메뉴 건너뛰기




Volumn 10, Issue 6, 2007, Pages 235-255

Therapeutic potential of AIF-mediated caspase-independent programmed cell death

Author keywords

AIF; Apoptosis; Calpains; Cancer therapy; Cathepsins; Degenerative diseases; DNA damage; Ischemia; Mitochondria; PARP 1; ROS

Indexed keywords

ABT 888; AFG 495; AG 014699; AK 275; AK 295; APOPTOSIS INDUCING FACTOR; ATIPRIMOD; BALICATIB; BZL101; CALPAIN; CARBOPLATIN; CATHEPSIN; CELECOXIB; CISPLATIN; CLADRIBINE; CRA 013783; DOCETAXEL; ESTRADIOL; ETOPOSIDE; FLAVOPIRIDOL; FLUOROURACIL; GPI 21016; INO 1001; KU 59436; MINOCYCLINE; NICOTINAMIDE; PACLITAXEL POLIGLUMEX; RELACATIB; RWJ 445380; SNJ 1945; THIOCTIC ACID; UNCLASSIFIED DRUG; VORINOSTAT; [1 [(1 FORMYL 2 PHENYLETHYL)CARBAMOYL] 2 METHYLPROPYL]CARBAMIC ACID BENZYL ESTER;

EID: 38549123294     PISSN: 13687646     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.drup.2007.11.001     Document Type: Article
Times cited : (128)

References (253)
  • 2
    • 33947387924 scopus 로고    scopus 로고
    • Expression of antiapoptotic and proapoptotic molecules in diabetic retinas
    • Abu El-Asrar A.M., Dralands L., Missotten L., and Geboes K. Expression of antiapoptotic and proapoptotic molecules in diabetic retinas. Eye 21 (2007) 238-245
    • (2007) Eye , vol.21 , pp. 238-245
    • Abu El-Asrar, A.M.1    Dralands, L.2    Missotten, L.3    Geboes, K.4
  • 3
    • 33745886796 scopus 로고    scopus 로고
    • PIONEER: a phase III randomized trial of paclitaxel poliglumex versus paclitaxel in chemotherapy-naive women with advanced-stage non-small-cell lung cancer and performance status of 2
    • Albain K.S., Belani C.P., Bonomi P., O'Byrne K.J., Schiller J.H., and Socinski M. PIONEER: a phase III randomized trial of paclitaxel poliglumex versus paclitaxel in chemotherapy-naive women with advanced-stage non-small-cell lung cancer and performance status of 2. Clin. Lung Cancer 7 (2006) 417-419
    • (2006) Clin. Lung Cancer , vol.7 , pp. 417-419
    • Albain, K.S.1    Belani, C.P.2    Bonomi, P.3    O'Byrne, K.J.4    Schiller, J.H.5    Socinski, M.6
  • 5
    • 0035166350 scopus 로고    scopus 로고
    • On the evolutionary conservation of the cell death pathway: mitochondrial release of an apoptosis-inducing factor during Dictyostelium discoideum cell death
    • Arnoult D., Tatischeff I., Estaquier J., Girard M., Sureau F., Tissier J.P., et al. On the evolutionary conservation of the cell death pathway: mitochondrial release of an apoptosis-inducing factor during Dictyostelium discoideum cell death. Mol. Biol. Cell 12 (2001) 3016-3030
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3016-3030
    • Arnoult, D.1    Tatischeff, I.2    Estaquier, J.3    Girard, M.4    Sureau, F.5    Tissier, J.P.6
  • 6
    • 20444375511 scopus 로고    scopus 로고
    • Proteolytic mechanisms in necrotic cell death and neurodegeneration
    • Artal-Sanz M., and Tavernarakis N. Proteolytic mechanisms in necrotic cell death and neurodegeneration. FEBS Lett. 579 (2005) 3287-3296
    • (2005) FEBS Lett. , vol.579 , pp. 3287-3296
    • Artal-Sanz, M.1    Tavernarakis, N.2
  • 7
    • 33748939906 scopus 로고    scopus 로고
    • CD44 ligation induces caspase-independent cell death via a novel calpain/AIF pathway in human erythroleukemia cells
    • Artus C., Maquarre E., Moubarak R.S., Delettre C., Jasmin C., Susin S.A., and Robert-Lezenes J. CD44 ligation induces caspase-independent cell death via a novel calpain/AIF pathway in human erythroleukemia cells. Oncogene 25 (2006) 5741-5751
    • (2006) Oncogene , vol.25 , pp. 5741-5751
    • Artus, C.1    Maquarre, E.2    Moubarak, R.S.3    Delettre, C.4    Jasmin, C.5    Susin, S.A.6    Robert-Lezenes, J.7
  • 8
    • 33747357533 scopus 로고    scopus 로고
    • Switch from caspase-dependent to caspase-independent death during heart development: essential role of Endonuclease G in ischemia-induced DNA processing of differentiated cardiomyocytes
    • Bahi N., Zhang J., Llovera M., Ballester M., Comella J.X., and Sanchis D. Switch from caspase-dependent to caspase-independent death during heart development: essential role of Endonuclease G in ischemia-induced DNA processing of differentiated cardiomyocytes. J. Biol. Chem. 281 (2006) 22943-22952
    • (2006) J. Biol. Chem. , vol.281 , pp. 22943-22952
    • Bahi, N.1    Zhang, J.2    Llovera, M.3    Ballester, M.4    Comella, J.X.5    Sanchis, D.6
  • 9
    • 0032820396 scopus 로고    scopus 로고
    • The fate of epithelial cells in the human large intestine
    • Barkla D.H., and Gibson P.R. The fate of epithelial cells in the human large intestine. Pathology 31 (1999) 230-238
    • (1999) Pathology , vol.31 , pp. 230-238
    • Barkla, D.H.1    Gibson, P.R.2
  • 10
    • 0028292190 scopus 로고
    • Postischemic administration of AK275, a calpain inhibitor, provides substantial protection against focal ischemic brain damage
    • Bartus R.T., Baker K.L., Heiser A.D., Sawyer S.D., Dean R.L., Elliott P.J., and Straub J.A. Postischemic administration of AK275, a calpain inhibitor, provides substantial protection against focal ischemic brain damage. J. Cereb. Blood Flow Metab. 14 (1994) 537-544
    • (1994) J. Cereb. Blood Flow Metab. , vol.14 , pp. 537-544
    • Bartus, R.T.1    Baker, K.L.2    Heiser, A.D.3    Sawyer, S.D.4    Dean, R.L.5    Elliott, P.J.6    Straub, J.A.7
  • 13
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N., Lorenzo H.K., Carmona S., Laforge M., Harper F., Dumont C., and Senik A. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J. Biol. Chem. 278 (2003) 31401-31411
    • (2003) J. Biol. Chem. , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 15
    • 2342467469 scopus 로고    scopus 로고
    • Prospective strategies to enforce selectively cell death in cancer cells
    • Blagosklonny M.V. Prospective strategies to enforce selectively cell death in cancer cells. Oncogene 23 (2004) 2967-2975
    • (2004) Oncogene , vol.23 , pp. 2967-2975
    • Blagosklonny, M.V.1
  • 16
    • 14844312089 scopus 로고    scopus 로고
    • Cancer cell death by programmed necrosis?
    • Borst P., and Rottenberg S. Cancer cell death by programmed necrosis?. Drug Resist. Updates 7 (2004) 321-324
    • (2004) Drug Resist. Updates , vol.7 , pp. 321-324
    • Borst, P.1    Rottenberg, S.2
  • 17
    • 36849028692 scopus 로고    scopus 로고
    • AIF-mediated programmed necrosis: A highly regulated way to die
    • Boujrad H., Gubkina O., Robert N., Krantic S., and Susin S.A. AIF-mediated programmed necrosis: A highly regulated way to die. Cell Cycle 6 (2007) 2611-2618
    • (2007) Cell Cycle , vol.6 , pp. 2611-2618
    • Boujrad, H.1    Gubkina, O.2    Robert, N.3    Krantic, S.4    Susin, S.A.5
  • 19
    • 0038677510 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine
    • Boya P., Gonzalez-Polo R.A., Poncet D., Andreau K., Vieira H.L., Roumier T., Perfettini J.L., and Kroemer G. Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine. Oncogene 22 (2003) 3927-3936
    • (2003) Oncogene , vol.22 , pp. 3927-3936
    • Boya, P.1    Gonzalez-Polo, R.A.2    Poncet, D.3    Andreau, K.4    Vieira, H.L.5    Roumier, T.6    Perfettini, J.L.7    Kroemer, G.8
  • 22
    • 1642576236 scopus 로고    scopus 로고
    • Cathepsin B mediates caspase-independent cell death induced by microtubule stabilizing agents in non-small cell lung cancer cells
    • Bröker L.E., Huisman C., Span S.W., Rodriguez J.A., Kruyt F.A., and Giaccone G. Cathepsin B mediates caspase-independent cell death induced by microtubule stabilizing agents in non-small cell lung cancer cells. Cancer Res. 64 (2004) 27-30
    • (2004) Cancer Res. , vol.64 , pp. 27-30
    • Bröker, L.E.1    Huisman, C.2    Span, S.W.3    Rodriguez, J.A.4    Kruyt, F.A.5    Giaccone, G.6
  • 23
    • 18244392443 scopus 로고    scopus 로고
    • Cell death independent of caspases: a review
    • Bröker L.E., Kruyt F.A., and Giaccone G. Cell death independent of caspases: a review. Clin. Cancer Res. 11 (2005) 3155-3162
    • (2005) Clin. Cancer Res. , vol.11 , pp. 3155-3162
    • Bröker, L.E.1    Kruyt, F.A.2    Giaccone, G.3
  • 26
    • 34548431366 scopus 로고    scopus 로고
    • Critical role of calpain I in mitochondrial release of apoptosis-inducing factor in ischemic neuronal injury
    • Cao G., Xing J., Xiao X., Liou A.K., Gao Y., Yin X.M., Clark R.S., Graham S.H., and Chen J. Critical role of calpain I in mitochondrial release of apoptosis-inducing factor in ischemic neuronal injury. J. Neurosci. 27 (2007) 9278-9293
    • (2007) J. Neurosci. , vol.27 , pp. 9278-9293
    • Cao, G.1    Xing, J.2    Xiao, X.3    Liou, A.K.4    Gao, Y.5    Yin, X.M.6    Clark, R.S.7    Graham, S.H.8    Chen, J.9
  • 27
    • 0141481980 scopus 로고    scopus 로고
    • Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax
    • Cao X., Deng X., and May W.S. Cleavage of Bax to p18 Bax accelerates stress-induced apoptosis, and a cathepsin-like protease may rapidly degrade p18 Bax. Blood 102 (2003) 2605-2614
    • (2003) Blood , vol.102 , pp. 2605-2614
    • Cao, X.1    Deng, X.2    May, W.S.3
  • 28
    • 1642565065 scopus 로고    scopus 로고
    • The p18 truncated form of Bax behaves like a Bcl-2 homology domain 3-only protein
    • Cartron P.F., Oliver L., Juin P., Meflah K., and Vallette F.M. The p18 truncated form of Bax behaves like a Bcl-2 homology domain 3-only protein. J. Biol. Chem. 279 (2004) 11503-11512
    • (2004) J. Biol. Chem. , vol.279 , pp. 11503-11512
    • Cartron, P.F.1    Oliver, L.2    Juin, P.3    Meflah, K.4    Vallette, F.M.5
  • 29
    • 0036403832 scopus 로고    scopus 로고
    • Beta-amyloid fragment 25-35 causes mitochondrial dysfunction in primary cortical neurons
    • Casley C.S., Land J.M., Sharpe M.A., Clark J.B., Duchen M.R., and Canevari L. Beta-amyloid fragment 25-35 causes mitochondrial dysfunction in primary cortical neurons. Neurobiol. Dis. 10 (2002) 258-267
    • (2002) Neurobiol. Dis. , vol.10 , pp. 258-267
    • Casley, C.S.1    Land, J.M.2    Sharpe, M.A.3    Clark, J.B.4    Duchen, M.R.5    Canevari, L.6
  • 30
    • 0033539141 scopus 로고    scopus 로고
    • Interdigital cell death can occur through a necrotic and caspase-independent pathway
    • Chautan M., Chazal G., Cecconi F., Gruss P., and Golstein P. Interdigital cell death can occur through a necrotic and caspase-independent pathway. Curr. Biol. 9 (1999) 967-970
    • (1999) Curr. Biol. , vol.9 , pp. 967-970
    • Chautan, M.1    Chazal, G.2    Cecconi, F.3    Gruss, P.4    Golstein, P.5
  • 31
    • 0035903235 scopus 로고    scopus 로고
    • Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion
    • Chen M., He H., Zhan S., Krajewski S., Reed J.C., and Gottlieb R.A. Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion. J. Biol. Chem. 276 (2001) 30724-30728
    • (2001) J. Biol. Chem. , vol.276 , pp. 30724-30728
    • Chen, M.1    He, H.2    Zhan, S.3    Krajewski, S.4    Reed, J.C.5    Gottlieb, R.A.6
  • 32
    • 4043066518 scopus 로고    scopus 로고
    • Mitochondrial-to-nuclear translocation of apoptosis-inducing factor in cardiac myocytes during oxidant stress: potential role of poly(ADP-ribose) polymerase-1
