메뉴 건너뛰기




Volumn 115, Issue 10, 2005, Pages 2610-2617

Pharmacological manipulation of cell death: Clinical applications in sight?

Author keywords

[No Author keywords available]

Indexed keywords

3 [2 [(2 TERT BUTYLPHENYLAMINOOXALYL)AMINO]PROPIONYLAMINO] 4 OXO 5 (2,3,5,6 TETRAFLUOROPHENOXY)PENTANOIC ACID; ADALIMUMAB; ADVEXIN; AEG 35156; AGO 14699; AMIFOSTINE; ANTIOXIDANT; APOPTOSIS INHIBITOR; BENZYLOXYCARBONYLASPARTYLGLUTAMYLVALYLASPARTYL FLUOROMETHYL KETONE; BENZYLOXYCARBONYLVALYLALANYLASPARTYL FLUOROMETHYL KETONE; BORTEZOMIB; CARRIER PROTEIN; CASPASE INHIBITOR; CEP 1347; CETUXIMAB; CISPLATIN; DEATH RECEPTOR; ERLOTINIB; ETANERCEPT; GEFITINIB; GOSSYPOL; IDEBENONE; IDN 6734; IMATINIB; INFLIXIMAB; INO 1001; ISIS 104828; LY 2181308; MINOCYCLINE; MITOCHONDRIAL OUTER MEMBRANE PERMEABILIZATION INHIBITOR; NICOTINAMIDE; NORPHENAZONE; OBLIMERSEN; ONYX 015; PRALNACASAN; PRO 1764; PROTEIN INHIBITOR; PROTEINASE; RASAGILINE; SCH 58500; SORAFENIB; TEMSIROLIMUS; TRANSCRIPTION FACTOR; TRASTUZUMAB; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 26444434342     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI26321     Document Type: Review
Times cited : (229)

References (78)
  • 1
    • 0019225636 scopus 로고
    • Cell death: The significance of apoptosis
    • Wyllie, A.M., Kerr, J.F., and Currie, A.R. 1980. Cell death: the significance of apoptosis. Int. Rev. Cytol. 68:251-306.
    • (1980) Int. Rev. Cytol. , vol.68 , pp. 251-306
    • Wyllie, A.M.1    Kerr, J.F.2    Currie, A.R.3
  • 2
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior, P., and Salvesen, G.S. 2004. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384:201-232.
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 3
    • 2342453921 scopus 로고    scopus 로고
    • Death receptors in chemotherapy and cancer
    • Debatin, K.M., and Krammer, P.H. 2004. Death receptors in chemotherapy and cancer. Oncogene. 23:2950-2966.
    • (2004) Oncogene , vol.23 , pp. 2950-2966
    • Debatin, K.M.1    Krammer, P.H.2
  • 4
    • 3442886811 scopus 로고    scopus 로고
    • The pathophysiology of mitochondrial cell death
    • Green, D.R., and Kroemer, G. 2004. The pathophysiology of mitochondrial cell death. Science. 305:626-629.
    • (2004) Science , vol.305 , pp. 626-629
    • Green, D.R.1    Kroemer, G.2
  • 5
    • 25444473105 scopus 로고    scopus 로고
    • Structure of Apaf-1 in the auto-inhibited form: A critical role for ADP
    • Bao, Q., Riedl, S.J., and Shi, Y. 2005. Structure of Apaf-1 in the auto-inhibited form: a critical role for ADP. Cell Cycle. 4:1001-1003.
    • (2005) Cell Cycle , vol.4 , pp. 1001-1003
    • Bao, Q.1    Riedl, S.J.2    Shi, Y.3
  • 6
    • 0036187036 scopus 로고    scopus 로고
    • Three-dimensional structure of the apoptosome: Implications for assembly, procaspase-9 binding, and activation
    • Acehan, D., et al. 2002. Three-dimensional structure of the apoptosome: implications for assembly, procaspase-9 binding, and activation. Mol. Cell. 9:423-432.
