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Volumn 5, Issue 2, 2004, Pages 101-110

Multiple cell death programs: Charon's lifts to Hades

Author keywords

Apoptosis; Autophagic cell death; Caspase dependent independent PCD; Cytoskeleton; Lysosomes; Mitochondria

Indexed keywords

DEATH ASSOCIATED PROTEIN KINASE;

EID: 5444230887     PISSN: 15671356     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsyr.2004.07.006     Document Type: Short Survey
Times cited : (46)

References (127)
  • 1
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • J.F.R. Kerr, A.H. Wyllie, and A.R. Currie Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics Brit. J. Cancer 26 1972 239 257
    • (1972) Brit. J. Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 3
    • 1642512361 scopus 로고    scopus 로고
    • Virus infection and apoptosis (issue II) an introduction: Cheating death or death as a fact of life?
    • Blaho, J.A. Virus infection and apoptosis (issue II) an introduction: cheating death or death as a fact of life? Int. Rev. Immunol. 23 (1-2), 1-6
    • Int. Rev. Immunol. , vol.23 , Issue.1-2 , pp. 1-6
    • Blaho, J.A.1
  • 4
    • 0035902115 scopus 로고    scopus 로고
    • Proliferation, cell cycle and apoptosis in cancer
    • G. Evan, and K.H. Vousden Proliferation, cell cycle and apoptosis in cancer Nature 411 2001 342 348
    • (2001) Nature , vol.411 , pp. 342-348
    • Evan, G.1    Vousden, K.H.2
  • 5
    • 0142200947 scopus 로고    scopus 로고
    • Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases
    • M. Hashimoto, E. Rockenstein, L. Crews, and E. Masliah Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases Neuromolecular Med. 4 1-2 2003 21 36
    • (2003) Neuromolecular Med. , vol.4 , Issue.12 , pp. 21-36
    • Hashimoto, M.1    Rockenstein, E.2    Crews, L.3    Masliah, E.4
  • 7
    • 0038725690 scopus 로고    scopus 로고
    • The ABCs of granule-mediated cytotoxicity: New weapons in the arsenal
    • J. Lieberman The ABCs of granule-mediated cytotoxicity: new weapons in the arsenal Nat. Rev. Immunol. 3 5 2003 361 370
    • (2003) Nat. Rev. Immunol. , vol.3 , Issue.5 , pp. 361-370
    • Lieberman, J.1
  • 8
    • 1142274315 scopus 로고    scopus 로고
    • Apoptosis in cancer-implications for therapy
    • H. Schulze-Bergkamen, and P.H. Krammer Apoptosis in cancer-implications for therapy Semin. Oncol. 1 2004 90 119
    • (2004) Semin. Oncol. , vol.1 , pp. 90-119
    • Schulze-Bergkamen, H.1    Krammer, P.H.2
  • 9
    • 1542514781 scopus 로고    scopus 로고
    • Regulation of radiation-induced apoptosis by early growth response-1 gene in solid tumors
    • M.M. Ahmed Regulation of radiation-induced apoptosis by early growth response-1 gene in solid tumors Curr. Cancer Drug Targets 4 1 2004 43 52
    • (2004) Curr. Cancer Drug Targets , vol.4 , Issue.1 , pp. 43-52
    • Ahmed, M.M.1
  • 10
    • 1042280304 scopus 로고    scopus 로고
    • Molecular therapy intervention prospects in prostate cancer
    • Y.D. Rege, and V.M. Rangnekar Molecular therapy intervention prospects in prostate cancer Curr. Pharm. Des. 10 5 2004 523 530
    • (2004) Curr. Pharm. Des. , vol.10 , Issue.5 , pp. 523-530
    • Rege, Y.D.1    Rangnekar, V.M.2
  • 11
    • 0842281645 scopus 로고    scopus 로고
    • Cell death: Critical control points
    • N.N. Danial, and S.J. Korsmeyer Cell death: critical control points Cell 116 2 2004 205 219
    • (2004) Cell , vol.116 , Issue.2 , pp. 205-219
    • Danial, N.N.1    Korsmeyer, S.J.2
  • 12
    • 0037233327 scopus 로고    scopus 로고
    • Survivin and apoptosis control
    • D.C. Altieri Survivin and apoptosis control Adv. Cancer Res. 88 2003 31 52
    • (2003) Adv. Cancer Res. , vol.88 , pp. 31-52
    • Altieri, D.C.1
  • 13
    • 1642474148 scopus 로고    scopus 로고
    • Caspases: An ancient cellular sword of Damocles
    • M. Boyce, A. Degterev, and J. Yuan Caspases: an ancient cellular sword of Damocles Cell Death Differ. 11 1 2004 29 37
    • (2004) Cell Death Differ. , vol.11 , Issue.1 , pp. 29-37
    • Boyce, M.1    Degterev, A.2    Yuan, J.3
  • 14
    • 0034440818 scopus 로고    scopus 로고
    • Proteases for cell suicide: Functions and regulation of caspases
    • H.Y. Chang, and X. Yang Proteases for cell suicide: functions and regulation of caspases Microbiol. Mol. Biol. Rev. 64 2000 821 846
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 821-846
    • Chang, H.Y.1    Yang, X.2
  • 15
    • 1642553461 scopus 로고    scopus 로고
    • The dark side of Ras: Regulation of apoptosis
    • A.D. Cox, and C.J. Der The dark side of Ras: regulation of apoptosis Oncogene 22 56 2003 8999 9006
