메뉴 건너뛰기




Volumn 46, Issue 9, 2011, Pages 3734-3747

Non-substituted N-heteroaromatic selenosemicarbazone metal complexes induce apoptosis in cancer cells via activation of mitochondrial pathway

Author keywords

Antiproliferative activity; Apoptosis; Selenosemicarbazone; Zn(II), Ni(II), and Cd(II) complexes

Indexed keywords

ANTINEOPLASTIC METAL COMPLEX; CADMIUM; CASPASE 3; CISPLATIN; CYTOCHROME C; MITOGEN ACTIVATED PROTEIN KINASE; NICKEL; PROTEIN BAX; PROTEIN P53; PROTEIN P73; ZINC;

EID: 80052960393     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2011.05.039     Document Type: Article
Times cited : (39)

References (71)
  • 1
    • 0035902067 scopus 로고    scopus 로고
    • Cancer epidemiology in the last century and the next decade
    • J. Peto Cancer epidemiology in the last century and the next decade Nature 411 2001 390 395
    • (2001) Nature , vol.411 , pp. 390-395
    • Peto, J.1
  • 2
    • 0035525733 scopus 로고    scopus 로고
    • Cellular stress response and apoptosis in cancer therapy
    • I. Herr, and K.M. Debatin Cellular stress response and apoptosis in cancer therapy Blood 98 2001 2603 2614
    • (2001) Blood , vol.98 , pp. 2603-2614
    • Herr, I.1    Debatin, K.M.2
  • 3
    • 0034057320 scopus 로고    scopus 로고
    • Apoptosis in cancer
    • S.W. Lowe, and A.W. Lin Apoptosis in cancer Carcinogenesis 21 2000 485 495
    • (2000) Carcinogenesis , vol.21 , pp. 485-495
    • Lowe, S.W.1    Lin, A.W.2
  • 4
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • M.O. Hengartner The biochemistry of apoptosis Nature 407 2000 770 776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 5
    • 0037069929 scopus 로고    scopus 로고
    • Chemotherapy: Targeting the mitochondrial cell death pathway
    • K.M. Debatin, D. Poncet, and G. Kroemer Chemotherapy: targeting the mitochondrial cell death pathway Oncogene 21 2002 8786 8803
    • (2002) Oncogene , vol.21 , pp. 8786-8803
    • Debatin, K.M.1    Poncet, D.2    Kroemer, G.3
  • 7
    • 0033600234 scopus 로고    scopus 로고
    • The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage
    • J.G. Gong, A. Costanzo, H.Q. Yang, G. Melino, W.G. Kaelin Jr., M. Levrero, and J.Y. Wang The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage Nature 399 1999 806 809
    • (1999) Nature , vol.399 , pp. 806-809
    • Gong, J.G.1    Costanzo, A.2    Yang, H.Q.3    Melino, G.4    Kaelin, Jr.W.G.5    Levrero, M.6    Wang, J.Y.7
  • 8
    • 0037169358 scopus 로고    scopus 로고
    • Apoptosis: A link between cancer genetics and chemotherapy
    • R.W. Johnstone, A.A. Ruefli, and S.W. Lowe Apoptosis: a link between cancer genetics and chemotherapy Cell 108 2002 153 164
    • (2002) Cell , vol.108 , pp. 153-164
    • Johnstone, R.W.1    Ruefli, A.A.2    Lowe, S.W.3
  • 10
    • 0014294260 scopus 로고
    • Effect of selenium organic compounds on the radiation effect of Phycomyces blakesleanus
    • W. Brucker, and H.G. Rohde Effect of selenium organic compounds on the radiation effect of Phycomyces blakesleanus Pharmazie 23 1968 310 315
    • (1968) Pharmazie , vol.23 , pp. 310-315
    • Brucker, W.1    Rohde, H.G.2
  • 12
    • 0022545746 scopus 로고