    • (2002) Mol. Cell , vol.9 , pp. 423-432
    • Acehan, D.1
  • 7
    • 14644412456 scopus 로고    scopus 로고
    • Do inducers of apoptosis trigger caspase-independent cell death?
    • Chipuk J.E., and Green, D.R. 2005. Do inducers of apoptosis trigger caspase-independent cell death? Nat. Rev. Mol. Cell Biol. 6:268-275.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 268-275
    • Chipuk, J.E.1    Green, D.R.2
  • 8
    • 22544444514 scopus 로고    scopus 로고
    • Caspase-independent cell death
    • Kroemer, G., and Martin, S.J. 2005. Caspase-independent cell death. Nat. Med. 11:725-730.
    • (2005) Nat. Med. , vol.11 , pp. 725-730
    • Kroemer, G.1    Martin, S.J.2
  • 9
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin, S.A., et al. 1999. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature. 397:441-446.
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1
  • 10
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li, L.Y., Luo, X., and Wang, X. 2001. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature. 412:95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 11
    • 0842307483 scopus 로고    scopus 로고
    • The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore
    • Kokoszka, J.E., et al. 2004. The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore. Nature. 427:461-465.
    • (2004) Nature , vol.427 , pp. 461-465
    • Kokoszka, J.E.1
  • 12
    • 15844407874 scopus 로고    scopus 로고
    • Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death
    • Nakagawa, T., et al. 2005. Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death. Nature. 434:652-658.
    • (2005) Nature , vol.434 , pp. 652-658
    • Nakagawa, T.1
  • 13
    • 15844375853 scopus 로고    scopus 로고
    • Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death
    • Baines, C.P., et al. 2005. Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death. Nature. 434:658-662.
    • (2005) Nature , vol.434 , pp. 658-662
    • Baines, C.P.1
  • 14
    • 21244446551 scopus 로고    scopus 로고
    • Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D
    • Basso, E., et al. 2005. Properties of the permeability transition pore in mitochondria devoid of Cyclophilin D. J. Biol. Chem. 280:18558-18561.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18558-18561
    • Basso, E.1
  • 15
    • 0036850312 scopus 로고    scopus 로고
    • Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane
    • Kuwana, T., et al. 2002. Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane. Cell. 111:331-342.
    • (2002) Cell , vol.111 , pp. 331-342
    • Kuwana, T.1
  • 16
    • 13944277343 scopus 로고    scopus 로고
    • BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly
    • Kuwana, T., et al. 2005. BH3 domains of BH3-only proteins differentially regulate Bax-mediated mitochondrial membrane permeabilization both directly and indirectly. Mol. Cell. 17:525-535.
    • (2005) Mol. Cell , vol.17 , pp. 525-535
    • Kuwana, T.1
  • 17
    • 0035957653 scopus 로고    scopus 로고
    • Proapoptotic BAX and BAK: A requisite gateway to mitochondrial dysfunction and death
    • Wei, M.C., et al. 2001. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science. 292:727-730.
    • (2001) Science , vol.292 , pp. 727-730
    • Wei, M.C.1
  • 18
    • 0036728834 scopus 로고    scopus 로고
    • Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics
    • Letai, A., et al. 2002. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell. 2:183-192.
    • (2002) Cancer Cell , vol.2 , pp. 183-192
    • Letai, A.1
  • 19
    • 19944432123 scopus 로고    scopus 로고
    • Differential targeting of pro-survival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function
    • Chen, L., et al. 2005. Differential targeting of pro-survival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function. Mol. Cell. 17:393-403.
    • (2005) Mol. Cell , vol.17 , pp. 393-403
    • Chen, L.1
  • 20
    • 20444486559 scopus 로고    scopus 로고
    • An inhibitor of Bcl-2 family proteins induces regression of solid tumours
    • Oltersdorf, T., et al. 2005. An inhibitor of Bcl-2 family proteins induces regression of solid tumours. Nature. 435:677-681.
