
  • 47
    • 0034724190 scopus 로고    scopus 로고
    • BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death
    • Shimizu S, Konishi A, Kodama T, Tsujimoto Y., BH4 domain of antiapoptotic Bcl-2 family members closes voltage-dependent anion channel and inhibits apoptotic mitochondrial changes and cell death. Proc Natl Acad Sci U S A 2000; 97: 3100-3105.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 3100-3105
    • Shimizu, S.1    Konishi, A.2    Kodama, T.3    Tsujimoto, Y.4
  • 48
    • 0029917541 scopus 로고    scopus 로고
    • Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2
    • Zha H, Aimé-Sempé C, Sato T, Reed JC., Proapoptotic protein Bax heterodimerizes with Bcl-2 and homodimerizes with Bax via a novel domain (BH3) distinct from BH1 and BH2. J Biol Chem 1996; 271: 7440-7444.
    • (1996) J Biol Chem , vol.271 , pp. 7440-7444
    • Zha, H.1    Aimé-Sempé, C.2    Sato, T.3    Reed, J.C.4
  • 49
    • 0033981577 scopus 로고    scopus 로고
    • Bid induces The oligomerization and insertion of Bax into The outer mitochondrial membrane
    • Eskes R, Desagher S, Antonsson B, Martinou JC., Bid induces The oligomerization and insertion of Bax into The outer mitochondrial membrane. Mol Cell Biol 2000; 20: 929-935.
    • (2000) Mol Cell Biol , vol.20 , pp. 929-935
    • Eskes, R.1    Desagher, S.2    Antonsson, B.3    Martinou, J.C.4
  • 50
    • 0042090307 scopus 로고    scopus 로고
    • BCL-2 selectively interacts with The BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization
    • Ruffolo SC, Shore GC., BCL-2 selectively interacts with The BID-induced open conformer of BAK, inhibiting BAK auto-oligomerization. J Biol Chem 2003; 278: 25039-25045. doi: 10.1074/jbc.M302930200.
    • (2003) J Biol Chem , vol.278 , pp. 25039-25045
    • Ruffolo, S.C.1    Shore, G.C.2
  • 52
    • 67349117275 scopus 로고    scopus 로고
    • What is The mitochondrial permeability transition pore?
    • Halestrap AP., What is The mitochondrial permeability transition pore? J Mol Cell Cardiol 2009; 46: 821-831. doi: 10.1016/j.yjmcc.2009.02.021.
    • (2009) J Mol Cell Cardiol , vol.46 , pp. 821-831
    • Halestrap, A.P.1
  • 55
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa T, Shimizu S, Watanabe T, Yamaguchi O, Otsu K, Yamagata H, Inohara H, Kubo T, Tsujimoto Y., Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature 2005; 434: 652-658. doi: 10.1038/nature03317.
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1    Shimizu, S.2    Watanabe, T.3    Yamaguchi, O.4    Otsu, K.5    Yamagata, H.6    Inohara, H.7    Kubo, T.8    Tsujimoto, Y.9
  • 57
    • 78651285839 scopus 로고    scopus 로고
    • Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury
    • Ramachandran A, Lebofsky M, Baines CP, Lemasters JJ, Jaeschke H., Cyclophilin D deficiency protects against acetaminophen-induced oxidant stress and liver injury. Free Radic Res 2011; 45: 156-164. doi: 10.3109/10715762.2010.520319.
    • (2011) Free Radic Res , vol.45 , pp. 156-164
    • Ramachandran, A.1    Lebofsky, M.2    Baines, C.P.3    Lemasters, J.J.4    Jaeschke, H.5
  • 58
    • 77449106556 scopus 로고    scopus 로고
    • RIP kinases initiate programmed necrosis
    • Galluzzi L, Kepp O, Kroemer G., RIP kinases initiate programmed necrosis. J Mol Cell Biol 2009; 1: 8-10. doi: 10.1093/jmcb/mjp007.