    • Chen M., Zsengeller Z., Xiao C.Y., and Szabo C. Mitochondrial-to-nuclear translocation of apoptosis-inducing factor in cardiac myocytes during oxidant stress: potential role of poly(ADP-ribose) polymerase-1. Cardiovasc. Res. 63 (2004) 682-688
    • (2004) Cardiovasc. Res. , vol.63 , pp. 682-688
    • Chen, M.1    Zsengeller, Z.2    Xiao, C.Y.3    Szabo, C.4
  • 33
    • 28844490007 scopus 로고    scopus 로고
    • The lysosome-associated apoptosis-inducing protein containing the pleckstrin homology (PH) and FYVE domains (LAPF), representative of a novel family of PH and FYVE domain-containing proteins, induces caspase-independent apoptosis via the lysosomal-mitochondrial pathway
    • Chen W., Li N., Chen T., Han Y., Li C., Wang Y., He W., Zhang L., Wan T., and Cao X. The lysosome-associated apoptosis-inducing protein containing the pleckstrin homology (PH) and FYVE domains (LAPF), representative of a novel family of PH and FYVE domain-containing proteins, induces caspase-independent apoptosis via the lysosomal-mitochondrial pathway. J. Biol. Chem. 280 (2005) 40985-40995
    • (2005) J. Biol. Chem. , vol.280 , pp. 40985-40995
    • Chen, W.1    Li, N.2    Chen, T.3    Han, Y.4    Li, C.5    Wang, Y.6    He, W.7    Zhang, L.8    Wan, T.9    Cao, X.10
  • 34
    • 33847283606 scopus 로고    scopus 로고
    • Novel pycnodysostosis mouse model uncovers cathepsin K function as a potential regulator of osteoclast apoptosis and senescence
    • Chen W., Yang S., Abe Y., Li M., Wang Y., Shao J., Li E., and Li Y.P. Novel pycnodysostosis mouse model uncovers cathepsin K function as a potential regulator of osteoclast apoptosis and senescence. Hum. Mol. Genet. 16 (2007) 410-423
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 410-423
    • Chen, W.1    Yang, S.2    Abe, Y.3    Li, M.4    Wang, Y.5    Shao, J.6    Li, E.7    Li, Y.P.8
  • 35
    • 33748341710 scopus 로고    scopus 로고
    • Dissociating the dual roles of apoptosis-inducing factor in maintaining mitochondrial structure and apoptosis
    • Cheung E.C., Joza N., Steenaart N.A., McClellan K.A., Neuspiel M., McNamara S., et al. Dissociating the dual roles of apoptosis-inducing factor in maintaining mitochondrial structure and apoptosis. EMBO J. 25 (2006) 4061-4073
    • (2006) EMBO J. , vol.25 , pp. 4061-4073
    • Cheung, E.C.1    Joza, N.2    Steenaart, N.A.3    McClellan, K.A.4    Neuspiel, M.5    McNamara, S.6
  • 37
    • 19444364781 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation and stroke
    • Chiarugi A. Poly(ADP-ribosyl)ation and stroke. Pharmacol. Res. 52 (2005) 15-24
    • (2005) Pharmacol. Res. , vol.52 , pp. 15-24
    • Chiarugi, A.1
  • 38
    • 34548626932 scopus 로고    scopus 로고
    • Biological and clinical characterization of paclitaxel poliglumex (PPX, CT-2103), a macromolecular polymer-drug conjugate
    • Chipman S.D., Oldham F.B., Pezzoni G., and Singer J.W. Biological and clinical characterization of paclitaxel poliglumex (PPX, CT-2103), a macromolecular polymer-drug conjugate. Int. J. Nanomed. 1 (2006) 375-383
    • (2006) Int. J. Nanomed. , vol.1 , pp. 375-383
    • Chipman, S.D.1    Oldham, F.B.2    Pezzoni, G.3    Singer, J.W.4
  • 39
    • 34249330344 scopus 로고    scopus 로고
    • Cell death in the cardiovascular system
    • Clarke M., Bennett M., and Littlewood T. Cell death in the cardiovascular system. Heart 93 (2007) 659-664
    • (2007) Heart , vol.93 , pp. 659-664
    • Clarke, M.1    Bennett, M.2    Littlewood, T.3
  • 40
    • 0025283961 scopus 로고
    • Developmental cell death: morphological diversity and multiple mechanisms
    • Clarke P.G. Developmental cell death: morphological diversity and multiple mechanisms. Anat. Embryol. 181 (1990) 195-213
    • (1990) Anat. Embryol. , vol.181 , pp. 195-213
    • Clarke, P.G.1
  • 41
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signaling: their role in cell survival and cell death
    • Codogno P., and Meijer A.J. Autophagy and signaling: their role in cell survival and cell death. Cell Death Differ. 12 Suppl. 2 (2005) 1509-1518
    • (2005) Cell Death Differ. , vol.12 , Issue.SUPPL. 2 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 42
    • 0027133424 scopus 로고
    • Apoptosis: the physiologic pathway of cell death
    • Cohen J.J. Apoptosis: the physiologic pathway of cell death. Hosp. Pract. (Off Ed.) 28 (1993) 35-43
    • (1993) Hosp. Pract. (Off Ed.) , vol.28 , pp. 35-43
    • Cohen, J.J.1
  • 43
    • 0033152431 scopus 로고    scopus 로고
    • Electron microscopic evidence against apoptosis as the mechanism of neuronal death in global ischemia
    • Colbourne F., Sutherland G.R., and Auer R.N. Electron microscopic evidence against apoptosis as the mechanism of neuronal death in global ischemia. J. Neurosci. 19 (1999) 4200-4210
    • (1999) J. Neurosci. , vol.19 , pp. 4200-4210
    • Colbourne, F.1    Sutherland, G.R.2    Auer, R.N.3
  • 44
    • 8844280276 scopus 로고    scopus 로고
    • Induction of antiproliferative effect by diosgenin through activation of p53, release of apoptosis-inducing factor (AIF) and modulation of caspase-3 activity in different human cancer cells
    • Corbiere C., Liagre B., Terro F., and Beneytout J.L. Induction of antiproliferative effect by diosgenin through activation of p53, release of apoptosis-inducing factor (AIF) and modulation of caspase-3 activity in different human cancer cells. Cell Res. 14 (2004) 188-196
    • (2004) Cell Res. , vol.14 , pp. 188-196
    • Corbiere, C.1    Liagre, B.2    Terro, F.3    Beneytout, J.L.4
  • 45
    • 2442621492 scopus 로고    scopus 로고
    • Role of AIF in caspase-dependent and caspase-independent cell death
    • Cregan S.P., Dawson V.L., and Slack R.S. Role of AIF in caspase-dependent and caspase-independent cell death. Oncogene 23 (2004) 2785-2796
    • (2004) Oncogene , vol.23 , pp. 2785-2796
    • Cregan, S.P.1    Dawson, V.L.2    Slack, R.S.3
  • 47
    • 0038380524 scopus 로고    scopus 로고
    • Inhibition of calpains prevents neuronal and behavioral deficits in an MPTP mouse model of Parkinson's disease
    • Crocker S.J., Smith P.D., Jackson-Lewis V., Lamba W.R., Hayley S.P., Grimm E., et al. Inhibition of calpains prevents neuronal and behavioral deficits in an MPTP mouse model of Parkinson's disease. J. Neurosci. 23 (2003) 4081-4091
    • (2003) J. Neurosci. , vol.23 , pp. 4081-4091
    • Crocker, S.J.1    Smith, P.D.2    Jackson-Lewis, V.3    Lamba, W.R.4    Hayley, S.P.5    Grimm, E.6
  • 48
    • 28844491633 scopus 로고    scopus 로고
    • Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: the importance of primed side interactions
    • Cuerrier D., Moldoveanu T., and Davies P.L. Determination of peptide substrate specificity for mu-calpain by a peptide library-based approach: the importance of primed side interactions. J. Biol. Chem. 280 (2005) 40632-40641
    • (2005) J. Biol. Chem. , vol.280 , pp. 40632-40641
    • Cuerrier, D.1    Moldoveanu, T.2    Davies, P.L.3
  • 49
    • 33745165901 scopus 로고    scopus 로고
    • Calpain inhibition by alpha-ketoamide and cyclic hemiacetal inhibitors revealed by X-ray crystallography
    • Cuerrier D., Moldoveanu T., Inoue J., Davies P.L., and Campbell R.L. Calpain inhibition by alpha-ketoamide and cyclic hemiacetal inhibitors revealed by X-ray crystallography. Biochemistry 45 (2006) 7446-7452
    • (2006) Biochemistry , vol.45 , pp. 7446-7452
    • Cuerrier, D.1    Moldoveanu, T.2    Inoue, J.3    Davies, P.L.4    Campbell, R.L.5
  • 50
    • 34248641996 scopus 로고    scopus 로고
    • Targeting Bid to prevent programmed cell death in neurons
    • Culmsee C., and Plesnila N. Targeting Bid to prevent programmed cell death in neurons. Biochem. Soc. Trans. 34 (2006) 1334-1340
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 1334-1340
    • Culmsee, C.1    Plesnila, N.2
  • 51
    • 27744476223 scopus 로고    scopus 로고
    • Apoptosis-inducing factor triggered by poly(ADP-ribose) polymerase and Bid mediates neuronal cell death after oxygen-glucose deprivation and focal cerebral ischemia
    • Culmsee C., Zhu C., Landshamer S., Becattini B., Wagner E., Pellecchia M., Blomgren K., and Plesnila N. Apoptosis-inducing factor triggered by poly(ADP-ribose) polymerase and Bid mediates neuronal cell death after oxygen-glucose deprivation and focal cerebral ischemia. J. Neurosci. 25 (2005) 10262-10272
    • (2005) J. Neurosci. , vol.25 , pp. 10262-10272
    • Culmsee, C.1    Zhu, C.2    Landshamer, S.3    Becattini, B.4    Wagner, E.5    Pellecchia, M.6    Blomgren, K.7    Plesnila, N.8
  • 52
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: critical control points
    • Danial N.N., and Korsmeyer S.J. Cell death: critical control points. Cell 116 (2004) 205-219
    • (2004) Cell , vol.116 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 53
    • 34447528828 scopus 로고    scopus 로고
    • The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions
    • Daugaard M., Rohde M., and Jaattela M. The heat shock protein 70 family: highly homologous proteins with overlapping and distinct functions. FEBS Lett. 581 (2007) 3702-3710
    • (2007) FEBS Lett. , vol.581 , pp. 3702-3710
    • Daugaard, M.1    Rohde, M.2    Jaattela, M.3
  • 54
    • 0034617449 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis
    • Daugas E., Nochy D., Ravagnan L., Loeffler M., Susin S.A., Zamzami N., and Kroemer G. Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis. FEBS Lett. 476 (2000) 118-123
    • (2000) FEBS Lett. , vol.476 , pp. 118-123
    • Daugas, E.1    Nochy, D.2    Ravagnan, L.3    Loeffler, M.4    Susin, S.A.5    Zamzami, N.6    Kroemer, G.7
  • 56
    • 33745864801 scopus 로고    scopus 로고
    • Identification and characterization of AIFsh2, a mitochondrial apoptosis-inducing factor (AIF) isoform with NADH Oxidase activity
    • Delettre C., Yuste V.J., Moubarak R.S., Bras M., Robert N., and Susin S.A. Identification and characterization of AIFsh2, a mitochondrial apoptosis-inducing factor (AIF) isoform with NADH Oxidase activity. J. Biol. Chem. 281 (2006) 18507-18518
    • (2006) J. Biol. Chem. , vol.281 , pp. 18507-18518
    • Delettre, C.1    Yuste, V.J.2    Moubarak, R.S.3    Bras, M.4    Robert, N.5    Susin, S.A.6
  • 57
    • 10744222634 scopus 로고    scopus 로고
    • Left ventricular wall stress as a direct correlate of cardiomyocyte apoptosis in patients with severe dilated cardiomyopathy
    • Di Napoli P., Taccardi A.A., Grilli A., Felaco M., Balbone A., Angelucci D., et al. Left ventricular wall stress as a direct correlate of cardiomyocyte apoptosis in patients with severe dilated cardiomyopathy. Am. Heart J. 146 (2003) 1105-1111
    • (2003) Am. Heart J. , vol.146 , pp. 1105-1111
    • Di Napoli, P.1    Taccardi, A.A.2    Grilli, A.3    Felaco, M.4    Balbone, A.5    Angelucci, D.6
  • 59
    • 0035850884 scopus 로고    scopus 로고
    • Long-term neuroprotective effect of inhibiting poly(ADP-ribose) polymerase in rats with middle cerebral artery occlusion using a behavioral assessment.