    • Structure-activity relationships among alpha-(N)-heterocyclic acyl thiosemicarbazones and related compounds as inhibitors of herpes simplex virus type 1-specified ribonucleoside diphosphate reductase
    • S.R. Turk, C. Shipman Jr., and J.C. Drach Structure-activity relationships among alpha-(N)-heterocyclic acyl thiosemicarbazones and related compounds as inhibitors of herpes simplex virus type 1-specified ribonucleoside diphosphate reductase J. Gen. Virol. 67 1986 1625 1632
    • (1986) J. Gen. Virol. , vol.67 , pp. 1625-1632
    • Turk, S.R.1    Shipman, Jr.C.2    Drach, J.C.3
  • 13
    • 0020527080 scopus 로고
    • 2-Acetylpyridine thiosemicarbazones. 6.2-Acetylpyridine and 2-butyrylpyridine thiosemicarbazones as antileukemic agents
    • D.L. Klayman, J.P. Scovill, C.J. Mason, J.F. Bartosevich, J. Bruce, and A.J. Lin 2-Acetylpyridine thiosemicarbazones. 6.2-Acetylpyridine and 2-butyrylpyridine thiosemicarbazones as antileukemic agents Arzneim. Forsch 33 1983 909 912
    • (1983) Arzneim. Forsch , vol.33 , pp. 909-912
    • Klayman, D.L.1    Scovill, J.P.2    Mason, C.J.3    Bartosevich, J.F.4    Bruce, J.5    Lin, A.J.6
  • 14
    • 0019388387 scopus 로고
    • 2-Acetylpyridine thiosemicarbazones. 1. A new class of potential antimalarial agents
    • D.L. Klayman, J.P. Scovill, J.F. Bartosevich, and C.J. Mason 2-Acetylpyridine thiosemicarbazones. 1. A new class of potential antimalarial agents Eur. J. Med. Chem. 16 1981 317 320
    • (1981) Eur. J. Med. Chem. , vol.16 , pp. 317-320
    • Klayman, D.L.1    Scovill, J.P.2    Bartosevich, J.F.3    Mason, C.J.4
  • 15
    • 0020519185 scopus 로고
    • 2-Acetylpyridine thiosemicarbazones. 5. 1-[1-(2-Pyridyl)ethyl]-3- thiosemicarbazides as potential antimalarial agents
    • D.L. Klayman, J.P. Scovill, J.F. Bartosevich, and J. Bruce 2-Acetylpyridine thiosemicarbazones. 5. 1-[1-(2-Pyridyl)ethyl]-3- thiosemicarbazides as potential antimalarial agents J. Med. Chem. 26 1983 35 39
    • (1983) J. Med. Chem. , vol.26 , pp. 35-39
    • Klayman, D.L.1    Scovill, J.P.2    Bartosevich, J.F.3    Bruce, J.4
  • 16
    • 0015835386 scopus 로고
    • Development of inhibitors of alkaline phosphatase-an enzyme involved in resistance of sarcoma 180-TG to 6-thiopurines
    • M.H. Lee, E. Sznycer-Bochner, K.C. Agrawal, M.K. Wolpert, and A.C. Sartorelli Development of inhibitors of alkaline phosphatase-an enzyme involved in resistance of sarcoma 180-TG to 6-thiopurines Biochem. Pharmacol. 22 1973 1477 1485
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 1477-1485
    • Lee, M.H.1    Sznycer-Bochner, E.2    Agrawal, K.C.3    Wolpert, M.K.4    Sartorelli, A.C.5
  • 17
    • 0016244214 scopus 로고
    • Comparative studies of the antineoplastic activity of 5-hydroxy-2-formylpyridine thiosemicarbazone and its seleno-semicarbazone, guanylhydrazone and semicarbazone analogs
    • K.C. Agrawal, B.A. Booth, R.L. Michaud, E.C. Moore, and A.C. Sartorelli Comparative studies of the antineoplastic activity of 5-hydroxy-2-formylpyridine thiosemicarbazone and its seleno-semicarbazone, guanylhydrazone and semicarbazone analogs Biochem. Pharmacol. 23 1974 2421 2429
    • (1974) Biochem. Pharmacol. , vol.23 , pp. 2421-2429
    • Agrawal, K.C.1    Booth, B.A.2    Michaud, R.L.3    Moore, E.C.4    Sartorelli, A.C.5
  • 18
    • 0026620075 scopus 로고