    • (2003) Oncogene , vol.22 , Issue.56 , pp. 8999-9006
    • Cox, A.D.1    Der, C.J.2
  • 16
    • 0347601880 scopus 로고    scopus 로고
    • A decade of caspases
    • A. Degterev, M. Boyce, and J. Yuan A decade of caspases Oncogene 22 53 2003 8543 8567
    • (2003) Oncogene , vol.22 , Issue.53 , pp. 8543-8567
    • Degterev, A.1    Boyce, M.2    Yuan, J.3
  • 17
    • 0141953270 scopus 로고    scopus 로고
    • A JNK-dependent pathway is required for TNFα-induced apoptosis
    • Y. Deng, X. Ren, L. Yang, Y. Lin, and X. Wu A JNK-dependent pathway is required for TNFα-induced apoptosis Cell 115 1 2003 61 70
    • (2003) Cell , vol.115 , Issue.1 , pp. 61-70
    • Deng, Y.1    Ren, X.2    Yang, L.3    Lin, Y.4    Wu, X.5
  • 18
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • M. Jäättelä, and J. Tschopp Caspase-independent cell death in T lymphocytes Nat. Immunol. 4 5 2003 416 423
    • (2003) Nat. Immunol. , vol.4 , Issue.5 , pp. 416-423
    • Jäättelä, M.1    Tschopp, J.2
  • 19
    • 0344629380 scopus 로고    scopus 로고
    • Bcl-2 family members as sentinels of cellular integrity and role of mitochondrial intermembrane space proteins in apoptotic cell death
    • N. Festjens, M. van Gurp, G. van Loo, X. Saelens, and P. Vandenabeele Bcl-2 family members as sentinels of cellular integrity and role of mitochondrial intermembrane space proteins in apoptotic cell death Acta Haematol. 111 1-2 2004 7 27
    • (2004) Acta Haematol. , vol.111 , Issue.12 , pp. 7-27
    • Festjens, N.1    Van Gurp, M.2    Van Loo, G.3    Saelens, X.4    Vandenabeele, P.5
  • 22
    • 1642491755 scopus 로고    scopus 로고
    • Mitochondrial effectors in caspase-independent cell death
    • H.K. Lorenzo, and S.A. Susin Mitochondrial effectors in caspase-independent cell death FEBS Lett. 557 1-3 2004 14 20
    • (2004) FEBS Lett. , vol.557 , Issue.13 , pp. 14-20
    • Lorenzo, H.K.1    Susin, S.A.2
  • 23
    • 0037276437 scopus 로고    scopus 로고
    • The CD95(APO-1/Fas) DISC and beyond
    • M.E. Peter, and P.H. Krammer The CD95(APO-1/Fas) DISC and beyond Cell Death Differ. 10 1 2003 26 35
    • (2003) Cell Death Differ. , vol.10 , Issue.1 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 24
    • 0038148105 scopus 로고    scopus 로고
    • Caspases and neuronal development
    • C.A. Ryan, and G.S. Salvesen Caspases and neuronal development Biol. Chem. 384 6 2003 855 861
    • (2003) Biol. Chem. , vol.384 , Issue.6 , pp. 855-861
    • Ryan, C.A.1    Salvesen, G.S.2
  • 25
    • 1642471825 scopus 로고    scopus 로고
    • Heat-shock proteins as regulators of apoptosis
    • S. Takayama, J.C. Reed, and S. Homma Heat-shock proteins as regulators of apoptosis Oncogene 22 56 2003 9041 9047
    • (2003) Oncogene , vol.22 , Issue.56 , pp. 9041-9047
    • Takayama, S.1    Reed, J.C.2    Homma, S.3
  • 26
    • 0015880897 scopus 로고
    • The morphology of various types of cell death in prenatal tissues
    • J.U. Schweichel, and H.J. Merker 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
  • 27
    • 0025283961 scopus 로고
    • Developmental cell death: Morphological diversity and multiple mechanisms
    • P.G.H. Clarke 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.H.1
  • 29
    • 0034948738 scopus 로고    scopus 로고
    • The autophagosomal-lysosomal compartment in programmed cell death Cell
    • W. Bursch The autophagosomal-lysosomal compartment in programmed cell death Cell Cell Death Differ. 8 2001 569 581
    • (2001) Cell Death Differ. , vol.8 , pp. 569-581
    • Bursch, W.1
  • 31
    • 1842524536 scopus 로고    scopus 로고
    • Autophagy and cancer
    • (Klionsky, D., Ed.), Landes Bioscience, Georgetown Texas, USA and Eurekah.com, Austin Texas, USA, 2004
    • Furuya, N., Liang, X.H. and Levine, B. (2004) Autophagy and cancer. In: Autophagy, (Klionsky, D., Ed.), pp. 241-255. Landes Bioscience, Georgetown Texas, USA and Eurekah.com, Austin Texas, USA, 2004
    • (2004) Autophagy , pp. 241-255
    • Furuya, N.1    Liang, X.H.2    Levine, B.3
  • 32
    • 0034537290 scopus 로고    scopus 로고
    • Autophagy as a regulated pathway of cellular degradation
    • D.J. Klionsky, and S.D. Emr Autophagy as a regulated pathway of cellular degradation Science 290 2000 1717 1721
    • (2000) Science , vol.290 , pp. 1717-1721
    • Klionsky, D.J.1    Emr, S.D.2
  • 33
    • 0036463736 scopus 로고    scopus 로고
    • Autophagy in the eukaryotic cell
    • F. Reggiori, and D.J. Klionsky Autophagy in the eukaryotic cell Eukaryot. Cell 1 1 2002 11 21
    • (2002) Eukaryot. Cell , vol.1 , Issue.1 , pp. 11-21