    • Ding Y., Zhou Y., Lai Q., Li J., Gordon V., and Diaz F.G. Long-term neuroprotective effect of inhibiting poly(ADP-ribose) polymerase in rats with middle cerebral artery occlusion using a behavioral assessment. Brain Res. 915 (2001) 210-217
    • (2001) Brain Res. , vol.915 , pp. 210-217
    • Ding, Y.1    Zhou, Y.2    Lai, Q.3    Li, J.4    Gordon, V.5    Diaz, F.G.6
  • 62
  • 63
    • 17144361820 scopus 로고    scopus 로고
    • Lysosomes as targets for cancer therapy
    • Fehrenbacher N., and Jaattela M. Lysosomes as targets for cancer therapy. Cancer Res. 65 (2005) 2993-2995
    • (2005) Cancer Res. , vol.65 , pp. 2993-2995
    • Fehrenbacher, N.1    Jaattela, M.2
  • 65
    • 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., and Vandenabeele P. Necrosis, a well-orchestrated form of cell demise: signalling cascades, important mediators and concomitant immune response. Biochim. Biophys. Acta 1757 (2006) 1371-1387
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1371-1387
    • Festjens, N.1    Vanden Berghe, T.2    Vandenabeele, P.3
  • 66
    • 33646428618 scopus 로고    scopus 로고
    • A novel paraptosis pathway involving LEI/L-DNaseII for EGF-induced cell death in somato-lactotrope pituitary cells
    • Fombonne J., Padron L., Enjalbert A., Krantic S., and Torriglia A. A novel paraptosis pathway involving LEI/L-DNaseII for EGF-induced cell death in somato-lactotrope pituitary cells. Apoptosis 11 (2006) 367-375
    • (2006) Apoptosis , vol.11 , pp. 367-375
    • Fombonne, J.1    Padron, L.2    Enjalbert, A.3    Krantic, S.4    Torriglia, A.5
  • 67
    • 0033811496 scopus 로고    scopus 로고
    • Seizure-induced neuronal necrosis: implications for programmed cell death mechanisms
    • Fujikawa D.G., Shinmei S.S., and Cai B. Seizure-induced neuronal necrosis: implications for programmed cell death mechanisms. Epilepsia 41 Suppl. 6 (2000) S9-S13
    • (2000) Epilepsia , vol.41 , Issue.SUPPL. 6
    • Fujikawa, D.G.1    Shinmei, S.S.2    Cai, B.3
  • 68
    • 34247898914 scopus 로고    scopus 로고
    • DY-9760e, a novel calmodulin inhibitor, exhibits cardioprotective effects in the ischemic heart
    • Fukunaga K., Han F., Shioda N., Moriguchi S., Kasahara J., and Shirasaki Y. DY-9760e, a novel calmodulin inhibitor, exhibits cardioprotective effects in the ischemic heart. Cardiovasc. Drug Rev. 24 (2006) 88-100
    • (2006) Cardiovasc. Drug Rev. , vol.24 , pp. 88-100
    • Fukunaga, K.1    Han, F.2    Shioda, N.3    Moriguchi, S.4    Kasahara, J.5    Shirasaki, Y.6
  • 69
    • 28244459490 scopus 로고    scopus 로고
    • Targeting PBR by hexaminolevulinate-mediated photodynamic therapy induces apoptosis through translocation of apoptosis-inducing factor in human leukemia cells
    • Furre I.E., Shahzidi S., Luksiene Z., Moller M.T., Borgen E., Morgan J., Tkacz-Stachowska K., Nesland J.M., and Peng Q. Targeting PBR by hexaminolevulinate-mediated photodynamic therapy induces apoptosis through translocation of apoptosis-inducing factor in human leukemia cells. Cancer Res. 65 (2005) 11051-11060
    • (2005) Cancer Res. , vol.65 , pp. 11051-11060
    • Furre, I.E.1    Shahzidi, S.2    Luksiene, Z.3    Moller, M.T.4    Borgen, E.5    Morgan, J.6    Tkacz-Stachowska, K.7    Nesland, J.M.8    Peng, Q.9
  • 71
    • 33846643454 scopus 로고    scopus 로고
    • Cysteine cathepsins and the cutting edge of cancer invasion
    • Gocheva V., and Joyce J.A. Cysteine cathepsins and the cutting edge of cancer invasion. Cell Cycle 6 (2007) 60-64
    • (2007) Cell Cycle , vol.6 , pp. 60-64
    • Gocheva, V.1    Joyce, J.A.2
  • 72
    • 33745591102 scopus 로고    scopus 로고
    • Multiple pathways of cytochrome c release from mitochondria in apoptosis
    • Gogvadze V., Orrenius S., and Zhivotovsky B. Multiple pathways of cytochrome c release from mitochondria in apoptosis. Biochim. Biophys. Acta 1757 (2006) 639-647
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 639-647
    • Gogvadze, V.1    Orrenius, S.2    Zhivotovsky, B.3
  • 75
    • 35549012269 scopus 로고    scopus 로고
    • A multiplicity of cell death pathways
    • Symposium on Apoptotic and Non-Apoptotic Cell Death Pathways
    • Golstein P., and Kroemer G. A multiplicity of cell death pathways. Symposium on Apoptotic and Non-Apoptotic Cell Death Pathways. EMBO Rep. 8 (2007) 829-833
    • (2007) EMBO Rep. , vol.8 , pp. 829-833
    • Golstein, P.1    Kroemer, G.2
  • 76
    • 33846018602 scopus 로고    scopus 로고
    • Cell death by necrosis: towards a molecular definition
    • Golstein P., and Kroemer G. Cell death by necrosis: towards a molecular definition. Trends Biochem. Sci. 32 (2007) 37-43
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 37-43
    • Golstein, P.1    Kroemer, G.2
  • 77
    • 0036218940 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase impairs early and long-term experimental stroke recovery
    • Goto S., Xue R., Sugo N., Sawada M., Blizzard K.K., Poitras M.F., et al. Poly(ADP-ribose) polymerase impairs early and long-term experimental stroke recovery. Stroke 33 (2002) 1101-1106
    • (2002) Stroke , vol.33 , pp. 1101-1106
    • Goto, S.1    Xue, R.2    Sugo, N.3    Sawada, M.4    Blizzard, K.K.5    Poitras, M.F.6
  • 79
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green D.R., and Reed J.C. Mitochondria and apoptosis. Science 281 (1998) 1309-1312
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 80
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A., McDonnell J.M., and Korsmeyer S.J. BCL-2 family members and the mitochondria in apoptosis. Genes Dev. 13 (1999) 1899-1911
    • (1999) Genes Dev. , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 82
    • 0242606282 scopus 로고    scopus 로고
    • Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor
    • Gurbuxani S., Schmitt E., Cande C., Parcellier A., Hammann A., Daugas E., et al. Heat shock protein 70 binding inhibits the nuclear import of apoptosis-inducing factor. Oncogene 22 (2003) 6669-6678
    • (2003) Oncogene , vol.22 , pp. 6669-6678
    • Gurbuxani, S.1    Schmitt, E.2    Cande, C.3    Parcellier, A.4    Hammann, A.5    Daugas, E.6
  • 83
    • 0033598713 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion
    • Ha H.C., and Snyder S.H. Poly(ADP-ribose) polymerase is a mediator of necrotic cell death by ATP depletion. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 13978-13982
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13978-13982
    • Ha, H.C.1    Snyder, S.H.2
  • 85
    • 33645889361 scopus 로고    scopus 로고
    • 3-[2-[4-(3-Chloro-2-methylphenylmethyl)-1-piperazinyl]ethyl]-5.6-dimethoxy -1-(4-imidazolylmethyl)-1H-indazole dihydro-chloride 3. 5 hydrate (DY-9760e) is neuroprotective in rat microsphere embolism: role of the cross-talk between calpain and caspase-3 through calpastatin
    • Han F., Shirasaki Y., and Fukunaga K. 3-[2-[4-(3-Chloro-2-methylphenylmethyl)-1-piperazinyl]ethyl]-5.6-dimethoxy -1-(4-imidazolylmethyl)-1H-indazole dihydro-chloride 3. 5 hydrate (DY-9760e) is neuroprotective in rat microsphere embolism: role of the cross-talk between calpain and caspase-3 through calpastatin. J. Pharmacol. Exp. Ther. 317 (2006) 529-536
    • (2006) J. Pharmacol. Exp. Ther. , vol.317 , pp. 529-536
    • Han, F.1    Shirasaki, Y.2    Fukunaga, K.3
  • 86
    • 34250748014 scopus 로고    scopus 로고
    • Shikonin circumvents cancer drug resistance by induction of a necroptotic death
    • Han W., Li L., Qiu S., Lu Q., Pan Q., Gu Y., Luo J., and Hu X. Shikonin circumvents cancer drug resistance by induction of a necroptotic death. Mol. Cancer Ther. 6 (2007) 1641-1649
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 1641-1649
    • Han, W.1    Li, L.2    Qiu, S.3    Lu, Q.4    Pan, Q.5    Gu, Y.6    Luo, J.7    Hu, X.8
  • 87
    • 2442661614 scopus 로고    scopus 로고
    • Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation
    • Heinrich M., Neumeyer J., Jakob M., Hallas C., Tchikov V., Winoto-Morbach S., et al. Cathepsin D links TNF-induced acid sphingomyelinase to Bid-mediated caspase-9 and -3 activation. Cell Death Differ. 11 (2004) 550-563
    • (2004) Cell Death Differ. , vol.11 , pp. 550-563
    • Heinrich, M.1    Neumeyer, J.2    Jakob, M.3    Hallas, C.4    Tchikov, V.5    Winoto-Morbach, S.6
  • 88
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner M.O. The biochemistry of apoptosis. Nature 407 (2000) 770-776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 89
    • 2442460088 scopus 로고    scopus 로고
    • Role of mitochondrial membrane permeabilization in apoptosis and cancer
    • Henry-Mowatt J., Dive C., Martinou J.C., and James D. Role of mitochondrial membrane permeabilization in apoptosis and cancer. Oncogene 23 (2004) 2850-2860
    • (2004) Oncogene , vol.23 , pp. 2850-2860
    • Henry-Mowatt, J.1    Dive, C.2    Martinou, J.C.3    James, D.4
  • 91
    • 5944233768 scopus 로고    scopus 로고
    • Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule
    • Holler N., Zaru R., Micheau O., Thome M., Attinger A., Valitutti S., et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat. Immunol. 1 (2000) 489-495
    • (2000) Nat. Immunol. , vol.1 , pp. 489-495
    • Holler, N.1    Zaru, R.2    Micheau, O.3    Thome, M.4    Attinger, A.5    Valitutti, S.6
  • 92
    • 2142694340 scopus 로고    scopus 로고
    • Nuclear and mitochondrial conversations in cell death: PARP-1 and AIF signaling
    • Hong S.J., Dawson T.M., and Dawson V.L. Nuclear and mitochondrial conversations in cell death: PARP-1 and AIF signaling. Trends Pharmacol. Sci. 25 (2004) 259-264
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 259-264
    • Hong, S.J.1    Dawson, T.M.2    Dawson, V.L.3
  • 93
    • 38449117512 scopus 로고    scopus 로고
    • Ascorbate (vitamin C) induces cell death through the apoptosis-inducing factor in human breast cancer cells
    • Hong S.W., Jin D.H., Hahm E.S., Yim S.H., Lim J.S., Kim K.I., et al. Ascorbate (vitamin C) induces cell death through the apoptosis-inducing factor in human breast cancer cells. Oncol. Rep. 18 (2007) 811-815
    • (2007) Oncol. Rep. , vol.18 , pp. 811-815
    • Hong, S.W.1    Jin, D.H.2    Hahm, E.S.3    Yim, S.H.4    Lim, J.S.5    Kim, K.I.6
  • 94
    • 0348038755 scopus 로고    scopus 로고
    • Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1)
    • Houseweart M.K., Vilaythong A., Yin X.M., Turk B., Noebels J.L., and Myers R.M. Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1). Cell Death Differ. 10 (2003) 1329-1335
    • (2003) Cell Death Differ. , vol.10 , pp. 1329-1335
    • Houseweart, M.K.1    Vilaythong, A.2    Yin, X.M.3    Turk, B.4    Noebels, J.L.5    Myers, R.M.6
  • 95
    • 0346873049 scopus 로고    scopus 로고
    • Anticancer therapy targeting the apoptotic pathway
    • Hu W., and Kavanagh J.J. Anticancer therapy targeting the apoptotic pathway. Lancet Oncol. 4 (2003) 721-729
    • (2003) Lancet Oncol. , vol.4 , pp. 721-729
    • Hu, W.1    Kavanagh, J.J.2
  • 96
    • 34250024884 scopus 로고    scopus 로고
    • Lysosomal cathepsin initiates apoptosis, which is regulated by photodamage to Bcl-2 at mitochondria in photodynamic therapy using a novel photosensitizer, ATX-s10 (Na)