    • Synthesis and antitumor activity of substituted benzaldehyde/ cinnamicaldehyde selenosemicarbazones
    • M. Liu, P.L. Xiu, and Z.J. Wang Synthesis and antitumor activity of substituted benzaldehyde/cinnamicaldehyde selenosemicarbazones Yao Xue Xue Bao 27 1992 388 393
    • (1992) Yao Xue Xue Bao , vol.27 , pp. 388-393
    • Liu, M.1    Xiu, P.L.2    Wang, Z.J.3
  • 19
    • 35348872557 scopus 로고    scopus 로고
    • Effect of metal ion complexation and chalcogen donor identity on the antiproliferative activity of 2-acetylpyridine N, N-dimethyl(chalcogen) semicarbazones
    • C.R. Kowol, R. Eichinger, M.A. Jakupec, M. Galanski, V.B. Arion, and B.K. Keppler Effect of metal ion complexation and chalcogen donor identity on the antiproliferative activity of 2-acetylpyridine N, N-dimethyl(chalcogen) semicarbazones J. Inorg. Biochem. 101 2007 1946 1957
    • (2007) J. Inorg. Biochem. , vol.101 , pp. 1946-1957
    • Kowol, C.R.1    Eichinger, R.2    Jakupec, M.A.3    Galanski, M.4    Arion, V.B.5    Keppler, B.K.6
  • 20
    • 61349170622 scopus 로고    scopus 로고
    • Synthesis and characterization of new Pt(II) and Pd(II) complexes with 2-quinolinecarboxaldehyde selenosemicarbazone: Cytotoxic activity evaluation of Cd(II), Zn(II), Ni(II), Pt(II) and Pd(II) complexes with heteroaromatic selenosemicarbazones
    • N. Gligorijević, T. Todorović, S. Radulović, D. Sladić, N. Filipović, D. Goevac, D. Jeremić, and K. Anelkovi&cacute Synthesis and characterization of new Pt(II) and Pd(II) complexes with 2-quinolinecarboxaldehyde selenosemicarbazone: cytotoxic activity evaluation of Cd(II), Zn(II), Ni(II), Pt(II) and Pd(II) complexes with heteroaromatic selenosemicarbazones Eur. J. Med. Chem. 44 2009 1623 1629
    • (2009) Eur. J. Med. Chem. , vol.44 , pp. 1623-1629
    • Gligorijević, N.1    Todorović, T.2    Radulović, S.3    Sladić, D.4    Filipović, N.5    Goevac, D.6    Jeremić, D.7    Anelkovi8    Cacute, K.9
  • 22
    • 77952553954 scopus 로고    scopus 로고
    • Synthesis, structure and characterization of novel Cd(II) and Zn(II) complexes with the condensation product of 2-formylpyridine and selenosemicarbazide antiproliferative activity of the synthesized complexes and related selenosemicarbazone complexes
    • S. Bjelogrlić, T. Todorović, A. Bacchi, M. Zec, D. Sladić, T. Srdić-Rajić, D. Radanović, S. Radulović, G. Pelizzi, and K. Anelković Synthesis, structure and characterization of novel Cd(II) and Zn(II) complexes with the condensation product of 2-formylpyridine and selenosemicarbazide antiproliferative activity of the synthesized complexes and related selenosemicarbazone complexes J. Inorg. Biochem. 104 2010 673 682
    • (2010) J. Inorg. Biochem. , vol.104 , pp. 673-682
    • Bjelogrlić, S.1    Todorović, T.2    Bacchi, A.3    Zec, M.4    Sladić, D.5    Srdić-Rajić, T.6    Radanović, D.7    Radulović, S.8    Pelizzi, G.9    Anelković, K.10
  • 23
    • 0031868515 scopus 로고    scopus 로고
    • Taxanes propagate apoptosis via two cell populations with distinctive cytological and molecular traits
    • P.J. Moos, and F.A. Fitzpatrick Taxanes propagate apoptosis via two cell populations with distinctive cytological and molecular traits Cell. Growth Differ. 9 1998 687 697