    • (2009) J Mol Cell Biol , vol.1 , pp. 8-10
    • Galluzzi, L.1    Kepp, O.2    Kroemer, G.3
  • 59
    • 2642536197 scopus 로고    scopus 로고
    • Alkylating DNA damage stimulates a regulated form of necrotic cell death
    • Zong WX, Ditsworth D, Bauer DE, Wang ZQ, Thompson CB., Alkylating DNA damage stimulates a regulated form of necrotic cell death. Genes Dev 2004; 18: 1272-1282. doi: 10.1101/gad.1199904.
    • (2004) Genes Dev , vol.18 , pp. 1272-1282
    • Zong, W.X.1    Ditsworth, D.2    Bauer, D.E.3    Wang, Z.Q.4    Thompson, C.B.5
  • 61
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death
    • Baines CP, Kaiser RA, Sheiko T, Craigen WJ, Molkentin JD., Voltage-dependent anion channels are dispensable for mitochondrial-dependent cell death. Nat Cell Biol 2007; 9: 550-555. doi: 10.1038/ncb1575.
    • (2007) Nat Cell Biol , vol.9 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 67
    • 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. doi: 10.1038/20959.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 68
    • 0034618269 scopus 로고    scopus 로고
    • Bax and Bcl-xL independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator
    • Shimizu S, Shinohara Y, Tsujimoto Y., Bax and Bcl-xL independently regulate apoptotic changes of yeast mitochondria that require VDAC but not adenine nucleotide translocator. Oncogene 2000; 19: 4309-4318. doi: 10.1038/sj.onc.1203788.
    • (2000) Oncogene , vol.19 , pp. 4309-4318
    • Shimizu, S.1    Shinohara, Y.2    Tsujimoto, Y.3
  • 69
    • 21444443226 scopus 로고    scopus 로고
    • Bax-dependent regulation of Bak by voltage-dependent anion channel 2
    • Chandra D, Choy G, Daniel PT, Tang DG., Bax-dependent regulation of Bak by voltage-dependent anion channel 2. J Biol Chem 2005; 280: 19051-19061. doi: 10.1074/jbc.M501391200.
    • (2005) J Biol Chem , vol.280 , pp. 19051-19061
    • Chandra, D.1    Choy, G.2    Daniel, P.T.3    Tang, D.G.4
  • 74
    • 4444283704 scopus 로고    scopus 로고
    • Bax does not directly participate in The Ca(2+)-induced permeability transition of isolated mitochondria
    • De Marchi U, Campello S, Szabò I, Tombola F, Martinou JC, Zoratti M., Bax does not directly participate in The Ca(2+)-induced permeability transition of isolated mitochondria. J Biol Chem 2004; 279: 37415-37422. doi: 10.1074/jbc.M314093200.
    • (2004) J Biol Chem , vol.279 , pp. 37415-37422
    • De Marchi, U.1    Campello, S.2    Szabò, I.3    Tombola, F.4    Martinou, J.C.5    Zoratti, M.6
  • 76
    • 80455129100 scopus 로고    scopus 로고
    • Bax forms two types of channels, one of which is voltage-gated
    • Lin SH, Perera MN, Nguyen T, Datskovskiy D, Miles M, Colombini M., Bax forms two types of channels, one of which is voltage-gated. Biophys J 2011; 101: 2163-2169. doi: 10.1016/j.bpj.2011.09.041.
    • (2011) Biophys J , vol.101 , pp. 2163-2169
    • Lin, S.H.1    Perera, M.N.2    Nguyen, T.3    Datskovskiy, D.4    Miles, M.5    Colombini, M.6
  • 78
    • 0032143986 scopus 로고    scopus 로고
    • Targeted disruption of The mouse caspase 8 gene ablates cell death induction by The TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally
    • Varfolomeev EE, Schuchmann M, Luria V, Targeted disruption of The mouse caspase 8 gene ablates cell death induction by The TNF receptors, Fas/Apo1, and DR3 and is lethal prenatally. Immunity 1998; 9: 267-276.