    • Ichinose S., Usuda J., Hirata T., Inoue T., Ohtani K., Maehara S., et al. Lysosomal cathepsin initiates apoptosis, which is regulated by photodamage to Bcl-2 at mitochondria in photodynamic therapy using a novel photosensitizer, ATX-s10 (Na). Int. J. Oncol. 29 (2006) 349-355
    • (2006) Int. J. Oncol. , vol.29 , pp. 349-355
    • Ichinose, S.1    Usuda, J.2    Hirata, T.3    Inoue, T.4    Ohtani, K.5    Maehara, S.6
  • 97
    • 0027310916 scopus 로고
    • On neuronal health
    • Isacson O. On neuronal health. Trends Neurosci. 16 (1993) 306-308
    • (1993) Trends Neurosci. , vol.16 , pp. 306-308
    • Isacson, O.1
  • 98
    • 3342986461 scopus 로고    scopus 로고
    • A novel and potent poly(ADP-ribose) polymerase-1 inhibitor, FR247304 (5-chloro-2-[3-(4-phenyl-3,6-dihydro-1(2H)-pyridinyl)propyl]-4(3H)-quinazo linone), attenuates neuronal damage in in vitro and in vivo models of cerebral ischemia
    • Iwashita A., Tojo N., Matsuura S., Yamazaki S., Kamijo K., Ishida J., et al. A novel and potent poly(ADP-ribose) polymerase-1 inhibitor, FR247304 (5-chloro-2-[3-(4-phenyl-3,6-dihydro-1(2H)-pyridinyl)propyl]-4(3H)-quinazo linone), attenuates neuronal damage in in vitro and in vivo models of cerebral ischemia. J. Pharmacol. Exp. Ther. 310 (2004) 425-436
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 425-436
    • Iwashita, A.1    Tojo, N.2    Matsuura, S.3    Yamazaki, S.4    Kamijo, K.5    Ishida, J.6
  • 99
    • 0036910734 scopus 로고    scopus 로고
    • Programmed cell death: many ways for cells to die decently
    • Jaattela M. Programmed cell death: many ways for cells to die decently. Ann. Med. 34 (2002) 480-488
    • (2002) Ann. Med. , vol.34 , pp. 480-488
    • Jaattela, M.1
  • 100
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • Jaattela M., and Tschopp J. Caspase-independent cell death in T lymphocytes. Nat. Immunol. 4 (2003) 416-423
    • (2003) Nat. Immunol. , vol.4 , pp. 416-423
    • Jaattela, M.1    Tschopp, J.2
  • 101
    • 2342603891 scopus 로고    scopus 로고
    • Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis
    • Joyce J.A., Baruch A., Chehade K., Meyer-Morse N., Giraudo E., Tsai F.Y., et al. Cathepsin cysteine proteases are effectors of invasive growth and angiogenesis during multistage tumorigenesis. Cancer Cell 5 (2004) 443-453
    • (2004) Cancer Cell , vol.5 , pp. 443-453
    • Joyce, J.A.1    Baruch, A.2    Chehade, K.3    Meyer-Morse, N.4    Giraudo, E.5    Tsai, F.Y.6
  • 102
    • 27944475065 scopus 로고    scopus 로고
    • Muscle-specific loss of apoptosis-inducing factor leads to mitochondrial dysfunction, skeletal muscle atrophy, and dilated cardiomyopathy
    • Joza N., Oudit G.Y., Brown D., Benit P., Kassiri Z., Vahsen N., et al. Muscle-specific loss of apoptosis-inducing factor leads to mitochondrial dysfunction, skeletal muscle atrophy, and dilated cardiomyopathy. Mol. Cell. Biol. 25 (2005) 10261-10272
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 10261-10272
    • Joza, N.1    Oudit, G.Y.2    Brown, D.3    Benit, P.4    Kassiri, Z.5    Vahsen, N.6
  • 103
    • 0035967169 scopus 로고    scopus 로고
    • Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death
    • Joza N., Susin S.A., Daugas E., Stanford W.L., Cho S.K., Li C.Y., et al. Essential role of the mitochondrial apoptosis-inducing factor in programmed cell death. Nature 410 (2001) 549-554
    • (2001) Nature , vol.410 , pp. 549-554
    • Joza, N.1    Susin, S.A.2    Daugas, E.3    Stanford, W.L.4    Cho, S.K.5    Li, C.Y.6
  • 104
    • 1042302101 scopus 로고    scopus 로고
    • Neuroprotective effect of 4-amino-1,8-napthalimide, a poly(ADP ribose) polymerase inhibitor in middle cerebral artery occlusion-induced focal cerebral ischemia in rat
    • Kabra D.G., Thiyagarajan M., Kaul C.L., and Sharma S.S. Neuroprotective effect of 4-amino-1,8-napthalimide, a poly(ADP ribose) polymerase inhibitor in middle cerebral artery occlusion-induced focal cerebral ischemia in rat. Brain Res. Bull. 62 (2004) 425-433
    • (2004) Brain Res. Bull. , vol.62 , pp. 425-433
    • Kabra, D.G.1    Thiyagarajan, M.2    Kaul, C.L.3    Sharma, S.S.4
  • 106
    • 0035887215 scopus 로고    scopus 로고
    • Sphingosine-induced apoptosis is dependent on lysosomal proteases
    • Kagedal K., Zhao M., Svensson I., and Brunk U.T. Sphingosine-induced apoptosis is dependent on lysosomal proteases. Biochem. J. 359 (2001) 335-343
    • (2001) Biochem. J. , vol.359 , pp. 335-343
    • Kagedal, K.1    Zhao, M.2    Svensson, I.3    Brunk, U.T.4
  • 107
    • 10844264632 scopus 로고    scopus 로고
    • Caspase-independent cell death by arsenic trioxide in human cervical cancer cells: reactive oxygen species-mediated poly(ADP-ribose) polymerase-1 activation signals apoptosis-inducing factor release from mitochondria
    • Kang Y.H., Yi M.J., Kim M.J., Park M.T., Bae S., Kang C.M., et al. Caspase-independent cell death by arsenic trioxide in human cervical cancer cells: reactive oxygen species-mediated poly(ADP-ribose) polymerase-1 activation signals apoptosis-inducing factor release from mitochondria. Cancer Res. 64 (2004) 8960-8967
    • (2004) Cancer Res. , vol.64 , pp. 8960-8967
    • Kang, Y.H.1    Yi, M.J.2    Kim, M.J.3    Park, M.T.4    Bae, S.5    Kang, C.M.6
  • 108
    • 0344393783 scopus 로고    scopus 로고
    • Alterations in the apoptotic machinery and their potential role in anticancer drug resistance
    • Kaufmann S.H., and Vaux D.L. Alterations in the apoptotic machinery and their potential role in anticancer drug resistance. Oncogene 22 (2003) 7414-7430
    • (2003) Oncogene , vol.22 , pp. 7414-7430
    • Kaufmann, S.H.1    Vaux, D.L.2
  • 109
    • 33646948530 scopus 로고    scopus 로고
    • Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled
    • Keeney P.M., Xie J., Capaldi R.A., and Bennett Jr. J.P. Parkinson's disease brain mitochondrial complex I has oxidatively damaged subunits and is functionally impaired and misassembled. J. Neurosci. 26 (2006) 5256-5264
    • (2006) J. Neurosci. , vol.26 , pp. 5256-5264
    • Keeney, P.M.1    Xie, J.2    Capaldi, R.A.3    Bennett Jr., J.P.4
  • 110
    • 33845931841 scopus 로고    scopus 로고
    • MNNG-induced cell death is controlled by interactions between PARP-1, poly(ADP-ribose) glycohydrolase, and XRCC1
    • Keil C., Grobe T., and Oei S.L. MNNG-induced cell death is controlled by interactions between PARP-1, poly(ADP-ribose) glycohydrolase, and XRCC1. J. Biol. Chem. 281 (2006) 34394-34405
    • (2006) J. Biol. Chem. , vol.281 , pp. 34394-34405
    • Keil, C.1    Grobe, T.2    Oei, S.L.3
  • 111
    • 0028329172 scopus 로고
    • Apoptosis. Its significance in cancer and cancer therapy
    • Kerr J.F., Winterford C.M., and Harmon B.V. Apoptosis. Its significance in cancer and cancer therapy. Cancer 73 (1994) 2013-2026
    • (1994) Cancer , vol.73 , pp. 2013-2026
    • Kerr, J.F.1    Winterford, C.M.2    Harmon, B.V.3
  • 112
    • 0015383455 scopus 로고
    • Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr J.F., Wyllie A.H., and Currie A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26 (1972) 239-257
    • (1972) Br. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 113
    • 0042330416 scopus 로고    scopus 로고
    • Role of apoptosis-inducing factor in myocardial cell death by ischemia-reperfusion
    • Kim G.T., Chun Y.S., Park J.W., and Kim M.S. Role of apoptosis-inducing factor in myocardial cell death by ischemia-reperfusion. Biochem. Biophys. Res. Commun. 309 (2003) 619-624
    • (2003) Biochem. Biophys. Res. Commun. , vol.309 , pp. 619-624
    • Kim, G.T.1    Chun, Y.S.2    Park, J.W.3    Kim, M.S.4
  • 116
    • 19444374556 scopus 로고    scopus 로고
    • Mediation of cell death by poly(ADP-ribose) polymerase-1
    • Koh D.W., Dawson T.M., and Dawson V.L. Mediation of cell death by poly(ADP-ribose) polymerase-1. Pharmacol. Res. 52 (2005) 5-14
    • (2005) Pharmacol. Res. , vol.52 , pp. 5-14
    • Koh, D.W.1    Dawson, T.M.2    Dawson, V.L.3
  • 117
    • 17144434775 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase inhibition protect neurons and the white matter and regulates the translocation of apoptosis-inducing factor in stroke
    • Komjati K., Mabley J.G., Virag L., Southan G.J., Salzman A.L., and Szabo C. Poly(ADP-ribose) polymerase inhibition protect neurons and the white matter and regulates the translocation of apoptosis-inducing factor in stroke. Int. J. Mol. Med. 13 (2004) 373-382
    • (2004) Int. J. Mol. Med. , vol.13 , pp. 373-382
    • Komjati, K.1    Mabley, J.G.2    Virag, L.3    Southan, G.J.4    Salzman, A.L.5    Szabo, C.6
  • 118
    • 0036316720 scopus 로고    scopus 로고
    • Origin and evolution of eukaryotic apoptosis: the bacterial connection
    • Koonin E.V., and Aravind L. Origin and evolution of eukaryotic apoptosis: the bacterial connection. Cell Death Differ. 9 (2002) 394-404
    • (2002) Cell Death Differ. , vol.9 , pp. 394-404
    • Koonin, E.V.1    Aravind, L.2
  • 119
    • 33847134493 scopus 로고    scopus 로고
    • Apoptosis-inducing factor: a matter of neuron life and death
    • Krantic S., Mechawar N., Reix S., and Quirion R. Apoptosis-inducing factor: a matter of neuron life and death. Prog. Neurobiol. 81 (2007) 179-196
    • (2007) Prog. Neurobiol. , vol.81 , pp. 179-196
    • Krantic, S.1    Mechawar, N.2    Reix, S.3    Quirion, R.4
  • 120
    • 27844495164 scopus 로고    scopus 로고
    • Molecular basis of programmed cell death involved in neurodegeneration
    • Krantic S., Mechawar N., Reix S., and Quirion R. Molecular basis of programmed cell death involved in neurodegeneration. Trends Neurosci. 28 (2005) 670-676
    • (2005) Trends Neurosci. , vol.28 , pp. 670-676
    • Krantic, S.1    Mechawar, N.2    Reix, S.3    Quirion, R.4
  • 121
    • 22544432640 scopus 로고    scopus 로고
    • Classification of cell death: recommendations of the nomenclature committee on cell death
    • Kroemer G., El-Deiry W.S., Golstein P., Peter M.E., Vaux D., Vandenabeele P., et al. Classification of cell death: recommendations of the nomenclature committee on cell death. Cell Death Differ. 12 Suppl. 2 (2005) 1463-1467
    • (2005) Cell Death Differ. , vol.12 , Issue.SUPPL. 2 , pp. 1463-1467
    • Kroemer, G.1    El-Deiry, W.S.2    Golstein, P.3    Peter, M.E.4    Vaux, D.5    Vandenabeele, P.6
  • 124
    • 0037069451 scopus 로고    scopus 로고
    • Caspase activation and neuroprotection in caspase-3-deficient mice after in vivo cerebral ischemia and in vitro oxygen glucose deprivation
    • Le D.A., Wu Y., Huang Z., Matsushita K., Plesnila N., Augustinack J.C., et al. Caspase activation and neuroprotection in caspase-3-deficient mice after in vivo cerebral ischemia and in vitro oxygen glucose deprivation. Proc. Natl. Acad. Sci. U.S.A. 99 (2002) 15188-15193
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 15188-15193
    • Le, D.A.1    Wu, Y.2    Huang, Z.3    Matsushita, K.4    Plesnila, N.5    Augustinack, J.C.6
  • 125
    • 33644663413 scopus 로고    scopus 로고