    • Reggiori, F.1    Klionsky, D.J.2
  • 34
    • 0022411742 scopus 로고
    • Quantitative histological and histochemical studies on the occurrence and stages of apoptosis (controlled cell death) during regression of rat liver hyperplasia
    • W. Bursch, H.S. Taper, B. Lauer, and R. Schulte-Hermann Quantitative histological and histochemical studies on the occurrence and stages of apoptosis (controlled cell death) during regression of rat liver hyperplasia Virchows Arch. Abtl. B. Zellpathologie 50 1985 153 166
    • (1985) Virchows Arch. Abtl. B. Zellpathologie , vol.50 , pp. 153-166
    • Bursch, W.1    Taper, H.S.2    Lauer, B.3    Schulte-Hermann, R.4
  • 35
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • R.V. Rao, H.M. Ellerby, and D.E. Bredesen Coupling endoplasmic reticulum stress to the cell death program Cell Death Differ. 11 4 2004 372 380
    • (2004) Cell Death Differ. , vol.11 , Issue.4 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 37
    • 0035986219 scopus 로고    scopus 로고
    • Regulating cysteine protease activity: Essential role of protease inhibitors as guardians and regulators
    • B. Turk, D. Turk, and G.S. Salvesen Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators Curr. Pharm. 8 2002 1623 1637
    • (2002) Curr. Pharm. , vol.8 , pp. 1623-1637
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 38
    • 1542543543 scopus 로고    scopus 로고
    • Reactive oxygen species-producing site in radiation-induced apoptosis of human peripheral T cells: Involvement of lysosomal membrane destabilization
    • Y. Ogawa, T. Kobayashi, A. Nishioka, S. Kariya, T. Ohnishi, S. Hamasato, H. Seguchi, and S. Yoshida Reactive oxygen species-producing site in radiation-induced apoptosis of human peripheral T cells: involvement of lysosomal membrane destabilization Int. J. Mol. Med. 13 1 2004 69 73
    • (2004) Int. J. Mol. Med. , vol.13 , Issue.1 , pp. 69-73
    • Ogawa, Y.1    Kobayashi, T.2    Nishioka, A.3    Kariya, S.4    Ohnishi, T.5    Hamasato, S.6    Seguchi, H.7    Yoshida, S.8
  • 39
    • 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
    • N. Bidere, H.K. Lorenzo, S. Carmona, M. Laforge, F. Harper, C. Dumont, and A. Senik 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 33 2003 31401 31411
    • (2003) J. Biol. Chem. , vol.278 , Issue.33 , 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
  • 40
    • 0038697678 scopus 로고    scopus 로고
    • Golgi disassembly in apoptosis: Cause or effect?
    • C.E. Machamer Golgi disassembly in apoptosis: cause or effect? Trends Cell Biol. 13 6 2003 279 281
    • (2003) Trends Cell Biol. , vol.13 , Issue.6 , pp. 279-281
    • MacHamer, C.E.1
  • 41
    • 0036098594 scopus 로고    scopus 로고
    • Rho GTPase signalling pathways in the morphological changes associated with apoptosis
    • M.L. Coleman, and M.F. Olson Rho GTPase signalling pathways in the morphological changes associated with apoptosis Cell Death Differ. 9 2002 493 504
    • (2002) Cell Death Differ. , vol.9 , pp. 493-504
    • Coleman, M.L.1    Olson, M.F.2
  • 43
    • 1842419926 scopus 로고    scopus 로고
    • Structural aspects of mammalian autophagy
    • (Klionsky, D., (Ed.), Landes Bioscience (Eurekah.com).
    • Fengsrud, M., Lunde Snedve, M., Øverbye, A. and Seglen, P.O. (2004) Structural aspects of mammalian autophagy. In: Autophagy (Klionsky, D., (Ed.), pp. 11-25. Landes Bioscience (Eurekah.com)
    • (2004) Autophagy , pp. 11-25
    • Fengsrud, M.1    Lunde Snedve, M.2    Øverbye, A.3    Seglen, P.O.4
  • 44
    • 0029741890 scopus 로고    scopus 로고
    • Active cell death induced by antiestrogens tamoxifen and ICI 164384 in human mammary carcinoma cells (MCF-7) in culture: The role of autophagy
    • W. Bursch, H. Kienzl, A. Ellinger, L. Török, R. Walker, M. Sikorska, S. Pandey, and R. Schulte-Hermann Active cell death induced by antiestrogens tamoxifen and ICI 164384 in human mammary carcinoma cells (MCF-7) in culture: the role of autophagy Carcinogenesis 17 1996 1595 1607
    • (1996) Carcinogenesis , vol.17 , pp. 1595-1607
    • Bursch, W.1    Kienzl, H.2    Ellinger, A.3    Török, L.4    Walker, R.5    Sikorska, M.6    Pandey, S.7    Schulte-Hermann, R.8
  • 45
    • 0034012322 scopus 로고    scopus 로고
    • Different fates of cytoskeletal filaments during autophagic and apoptotic types of programmed cell death in mammary carcinoma cells (MCF-7) and colon carcinoma cells (HT29HI1)
    • W. Bursch, K. Hochegger, L. Török, B. Marian, A. Ellinger, and R. Schulte-Hermann Different fates of cytoskeletal filaments during autophagic and apoptotic types of programmed cell death in mammary carcinoma cells (MCF-7) and colon carcinoma cells (HT29HI1) J. Cell Sci. 113 2000 1189 1198