    • (1998) Cell. Growth Differ. , vol.9 , pp. 687-697
    • Moos, P.J.1    Fitzpatrick, F.A.2
  • 24
    • 0034671751 scopus 로고    scopus 로고
    • Requirement for ERK activation in cisplatin-induced apoptosis
    • X. Wang, J.L. Martindale, and N.J. Holbrook Requirement for ERK activation in cisplatin-induced apoptosis J. Biol. Chem. 275 2000 39435 39443
    • (2000) J. Biol. Chem. , vol.275 , pp. 39435-39443
    • Wang, X.1    Martindale, J.L.2    Holbrook, N.J.3
  • 25
    • 0035890335 scopus 로고    scopus 로고
    • Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate
    • G.W. Makin, B.M. Corfe, G.J. Griffiths, A. Thistlethwaite, J.A. Hickman, and C. Dive Damage-induced Bax N-terminal change, translocation to mitochondria and formation of Bax dimers/complexes occur regardless of cell fate EMBO J. 20 2001 6306 6315
    • (2001) EMBO J. , vol.20 , pp. 6306-6315
    • Makin, G.W.1    Corfe, B.M.2    Griffiths, G.J.3    Thistlethwaite, A.4    Hickman, J.A.5    Dive, C.6
  • 26
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • W.C. Earnshaw, L.M. Martins, and S.H. Kaufmann Mammalian caspases: structure, activation, substrates, and functions during apoptosis Annu. Rev. Biochem. 68 1999 383 424
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 27
    • 0032505127 scopus 로고    scopus 로고
    • Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade
    • P. Juo, C.J. Kuo, J. Yuan, and J. Blenis Essential requirement for caspase-8/FLICE in the initiation of the Fas-induced apoptotic cascade Curr. Biol. 8 1998 1001 1008
    • (1998) Curr. Biol. , vol.8 , pp. 1001-1008
    • Juo, P.1    Kuo, C.J.2    Yuan, J.3    Blenis, J.4
  • 29
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • R.U. Janicke, 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
    • Janicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 30
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • S. Shimizu, M. Narita, and Y. Tsujimoto Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC Nature 399 1997 483 487
    • (1997) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 32
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • D.R. Green, and J.C. Reed Mitochondria and apoptosis Anticancer. Res. 281 1998 1309 1312
    • (1998) Anticancer. Res. , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 33
    • 0034630167 scopus 로고    scopus 로고
    • Induction of apoptosis by cancer chemotherapy
    • S.H. Kaufmann, and W.C. Earnshaw Induction of apoptosis by cancer chemotherapy Exp. Cell Res. 256 2000 42 49
    • (2000) Exp. Cell Res. , vol.256 , pp. 42-49
    • Kaufmann, S.H.1    Earnshaw, W.C.2
  • 34
    • 0033400809 scopus 로고    scopus 로고
    • Apoptosis and cancer drug targeting
    • W.R. Sellers, and D.E. Fisher Apoptosis and cancer drug targeting J. Clin. Invest. 104 1999 1655 1661
    • (1999) J. Clin. Invest. , vol.104 , pp. 1655-1661
    • Sellers, W.R.1    Fisher, D.E.2
  • 35
    • 0028025563 scopus 로고
    • Apoptosis in cancer therapy: Crossing the threshold
    • D.E. Fisher Apoptosis in cancer therapy: crossing the threshold Cell 78 1994 539 542
    • (1994) Cell , vol.78 , pp. 539-542
    • Fisher, D.E.1
  • 37
    • 0030828981 scopus 로고    scopus 로고