    • Metalloporphyrin-based superoxide dismutase mimic attenuates the nuclear translocation of apoptosis-inducing factor and the subsequent DNA fragmentation after permanent focal cerebral ischemia in mice
    • Lee B.I., Chan P.H., and Kim G.W. Metalloporphyrin-based superoxide dismutase mimic attenuates the nuclear translocation of apoptosis-inducing factor and the subsequent DNA fragmentation after permanent focal cerebral ischemia in mice. Stroke 36 (2005) 2712-2717
    • (2005) Stroke , vol.36 , pp. 2712-2717
    • Lee, B.I.1    Chan, P.H.2    Kim, G.W.3
  • 126
    • 34249027558 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase inhibition by cilostazol is implicated in the neuroprotective effect against focal cerebral ischemic infarct in rat
    • Lee J.H., Park S.Y., Shin H.K., Kim C.D., Lee W.S., and Hong K.W. Poly(ADP-ribose) polymerase inhibition by cilostazol is implicated in the neuroprotective effect against focal cerebral ischemic infarct in rat. Brain Res. 1152 (2007) 182-190
    • (2007) Brain Res. , vol.1152 , pp. 182-190
    • Lee, J.H.1    Park, S.Y.2    Shin, H.K.3    Kim, C.D.4    Lee, W.S.5    Hong, K.W.6
  • 127
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: from caspases to alternative mechanisms
    • Leist M., and Jaattela M. Four deaths and a funeral: from caspases to alternative mechanisms. Nat. Rev. Mol. Cell. Biol. 2 (2001) 589-598
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 128
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai A., Bassik M.C., Walensky L.D., Sorcinelli M.D., Weiler S., and Korsmeyer S.J. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell 2 (2002) 183-192
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1    Bassik, M.C.2    Walensky, L.D.3    Sorcinelli, M.D.4    Weiler, S.5    Korsmeyer, S.J.6
  • 129
    • 34250304602 scopus 로고    scopus 로고
    • Honokiol induces a necrotic cell death through the mitochondrial permeability transition pore
    • Li L., Han W., Gu Y., Qiu S., Lu Q., Jin J., Luo J., and Hu X. Honokiol induces a necrotic cell death through the mitochondrial permeability transition pore. Cancer Res. 67 (2007) 4894-4903
    • (2007) Cancer Res. , vol.67 , pp. 4894-4903
    • Li, L.1    Han, W.2    Gu, Y.3    Qiu, S.4    Lu, Q.5    Jin, J.6    Luo, J.7    Hu, X.8
  • 131
    • 33751500940 scopus 로고    scopus 로고
    • Influence of duration of focal cerebral ischemia and neuronal nitric oxide synthase on translocation of apoptosis-inducing factor to the nucleus
    • Li X., Nemoto M., Xu Z., Yu S.W., Shimoji M., Andrabi S.A., Haince J.F., et al. Influence of duration of focal cerebral ischemia and neuronal nitric oxide synthase on translocation of apoptosis-inducing factor to the nucleus. Neuroscience 144 (2007) 56-65
    • (2007) Neuroscience , vol.144 , pp. 56-65
    • Li, X.1    Nemoto, M.2    Xu, Z.3    Yu, S.W.4    Shimoji, M.5    Andrabi, S.A.6    Haince, J.F.7
  • 132
    • 26844570219 scopus 로고    scopus 로고
    • Lysosomes and endoplasmic reticulum: targets for improved, selective anticancer therapy
    • Linder S., and Shoshan M.C. Lysosomes and endoplasmic reticulum: targets for improved, selective anticancer therapy. Drug Resist. Updates 8 (2005) 199-204
    • (2005) Drug Resist. Updates , vol.8 , pp. 199-204
    • Linder, S.1    Shoshan, M.C.2
  • 133
  • 134
    • 27144528184 scopus 로고    scopus 로고
    • Wood smoke extract induces oxidative stress-mediated caspase-independent apoptosis in human lung endothelial cells: role of AIF and EndoG
    • Liu P.L., Chen Y.L., Chen Y.H., Lin S.J., and Kou Y.R. Wood smoke extract induces oxidative stress-mediated caspase-independent apoptosis in human lung endothelial cells: role of AIF and EndoG. Am. J. Physiol. Lung Cell. Mol. Physiol. 289 (2005) L739-L749
    • (2005) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.289
    • Liu, P.L.1    Chen, Y.L.2    Chen, Y.H.3    Lin, S.J.4    Kou, Y.R.5
  • 135
    • 0942290423 scopus 로고    scopus 로고
    • Rapid induction of mitochondrial events and caspase-independent apoptosis in Survivin-targeted melanoma cells
    • Liu T., Brouha B., and Grossman D. Rapid induction of mitochondrial events and caspase-independent apoptosis in Survivin-targeted melanoma cells. Oncogene 23 (2004) 39-48
    • (2004) Oncogene , vol.23 , pp. 39-48
    • Liu, T.1    Brouha, B.2    Grossman, D.3
  • 137
    • 1642491755 scopus 로고    scopus 로고
    • Mitochondrial effectors in caspase-independent cell death
    • Lorenzo H.K., and Susin S.A. Mitochondrial effectors in caspase-independent cell death. FEBS Lett. 557 (2004) 14-20
    • (2004) FEBS Lett. , vol.557 , pp. 14-20
    • Lorenzo, H.K.1    Susin, S.A.2
  • 138
    • 0033010612 scopus 로고    scopus 로고
    • Apoptosis inducing factor (AIF): a phylogenetically old, caspase-independent effector of cell death
    • Lorenzo H.K., Susin S.A., Penninger J., and Kroemer G. Apoptosis inducing factor (AIF): a phylogenetically old, caspase-independent effector of cell death. Cell Death Differ. 6 (1999) 516-524
    • (1999) Cell Death Differ. , vol.6 , pp. 516-524
    • Lorenzo, H.K.1    Susin, S.A.2    Penninger, J.3    Kroemer, G.4
  • 139
    • 34247371033 scopus 로고    scopus 로고
    • Cell survival, cell death and cell cycle pathways are interconnected: implications for cancer therapy
    • Maddika S., Ande S.R., Panigrahi S., et al. Cell survival, cell death and cell cycle pathways are interconnected: implications for cancer therapy. Drug Resist. Updates 10 (2007) 13-29
    • (2007) Drug Resist. Updates , vol.10 , pp. 13-29
    • Maddika, S.1    Ande, S.R.2    Panigrahi, S.3
  • 142
    • 33644832665 scopus 로고    scopus 로고
    • Defects of the apoptotic pathway as therapeutic target against cancer
    • Mashima T., and Tsuruo T. Defects of the apoptotic pathway as therapeutic target against cancer. Drug Resist. Updates 8 (2005) 339-343
    • (2005) Drug Resist. Updates , vol.8 , pp. 339-343
    • Mashima, T.1    Tsuruo, T.2
  • 145
    • 27644504634 scopus 로고    scopus 로고
    • How many ways to die? How many different models of cell death?
    • Melino G., Knight R.A., and Nicotera P. How many ways to die? How many different models of cell death?. Cell Death Differ. 12 Suppl. 2 (2005) 1457-1462
    • (2005) Cell Death Differ. , vol.12 , Issue.SUPPL. 2 , pp. 1457-1462
    • Melino, G.1    Knight, R.A.2    Nicotera, P.3
  • 147
    • 34648823750 scopus 로고    scopus 로고
    • Autophagy signaling in cancer and its potential as novel target to improve anticancer therapy
    • Moretti L., Yang E.S., Kim K.W., and Lu B. Autophagy signaling in cancer and its potential as novel target to improve anticancer therapy. Drug Resist. Updates 10 (2007) 135-143
    • (2007) Drug Resist. Updates , vol.10 , pp. 135-143
    • Moretti, L.1    Yang, E.S.2    Kim, K.W.3    Lu, B.4
  • 148
    • 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 R.S., Yuste V.J., Artus C., Bouharrour A., Greer P.A., Menissier-de Murcia J., and Susin S.A. Sequential activation of poly(ADP-ribose) polymerase 1, calpains, and Bax is essential in apoptosis-inducing factor-mediated programmed necrosis. Mol. Cell. Biol. 27 (2007) 4844-4862
    • (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
  • 149
    • 3042662255 scopus 로고    scopus 로고
    • MGLuR5 activation reduces beta-amyloid-induced cell death in primary neuronal cultures and attenuates translocation of cytochrome c and apoptosis-inducing factor
    • Movsesyan V.A., Stoica B.A., and Faden A.I. MGLuR5 activation reduces beta-amyloid-induced cell death in primary neuronal cultures and attenuates translocation of cytochrome c and apoptosis-inducing factor. J. Neurochem. 89 (2004) 1528-1536
    • (2004) J. Neurochem. , vol.89 , pp. 1528-1536
    • Movsesyan, V.A.1    Stoica, B.A.2    Faden, A.I.3
  • 150
    • 33746827856 scopus 로고    scopus 로고
    • Different mitochondrial intermembrane space proteins are released during apoptosis in a manner that is coordinately initiated but can vary in duration
    • Munoz-Pinedo C., Guio-Carrion A., Goldstein J.C., Fitzgerald P., Newmeyer D.D., and Green D.R. Different mitochondrial intermembrane space proteins are released during apoptosis in a manner that is coordinately initiated but can vary in duration. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 11573-11578
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11573-11578
    • Munoz-Pinedo, C.1    Guio-Carrion, A.2    Goldstein, J.C.3    Fitzgerald, P.4    Newmeyer, D.D.5    Green, D.R.6
  • 151
    • 13244267045 scopus 로고    scopus 로고
    • A newly synthesized poly(ADP-ribose)polymerase inhibitor, DR2313 [2-methyl-3,5,7,8- tetrahydro-thio-pyrano[4,3-d]-pyrimidine-4-one]: pharmacological profiles, neuroprotective effects, and therapeutic time window in cerebral ischemia in rats
    • Nakajima H., Kakui N., Ohkuma K., Ishikawa M., and Hasegawa T. A newly synthesized poly(ADP-ribose)polymerase inhibitor, DR2313 [2-methyl-3,5,7,8- tetrahydro-thio-pyrano[4,3-d]-pyrimidine-4-one]: pharmacological profiles, neuroprotective effects, and therapeutic time window in cerebral ischemia in rats. J. Pharmacol. Exp. Ther. 312 (2005) 472-481
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 472-481
    • Nakajima, H.1    Kakui, N.2    Ohkuma, K.3    Ishikawa, M.4    Hasegawa, T.5
  • 152
    • 0029854806 scopus 로고    scopus 로고
    • Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1 beta-converting-enzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis
    • Nath R., Raser K.J., Stafford D., Hajimohammadreza I., Posner A., Allen H., et al. Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1 beta-converting-enzyme-like protease(s) in apoptotic cells: contributory roles of both protease families in neuronal apoptosis. Biochem. J. 319 Pt 3 (1996) 683-690
    • (1996) Biochem. J. , vol.319 , Issue.PART 3 , pp. 683-690
    • Nath, R.1    Raser, K.J.2    Stafford, D.3    Hajimohammadreza, I.4    Posner, A.5    Allen, H.6
  • 153
    • 0141499968 scopus 로고    scopus 로고
    • Flavopiridol induces mitochondrial-mediated apoptosis in murine glioma GL261 cells via release of cytochrome c and apoptosis inducing factor
    • Newcomb E.W., Tamasdan C., Entzminger Y., Alonso J., Friedlander D., Crisan D., Miller D.C., and Zagzag D. Flavopiridol induces mitochondrial-mediated apoptosis in murine glioma GL261 cells via release of cytochrome c and apoptosis inducing factor. Cell Cycle 2 (2003) 243-250
    • (2003) Cell Cycle , vol.2 , pp. 243-250
    • Newcomb, E.W.1    Tamasdan, C.2    Entzminger, Y.3    Alonso, J.4    Friedlander, D.5    Crisan, D.6    Miller, D.C.7    Zagzag, D.8
  • 154
    • 0033290849 scopus 로고    scopus 로고
    • Apoptosis and necrosis: different execution of the same death
    • Nicotera P., Leist M., and Ferrando-May E. Apoptosis and necrosis: different execution of the same death. Biochem. Soc. Symp. 66 (1999) 69-73
    • (1999) Biochem. Soc. Symp. , vol.66 , pp. 69-73
    • Nicotera, P.1    Leist, M.2    Ferrando-May, E.3
  • 155
    • 0033083559 scopus 로고    scopus 로고
    • Neuronal cell death: a demise with different shapes