    • (2000) J. Cell Sci. , vol.113 , pp. 1189-1198
    • Bursch, W.1    Hochegger, K.2    Török, L.3    Marian, B.4    Ellinger, A.5    Schulte-Hermann, R.6
  • 47
    • 0036469777 scopus 로고    scopus 로고
    • Apoptotic DNA fragmentation and tissue homeostasis
    • J. Zhang, and M. Xu Apoptotic DNA fragmentation and tissue homeostasis Trends Cell Biol. 12 2002 84 89
    • (2002) Trends Cell Biol. , vol.12 , pp. 84-89
    • Zhang, J.1    Xu, M.2
  • 48
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • R.U. Jänicke, M.L. Sprengart, M.R. Wati, and A.G. Porter Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis J. Biol. Chem. 273 1998 9357 9360
    • (1998) J. Biol. Chem. , vol.273 , pp. 9357-9360
    • Jänicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 51
    • 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
    • D. Arnoult, I. Tatischeff, J. Estaquier, and J.C. Ameisen On the evolutionary conservation of the cell death pathway: mitochondrial release of an apoptosis-inducing factor during Dictyostelium discoideum cell death Mol. Biol. Cell 1230 2001 16 30
    • (2001) Mol. Biol. Cell , vol.1230 , pp. 16-30
    • Arnoult, D.1    Tatischeff, I.2    Estaquier, J.3    Ameisen, J.C.4
  • 53
    • 0347991777 scopus 로고    scopus 로고
    • Programmed cell clearance
    • B. Fadeel Programmed cell clearance Cell Mol. Life Sci. 60 12 2003 2575 2585
    • (2003) Cell Mol. Life Sci. , vol.60 , Issue.12 , pp. 2575-2585
    • Fadeel, B.1
  • 54
    • 0242577378 scopus 로고    scopus 로고
    • Phagocytosis of apoptotic cells and the resolution of inflammation
    • P. Maderna, and C. Godson Phagocytosis of apoptotic cells and the resolution of inflammation Biochim. Biophys. Acta 1639 3 2003 141 151
    • (2003) Biochim. Biophys. Acta , vol.1639 , Issue.3 , pp. 141-151
    • Maderna, P.1    Godson, C.2
  • 55
    • 0041423663 scopus 로고    scopus 로고
    • Apoptosis: Giving phosphatidylserine recognition an assist â€" with a twist
    • V.A. Fadok, and P.M. Henson Apoptosis: giving phosphatidylserine recognition an assist â€" with a twist Curr. Biol. 13 16 2003 R655 657
    • (2003) Curr. Biol. , vol.13 , Issue.16
    • Fadok, V.A.1    Henson, P.M.2
  • 56
  • 57
    • 0035209395 scopus 로고    scopus 로고
    • The phagocytosis of apoptotic cells
    • V.A. Fadok, and G. Chimini The phagocytosis of apoptotic cells Semin. Immunol. 13 2001 365 372
    • (2001) Semin. Immunol. , vol.13 , pp. 365-372
    • Fadok, V.A.1    Chimini, G.2
  • 58
    • 0005677775 scopus 로고
    • 3-Methyladenine, a specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes
    • P.O. Seglen, and P.B. Jordan 3-Methyladenine, a specific inhibitor of autophagic/lysosomal protein degradation in isolated rat hepatocytes Proc. Natl. Acad. Sci. USA 79 1982 1889 1892
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1889-1892
    • Seglen, P.O.1    Jordan, P.B.2
  • 59
    • 0033978633 scopus 로고    scopus 로고
    • Distinct classes of phosphatidylinositol 3′-kinases are involved in signalling pathways that control macroautophagy in HT-29 cells
    • A. Petiot, E. Ogier-Denis, E.F.C. Blommaart, A.J. Meijer, and P. Codogno Distinct classes of phosphatidylinositol 3′-kinases are involved in signalling pathways that control macroautophagy in HT-29 cells J. Biol. Chem. 275 2000 992 998
    • (2000) J. Biol. Chem. , vol.275 , pp. 992-998
    • Petiot, A.1    Ogier-Denis, E.2    Blommaart, E.F.C.3    Meijer, A.J.4    Codogno, P.5
  • 60
    • 0032971161 scopus 로고    scopus 로고
    • Caspase-independent programmed cell death with necrotic morphology
    • C. Kitanaka, and Y. Kuchino Caspase-independent programmed cell death with necrotic morphology Cell Death Diff. 6 1999 508 515
    • (1999) Cell Death Diff. , vol.6 , pp. 508-515
    • Kitanaka, C.1    Kuchino, Y.2
  • 61
    • 1842865745 scopus 로고    scopus 로고
    • Role of autophagy in temozolomide-induced cytotoxicity for malignant glioma cells
    • T. Kanzawa, I.M. Germano, T. Komata, H. Ito, Y. Kondo, and S. Kondo Role of autophagy in temozolomide-induced cytotoxicity for malignant glioma cells Cell Death Differ. 211 4 2004 448 457
    • (2004) Cell Death Differ. , vol.211 , Issue.4 , pp. 448-457
    • Kanzawa, T.1    Germano, I.M.2    Komata, T.3    Ito, H.4    Kondo, Y.5    Kondo, S.6
  • 62
    • 0043173825 scopus 로고    scopus 로고
    • Dopamine induces autophagic cell death and α-synuclein increase in human neuroblastoma SH-SY5Y cells