    • Requirement of the caspase-3/CPP32 protease cascade for apoptotic death following cytokine deprivation in hematopoietic cells
    • T. Ohta, T. Kinoshita, M. Naito, T. Nozaki, M. Masutani, T. Tsuruo, and A. Miyajima Requirement of the caspase-3/CPP32 protease cascade for apoptotic death following cytokine deprivation in hematopoietic cells J. Biol. Chem. 272 1997 23111 23116
    • (1997) J. Biol. Chem. , vol.272 , pp. 23111-23116
    • Ohta, T.1    Kinoshita, T.2    Naito, M.3    Nozaki, T.4    Masutani, M.5    Tsuruo, T.6    Miyajima, A.7
  • 39
    • 0033552638 scopus 로고    scopus 로고
    • Twenty years of p53 research: Structural and functional aspects of the p53 protein
    • P. May, and E. May Twenty years of p53 research: structural and functional aspects of the p53 protein Oncogene 18 1999 7621 7636
    • (1999) Oncogene , vol.18 , pp. 7621-7636
    • May, P.1    May, E.2
  • 40
    • 0034576495 scopus 로고    scopus 로고
    • P63 and P73: P53 mimics, menaces and more
    • A. Yang, and F. McKeon P63 and P73: P53 mimics, menaces and more Nat. Rev. Mol. Cell Biol. 1 2000 199 207
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 199-207
    • Yang, A.1    McKeon, F.2
  • 42
    • 0031564954 scopus 로고    scopus 로고
    • P73 is a simian [correction of human] p53-related protein that can induce apoptosis
    • C.A. Jost, M.C. Marin, and W.G. Kaelin Jr. p73 is a simian [correction of human] p53-related protein that can induce apoptosis Nature 389 1997 191 194
    • (1997) Nature , vol.389 , pp. 191-194
    • Jost, C.A.1    Marin, M.C.2    Kaelin, Jr.W.G.3
  • 43
    • 0032533514 scopus 로고    scopus 로고
    • The potential tumor suppressor p73 differentially regulates cellular p53 target genes
    • J. Zhu, J. Jiang, W. Zhou, and X. Chen The potential tumor suppressor p73 differentially regulates cellular p53 target genes Cancer Res. 58 1998 5061 5065
    • (1998) Cancer Res. , vol.58 , pp. 5061-5065
    • Zhu, J.1    Jiang, J.2    Zhou, W.3    Chen, X.4
  • 44
    • 0032951530 scopus 로고    scopus 로고
    • P73 function is inhibited by tumor-derived p53 mutants in mammalian cells
    • C.J. di Como, C. Gaiddon, and C. Prives p73 function is inhibited by tumor-derived p53 mutants in mammalian cells Mol. Cell. Biol. 19 1999 1438 1449
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 1438-1449
    • Di Como, C.J.1    Gaiddon, C.2    Prives, C.3
  • 46
    • 0033602462 scopus 로고    scopus 로고
    • Inactivation of the p53-homologue p73 by the mdm2-oncoprotein
    • M. Dobbelstein, S. Wienzek, C. Konig, and J. Roth Inactivation of the p53-homologue p73 by the mdm2-oncoprotein Oncogene 18 1999 2101 2106
    • (1999) Oncogene , vol.18 , pp. 2101-2106
    • Dobbelstein, M.1    Wienzek, S.2    Konig, C.3    Roth, J.4
  • 47
    • 0027166048 scopus 로고
    • Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death
    • Z.N. Oltvai, C.L. Milliman, and S.J. Korsmeyer Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death Cell 74 1993 609 619
    • (1993) Cell , vol.74 , pp. 609-619
    • Oltvai, Z.N.1    Milliman, C.L.2    Korsmeyer, S.J.3
  • 49
    • 0030963602 scopus 로고    scopus 로고
    • Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis
    • Y.T. Hsu, K.G. Wolter, and R.J. Youle Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis Proc. Natl. Acad. Sci. U. S. A. 94 1997 3668 3672
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 3668-3672
    • Hsu, Y.T.1    Wolter, K.G.2    Youle, R.J.3
  • 55
    • 0033603460 scopus 로고    scopus 로고
    • Bcl-2 and caspase inhibition cooperate to inhibit tumor necrosis factor-alpha-induced cell death in a Bcl-2 cleavage-independent fashion
    • B.W. Johnson, and L.H. Boise Bcl-2 and caspase inhibition cooperate to inhibit tumor necrosis factor-alpha-induced cell death in a Bcl-2 cleavage-independent fashion J. Biol. Chem. 274 1999 18552 18558
    • (1999) J. Biol. Chem. , vol.274 , pp. 18552-18558
    • Johnson, B.W.1    Boise, L.H.2
  • 57
    • 0033580926 scopus 로고    scopus 로고
    • Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation
    • A. Saleh, S.M. Srinivasula, S. Acharya, R. Fishel, and E.S. Alnemri Cytochrome c and dATP-mediated oligomerization of Apaf-1 is a prerequisite for procaspase-9 activation J. Biol. Chem. 274 1999 17941 17945
    • (1999) J. Biol. Chem. , vol.274 , pp. 17941-17945
    • Saleh, A.1    Srinivasula, S.M.2    Acharya, S.3    Fishel, R.4    Alnemri, E.S.5
  • 58
    • 77952671266 scopus 로고    scopus 로고
    • Induction of apoptosis by the transcription factor c-Jun
    • E. Bossy-Wetzel, D.D. Newmeyer, and D.R. Green Induction of apoptosis by the transcription factor c-Jun EMBO J. 17 1997 37 49
    • (1997) EMBO J. , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 59
    • 17444386342 scopus 로고    scopus 로고
    • Pharmacological inhibitors of extracellular signal-regulated protein kinases attenuate the apoptotic action of cisplatin in human myeloid leukemia cells via glutathione-independent reduction in intracellular drug accumulation
    • D. Amran, P. Sancho, C. Fernandez, D. Esteban, A.M. Ramos, E. de Blas, M. Gomez, M.A. Palacios, and P. Aller Pharmacological inhibitors of extracellular signal-regulated protein kinases attenuate the apoptotic action of cisplatin in human myeloid leukemia cells via glutathione-independent reduction in intracellular drug accumulation Biochimi. Biophys. Acta 1743 2005 269 279
    • (2005) Biochimi. Biophys. Acta , vol.1743 , pp. 269-279
    • Amran, D.1    Sancho, P.2    Fernandez, C.3    Esteban, D.4    Ramos, A.M.5    De Blas, E.6    Gomez, M.7    Palacios, M.A.8    Aller, P.9
  • 60
    • 5644300463 scopus 로고    scopus 로고
    • Ultraviolet A-induced modulation of Bcl-XL by p38 MAPK in human Keratinocytes: Post-transcriptional regulation through the 3'-untranslated region
    • M.A. Bachelor, and G.T. Bowden Ultraviolet A-induced modulation of Bcl-XL by p38 MAPK in human Keratinocytes: post-transcriptional regulation through the 3'-untranslated region J. Biol. Chem. 279 2003 42658 42668
    • (2003) J. Biol. Chem. , vol.279 , pp. 42658-42668
    • Bachelor, M.A.1    Bowden, G.T.2
  • 61
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • G. Kroemer, B. Dallaporta, and M. Resche-Rigon The mitochondrial death/life regulator in apoptosis and necrosis Annu. Rev. Physiol. 60 1998 619 642
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 62
    • 0032404536 scopus 로고    scopus 로고
    • The central executioners of apoptosis: Caspases or mitochondria?