    • Nicotera P., Leist M., and Manzo L. Neuronal cell death: a demise with different shapes. Trends Pharmacol. Sci. 20 (1999) 46-51
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 46-51
    • Nicotera, P.1    Leist, M.2    Manzo, L.3
  • 156
    • 34447529458 scopus 로고    scopus 로고
    • BUB1 mediation of caspase-independent mitotic death determines cell fate
    • Niikura Y., Dixit A., Scott R., Perkins G., and Kitagawa K. BUB1 mediation of caspase-independent mitotic death determines cell fate. J. Cell Biol. 178 (2007) 283-296
    • (2007) J. Cell Biol. , vol.178 , pp. 283-296
    • Niikura, Y.1    Dixit, A.2    Scott, R.3    Perkins, G.4    Kitagawa, K.5
  • 158
    • 0023905240 scopus 로고
    • Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro
    • Nishimura Y., Kawabata T., and Kato K. Identification of latent procathepsins B and L in microsomal lumen: characterization of enzymatic activation and proteolytic processing in vitro. Arch. Biochem. Biophys. 261 (1988) 64-71
    • (1988) Arch. Biochem. Biophys. , vol.261 , pp. 64-71
    • Nishimura, Y.1    Kawabata, T.2    Kato, K.3
  • 159
    • 7544243762 scopus 로고    scopus 로고
    • Geldanamycin induces mitotic catastrophe and subsequent apoptosis in human glioma cells
    • Nomura M., Nomura N., Newcomb E.W., Lukyanov Y., Tamasdan C., and Zagzag D. Geldanamycin induces mitotic catastrophe and subsequent apoptosis in human glioma cells. J. Cell. Physiol. 201 (2004) 374-384
    • (2004) J. Cell. Physiol. , vol.201 , pp. 374-384
    • Nomura, M.1    Nomura, N.2    Newcomb, E.W.3    Lukyanov, Y.4    Tamasdan, C.5    Zagzag, D.6
  • 161
    • 3543092021 scopus 로고    scopus 로고
    • Pathways of apoptotic and non-apoptotic death in tumour cells
    • Okada H., and Mak T.W. Pathways of apoptotic and non-apoptotic death in tumour cells. Nat. Rev. Cancer 4 (2004) 592-603
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 592-603
    • Okada, H.1    Mak, T.W.2
  • 162
    • 17844394478 scopus 로고    scopus 로고
    • Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space
    • Otera H., Ohsakaya S., Nagaura Z., Ishihara N., and Mihara K. Export of mitochondrial AIF in response to proapoptotic stimuli depends on processing at the intermembrane space. EMBO J. 24 (2005) 1375-1386
    • (2005) EMBO J. , vol.24 , pp. 1375-1386
    • Otera, H.1    Ohsakaya, S.2    Nagaura, Z.3    Ishihara, N.4    Mihara, K.5
  • 163
    • 0035421688 scopus 로고    scopus 로고
    • A role of the mitochondrial apoptosis-inducing factor in granulysin-induced apoptosis
    • Pardo J., Perez-Galan P., Gamen S., Marzo I., Monleon I., Kaspar A.A., et al. A role of the mitochondrial apoptosis-inducing factor in granulysin-induced apoptosis. J. Immunol. 167 (2001) 1222-1229
    • (2001) J. Immunol. , vol.167 , pp. 1222-1229
    • Pardo, J.1    Perez-Galan, P.2    Gamen, S.3    Marzo, I.4    Monleon, I.5    Kaspar, A.A.6
  • 164
    • 13544276189 scopus 로고    scopus 로고
    • Phytosphingosine in combination with ionizing radiation enhances apoptotic cell death in radiation-resistant cancer cells through ROS-dependent and -independent AIF release
    • Park M.T., Kim M.J., Kang Y.H., Choi S.Y., Lee J.H., Choi J.A., et al. Phytosphingosine in combination with ionizing radiation enhances apoptotic cell death in radiation-resistant cancer cells through ROS-dependent and -independent AIF release. Blood 105 (2005) 1724-1733
    • (2005) Blood , vol.105 , pp. 1724-1733
    • Park, M.T.1    Kim, M.J.2    Kang, Y.H.3    Choi, S.Y.4    Lee, J.H.5    Choi, J.A.6
  • 165
    • 23144445839 scopus 로고    scopus 로고
    • Sulindac activates nuclear translocation of AIF. DFF40 and Endonuclease G but not induces oligonucleosomal DNA fragmentation in HT-29 cells
    • Park Y.C., Jeong J.H., Park K.J., Choi H.J., Park Y.M., Jeong B.K., Higuchi Y., and Yoo Y.H. Sulindac activates nuclear translocation of AIF. DFF40 and Endonuclease G but not induces oligonucleosomal DNA fragmentation in HT-29 cells. Life Sci. 77 (2005) 2059-2070
    • (2005) Life Sci. , vol.77 , pp. 2059-2070
    • Park, Y.C.1    Jeong, J.H.2    Park, K.J.3    Choi, H.J.4    Park, Y.M.5    Jeong, B.K.6    Higuchi, Y.7    Yoo, Y.H.8
  • 166
    • 0036799354 scopus 로고    scopus 로고
    • Role of caspases and apoptosis-inducing factor (AIF) in cladribine-induced apoptosis of B cell chronic lymphocytic leukemia
    • Perez-Galan P., Marzo I., Giraldo P., Rubio-Felix D., Lasierra P., Larrad L., Anel A., and Naval J. Role of caspases and apoptosis-inducing factor (AIF) in cladribine-induced apoptosis of B cell chronic lymphocytic leukemia. Leukemia 16 (2002) 2106-2114
    • (2002) Leukemia , vol.16 , pp. 2106-2114
    • Perez-Galan, P.1    Marzo, I.2    Giraldo, P.3    Rubio-Felix, D.4    Lasierra, P.5    Larrad, L.6    Anel, A.7    Naval, J.8
  • 167
    • 0037448064 scopus 로고    scopus 로고
    • Prevention of oxidant-induced cell death by lysosomotropic iron chelators
    • Persson H.L., Yu Z., Tirosh O., Eaton J.W., and Brunk U.T. Prevention of oxidant-induced cell death by lysosomotropic iron chelators. Free Radic. Biol. Med. 34 (2003) 1295-1305
    • (2003) Free Radic. Biol. Med. , vol.34 , pp. 1295-1305
    • Persson, H.L.1    Yu, Z.2    Tirosh, O.3    Eaton, J.W.4    Brunk, U.T.5
  • 168
    • 12344289049 scopus 로고    scopus 로고
    • Increased expression of poly(ADP-ribose) polymerase-1 contributes to caspase-independent myocyte cell death during heart failure
    • Pillai J.B., Russell H.M., Raman J., Jeevanandam V., and Gupta M.P. Increased expression of poly(ADP-ribose) polymerase-1 contributes to caspase-independent myocyte cell death during heart failure. Am. J. Physiol. Heart Circ. Physiol. 288 (2005) H486-H496
    • (2005) Am. J. Physiol. Heart Circ. Physiol. , vol.288
    • Pillai, J.B.1    Russell, H.M.2    Raman, J.3    Jeevanandam, V.4    Gupta, M.P.5
  • 169
    • 4544355019 scopus 로고    scopus 로고
    • Role of mitochondrial proteins for neuronal cell death after focal cerebral ischemia
    • Plesnila N. Role of mitochondrial proteins for neuronal cell death after focal cerebral ischemia. Acta Neurochir. Suppl. 89 (2004) 15-19
    • (2004) Acta Neurochir. Suppl. , vol.89 , pp. 15-19
    • Plesnila, N.1
  • 170
    • 14844328621 scopus 로고    scopus 로고
    • Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria
    • Polster B.M., Basanez G., Etxebarria A., Hardwick J.M., and Nicholls D.G. Calpain I induces cleavage and release of apoptosis-inducing factor from isolated mitochondria. J. Biol. Chem. 280 (2005) 6447-6454
    • (2005) J. Biol. Chem. , vol.280 , pp. 6447-6454
    • Polster, B.M.1    Basanez, G.2    Etxebarria, A.3    Hardwick, J.M.4    Nicholls, D.G.5
  • 172
    • 33846610017 scopus 로고    scopus 로고
    • Expression of cortical and hippocampal apoptosis-inducing factor (AIF) in aging and Alzheimer's disease
    • Reix S., Mechawar N., Susin S.A., Quirion R., and Krantic S. Expression of cortical and hippocampal apoptosis-inducing factor (AIF) in aging and Alzheimer's disease. Neurobiol. Aging 28 (2007) 351-356
    • (2007) Neurobiol. Aging , vol.28 , pp. 351-356
    • Reix, S.1    Mechawar, N.2    Susin, S.A.3    Quirion, R.4    Krantic, S.5
  • 173
    • 0036310279 scopus 로고    scopus 로고
    • Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts
    • Roberg K., Kagedal K., and Ollinger K. Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts. Am. J. Pathol. 161 (2002) 89-96
    • (2002) Am. J. Pathol. , vol.161 , pp. 89-96
    • Roberg, K.1    Kagedal, K.2    Ollinger, K.3
  • 174
    • 0026664252 scopus 로고
    • Rat procathepsin B. Proteolytic processing to the mature form in vitro
    • Rowan A.D., Mason P., Mach L., and Mort J.S. Rat procathepsin B. Proteolytic processing to the mature form in vitro. J. Biol. Chem. 267 (1992) 15993-15999
    • (1992) J. Biol. Chem. , vol.267 , pp. 15993-15999
    • Rowan, A.D.1    Mason, P.2    Mach, L.3    Mort, J.S.4
  • 175
    • 33646384157 scopus 로고    scopus 로고
    • Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation
    • Ruchalski K., Mao H., Li Z., Wang Z., Gillers S., Wang Y., et al. Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation. J. Biol. Chem. 281 (2006) 7873-7880
    • (2006) J. Biol. Chem. , vol.281 , pp. 7873-7880
    • Ruchalski, K.1    Mao, H.2    Li, Z.3    Wang, Z.4    Gillers, S.5    Wang, Y.6
  • 178
    • 33748902211 scopus 로고    scopus 로고
    • The therapeutic potential of the calpain family: new aspects
    • Saez M.E., Ramirez-Lorca R., Moron F.J., and Ruiz A. The therapeutic potential of the calpain family: new aspects. Drug Discov. Today 11 (2006) 917-923
    • (2006) Drug Discov. Today , vol.11 , pp. 917-923
    • Saez, M.E.1    Ramirez-Lorca, R.2    Moron, F.J.3    Ruiz, A.4
  • 179
    • 33751239138 scopus 로고    scopus 로고
    • Apoptosis in retinal degeneration involves cross-talk between apoptosis-inducing factor (AIF) and caspase-12 and is blocked by calpain inhibitors
    • Sanges D., Comitato A., Tammaro R., and Marigo V. Apoptosis in retinal degeneration involves cross-talk between apoptosis-inducing factor (AIF) and caspase-12 and is blocked by calpain inhibitors. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 17366-17371
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 17366-17371
    • Sanges, D.1    Comitato, A.2    Tammaro, R.3    Marigo, V.4
  • 180
    • 33747415096 scopus 로고    scopus 로고
    • Cross-talk between two apoptotic pathways activated by endoplasmic reticulum stress: differential contribution of caspase-12 and AIF
    • Sanges D., and Marigo V. Cross-talk between two apoptotic pathways activated by endoplasmic reticulum stress: differential contribution of caspase-12 and AIF. Apoptosis 11 (2006) 1629-1641
    • (2006) Apoptosis , vol.11 , pp. 1629-1641
    • Sanges, D.1    Marigo, V.2
  • 182
    • 0032490091 scopus 로고    scopus 로고
    • Human complex I defects in neurodegenerative diseases
    • Schapira A.H. Human complex I defects in neurodegenerative diseases. Biochim. Biophys. Acta 1364 (1998) 261-270
    • (1998) Biochim. Biophys. Acta , vol.1364 , pp. 261-270
    • Schapira, A.H.1
  • 183
    • 10744227948 scopus 로고    scopus 로고
    • Chemosensitization by a non-apoptogenic heat shock protein 70-binding apoptosis-inducing factor mutant
    • Schmitt E., Parcellier A., Gurbuxani S., Cande C., Hammann A., Morales M.C., et al. Chemosensitization by a non-apoptogenic heat shock protein 70-binding apoptosis-inducing factor mutant. Cancer Res. 63 (2003) 8233-8240
    • (2003) Cancer Res. , vol.63 , pp. 8233-8240
    • Schmitt, E.1    Parcellier, A.2    Gurbuxani, S.3    Cande, C.4    Hammann, A.5    Morales, M.C.6
  • 184
    • 0015880897 scopus 로고
    • The morphology of various types of cell death in prenatal tissues
    • Schweichel J.U., and Merker H.J. The morphology of various types of cell death in prenatal tissues. Teratology 7 (1973) 253-266
    • (1973) Teratology , vol.7 , pp. 253-266
    • Schweichel, J.U.1    Merker, H.J.2
  • 186
    • 0034733928 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model?