    • C. Gomez-Santos, I. Ferrer, A.F. Santidrian, M. Barrachina, J. Gil, and S. Ambrosio Dopamine induces autophagic cell death and α-synuclein increase in human neuroblastoma SH-SY5Y cells J. Neurosci. Res. 73 2003 341 350
    • (2003) J. Neurosci. Res. , vol.73 , pp. 341-350
    • Gomez-Santos, C.1    Ferrer, I.2    Santidrian, A.F.3    Barrachina, M.4    Gil, J.5    Ambrosio, S.6
  • 63
    • 0032870475 scopus 로고    scopus 로고
    • Autophagy is activated by apoptotic signalling in sympathetic neurons: An alternative mechanism of death execution
    • L. Xue, G.C. Fletcher, and A.M. Tolkovsky Autophagy is activated by apoptotic signalling in sympathetic neurons: an alternative mechanism of death execution Mol. Cell Neurosci. 14 1999 180 198
    • (1999) Mol. Cell Neurosci. , vol.14 , pp. 180-198
    • Xue, L.1    Fletcher, G.C.2    Tolkovsky, A.M.3
  • 64
    • 0030883558 scopus 로고    scopus 로고
    • Inhibition of autophagy abrogates tumour necrosis factor alpha induced apoptosis in human T-lymphoblastic leukaemic cells
    • L. Jia, R.R. Dourmashkin, P.D. Allen, A.B. Gray, A.C. Newland, and S.M. Kelsey Inhibition of autophagy abrogates tumour necrosis factor alpha induced apoptosis in human T-lymphoblastic leukaemic cells Brit. J. Haematol. 98 1997 673 685
    • (1997) Brit. J. Haematol. , vol.98 , pp. 673-685
    • Jia, L.1    Dourmashkin, R.R.2    Allen, P.D.3    Gray, A.B.4    Newland, A.C.5    Kelsey, S.M.6
  • 65
    • 0026683322 scopus 로고
    • Toxin-induced cell lysis: Protection by 3-methyladenine and cycloheximide
    • K. Sandvig, and B. van Deurs Toxin-induced cell lysis: protection by 3-methyladenine and cycloheximide Exp. Cell Res. 200 1992 253 262
    • (1992) Exp. Cell Res. , vol.200 , pp. 253-262
    • Sandvig, K.1    Van Deurs, B.2
  • 66
    • 0038127194 scopus 로고    scopus 로고
    • Endostatin induces autophagic cell death in EAhy926 human endothelial cells
    • Y.P. Chau, S.Y. Lin, J.H. Chen, and M.H. Tai Endostatin induces autophagic cell death in EAhy926 human endothelial cells Histol. Histopathol. 18 2003 715 726
    • (2003) Histol. Histopathol. , vol.18 , pp. 715-726
    • Chau, Y.P.1    Lin, S.Y.2    Chen, J.H.3    Tai, M.H.4
  • 67
    • 0346753579 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase accelerates autophagic cell death during glucose deprivation in the rat cardiomyocyte-derived cell line H9c2
    • T. Aki, K. Yamaguchi, T. Fujimiya, and Y. Mizukami Phosphoinositide 3-kinase accelerates autophagic cell death during glucose deprivation in the rat cardiomyocyte-derived cell line H9c2 Oncogene 22 52 2003 8529 8535
    • (2003) Oncogene , vol.22 , Issue.52 , pp. 8529-8535
    • Aki, T.1    Yamaguchi, K.2    Fujimiya, T.3    Mizukami, Y.4
  • 69
    • 0036479052 scopus 로고    scopus 로고
    • Mitochondrial disppearance from cells: A clue to the role of autophagy in programmed cell death and disease?
    • A.M. Tolkovsky, I. Xue, C.F. Graham, and V. Borutaite Mitochondrial disppearance from cells: a clue to the role of autophagy in programmed cell death and disease? Biochemie 84 2002 233 240
    • (2002) Biochemie , vol.84 , pp. 233-240
    • Tolkovsky, A.M.1    Xue, I.2    Graham, C.F.3    Borutaite, V.4
  • 70
    • 5444257499 scopus 로고    scopus 로고
    • N-methyl-d-aspartate-triggered neuronal death in organotypic hippocampal cultures is endocytic, autophagic and mediated by the c-Jun N-terminal kinase pathway
    • T. Borsello, K. Croquelois, J.P. Hornung, and P.G. Clarke N-methyl-d-aspartate-triggered neuronal death in organotypic hippocampal cultures is endocytic, autophagic and mediated by the c-Jun N-terminal kinase pathway Eur. J. Neurosci. 184 2003 73 85
    • (2003) Eur. J. Neurosci. , vol.184 , pp. 73-85
    • Borsello, T.1    Croquelois, K.2    Hornung, J.P.3    Clarke, P.G.4
  • 72
    • 0037193474 scopus 로고    scopus 로고
    • DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death
    • B. Inbal, S. Bialik, I. Sabanay, G. Shani, and A. Kimchi DAP kinase and DRP-1 mediate membrane blebbing and the formation of autophagic vesicles during programmed cell death J. Cell Biol. 157 2002 455 468
    • (2002) J. Cell Biol. , vol.157 , pp. 455-468
    • Inbal, B.1    Bialik, S.2    Sabanay, I.3    Shani, G.4    Kimchi, A.5
  • 73
    • 0035133960 scopus 로고    scopus 로고
    • DAP-kinase: From functional gene cloning to establishment of its role in apoptosis and cancer
    • O. Cohen, and A. Kimchi DAP-kinase: from functional gene cloning to establishment of its role in apoptosis and cancer Cell Death Differ. 8 2001 6 15
    • (2001) Cell Death Differ. , vol.8 , pp. 6-15