    • D. Green, and G. Kroemer The central executioners of apoptosis: caspases or mitochondria? Trends Cell Biol. 8 1998 267 271
    • (1998) Trends Cell Biol. , vol.8 , pp. 267-271
    • Green, D.1    Kroemer, G.2
  • 63
    • 1642494810 scopus 로고    scopus 로고
    • F16, a mitochondriotoxic compound, triggers apoptosis or necrosis depending on the genetic background of the target carcinoma cell
    • V.R. Fantin, and P. Leder F16, a mitochondriotoxic compound, triggers apoptosis or necrosis depending on the genetic background of the target carcinoma cell Cancer Research 64 2004 329 336
    • (2004) Cancer Research , vol.64 , pp. 329-336
    • Fantin, V.R.1    Leder, P.2
  • 64
    • 0036561908 scopus 로고    scopus 로고
    • Modelling the molecular circuitry of cancer
    • W.C. Hahn, and R.A. Weinberg Modelling the molecular circuitry of cancer Nat. Rev. Cancer 2 2002 331 341
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 331-341
    • Hahn, W.C.1    Weinberg, R.A.2
  • 65
    • 0033047268 scopus 로고    scopus 로고
    • Apoptosis versus necrosis: Which should be the aim of cancer therapy?
    • H. Kiaris, and A.V. Schally Apoptosis versus necrosis: which should be the aim of cancer therapy? Proc. Soc. Exp. Biol. Med. 221 1999 87 88
    • (1999) Proc. Soc. Exp. Biol. Med. , vol.221 , pp. 87-88
    • Kiaris, H.1    Schally, A.V.2
  • 66
    • 0036889436 scopus 로고    scopus 로고
    • Comparison of anthracycline-induced death of human leukemia cells: Programmed cell death versus necrosis
    • D.C. Dartsch, A. Schaefer, S. Boldt, W. Kolch, and H. Marquardt Comparison of anthracycline-induced death of human leukemia cells: programmed cell death versus necrosis Apoptosis 7 2002 537 548
    • (2002) Apoptosis , vol.7 , pp. 537-548
    • Dartsch, D.C.1    Schaefer, A.2    Boldt, S.3    Kolch, W.4    Marquardt, H.5
  • 67
    • 0033566932 scopus 로고    scopus 로고
    • Cutting edge: Differential effect of apoptotic versus necrotic tumor cells on macrophage antitumor activities
    • I. Reiter, B. Krammer, and G. Schwamberger Cutting edge: differential effect of apoptotic versus necrotic tumor cells on macrophage antitumor activities J. Immunol. 163 1999 1730 1732
    • (1999) J. Immunol. , vol.163 , pp. 1730-1732
    • Reiter, I.1    Krammer, B.2    Schwamberger, G.3
  • 70
    • 0030745646 scopus 로고    scopus 로고
    • Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3
    • H. Zou, W.J. Henzel, X. Liu, A. Lutschg, and X. Wang Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3 Cell 90 1997 405 413
    • (1997) Cell , vol.90 , pp. 405-413
    • Zou, H.1    Henzel, W.J.2    Liu, X.3    Lutschg, A.4    Wang, X.5
  • 71
    • 34249859423 scopus 로고    scopus 로고
    • Ethanol induced mitochondria injury and permeability transition pore opening: Role of mitochondria in alcoholic liver disease
    • Y. Ming, Z. Ping, L. Hui-Min, Z. Hai-Tao, and L. Li Ethanol induced mitochondria injury and permeability transition pore opening: role of mitochondria in alcoholic liver disease World J. Gastroenterol. 13 2007 2352 2356
    • (2007) World J. Gastroenterol. , vol.13 , pp. 2352-2356
    • Ming, Y.1    Ping, Z.2    Hui-Min, L.3    Hai-Tao, Z.4    Li, L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.