    • (2005) Nature , vol.435 , pp. 677-681
    • Oltersdorf, T.1
  • 21
    • 0032514713 scopus 로고    scopus 로고
    • Resistance to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45
    • Zhang, J., Liu, X., Scherer, D.C., van Kaer, L., Wang, X., and Xu, M. 1998. Resistance to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45. Proc. Natl. Acad. Sci. U. S. A. 95:12480-12485.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12480-12485
    • Zhang, J.1    Liu, X.2    Scherer, D.C.3    Van Kaer, L.4    Wang, X.5    Xu, M.6
  • 22
    • 0034698733 scopus 로고    scopus 로고
    • Two distinct pathways leading to nuclear apoptosis
    • Susin, S.A., et al. 2000. Two distinct pathways leading to nuclear apoptosis. J. Exp. Med. 192:571-579.
    • (2000) J. Exp. Med. , vol.192 , pp. 571-579
    • Susin, S.A.1
  • 23
    • 2642553881 scopus 로고    scopus 로고
    • Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8
    • Yu, L., et al. 2004. Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8. Science. 304:1500-1502.
    • (2004) Science , vol.304 , pp. 1500-1502
    • Yu, L.1
  • 24
    • 0030698810 scopus 로고    scopus 로고
    • The apoptosis-necrosis paradox. Apoptogenic proteases activated after mitochondrial permeability transition determine the mode of cell death
    • Hirsch, T., et al. 1997. The apoptosis-necrosis paradox. Apoptogenic proteases activated after mitochondrial permeability transition determine the mode of cell death. Oncogens. 15:1573-1582.
    • (1997) Oncogens , vol.15 , pp. 1573-1582
    • Hirsch, T.1
  • 25
    • 8144231458 scopus 로고    scopus 로고
    • Expression of antiapoptotic genes bcl-xL and ced-9 in tomato enhances tolerance to viral-induced necrosis and abiotic stress
    • Xu, P., Rogers, S.J., and Roossinck, M.J. 2004. Expression of antiapoptotic genes bcl-xL and ced-9 in tomato enhances tolerance to viral-induced necrosis and abiotic stress. Proc. Natl. Acad. Sci. U. S. A. 101:15805-15810.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 15805-15810
    • Xu, P.1    Rogers, S.J.2    Roossinck, M.J.3
  • 26
    • 10344262564 scopus 로고    scopus 로고
    • A role of Bcl-2 family of proteins in non-apoptotic programmed cell death dependent on autophagy genes
    • Shimizu, S., et al. 2004. A role of Bcl-2 family of proteins in non-apoptotic programmed cell death dependent on autophagy genes. Nat. Cell Biol. 6:1221-1228.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1221-1228
    • Shimizu, S.1
  • 28
    • 4944256085 scopus 로고    scopus 로고
    • Caspase inhibitor z-DEVD-fmk attenuates calpain and necrotic cell death in vitro and after traumatic brain injury
    • Knoblach, S.M., et al. 2004. Caspase inhibitor z-DEVD-fmk attenuates calpain and necrotic cell death in vitro and after traumatic brain injury. J. Cereb. Blood Flow Metab. 24:1119-1132.
    • (2004) J. Cereb. Blood Flow Metab. , vol.24 , pp. 1119-1132
    • Knoblach, S.M.1
  • 29
    • 0037121812 scopus 로고    scopus 로고
    • In vivo role of caspases in excitotoxic neuronal death: Generation and analysis of transgenic mice expressing baculoviral caspase inhibitor, p35, in postnatal neurons
    • Tomioka, M., et al. 2002. In vivo role of caspases in excitotoxic neuronal death: generation and analysis of transgenic mice expressing baculoviral caspase inhibitor, p35, in postnatal neurons. Brain Res. Mol. Brain Res. 108:18-32.