    • Shall S., and de Murcia G. Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model?. Mutat. Res. 460 (2000) 1-15
    • (2000) Mutat. Res. , vol.460 , pp. 1-15
    • Shall, S.1    de Murcia, G.2
  • 187
    • 33645802169 scopus 로고    scopus 로고
    • Cyclin-dependent kinase pathways as targets for cancer treatment
    • Shapiro G.I. Cyclin-dependent kinase pathways as targets for cancer treatment. J. Clin. Oncol. 24 (2006) 1770-1783
    • (2006) J. Clin. Oncol. , vol.24 , pp. 1770-1783
    • Shapiro, G.I.1
  • 189
    • 33751169811 scopus 로고    scopus 로고
    • Involvement of caspase activation and mitochondrial stress in trichostatin A-induced apoptosis of Burkitt's lymphoma cell line
    • Son Y.O., Choi K.C., Lee J.C., Kook S.H., Lee H.J., Jeon Y.M., et al. Involvement of caspase activation and mitochondrial stress in trichostatin A-induced apoptosis of Burkitt's lymphoma cell line. Akata J. Cell. Biochem. 99 (2006) 1420-1430
    • (2006) Akata J. Cell. Biochem. , vol.99 , pp. 1420-1430
    • Son, Y.O.1    Choi, K.C.2    Lee, J.C.3    Kook, S.H.4    Lee, H.J.5    Jeon, Y.M.6
  • 190
    • 0034992155 scopus 로고    scopus 로고
    • The structure of calpain
    • Sorimachi H., and Suzuki K. The structure of calpain. J. Biochem. 129 (2001) 653-664
    • (2001) J. Biochem. , vol.129 , pp. 653-664
    • Sorimachi, H.1    Suzuki, K.2
  • 192
    • 0035793580 scopus 로고    scopus 로고
    • Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route
    • Stoka V., Turk B., Schendel S.L., Kim T.H., Cirman T., Snipas S.J., et al. Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J. Biol. Chem. 276 (2001) 3149-3157
    • (2001) J. Biol. Chem. , vol.276 , pp. 3149-3157
    • Stoka, V.1    Turk, B.2    Schendel, S.L.3    Kim, T.H.4    Cirman, T.5    Snipas, S.J.6
  • 193
    • 21344455498 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: structural features and their role in apoptosis
    • Stoka V., Turk B., and Turk V. Lysosomal cysteine proteases: structural features and their role in apoptosis. IUBMB Life 57 (2005) 347-353
    • (2005) IUBMB Life , vol.57 , pp. 347-353
    • Stoka, V.1    Turk, B.2    Turk, V.3
  • 194
    • 33645528734 scopus 로고    scopus 로고
    • Effect of 3-aminobenzamide on Bcl-2. Bax and AIF localization in hippocampal neurons altered by ischemia-reperfusion injury. the immunocytochemical study
    • Strosznajder R., and Gajkowska B. Effect of 3-aminobenzamide on Bcl-2. Bax and AIF localization in hippocampal neurons altered by ischemia-reperfusion injury. the immunocytochemical study. Acta Neurobiol. Exp. 66 (2006) 15-22
    • (2006) Acta Neurobiol. Exp. , vol.66 , pp. 15-22
    • Strosznajder, R.1    Gajkowska, B.2
  • 197
  • 198
    • 0030785790 scopus 로고    scopus 로고
    • The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis
    • Susin S.A., Zamzami N., Castedo M., Daugas E., Wang H.G., Geley S., Fassy F., Reed J.C., and Kroemer G. The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis. J. Exp. Med. 186 (1997) 25-37
    • (1997) J. Exp. Med. , vol.186 , pp. 25-37
    • Susin, S.A.1    Zamzami, N.2    Castedo, M.3    Daugas, E.4    Wang, H.G.5    Geley, S.6    Fassy, F.7    Reed, J.C.8    Kroemer, G.9
  • 200
    • 0032504575 scopus 로고    scopus 로고
    • Mitochondria as regulators of apoptosis: doubt no more
    • Susin S.A., Zamzami N., and Kroemer G. Mitochondria as regulators of apoptosis: doubt no more. Biochim. Biophys. Acta 1366 (1998) 151-165
    • (1998) Biochim. Biophys. Acta , vol.1366 , pp. 151-165
    • Susin, S.A.1    Zamzami, N.2    Kroemer, G.3
  • 202
    • 0033594743 scopus 로고    scopus 로고
    • Post-treatment with an inhibitor of poly(ADP-ribose) polymerase attenuates cerebral damage in focal ischemia
    • Takahashi K., Pieper A.A., Croul S.E., Zhang J., Snyder S.H., and Greenberg J.H. Post-treatment with an inhibitor of poly(ADP-ribose) polymerase attenuates cerebral damage in focal ischemia. Brain Res. 829 (1999) 46-54
    • (1999) Brain Res. , vol.829 , pp. 46-54
    • Takahashi, K.1    Pieper, A.A.2    Croul, S.E.3    Zhang, J.4    Snyder, S.H.5    Greenberg, J.H.6
  • 203
    • 18144407551 scopus 로고    scopus 로고
    • Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice
    • Takano J., Tomioka M., Tsubuki S., Higuchi M., Iwata N., Itohara S., Maki M., and Saido T.C. Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin mutant mice. J. Biol. Chem. 280 (2005) 16175-16184
    • (2005) J. Biol. Chem. , vol.280 , pp. 16175-16184
    • Takano, J.1    Tomioka, M.2    Tsubuki, S.3    Higuchi, M.4    Iwata, N.5    Itohara, S.6    Maki, M.7    Saido, T.C.8
  • 204
    • 33745686005 scopus 로고    scopus 로고
    • Conditional disruption of ubiquitous calpains in the mouse
    • Tan Y., Dourdin N., Wu C., De Veyra T., Elce J.S., and Greer P.A. Conditional disruption of ubiquitous calpains in the mouse. Genesis 44 (2006) 297-303
    • (2006) Genesis , vol.44 , pp. 297-303
    • Tan, Y.1    Dourdin, N.2    Wu, C.3    De Veyra, T.4    Elce, J.S.5    Greer, P.A.6
  • 206
    • 6944234914 scopus 로고    scopus 로고
    • Caspase-independent component of retinal ganglion cell death, in vitro
    • Tezel G., and Yang X. Caspase-independent component of retinal ganglion cell death, in vitro. Invest. Ophthalmol. Vis. Sci. 45 (2004) 4049-4059
    • (2004) Invest. Ophthalmol. Vis. Sci. , vol.45 , pp. 4049-4059
    • Tezel, G.1    Yang, X.2
  • 207
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • Thompson C.B. Apoptosis in the pathogenesis and treatment of disease. Science 267 (1995) 1456-1462
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 208
    • 33750292822 scopus 로고    scopus 로고
    • The murine TRAIL receptor signals caspase-independent cell death through ceramide
    • Thon L., Mathieu S., Kabelitz D., and Adam D. The murine TRAIL receptor signals caspase-independent cell death through ceramide. Exp. Cell Res. 312 (2006) 3808-3821
    • (2006) Exp. Cell Res. , vol.312 , pp. 3808-3821
    • Thon, L.1    Mathieu, S.2    Kabelitz, D.3    Adam, D.4
  • 210
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: enemies within
    • Thornberry N.A., and Lazebnik Y. Caspases: enemies within. Science 281 (1998) 1312-1316
    • (1998) Science , vol.281 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 211
    • 33845539936 scopus 로고    scopus 로고
    • Activation of poly(ADP-ribose) polymerase by myocardial ischemia and coronary reperfusion in human circulating leukocytes
    • Toth-Zsamboki E., Horvath E., Vargova K., Pankotai E., Murthy K., Zsengeller Z., et al. Activation of poly(ADP-ribose) polymerase by myocardial ischemia and coronary reperfusion in human circulating leukocytes. Mol. Med. 12 (2006) 221-228
    • (2006) Mol. Med. , vol.12 , pp. 221-228
    • Toth-Zsamboki, E.1    Horvath, E.2    Vargova, K.3    Pankotai, E.4    Murthy, K.5    Zsengeller, Z.6
  • 212
    • 0037469097 scopus 로고    scopus 로고
    • Calpain-induced Bax-cleavage product is a more potent inducer of apoptotic cell death than wild-type Bax
    • Toyota H., Yanase N., Yoshimoto T., Moriyama M., Sudo T., and Mizuguchi J. Calpain-induced Bax-cleavage product is a more potent inducer of apoptotic cell death than wild-type Bax. Cancer Lett. 189 (2003) 221-230
    • (2003) Cancer Lett. , vol.189 , pp. 221-230
    • Toyota, H.1    Yanase, N.2    Yoshimoto, T.3    Moriyama, M.4    Sudo, T.5    Mizuguchi, J.6
  • 213
    • 33745968813 scopus 로고    scopus 로고
    • Cathepsin and calpain inhibitor E64d attenuates matrix metalloproteinase-9 activity after focal cerebral ischemia in rats
    • Tsubokawa T., Solaroglu I., Yatsushige H., Cahill J., Yata K., and Zhang J.H. Cathepsin and calpain inhibitor E64d attenuates matrix metalloproteinase-9 activity after focal cerebral ischemia in rats. Stroke 37 (2006) 1888-1894
    • (2006) Stroke , vol.37 , pp. 1888-1894
    • Tsubokawa, T.1    Solaroglu, I.2    Yatsushige, H.3    Cahill, J.4    Yata, K.5    Zhang, J.H.6
  • 214
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: successes, failures and future prospects
    • Turk B. Targeting proteases: successes, failures and future prospects. Nat. Rev. Drug Discov. 5 (2006) 785-799
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 215
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: more than scavengers
    • Turk B., Turk D., and Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta 1477 (2000) 98-111
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 216
    • 2342551977 scopus 로고    scopus 로고
    • Cysteine cathepsins (proteases)-on the main stage of cancer?
    • Turk V., Kos J., and Turk B. Cysteine cathepsins (proteases)-on the main stage of cancer?. Cancer Cell 5 (2004) 409-410
    • (2004) Cancer Cell , vol.5 , pp. 409-410
    • Turk, V.1    Kos, J.2    Turk, B.3
  • 217
    • 0036374209 scopus 로고    scopus 로고
    • Lysosomal cathepsins: structure, role in antigen processing and presentation, and cancer
    • Turk V., Turk B., Guncar G., Turk D., and Kos J. Lysosomal cathepsins: structure, role in antigen processing and presentation, and cancer. Adv. Enzyme Regul. 42 (2002) 285-303
    • (2002) Adv. Enzyme Regul. , vol.42 , pp. 285-303
    • Turk, V.1    Turk, B.2    Guncar, G.3    Turk, D.4    Kos, J.5
  • 218
    • 12544251669 scopus 로고    scopus 로고
    • Mitochondrial release of pro-apoptotic proteins: electrostatic interactions can hold cytochrome c but not Smac/DIABLO to mitochondrial membranes
    • Uren R.T., Dewson G., Bonzon C., Lithgow T., Newmeyer D.D., and Kluck R.M. Mitochondrial release of pro-apoptotic proteins: electrostatic interactions can hold cytochrome c but not Smac/DIABLO to mitochondrial membranes. J. Biol. Chem. 280 (2005) 2266-2274
    • (2005) J. Biol. Chem. , vol.280 , pp. 2266-2274
    • Uren, R.T.1    Dewson, G.2    Bonzon, C.3    Lithgow, T.4    Newmeyer, D.D.5    Kluck, R.M.6
  • 221
    • 19544392547 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 mediated caspase-independent cell death after ischemia/reperfusion
    • van Wijk S.J., and Hageman G.J. Poly(ADP-ribose) polymerase-1 mediated caspase-independent cell death after ischemia/reperfusion. Free Radic. Biol. Med. 39 (2005) 81-90
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 81-90
    • van Wijk, S.J.1    Hageman, G.J.2
  • 222
    • 34250341608 scopus 로고    scopus 로고
    • NADPH oxidases: new players in TNF-induced necrotic cell death
    • Vanden Berghe T., Declercq W., and Vandenabeele P. NADPH oxidases: new players in TNF-induced necrotic cell death. Mol. Cell 26 (2007) 769-771
    • (2007) Mol. Cell , vol.26 , pp. 769-771
    • Vanden Berghe, T.1    Declercq, W.2    Vandenabeele, P.3
  • 224
    • 0142148159 scopus 로고    scopus 로고
    • Protective effect of amiodarone but not N-desethylamiodarone on postischemic hearts through the inhibition of mitochondrial permeability transition
    • Varbiro G., Toth A., Tapodi A., Bognar Z., Veres B., Sumegi B., and Gallyas Jr. F. Protective effect of amiodarone but not N-desethylamiodarone on postischemic hearts through the inhibition of mitochondrial permeability transition. J. Pharmacol. Exp. Ther. 307 (2003) 615-625
    • (2003) J. Pharmacol. Exp. Ther. , vol.307 , pp. 615-625
    • Varbiro, G.1    Toth, A.2    Tapodi, A.3    Bognar, Z.4    Veres, B.5    Sumegi, B.6    Gallyas Jr., F.7
  • 225
    • 0036733355 scopus 로고    scopus 로고
    • The therapeutic potential of poly(ADP-ribose) polymerase inhibitors