    • Cohen, O.1    Kimchi, A.2
  • 74
    • 0035283099 scopus 로고    scopus 로고
    • Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding
    • G. Shani, S. Henis-Korenblit, G. Jona, O. Gileadi, M. Eisenstein, T. Ziv, A. Admon, and A. Kimchi Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding EMBO J. 20 2001 1099 1113
    • (2001) EMBO J. , vol.20 , pp. 1099-1113
    • Shani, G.1    Henis-Korenblit, S.2    Jona, G.3    Gileadi, O.4    Eisenstein, M.5    Ziv, T.6    Admon, A.7    Kimchi, A.8
  • 75
    • 0036256178 scopus 로고    scopus 로고
    • Triggering caspase-independent cell death to combat cancer
    • I.S. Mathiasen, and M. Jäättelä Triggering caspase-independent cell death to combat cancer Trends Mol. Med. 8 5 2002 212 220
    • (2002) Trends Mol. Med. , vol.8 , Issue.5 , pp. 212-220
    • Mathiasen, I.S.1    Jäättelä, M.2
  • 76
    • 0036779576 scopus 로고    scopus 로고
    • Functional significance of the perforin/granzyme cell death pathway
    • J.A. Trapani, and M.J. Smyth Functional significance of the perforin/granzyme cell death pathway Nat. Rev. Immunol. 2 10 2002 735 747
    • (2002) Nat. Rev. Immunol. , vol.2 , Issue.10 , pp. 735-747
    • Trapani, J.A.1    Smyth, M.J.2
  • 77
    • 0742289483 scopus 로고    scopus 로고
    • Lysosomes and mitochondria in the commitment to apoptosis: A potential role for cathepsin D and AIF
    • M. Jäättelä, C. Candé, and G. Kroemer Lysosomes and mitochondria in the commitment to apoptosis: a potential role for cathepsin D and AIF Cell Death Differ. 11 2 2004 135 136
    • (2004) Cell Death Differ. , vol.11 , Issue.2 , pp. 135-136
    • Jäättelä, M.1    Candé, C.2    Kroemer, G.3
  • 79
    • 0036308059 scopus 로고    scopus 로고
    • Mitochondria, the killer organelles and their weapons
    • L. Ravagnan, T. Roumier, and G. Kroemer Mitochondria, the killer organelles and their weapons J. Cell Physiol. 192 2002 131 137
    • (2002) J. Cell Physiol. , vol.192 , pp. 131-137
    • Ravagnan, L.1    Roumier, T.2    Kroemer, G.3
  • 80
    • 18544386724 scopus 로고    scopus 로고
    • Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction
    • Y. Lazebnik, A.S. Zervos, T. Fernandes-Alnemri, and E.S. Alnemri Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction J. Biol. Chem. 277 2002 432 438
    • (2002) J. Biol. Chem. , vol.277 , pp. 432-438
    • Lazebnik, Y.1    Zervos, A.S.2    Fernandes-Alnemri, T.3    Alnemri, E.S.4
  • 81
    • 0346880501 scopus 로고    scopus 로고
    • The inhibitors of apoptosis: There is more to life than Bcl2
    • P. Liston, W.G. Fong, and R.G. Korneluk The inhibitors of apoptosis: there is more to life than Bcl2 Oncogene 22 53 2003 8568 8580
    • (2003) Oncogene , vol.22 , Issue.53 , pp. 8568-8580
    • Liston, P.1    Fong, W.G.2    Korneluk, R.G.3
  • 82
    • 0037138438 scopus 로고    scopus 로고
    • Lysosomal proteases as potential targets for the induction of apoptotic cell death in human neuroblastomas
    • R. Castino, D. Pace, M. Demoz, M. Gargiulo, C. Ariatta, F. Raiteri, and C. Isidoro Lysosomal proteases as potential targets for the induction of apoptotic cell death in human neuroblastomas Int. J. Cancer 97 2002 775 779
    • (2002) Int. J. Cancer , vol.97 , pp. 775-779
    • Castino, R.1    Pace, D.2    Demoz, M.3    Gargiulo, M.4    Ariatta, C.5    Raiteri, F.6    Isidoro, C.7
  • 84
    • 0037012040 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is an essential step for killing of non-small cell lung carcinomas resistant to conventional treatment
    • B. Joseph, P. Marchetti, P. Formstecher, G. Kroemer, R. Lewensohn, and B. Zhivotovsky Mitochondrial dysfunction is an essential step for killing of non-small cell lung carcinomas resistant to conventional treatment Oncogene 21 2002 65 77
    • (2002) Oncogene , vol.21 , pp. 65-77
    • Joseph, B.1    Marchetti, P.2    Formstecher, P.3    Kroemer, G.4    Lewensohn, R.5    Zhivotovsky, B.6
  • 86
    • 0035892135 scopus 로고    scopus 로고
    • Activation of apoptosis pathways in peripheral blood lymphocytes by in vivo chemotherapy
    • K. Stahnke, S. Fulda, C. Friesen, G. Strauss, and K.M. Debatin Activation of apoptosis pathways in peripheral blood lymphocytes by in vivo chemotherapy Blood 98 2001 3066 3073
    • (2001) Blood , vol.98 , pp. 3066-3073
    • Stahnke, K.1    Fulda, S.2    Friesen, C.3    Strauss, G.4    Debatin, K.M.5
  • 87
    • 0035965345 scopus 로고    scopus 로고
    • A kinase-independent function of Ask1 in caspase-independent cell death
    • S.J. Charette, H. Lambert, and J. Landry A kinase-independent function of Ask1 in caspase-independent cell death J. Biol. Chem. 276 2001 36071 36074