    • (2002) Brain Res. Mol. Brain Res. , vol.108 , pp. 18-32
    • Tomioka, M.1
  • 30
    • 0035736259 scopus 로고    scopus 로고
    • Organelle-specific initiation of cell death pathways
    • Ferri, K.F., and Kroemer, G.K. 2001. Organelle-specific initiation of cell death pathways. Nat. Cell Biol. 3:E255-E263.
    • (2001) Nat. Cell Biol. , vol.3
    • Ferri, K.F.1    Kroemer, G.K.2
  • 31
    • 0034717014 scopus 로고    scopus 로고
    • Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling
    • Marchenko, N.D., Zaika, A., and Moll, U.M. 2000. Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling. J. Biol. Chem. 275:16202-16212.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16202-16212
    • Marchenko, N.D.1    Zaika, A.2    Moll, U.M.3
  • 32
    • 0842278331 scopus 로고    scopus 로고
    • Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis
    • Chipuk, J.E., et al. 2004. Direct activation of Bax by p53 mediates mitochondrial membrane permeabilization and apoptosis. Science. 303:1010-1014.
    • (2004) Science , vol.303 , pp. 1010-1014
    • Chipuk, J.E.1
  • 33
    • 2342553892 scopus 로고    scopus 로고
    • Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex
    • Leu, J.I., Dumont, P., Hafey, M., Murphy, M.E., and George, D.L. 2004. Mitochondrial p53 activates Bak and causes disruption of a Bak-Mcl1 complex. Nat. Cell Biol. 6:443-450.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 443-450
    • Leu, J.I.1    Dumont, P.2    Hafey, M.3    Murphy, M.E.4    George, D.L.5
  • 34
    • 0038529617 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization induces cell death in a mitochondrion-dependent fashion
    • Boya, P., et al. 2003. Lysosomal membrane permeabilization induces cell death in a mitochondrion-dependent fashion. J. Exp. Med. 197:1323-1334.
    • (2003) J. Exp. Med. , vol.197 , pp. 1323-1334
    • Boya, P.1
  • 35
    • 11844294713 scopus 로고    scopus 로고
    • Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis
    • Erdal, H., et al. 2005. Induction of lysosomal membrane permeabilization by compounds that activate p53-independent apoptosis. Proc. Natl. Acad. Sci. U. S. A. 102:192-197.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 192-197
    • Erdal, H.1
  • 36
    • 0038529617 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization induces cell death in a mitochondrion-dependent fashion
    • Boya, P., et al. 2003. Lysosomal membrane permeabilization induces cell death in a mitochondrion-dependent fashion. J. Exp. Med. 197:1323-1334.
    • (2003) J. Exp. Med. , vol.197 , pp. 1323-1334
    • Boya, P.1
  • 37
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • Green, D.R., and Evan, G.I. 2002. A matter of life and death. Cancer Cell. 1:19-30.
    • (2002) Cancer Cell , vol.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 38
    • 0033585504 scopus 로고    scopus 로고
    • In vivo eradication of human BCR/ABL-positive leukemia cells with an ABL kinase inhibitor
    • le Coutre, P., et al. 1999. In vivo eradication of human BCR/ABL-positive leukemia cells with an ABL kinase inhibitor. J. Natl. Cancer Inst. 91:163-168.
    • (1999) J. Natl. Cancer Inst. , vol.91 , pp. 163-168
    • Le Coutre, P.1
  • 39
    • 1542283719 scopus 로고    scopus 로고
    • A novel mechanism for imatinib mesylate-induced cell death of BCR-ABL-positive human leukemic cells: Caspase-independent, necrosis-like programmed cell death mediated by serine protease activity
    • Okada, M. et al. 2004. A novel mechanism for imatinib mesylate-induced cell death of BCR-ABL-positive human leukemic cells: caspase-independent, necrosis-like programmed cell death mediated by serine protease activity. Blood. 103:2299-2307.