    • (1998) Immunity , vol.9 , pp. 267-276
    • Varfolomeev, E.E.1    Schuchmann, M.2    Luria, V.3
  • 81
    • 66449133280 scopus 로고    scopus 로고
    • Phosphorylation-driven assembly of The RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation
    • Cho YS, Challa S, Moquin D, Genga R, Ray TD, Guildford M, Chan FK., Phosphorylation-driven assembly of The RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 2009; 137: 1112-1123. doi: 10.1016/j.cell.2009.05.037.
    • (2009) Cell , vol.137 , pp. 1112-1123
    • Cho, Y.S.1    Challa, S.2    Moquin, D.3    Genga, R.4    Ray, T.D.5    Guildford, M.6    Chan, F.K.7
  • 82
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • He S, Wang L, Miao L, Wang T, Du F, Zhao L, Wang X., Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 2009; 137: 1100-1111. doi: 10.1016/j.cell.2009.05.021.
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1    Wang, L.2    Miao, L.3    Wang, T.4    Du, F.5    Zhao, L.6    Wang, X.7
  • 85
    • 36849056027 scopus 로고    scopus 로고
    • The cardioprotective effect of necrostatin requires The cyclophilin-D component of The mitochondrial permeability transition pore
    • Lim SY, Davidson SM, Mocanu MM, Yellon DM, Smith CC., The cardioprotective effect of necrostatin requires The cyclophilin-D component of The mitochondrial permeability transition pore. Cardiovasc Drugs Ther 2007; 21: 467-469. doi: 10.1007/s10557-007-6067-6.
    • (2007) Cardiovasc Drugs Ther , vol.21 , pp. 467-469
    • Lim, S.Y.1    Davidson, S.M.2    Mocanu, M.M.3    Yellon, D.M.4    Smith, C.C.5
  • 86
    • 77952059124 scopus 로고    scopus 로고
    • Necroptosis, a novel form of caspase-independent cell death, contributes to neuronal damage in a retinal ischemia-reperfusion injury model
    • Rosenbaum DM, Degterev A, David J, Rosenbaum PS, Roth S, Grotta JC, Cuny GD, Yuan J, Savitz SI., Necroptosis, a novel form of caspase-independent cell death, contributes to neuronal damage in a retinal ischemia-reperfusion injury model. J Neurosci Res 2010; 88: 1569-1576. doi: 10.1002/jnr.22314.
    • (2010) J Neurosci Res , vol.88 , pp. 1569-1576
    • Rosenbaum, D.M.1    Degterev, A.2    David, J.3    Rosenbaum, P.S.4    Roth, S.5    Grotta, J.C.6    Cuny, G.D.7    Yuan, J.8    Savitz, S.I.9
  • 87
    • 34548437549 scopus 로고    scopus 로고
    • Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain
    • Feng S, Yang Y, Mei Y, Ma L, Zhu DE, Hoti N, Castanares M, Wu M., Cleavage of RIP3 inactivates its caspase-independent apoptosis pathway by removal of kinase domain. Cell Signal 2007; 19: 2056-2067. doi: 10.1016/j.cellsig.2007.05.016.
    • (2007) Cell Signal , vol.19 , pp. 2056-2067
    • Feng, S.1    Yang, Y.2    Mei, Y.3    Ma, L.4    Zhu, D.E.5    Hoti, N.6    Castanares, M.7    Wu, M.8
  • 88
    • 67650812332 scopus 로고    scopus 로고
    • RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis
    • Zhang DW, Shao J, Lin J, Zhang N, Lu BJ, Lin SC, Dong MQ, Han J., RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis. Science 2009; 325: 332-336. doi: 10.1126/science.1172308.