    • (2001) J. Biol. Chem. , vol.276 , pp. 36071-36074
    • Charette, S.J.1    Lambert, H.2    Landry, J.3
  • 88
    • 0035503898 scopus 로고    scopus 로고
    • Cladribine induces apoptosis in human leukaemia cells by caspase-dependent and -independent pathways acting on mitochondria
    • I. Marzo, P. Perez-Galan, P. Giraldo, D. Rubio-Felix, A. Anel, and J. Naval Cladribine induces apoptosis in human leukaemia cells by caspase-dependent and -independent pathways acting on mitochondria Biochem. J. 359 Pt 3 2001 537 546
    • (2001) Biochem. J. , vol.359 , Issue.3 , pp. 537-546
    • Marzo, I.1    Perez-Galan, P.2    Giraldo, P.3    Rubio-Felix, D.4    Anel, A.5    Naval, J.6
  • 89
    • 0037165219 scopus 로고    scopus 로고
    • Basic fibroblast growth factor (bFGF)-induced cell death is mediated through a caspase-dependent and p53-independent cell death receptor pathway
    • G. Westwood, B.C. Dibling, D. Cuthbert-Heavens, and S.A. Burchill Basic fibroblast growth factor (bFGF)-induced cell death is mediated through a caspase-dependent and p53-independent cell death receptor pathway Oncogene 21 2002 809 824
    • (2002) Oncogene , vol.21 , pp. 809-824
    • Westwood, G.1    Dibling, B.C.2    Cuthbert-Heavens, D.3    Burchill, S.A.4
  • 92
    • 0038743077 scopus 로고    scopus 로고
    • Induction of autophagic cell death in malignant glioma cells by arsenic trioxide
    • T. Kanzawa, Y. Kondo, H. Ito, S. Kondo, and I. Germano Induction of autophagic cell death in malignant glioma cells by arsenic trioxide Cancer Res. 63 2003 2103 2108
    • (2003) Cancer Res. , vol.63 , pp. 2103-2108
    • Kanzawa, T.1    Kondo, Y.2    Ito, H.3    Kondo, S.4    Germano, I.5
  • 94
    • 0034689052 scopus 로고    scopus 로고
    • Active caspases and cytokeratins are sequestered into cytoplasmic inclusions in TRAIL-induced apoptosis
    • M. MacFarlane, W. Merrison, D. Dinsdale, and G.M. Cohen Active caspases and cytokeratins are sequestered into cytoplasmic inclusions in TRAIL-induced apoptosis J. Cell Biol. 148 2000 1239 1252
    • (2000) J. Cell Biol. , vol.148 , pp. 1239-1252
    • MacFarlane, M.1    Merrison, W.2    Dinsdale, D.3    Cohen, G.M.4
  • 96
    • 0041411115 scopus 로고    scopus 로고
    • Autophagic programmed cell death in Drosophila
    • E.H. Baehrecke Autophagic programmed cell death in Drosophila Cell Death Differ. 10 9 2003 940 945
    • (2003) Cell Death Differ. , vol.10 , Issue.9 , pp. 940-945
    • Baehrecke, E.H.1
  • 97
    • 0037452653 scopus 로고    scopus 로고
    • Genome-wide analyses of steroid- and radiation-triggered programmed cell death in Drosophila
    • C.Y. Lee, E.A. Clough, P. Yellon, T.M. Teslovich, D.A. Stephan, and E.H. Baehrecke Genome-wide analyses of steroid- and radiation-triggered programmed cell death in Drosophila Curr. Biol. 13 2003 350 357
    • (2003) Curr. Biol. , vol.13 , pp. 350-357
    • Lee, C.Y.1    Clough, E.A.2    Yellon, P.3    Teslovich, T.M.4    Stephan, D.A.5    Baehrecke, E.H.6
  • 98
    • 0842279780 scopus 로고    scopus 로고
    • Caspases function in autophagic programmed cell death in Drosophila
    • D.N. Martin, and E.H. Baehrecke Caspases function in autophagic programmed cell death in Drosophila Development 131 2 2004 275 284
    • (2004) Development , vol.131 , Issue.2 , pp. 275-284
    • Martin, D.N.1    Baehrecke, E.H.2
  • 103
    • 0037351752 scopus 로고    scopus 로고
    • Programmed cell death in trypanosomatids and other unicellular organisms
    • A. Debrabant, N. Lee, S. Bertholet, R. Duncan, and H.L. Nakhasi Programmed cell death in trypanosomatids and other unicellular organisms Int. J. Parasitol. 33 3 2003 257 267
    • (2003) Int. J. Parasitol. , vol.33 , Issue.3 , pp. 257-267
    • Debrabant, A.1    Lee, N.2    Bertholet, S.3    Duncan, R.4    Nakhasi, H.L.5
  • 104
    • 0036316720 scopus 로고    scopus 로고
    • Origin and evolution of eukaryotic apoptosis: The bacterial connection
    • E.V. Koonin, and L. Aravind Origin and evolution of eukaryotic apoptosis: the bacterial connection Cell Death Differ. 9 4 2002 394 404
    • (2002) Cell Death Differ. , vol.9 , Issue.4 , pp. 394-404
    • Koonin, E.V.1    Aravind, L.2
  • 106
    • 0030667206 scopus 로고    scopus 로고
    • A yeast mutant showing diagnostic markers of early and late apoptosis
    • F. Madeo, E. Fröhlich, and K.U. Fröhlich A yeast mutant showing diagnostic markers of early and late apoptosis J. Cell Biol. 139 3 1997 729 734
    • (1997) J. Cell Biol. , vol.139 , Issue.3 , pp. 729-734
    • Madeo, F.1    Fröhlich, E.2    Fröhlich, K.U.3