    • (2004) Blood , vol.103 , pp. 2299-2307
    • Okada, M.1
  • 40
    • 26444448463 scopus 로고    scopus 로고
    • The survival kinases Akt and Pim as potential pharmacological targets
    • doi:10.1172/JCI26273
    • Amaravadi, R., and Thompson, C.B. 2005. The survival kinases Akt and Pim as potential pharmacological targets. J. Clin. Invest. 115:2618-2624. doi:10.1172/JCI26273.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2618-2624
    • Amaravadi, R.1    Thompson, C.B.2
  • 41
    • 26444605834 scopus 로고    scopus 로고
    • IKK/NF-κB signaling: Balancing life and death - A new approach to cancer therapy
    • doi:10.1172/JCI26322
    • Luo, J.-L., Kamata, H., and Karin, M. 2005. IKK/NF-κB signaling: balancing life and death - a new approach to cancer therapy. J. Clin. Invest. 115:2625-2632. doi:10.1172/JCI26322.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2625-2632
    • Luo, J.-L.1    Kamata, H.2    Karin, M.3
  • 42
    • 26444495615 scopus 로고    scopus 로고
    • Death versus survival: Functional interaction between the apoptotic and stress-inducible heat shock protein pathways
    • doi:10.1172/JCI26471
    • Beere, H.M. 2005. Death versus survival: functional interaction between the apoptotic and stress-inducible heat shock protein pathways. J. Clin. Invest. 115:2633-2639. doi:10.1172/JCI26471.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2633-2639
    • Beere, H.M.1
  • 43
    • 26444468146 scopus 로고    scopus 로고
    • Mitochondria: Pharmacological manipulation of cell death
    • doi:10.1172/JCI26274
    • Bouchier-Hayes, L., Lartigue, L., and Newmeyer, D.D. 2005. Mitochondria: pharmacological manipulation of cell death. J. Clin. Invest. 115:2640-2647. doi:10.1172/JCI26274.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2640-2647
    • Bouchier-Hayes, L.1    Lartigue, L.2    Newmeyer, D.D.3
  • 44
    • 26444558130 scopus 로고    scopus 로고
    • Pharmacological manipulation of Bcl-2 family members to control cell death
    • doi:10.1172/JCI26250
    • Letai, A. 2005. Pharmacological manipulation of Bcl-2 family members to control cell death. J. Clin. Invest. 115:2648-2655. doi:10.1172/JCI26250.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2648-2655
    • Letai, A.1
  • 45
    • 26444442450 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Cell life and death decisions
    • doi:10.1172/JCI26373
    • Xu, C., Bailly-Maitre, B., and Reed, J.C. 2005. Endoplasmic reticulum stress: cell life and death decisions. J. Clin. Invest. 115:2656-2664. doi:10.1172/JCI26373.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2656-2664
    • Xu, C.1    Bailly-Maitre, B.2    Reed, J.C.3
  • 46
    • 26444560960 scopus 로고    scopus 로고
    • Caspases: Pharmacological manipulation of cell death
    • doi:10.1172/JCI26252
    • Lavrik, I.N., Golks, A., and Krammer, P.H. 2005. Caspases: pharmacological manipulation of cell death. J. Clin. Invest. 115:2665-2672. doi:10.1172/JCI26252.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2665-2672
    • Lavrik, I.N.1    Golks, A.2    Krammer, P.H.3
  • 47
    • 26444470888 scopus 로고    scopus 로고
    • Reawakening the cellular death program in neoplasia through the therapeutic blockade of IAP function
    • doi:10.1172/JCI26251
    • Wright, C.W., and Duckett, C.S. 2005. Reawakening the cellular death program in neoplasia through the therapeutic blockade of IAP function. J. Clin. Invest. 115:2673-2678. doi:10.1172/JCI26251.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2673-2678
    • Wright, C.W.1    Duckett, C.S.2
  • 48
    • 25144506835 scopus 로고    scopus 로고
    • Autophagy in cell death: An innocent convict?
    • doi:10.1172/JCI26390
    • Levine, B., and Yuan, J. 2005. Autophagy in cell death: an innocent convict? J. Clin. Invest. 115:2679-2688. doi:10.1172/JCI26390.