    • (2009) Science , vol.325 , pp. 332-336
    • Zhang, D.W.1    Shao, J.2    Lin, J.3    Zhang, N.4    Lu, B.J.5    Lin, S.C.6    Dong, M.Q.7    Han, J.8
  • 89
    • 66749183275 scopus 로고    scopus 로고
    • Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha
    • He S, Wang L, Miao L, Wang T, Du F, Zhao L, Wang X., Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell 2009; 137: 1100-1111. doi: 10.1016/j.cell.2009.05.021.
    • (2009) Cell , vol.137 , pp. 1100-1111
    • He, S.1    Wang, L.2    Miao, L.3    Wang, T.4    Du, F.5    Zhao, L.6    Wang, X.7
  • 90
    • 84893728596 scopus 로고    scopus 로고
    • MLKL regulates necrotic plasma membrane permeabilization
    • Galluzzi L, Kepp O, Kroemer G., MLKL regulates necrotic plasma membrane permeabilization. Cell Res 2014; 24: 139-140. doi: 10.1038/cr.2014.8.
    • (2014) Cell Res , vol.24 , pp. 139-140
    • Galluzzi, L.1    Kepp, O.2    Kroemer, G.3
  • 92
    • 84862907788 scopus 로고    scopus 로고
    • Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase
    • Sun L, Wang H, Wang Z, He S, Chen S, Liao D, Wang L, Yan J, Liu W, Lei X, Wang X., Mixed lineage kinase domain-like protein mediates necrosis signaling downstream of RIP3 kinase. Cell 2012; 148: 213-227. doi: 10.1016/j.cell.2011.11.031.
    • (2012) Cell , vol.148 , pp. 213-227
    • Sun, L.1    Wang, H.2    Wang, Z.3    He, S.4    Chen, S.5    Liao, D.6    Wang, L.7    Yan, J.8    Liu, W.9    Lei, X.10    Wang, X.11
  • 93
    • 84891343566 scopus 로고    scopus 로고
    • Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
    • Cai Z, Jitkaew S, Zhao J, Chiang HC, Choksi S, Liu J, Ward Y, Wu LG, Liu ZG., Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis. Nat Cell Biol 2014; 16: 55-65. doi: 10.1038/ncb2883.
    • (2014) Nat Cell Biol , vol.16 , pp. 55-65
    • Cai, Z.1    Jitkaew, S.2    Zhao, J.3    Chiang, H.C.4    Choksi, S.5    Liu, J.6    Ward, Y.7    Wu, L.G.8    Liu, Z.G.9
  • 94
    • 84888438277 scopus 로고    scopus 로고
    • Widespread mitochondrial depletion via mitophagy does not compromise necroptosis
    • Tait SW, Oberst A, Quarato G, Widespread mitochondrial depletion via mitophagy does not compromise necroptosis. Cell Rep 2013; 5: 878-885. doi: 10.1016/j.celrep.2013.10.034.
    • (2013) Cell Rep , vol.5 , pp. 878-885
    • Tait, S.W.1    Oberst, A.2    Quarato, G.3
  • 95
    • 84868100171 scopus 로고    scopus 로고
    • Necrosis-like death can engage multiple pro-apoptotic Bcl-2 protein family members
    • Tischner D, Manzl C, Soratroi C, Villunger A, Krumschnabel G., Necrosis-like death can engage multiple pro-apoptotic Bcl-2 protein family members. Apoptosis 2012; 17: 1197-1209. doi: 10.1007/s10495-012-0756-8.
    • (2012) Apoptosis , vol.17 , pp. 1197-1209
    • Tischner, D.1    Manzl, C.2    Soratroi, C.3    Villunger, A.4    Krumschnabel, G.5
  • 97
    • 36849056027 scopus 로고    scopus 로고
    • The cardioprotective effect of necrostatin requires The cyclophilin-D component of The mitochondrial permeability transition pore
    • Lim SY, Davidson SM, Mocanu MM, Yellon DM, Smith CC., The cardioprotective effect of necrostatin requires The cyclophilin-D component of The mitochondrial permeability transition pore. Cardiovasc Drugs Ther 2007; 21: 467-469. doi: 10.1007/s10557-007-6067-6.