  • 107
    • 0035206962 scopus 로고    scopus 로고
    • Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/CIA1
    • M. Yamaki, T. Umehara, T. Chimura, and M. Horikoshi Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/CIA1 Genes to Cells 6 12 2001 1043 1054
    • (2001) Genes to Cells , vol.6 , Issue.12 , pp. 1043-1054
    • Yamaki, M.1    Umehara, T.2    Chimura, T.3    Horikoshi, M.4
  • 109
    • 0033638182 scopus 로고    scopus 로고
    • Identification of paracaspases and metacaspases: Two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma
    • A.G. Uren, K. O'Rourke, L.A. Aravind, M.T. Pisabarro, S. Seshagiri, E.V. Koonin, and V.M. Dixit Identification of paracaspases and metacaspases: two ancient families of caspase-like proteins, one of which plays a key role in MALT lymphoma Mol. Cell 6 4 2000 961 967
    • (2000) Mol. Cell , vol.6 , Issue.4 , pp. 961-967
    • Uren, A.G.1    O'Rourke, K.2    Aravind, L.A.3    Pisabarro, M.T.4    Seshagiri, S.5    Koonin, E.V.6    Dixit, V.M.7
  • 111
    • 0142169979 scopus 로고    scopus 로고
    • Making yeast tremble: Yeast models as tools to study neurodegenerative disorders
    • M.Y. Sherman, and P.J. Muchowski Making yeast tremble: yeast models as tools to study neurodegenerative disorders Neuromolecular Med. 4 1-2 2003 133 146
    • (2003) Neuromolecular Med. , vol.4 , Issue.12 , pp. 133-146
    • Sherman, M.Y.1    Muchowski, P.J.2
  • 114
    • 0038215541 scopus 로고    scopus 로고
    • Respiratory oscillations in yeast: Mitochondrial reactive oxygen species, apoptosis and time; A hypothesis
    • D. Lloyd, K.M. Lemar, L.E. Salgado, T.M. Gould, and D.B. Murray Respiratory oscillations in yeast: mitochondrial reactive oxygen species, apoptosis and time; a hypothesis FEMS Yeast Res. 3 4 2003 333 339
    • (2003) FEMS Yeast Res. , vol.3 , Issue.4 , pp. 333-339
    • Lloyd, D.1    Lemar, K.M.2    Salgado, L.E.3    Gould, T.M.4    Murray, D.B.5
  • 116
    • 0242354121 scopus 로고    scopus 로고
    • Clues to catastrophic telomere loss in mammals from yeast telomere rapid deletion
    • A.J. Lustig Clues to catastrophic telomere loss in mammals from yeast telomere rapid deletion Nat. Rev. Genet. 4 11 2003 916 923
    • (2003) Nat. Rev. Genet. , vol.4 , Issue.11 , pp. 916-923
    • Lustig, A.J.1
  • 117
    • 1542465944 scopus 로고    scopus 로고
    • Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism
    • J.E. Vance Molecular and cell biology of phosphatidylserine and phosphatidylethanolamine metabolism Prog. Nucleic Acid Res. Mol. Biol. 75 2003 69 111
    • (2003) Prog. Nucleic Acid Res. Mol. Biol. , vol.75 , pp. 69-111
    • Vance, J.E.1
  • 121
    • 0347627140 scopus 로고    scopus 로고
    • Amino acid signalling and the integration of metabolism
    • A.J. Meijer, and P.F. Dubbelhuis Amino acid signalling and the integration of metabolism Biochem. Biophys. Res. Commun. 313 2 2004 397 403
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , Issue.2 , pp. 397-403
    • Meijer, A.J.1    Dubbelhuis, P.F.2
  • 123
    • 0842304369 scopus 로고    scopus 로고
    • Mammalian target of rapamycin inhibition as therapy for hematologic malignancies
    • A. Panwalkar, S. Verstovsek, and F.J. Giles Mammalian target of rapamycin inhibition as therapy for hematologic malignancies Cancer 100 4 2004 657 666
    • (2004) Cancer , vol.100 , Issue.4 , pp. 657-666
    • Panwalkar, A.1    Verstovsek, S.2    Giles, F.J.3
  • 126
    • 0037194894 scopus 로고    scopus 로고
    • A novel protein complex linking the δ2-glutamate receptor and autophagy. Implications for neurodegeneration in Lurcher mice
    • Z. Yue, A. Horton, M. Bravin, P. DeJager, F. Selimi, and N. Heintz A novel protein complex linking the δ2-glutamate receptor and autophagy. Implications for neurodegeneration in Lurcher mice Neuron 35 2002 921 933
    • (2002) Neuron , vol.35 , pp. 921-933
    • Yue, Z.1    Horton, A.2    Bravin, M.3    Dejager, P.4    Selimi, F.5    Heintz, N.6
  • 127
    • 0037238512 scopus 로고    scopus 로고
    • The product of the UTH1 gene, required for Bax-induced cell death in yeast, is involved in the response to rapamycin
    • N. Camougrand, A. Grelaud-Coq, E. Marza, M. Priault, J.J. Bessoule, and S. Manon The product of the UTH1 gene, required for Bax-induced cell death in yeast, is involved in the response to rapamycin Mol. Microbiol. 47 2 2003 495 506
    • (2003) Mol. Microbiol. , vol.47 , Issue.2 , pp. 495-506
    • Camougrand, N.1    Grelaud-Coq, A.2    Marza, E.3    Priault, M.4    Bessoule, J.J.5    Manon, S.6


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