    • (2005) J. Clin. Invest. , vol.115 , pp. 2679-2688
    • Levine, B.1    Yuan, J.2
  • 49
    • 0036663014 scopus 로고    scopus 로고
    • In vivo delivery of a Bcl-xL fusion protein containing the TAT protein transduction domain protects against ischemic brain injury and neuronal apoptosis
    • Cao, G., et al. 2002. In vivo delivery of a Bcl-xL fusion protein containing the TAT protein transduction domain protects against ischemic brain injury and neuronal apoptosis. J. Neurosci. 22:5423-5431.
    • (2002) J. Neurosci. , vol.22 , pp. 5423-5431
    • Cao, G.1
  • 50
    • 0346753589 scopus 로고    scopus 로고
    • BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo
    • Sugioka, R., et al. 2003. BH4-domain peptide from Bcl-xL exerts anti-apoptotic activity in vivo. Oncogene. 22:8432-8440.
    • (2003) Oncogene , vol.22 , pp. 8432-8440
    • Sugioka, R.1
  • 51
    • 1442359840 scopus 로고    scopus 로고
    • Bcl-2 family regulation of neuronal development and neurodegeneration
    • Akhtar, R.S., Ness, J.M., and Roth, K.A. 2004. Bcl-2 family regulation of neuronal development and neurodegeneration. Biochim. Biophys. Acta. 1644:189-203.
    • (2004) Biochim. Biophys. Acta , vol.1644 , pp. 189-203
    • Akhtar, R.S.1    Ness, J.M.2    Roth, K.A.3
  • 52
    • 9444263717 scopus 로고    scopus 로고
    • Cardiomyocyte-specific Bcl-2 overexpression attenuates ischemia-reperfusion injury, immune response during acute rejection, and graft coronary artery disease
    • Tanaka, M., et al. 2004. Cardiomyocyte-specific Bcl-2 overexpression attenuates ischemia-reperfusion injury, immune response during acute rejection, and graft coronary artery disease. Blood. 104:3789-3796.
    • (2004) Blood , vol.104 , pp. 3789-3796
    • Tanaka, M.1
  • 53
    • 1642433232 scopus 로고    scopus 로고
    • Bcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathy
    • Weisleder, N., Taffet, G.E., and Capetanaki, Y. 2004. Bcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathy. Proc. Natl. Acad. Sci. U. S. A. 101:769-774.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 769-774
    • Weisleder, N.1    Taffet, G.E.2    Capetanaki, Y.3
  • 54
    • 5144225191 scopus 로고    scopus 로고
    • A novel systemically active caspase inhibitor attenuates the toxicities of MPTP, malonate, and 3NP in vivo
    • Yang, L., et al. 2004. A novel systemically active caspase inhibitor attenuates the toxicities of MPTP, malonate, and 3NP in vivo. Neurobiol. Dis. 17:250-259.
    • (2004) Neurobiol. Dis. , vol.17 , pp. 250-259
    • Yang, L.1
  • 55
    • 1642500084 scopus 로고    scopus 로고
    • Differential efficacy of caspase inhibitors on apoptosis markers during sepsis in rats and implication for fractional inhibition requirements for therapeutics
    • Methot, N., et al. 2004. Differential efficacy of caspase inhibitors on apoptosis markers during sepsis in rats and implication for fractional inhibition requirements for therapeutics. J. Exp. Med. 199:199-207.
    • (2004) J. Exp. Med. , vol.199 , pp. 199-207
    • Methot, N.1
  • 56
    • 10844259971 scopus 로고    scopus 로고
    • Caspase inhibitors, but not c-Jun NH2-terminal kinase inhibitor treatment, prevent cisplatin-induced hearing loss
    • Wang, J., et al. 2004. Caspase inhibitors, but not c-Jun NH2-terminal kinase inhibitor treatment, prevent cisplatin-induced hearing loss. Cancer Res. 64:9217-9224.