    • Virag L., and Szabo C. The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Pharmacol. Rev. 54 (2002) 375-429
    • (2002) Pharmacol. Rev. , vol.54 , pp. 375-429
    • Virag, L.1    Szabo, C.2
  • 227
    • 34249996013 scopus 로고    scopus 로고
    • Atiprimod inhibits the growth of mantle cell lymphoma in vitro and in vivo and induces apoptosis via activating the mitochondrial pathways
    • Wang M., Zhang L., Han X., Yang J., Qian J., Hong S., Samaniego F., Romaguera J., and Yi Q. Atiprimod inhibits the growth of mantle cell lymphoma in vitro and in vivo and induces apoptosis via activating the mitochondrial pathways. Blood 109 (2007) 5455-5462
    • (2007) Blood , vol.109 , pp. 5455-5462
    • Wang, M.1    Zhang, L.2    Han, X.3    Yang, J.4    Qian, J.5    Hong, S.6    Samaniego, F.7    Romaguera, J.8    Yi, Q.9
  • 228
    • 34247862351 scopus 로고    scopus 로고
    • C. elegans mitochondrial factor WAH-1 promotes phosphatidylserine externalization in apoptotic cells through phospholipid scramblase SCRM-1
    • Wang X., Wang J., Gengyo-Ando K., Gu L., Sun C.L., Yang C., et al. C. elegans mitochondrial factor WAH-1 promotes phosphatidylserine externalization in apoptotic cells through phospholipid scramblase SCRM-1. Nat. Cell Biol. 9 (2007) 541-549
    • (2007) Nat. Cell Biol. , vol.9 , pp. 541-549
    • Wang, X.1    Wang, J.2    Gengyo-Ando, K.3    Gu, L.4    Sun, C.L.5    Yang, C.6
  • 229
    • 0037159784 scopus 로고    scopus 로고
    • Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans
    • Wang X., Yang C., Chai J., Shi Y., and Xue D. Mechanisms of AIF-mediated apoptotic DNA degradation in Caenorhabditis elegans. Science 298 (2002) 1587-1592
    • (2002) Science , vol.298 , pp. 1587-1592
    • Wang, X.1    Yang, C.2    Chai, J.3    Shi, Y.4    Xue, D.5
  • 231
    • 0042195867 scopus 로고    scopus 로고
    • Non-apoptogenic killing of hela cervical carcinoma cells after short exposure to the alkylating agent N-methyl-N′-nitro-N-nitrosoguanidine (MNNG)
    • Wesierska-Gadek J., Gueorguieva M., Schloffer D., Uhl M., and Wojciechowski J. Non-apoptogenic killing of hela cervical carcinoma cells after short exposure to the alkylating agent N-methyl-N′-nitro-N-nitrosoguanidine (MNNG). J. Cell. Biochem. 89 (2003) 1222-1234
    • (2003) J. Cell. Biochem. , vol.89 , pp. 1222-1234
    • Wesierska-Gadek, J.1    Gueorguieva, M.2    Schloffer, D.3    Uhl, M.4    Wojciechowski, J.5
  • 233
    • 14344266084 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase promotes cardiac remodeling, contractile failure, and translocation of apoptosis-inducing factor in a murine experimental model of aortic banding and heart failure
    • Xiao C.Y., Chen M., Zsengeller Z., Li H., Kiss L., Kollai M., and Szabo C. Poly(ADP-ribose) polymerase promotes cardiac remodeling, contractile failure, and translocation of apoptosis-inducing factor in a murine experimental model of aortic banding and heart failure. J. Pharmacol. Exp. Ther. 312 (2005) 891-898
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 891-898
    • Xiao, C.Y.1    Chen, M.2    Zsengeller, Z.3    Li, H.4    Kiss, L.5    Kollai, M.6    Szabo, C.7
  • 234
    • 3342958962 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase contributes to the development of myocardial infarction in diabetic rats and regulates the nuclear translocation of apoptosis-inducing factor
    • Xiao C.Y., Chen M., Zsengeller Z., and Szabo C. Poly(ADP-ribose) polymerase contributes to the development of myocardial infarction in diabetic rats and regulates the nuclear translocation of apoptosis-inducing factor. J. Pharmacol. Exp. Ther. 310 (2004) 498-504
    • (2004) J. Pharmacol. Exp. Ther. , vol.310 , pp. 498-504
    • Xiao, C.Y.1    Chen, M.2    Zsengeller, Z.3    Szabo, C.4
  • 235
    • 33646827842 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 signaling to mitochondria in necrotic cell death requires RIP1/TRAF2-mediated JNK1 activation
    • Xu Y., Huang S., Liu Z.G., and Han J. Poly(ADP-ribose) polymerase-1 signaling to mitochondria in necrotic cell death requires RIP1/TRAF2-mediated JNK1 activation. J. Biol. Chem. 281 (2006) 8788-8795
    • (2006) J. Biol. Chem. , vol.281 , pp. 8788-8795
    • Xu, Y.1    Huang, S.2    Liu, Z.G.3    Han, J.4
  • 236
    • 33746238112 scopus 로고    scopus 로고
    • OSU-03012 promotes caspase-independent but PERK-, cathepsin B-, BID-, and AIF-dependent killing of transformed cells
    • Yacoub A., Park M.A., Hanna D., Hong Y., Mitchell C., Pandya A.P., et al. OSU-03012 promotes caspase-independent but PERK-, cathepsin B-, BID-, and AIF-dependent killing of transformed cells. Mol. Pharmacol. 70 (2006) 589-603
    • (2006) Mol. Pharmacol. , vol.70 , pp. 589-603
    • Yacoub, A.1    Park, M.A.2    Hanna, D.3    Hong, Y.4    Mitchell, C.5    Pandya, A.P.6
  • 238
    • 33745244111 scopus 로고    scopus 로고
    • Restoring p53-mediated apoptosis in cancer cells: new opportunities for cancer therapy
    • Yu Q. Restoring p53-mediated apoptosis in cancer cells: new opportunities for cancer therapy. Drug Resist. Updates 9 (2006) 19-25
    • (2006) Drug Resist. Updates , vol.9 , pp. 19-25
    • Yu, Q.1
  • 240
    • 0348109491 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 and apoptosis inducing factor in neurotoxicity
    • Yu S.W., Wang H., Dawson T.M., and Dawson V.L. Poly(ADP-ribose) polymerase-1 and apoptosis inducing factor in neurotoxicity. Neurobiol. Dis. 14 (2003) 303-317
    • (2003) Neurobiol. Dis. , vol.14 , pp. 303-317
    • Yu, S.W.1    Wang, H.2    Dawson, T.M.3    Dawson, V.L.4
  • 241
    • 0037067317 scopus 로고    scopus 로고
    • Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor
    • Yu S.W., Wang H., Poitras M.F., Coombs C., Bowers W.J., Federoff H.J., et al. Mediation of poly(ADP-ribose) polymerase-1-dependent cell death by apoptosis-inducing factor. Science 297 (2002) 259-263
    • (2002) Science , vol.297 , pp. 259-263
    • Yu, S.W.1    Wang, H.2    Poitras, M.F.3    Coombs, C.4    Bowers, W.J.5    Federoff, H.J.6
  • 242
    • 0141884305 scopus 로고    scopus 로고
    • Diversity in the mechanisms of neuronal cell death
    • Yuan J., Lipinski M., and Degterev A. Diversity in the mechanisms of neuronal cell death. Neuron 40 (2003) 401-413
    • (2003) Neuron , vol.40 , pp. 401-413
    • Yuan, J.1    Lipinski, M.2    Degterev, A.3
  • 244
    • 27444441304 scopus 로고    scopus 로고
    • The contribution of apoptosis-inducing factor, caspase-activated DNase, and inhibitor of caspase-activated DNase to the nuclear phenotype and DNA
    • Yuste V.J., Sanchez-Lopez I., Sole C., Moubarak R.S., Bayascas J.R., Dolcet X., Encinas M., Susin S.A., and Comella J.X. The contribution of apoptosis-inducing factor, caspase-activated DNase, and inhibitor of caspase-activated DNase to the nuclear phenotype and DNA. J. Biol. Chem. 280 (2005) 35670-35683
    • (2005) J. Biol. Chem. , vol.280 , pp. 35670-35683
    • Yuste, V.J.1    Sanchez-Lopez, I.2    Sole, C.3    Moubarak, R.S.4    Bayascas, J.R.5    Dolcet, X.6    Encinas, M.7    Susin, S.A.8    Comella, J.X.9
  • 245
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: how Pandora's box opens
    • Zamzami N., and Kroemer G. The mitochondrion in apoptosis: how Pandora's box opens. Nat. Rev. Mol. Cell. Biol. 2 (2001) 67-71
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 247
    • 24644461049 scopus 로고    scopus 로고
    • Caspase-independent death of Leber's hereditary optic neuropathy cybrids is driven by energetic failure and mediated by AIF and Endonuclease G
    • Zanna C., Ghelli A., Porcelli A.M., Martinuzzi A., Carelli V., and Rugolo M. Caspase-independent death of Leber's hereditary optic neuropathy cybrids is driven by energetic failure and mediated by AIF and Endonuclease G. Apoptosis 10 (2005) 997-1007
    • (2005) Apoptosis , vol.10 , pp. 997-1007
    • Zanna, C.1    Ghelli, A.2    Porcelli, A.M.3    Martinuzzi, A.4    Carelli, V.5    Rugolo, M.6
  • 248
    • 34548060313 scopus 로고    scopus 로고
    • OSU-03012, a novel celecoxib derivative, is cytotoxic to myeloma cells and acts through multiple mechanisms
    • Zhang S., Suvannasankha A., Crean C.D., White V.L., Johnson A., Chen C.S., and Farag S.S. OSU-03012, a novel celecoxib derivative, is cytotoxic to myeloma cells and acts through multiple mechanisms. Clin. Cancer Res. 13 (2007) 4750-4758
    • (2007) Clin. Cancer Res. , vol.13 , pp. 4750-4758
    • Zhang, S.1    Suvannasankha, A.2    Crean, C.D.3    White, V.L.4    Johnson, A.5    Chen, C.S.6    Farag, S.S.7
  • 249
    • 20244364788 scopus 로고    scopus 로고
    • Intranuclear localization of apoptosis-inducing factor (AIF) and large scale DNA fragmentation after traumatic brain injury in rats and in neuronal cultures exposed to peroxynitrite
    • Zhang X., Chen J., Graham S.H., Du L., Kochanek P.M., Draviam R., et al. Intranuclear localization of apoptosis-inducing factor (AIF) and large scale DNA fragmentation after traumatic brain injury in rats and in neuronal cultures exposed to peroxynitrite. J. Neurochem. 82 (2002) 181-191
    • (2002) J. Neurochem. , vol.82 , pp. 181-191
    • Zhang, X.1    Chen, J.2    Graham, S.H.3    Du, L.4    Kochanek, P.M.5    Draviam, R.6
  • 250
    • 2642560525 scopus 로고    scopus 로고
    • Bcl-2 transfection via herpes simplex virus blocks apoptosis-inducing factor translocation after focal ischemia in the rat
    • Zhao H., Yenari M.A., Cheng D., Barreto-Chang O.L., Sapolsky R.M., and Steinberg G.K. Bcl-2 transfection via herpes simplex virus blocks apoptosis-inducing factor translocation after focal ischemia in the rat. J. Cereb. Blood Flow Metab. 24 (2004) 681-692
    • (2004) J. Cereb. Blood Flow Metab. , vol.24 , pp. 681-692
    • Zhao, H.1    Yenari, M.A.2    Cheng, D.3    Barreto-Chang, O.L.4    Sapolsky, R.M.5    Steinberg, G.K.6
  • 251
    • 0038493644 scopus 로고    scopus 로고
    • Involvement of apoptosis-inducing factor in neuronal death after hypoxia-ischemia in the neonatal rat brain
    • Zhu C., Qiu L., Wang X., Hallin U., Cande C., Kroemer G., Hagberg H., and Blomgren K. Involvement of apoptosis-inducing factor in neuronal death after hypoxia-ischemia in the neonatal rat brain. J. Neurochem. 86 (2003) 306-317
    • (2003) J. Neurochem. , vol.86 , pp. 306-317
    • Zhu, C.1    Qiu, L.2    Wang, X.3    Hallin, U.4    Cande, C.5    Kroemer, G.6    Hagberg, H.7    Blomgren, K.8
  • 252
    • 34547759778 scopus 로고    scopus 로고
    • Cyclophilin A participates in the nuclear translocation of apoptosis-inducing factor in neurons after cerebral hypoxia-ischemia
    • Zhu C., Wang X., Deinum J., Huang Z., Gao J., Modjtahedi N., et al. Cyclophilin A participates in the nuclear translocation of apoptosis-inducing factor in neurons after cerebral hypoxia-ischemia. J. Exp. Med. 204 (2007) 1741-1748
    • (2007) J. Exp. Med. , vol.204 , pp. 1741-1748
    • Zhu, C.1    Wang, X.2    Deinum, J.3    Huang, Z.4    Gao, J.5    Modjtahedi, N.6
  • 253
    • 33947406873 scopus 로고    scopus 로고
    • Apoptosis-inducing factor is a major contributor to neuronal loss induced by neonatal cerebral hypoxia-ischemia
    • Zhu C., Wang X., Huang Z., Qiu L., Xu F., Vahsen N., et al. Apoptosis-inducing factor is a major contributor to neuronal loss induced by neonatal cerebral hypoxia-ischemia. Cell Death Differ. 14 (2007) 775-784
    • (2007) Cell Death Differ. , vol.14 , pp. 775-784
    • Zhu, C.1    Wang, X.2    Huang, Z.3    Qiu, L.4    Xu, F.5    Vahsen, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.