    • (2007) Cardiovasc Drugs Ther , vol.21 , pp. 467-469
    • Lim, S.Y.1    Davidson, S.M.2    Mocanu, M.M.3    Yellon, D.M.4    Smith, C.C.5
  • 98
    • 84938142624 scopus 로고    scopus 로고
    • Roles of NAD (+), PARP-1, and sirtuins in cell death, ischemic brain injury, and synchrotron radiation X-ray-induced tissue injury
    • Ying W., Roles of NAD (+), PARP-1, and sirtuins in cell death, ischemic brain injury, and synchrotron radiation X-ray-induced tissue injury. Scientifica (Cairo) 2013 2013 691251. doi: 10.1155/2013/691251.
    • (2013) Scientifica (Cairo) , vol.2013 , pp. 691251
    • Ying, W.1
  • 99
    • 2642536197 scopus 로고    scopus 로고
    • Alkylating DNA damage stimulates a regulated form of necrotic cell death
    • Zong WX, Ditsworth D, Bauer DE, Wang ZQ, Thompson CB., Alkylating DNA damage stimulates a regulated form of necrotic cell death. Genes Dev 2004; 18: 1272-1282. doi: 10.1101/gad.1199904.
    • (2004) Genes Dev , vol.18 , pp. 1272-1282
    • Zong, W.X.1    Ditsworth, D.2    Bauer, D.E.3    Wang, Z.Q.4    Thompson, C.B.5
  • 100
    • 34347344991 scopus 로고    scopus 로고
    • Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis
    • Moubarak RS, Yuste VJ, Artus C, Bouharrour A, Greer PA, Menissier-de Murcia J, Susin SA., Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis. Mol Cell Biol 2007; 27: 4844-4862. doi: 10.1128/MCB.02141-06.
    • (2007) Mol Cell Biol , vol.27 , pp. 4844-4862
    • Moubarak, R.S.1    Yuste, V.J.2    Artus, C.3    Bouharrour, A.4    Greer, P.A.5    Menissier-De Murcia, J.6    Susin, S.A.7
  • 102
    • 0034987156 scopus 로고    scopus 로고
    • Effect of poly(ADP-ribose) polymerase inhibitors on The ischemia-reperfusion-induced oxidative cell damage and mitochondrial metabolism in Langendorff heart perfusion system
    • Halmosi R, Berente Z, Osz E, Toth K, Literati-Nagy P, Sumegi B., Effect of poly(ADP-ribose) polymerase inhibitors on The ischemia-reperfusion-induced oxidative cell damage and mitochondrial metabolism in Langendorff heart perfusion system. Mol Pharmacol 2001; 59: 1497-1505.
    • (2001) Mol Pharmacol , vol.59 , pp. 1497-1505
    • Halmosi, R.1    Berente, Z.2    Osz, E.3    Toth, K.4    Literati-Nagy, P.5    Sumegi, B.6
  • 103
    • 0036858375 scopus 로고    scopus 로고
    • The novel PARP inhibitor 5-aminoisoquinolinone reduces The liver injury caused by ischemia and reperfusion in The rat
    • Mota-Filipe H, Sepodes B, McDonald MC, Cuzzocrea S, Pinto R, Thiemermann C., The novel PARP inhibitor 5-aminoisoquinolinone reduces The liver injury caused by ischemia and reperfusion in The rat. Med Sci Monit 2002 8 BR444 BR453
    • (2002) Med Sci Monit , vol.8 , pp. BR444-BR453
    • Mota-Filipe, H.1    Sepodes, B.2    McDonald, M.C.3    Cuzzocrea, S.4    Pinto, R.5    Thiemermann, C.6
  • 105
    • 0032518339 scopus 로고    scopus 로고
    • DNA repair: PARP -another guardian angel?
    • Jeggo PA., DNA repair: PARP-another guardian angel? Curr Biol 1998 8 R49 R51
    • (1998) Curr Biol , vol.8 , pp. R49-R51
    • Jeggo, P.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.