    • (2004) Cancer Res. , vol.64 , pp. 9217-9224
    • Wang, J.1
  • 57
    • 0038487667 scopus 로고    scopus 로고
    • Caspase inhibitors promote vestibular hair cell survival and function after aminoglycoside treatment in vivo
    • Matsui, J.I., et al. 2003. Caspase inhibitors promote vestibular hair cell survival and function after aminoglycoside treatment in vivo. J. Neurosci. 23:6111-6122.
    • (2003) J. Neurosci. , vol.23 , pp. 6111-6122
    • Matsui, J.I.1
  • 59
    • 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., et al. 2003. Inhibition of calpains prevents neuronal and behavioral deficits in an MPTP mouse model of Parkinson's disease. J. Neurosci. 23:4081-4091.
    • (2003) J. Neurosci. , vol.23 , pp. 4081-4091
    • Crocker, S.J.1
  • 60
    • 18144407551 scopus 로고    scopus 로고
    • Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: Evidence from calpastatin-mutant mice
    • Takano, J., et al. 2005. Calpain mediates excitotoxic DNA fragmentation via mitochondrial pathways in adult brains: evidence from calpastatin-mutant mice. J. Biol. Chem. 280:16175-16184.
    • (2005) J. Biol. Chem. , vol.280 , pp. 16175-16184
    • Takano, J.1
  • 61
    • 0036798005 scopus 로고    scopus 로고
    • Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology
    • Spencer, M.J., and Mellgren, R.L. 2002. Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology. Hum. Mol. Genet. 11:2645-2655.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2645-2655
    • Spencer, M.J.1    Mellgren, R.L.2
  • 63
    • 19944427658 scopus 로고    scopus 로고
    • Omi/HtrA2 protease mediates cisplatin-induced cell death in renal cells
    • Cilenti, L., et al. 2005. Omi/HtrA2 protease mediates cisplatin-induced cell death in renal cells. Am. J. Physiol. Renal Physiol. 288:F371-F379.
    • (2005) Am. J. Physiol. Renal Physiol. , vol.288
    • Cilenti, L.1
  • 64
    • 19944429185 scopus 로고    scopus 로고
    • Role of Omi/HtrA2 in apoptotic cell death after myocardial ischemia and reperfusion
    • Liu, H.R., et al. 2005. Role of Omi/HtrA2 in apoptotic cell death after myocardial ischemia and reperfusion. Circulation. 111:90-96.
    • (2005) Circulation , vol.111 , pp. 90-96
    • Liu, H.R.1
  • 65
    • 0036323443 scopus 로고    scopus 로고
    • Apoptosis-inducing factor is involved in the regulation of caspase-independent neuronal cell death
    • Cregan, S.P., et al. 2002. Apoptosis-inducing factor is involved in the regulation of caspase-independent neuronal cell death. J. Cell Biol. 158:507-517.
    • (2002) J. Cell Biol. , vol.158 , pp. 507-517
    • Cregan, S.P.1
  • 66
    • 11144354396 scopus 로고    scopus 로고
    • Neutralization of CD95 ligand promotes regeneration and functional recovery after spinal cord injury
    • Demjen, D., et al. 2004. Neutralization of CD95 ligand promotes regeneration and functional recovery after spinal cord injury. Nat. Med. 10:389-395.
    • (2004) Nat. Med. , vol.10 , pp. 389-395
    • Demjen, D.1
  • 67
    • 0034915133 scopus 로고    scopus 로고
    • Therapeutic neutralization of CD95-ligand and TNF attenuates brain damage in stroke
    • Martin-Villalba, A., et al. 2001. Therapeutic neutralization of CD95-ligand and TNF attenuates brain damage in stroke. Cell Death Differ. 8:679-686.
    • (2001) Cell Death Differ. , vol.8 , pp. 679-686
    • Martin-Villalba, A.1
  • 68
    • 4444377604 scopus 로고    scopus 로고
    • Neonatal mice lacking functional Fas death receptors are resistant to hypoxic-ischemic brain injury
    • Graham, E.M., et al. 2004. Neonatal mice lacking functional Fas death receptors are resistant to hypoxic-ischemic brain injury. Neurobiol. Dis. 17:89-98.
    • (2004) Neurobiol. Dis. , vol.17 , pp. 89-98
    • Graham, E.M.1
  • 69
    • 3042845128 scopus 로고    scopus 로고
    • The role of Fas-mediated apoptosis after traumatic spinal cord injury
    • Yoshino, O., et al. 2004. The role of Fas-mediated apoptosis after traumatic spinal cord injury. Spine. 29:1394-1404.
    • (2004) Spine , vol.29 , pp. 1394-1404
    • Yoshino, O.1
  • 70
    • 2942729545 scopus 로고    scopus 로고
    • Suramin inhibits death receptor-induced apoptosis in vitro and fulminant apoptotic liver damage in mice
    • Eichhorst, S.T., et al. 2004. Suramin inhibits death receptor-induced apoptosis in vitro and fulminant apoptotic liver damage in mice. Nat. Med. 10:602-609.
    • (2004) Nat. Med. , vol.10 , pp. 602-609
    • Eichhorst, S.T.1
  • 71
    • 0033543728 scopus 로고    scopus 로고
    • A chemical inhibitor of p53 that protects mice from the side effects of cancer therapy
    • Komarov, P.G., et al. 1999. A chemical inhibitor of p53 that protects mice from the side effects of cancer therapy. Science. 285:1733-1737.
    • (1999) Science , vol.285 , pp. 1733-1737
    • Komarov, P.G.1
  • 72
    • 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. 2004. Nuclear and mitochondrial conversations in cell death: PARP-1 and AIF signaling. Trends Pharmacol. Sci. 25:259-264.
    • (2004) Trends Pharmacol. Sci. , vol.25 , pp. 259-264
    • Hong, S.J.1    Dawson, T.M.2    Dawson, V.L.3
  • 73
    • 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.V., et al. 2005. 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. 312:891-898.
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 891-898
    • Xiao, C.V.1
  • 75
    • 3042694907 scopus 로고    scopus 로고
    • D-JNKI1, a cell-penetrating c-Jun-N-terminal kinase inhibitor, protects against cell death in severe cerebral ischemia
    • Hirt, L., et al. 2004. D-JNKI1, a cell-penetrating c-Jun-N-terminal kinase inhibitor, protects against cell death in severe cerebral ischemia. Stroke. 35:1738-1743.
    • (2004) Stroke , vol.35 , pp. 1738-1743
    • Hirt, L.1
  • 76
    • 10744229507 scopus 로고    scopus 로고
    • A critical role of neural-specific JNK3 for ischemic apoptosis
    • Kuan, C.V., et al. 2003. A critical role of neural-specific JNK3 for ischemic apoptosis. Proc. Natl. Acad. Sci. U. S. A. 100:15184-15189.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 15184-15189
    • Kuan, C.V.1
  • 77
    • 1342344813 scopus 로고    scopus 로고
    • Mixed-lineage kinases: A target for the prevention of neurodegeneration
    • Wang, L.H., Besirli, C.G., and Johnson, E.M., Jr. 2004. Mixed-lineage kinases: a target for the prevention of neurodegeneration. Annu. Rev. Pharmacol. Toxicol. 44:451-474.
    • (2004) Annu. Rev. Pharmacol. Toxicol. , vol.44 , pp. 451-474
    • Wang, L.H.1    Besirli, C.G.2    Johnson Jr., E.M.3
  • 78
    • 10044239265 scopus 로고    scopus 로고
    • One hundred consecutive isolated limb perfusions with TNF-alpha and melphalan in melanoma patients with multiple intransit metastases
    • Grunhagen, D.J., et al. 2004. One hundred consecutive isolated limb perfusions with TNF-alpha and melphalan in melanoma patients with multiple intransit metastases. Ann. Surg. 240:939-947.
    • (2004) Ann. Surg. , vol.240 , pp. 939-947
    • Grunhagen, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.