메뉴 건너뛰기




Volumn 10, Issue 19, 2004, Pages 6650-6660

Influence of casein kinase II in tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis in human rhabdomyosarcoma cells

Author keywords

[No Author keywords available]

Indexed keywords

5,6 DICHLOROBENZIMIDAZOLE; ADAPTOR PROTEIN; APOPTOSIS INDUCING FACTOR; CASEIN KINASE 2ALPHA; CASEIN KINASE 2ALPHA'; CASEIN KINASE II; CASPASE 3; CASPASE 6; CASPASE 8; CASPASE 9; CYSTEINE PROTEINASE; CYTOCHROME C; DEATH INDUCING SIGNALING COMPLEX; ENZYME INHIBITOR; FAS ASSOCIATED DEATH DOMAIN PROTEIN; INTERLEUKIN 1BETA CONVERTING ENZYME INHIBITOR; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PROCASPASE 8; PROTEIN BCL 2; PROTEIN BID; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; UNCLASSIFIED DRUG; X LINKED INHIBITOR OF APOPTOSIS;

EID: 5144220294     PISSN: 10780432     EISSN: None     Source Type: Journal    
DOI: 10.1158/1078-0432.CCR-04-0576     Document Type: Article
Times cited : (62)

References (58)
  • 1
    • 13344285339 scopus 로고
    • Identification and characterization of a new member of the TNF family that induces apoptosis
    • Wiley SR, Schooley K, Smolak PJ, et al. Identification and characterization of a new member of the TNF family that induces apoptosis. Immunity 1995;3:673-82.
    • (1995) Immunity , vol.3 , pp. 673-682
    • Wiley, S.R.1    Schooley, K.2    Smolak, P.J.3
  • 2
    • 17544367410 scopus 로고    scopus 로고
    • Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family
    • Pitti RM, Marsters SA, Ruppert S, et al. Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. J Biol Chem 1996;271:12687-90.
    • (1996) J Biol Chem , vol.271 , pp. 12687-12690
    • Pitti, R.M.1    Marsters, S.A.2    Ruppert, S.3
  • 3
    • 0031782909 scopus 로고    scopus 로고
    • TRAIL: A molecule with multiple receptors and control mechanisms
    • Griffith TS, Lynch DH. TRAIL: a molecule with multiple receptors and control mechanisms. Curr Opin Immunol 1998;10:559-63.
    • (1998) Curr Opin Immunol , vol.10 , pp. 559-563
    • Griffith, T.S.1    Lynch, D.H.2
  • 4
    • 0032713075 scopus 로고    scopus 로고
    • Safety and antitumor activity of recombinant soluble Apo2 ligand
    • Ashkenazi A, Pai RC, Fong S, et al. Safety and antitumor activity of recombinant soluble Apo2 ligand. J Clin Investig 1999;104:155-62.
    • (1999) J Clin Investig , vol.104 , pp. 155-162
    • Ashkenazi, A.1    Pai, R.C.2    Fong, S.3
  • 5
    • 0032929520 scopus 로고    scopus 로고
    • Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo
    • Walczak H, Miller RE, Ariail K, et al. Tumoricidal activity of tumor necrosis factor-related apoptosis-inducing ligand in vivo. Nat Med 1999;5:157-63.
    • (1999) Nat Med , vol.5 , pp. 157-163
    • Walczak, H.1    Miller, R.E.2    Ariail, K.3
  • 6
    • 0033572413 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand's antitumor activity in vivo is enhanced by the chemotherapeutic agent CPT-11
    • Gliniak B, Le T. Tumor necrosis factor-related apoptosis-inducing ligand's antitumor activity in vivo is enhanced by the chemotherapeutic agent CPT-11. Cancer Res 1999;59:6153-8.
    • (1999) Cancer Res , vol.59 , pp. 6153-6158
    • Gliniak, B.1    Le, T.2
  • 7
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Wash DC
    • Ashkenazi A, Dixit VM. Death receptors: signaling and modulation. Science (Wash DC) 1998;281:1305-8.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 8
    • 0032530612 scopus 로고    scopus 로고
    • Intracellular regulation of TRAIL-induced apoptosis in human melanoma cells
    • Griffith TS, Chin WA, Jackson GC, et al. Intracellular regulation of TRAIL-induced apoptosis in human melanoma cells. J Immunol 1998; 161:2833-40.
    • (1998) J Immunol , vol.161 , pp. 2833-2840
    • Griffith, T.S.1    Chin, W.A.2    Jackson, G.C.3
  • 9
    • 0030954209 scopus 로고    scopus 로고
    • The CARD domain: A new apoptotic signalling motif
    • Hofmann K, Bucher P, Tschopp J. The CARD domain: a new apoptotic signalling motif. Trends Biochem Sci 1997;22:155-6.
    • (1997) Trends Biochem Sci , vol.22 , pp. 155-156
    • Hofmann, K.1    Bucher, P.2    Tschopp, J.3
  • 10
    • 0030155964 scopus 로고    scopus 로고
    • Activation of apoptosis by Apo-2 ligand is independent of FADD but blocked by CrmA
    • Marsters SA, Pitti RM, Donahue CJ, et al. Activation of apoptosis by Apo-2 ligand is independent of FADD but blocked by CrmA. Curr Biol 1996;6:750-2.
    • (1996) Curr Biol , vol.6 , pp. 750-752
    • Marsters, S.A.1    Pitti, R.M.2    Donahue, C.J.3
  • 11
    • 0032518446 scopus 로고    scopus 로고
    • Dominant-negative FADD inhibits TNFR60-, Fas/Apo1- And TRAIL-R/Apo2-mediated cell death but not gene induction
    • Wajant H, Johannes FJ, Haas E, et al. Dominant-negative FADD inhibits TNFR60-, Fas/Apo1- and TRAIL-R/Apo2-mediated cell death but not gene induction. Curr Biol 1998;8:113-6.
    • (1998) Curr Biol , vol.8 , pp. 113-116
    • Wajant, H.1    Johannes, F.J.2    Haas, E.3
  • 12
    • 0031405585 scopus 로고    scopus 로고
    • TRAIL receptors 1 (DR4) and 2 (DR5) signal FADD-dependent apoptosis and activate NF-kappaB
    • Schneider P, Thome M, Burns K, et al. TRAIL receptors 1 (DR4) and 2 (DR5) signal FADD-dependent apoptosis and activate NF-kappaB. Immunity 1997;7:831-6.
    • (1997) Immunity , vol.7 , pp. 831-836
    • Schneider, P.1    Thome, M.2    Burns, K.3
  • 13
    • 7144263731 scopus 로고    scopus 로고
    • FADD: Essential for embryo development and signaling from some, but not all, inducers of apoptosis
    • Wash DC
    • Yeh WC, Pompa JL, McCurrach ME, et al. FADD: essential for embryo development and signaling from some, but not all, inducers of apoptosis. Science (Wash DC) 1998;279:1954-8.
    • (1998) Science , vol.279 , pp. 1954-1958
    • Yeh, W.C.1    Pompa, J.L.2    McCurrach, M.E.3
  • 14
    • 0037607536 scopus 로고    scopus 로고
    • A caspase-8-independent component in TRAIL/Apo-2L-induced cell death in human rhabdomyosarcoma cells
    • Petak I, Vernes R, Szucs KS, et al. A caspase-8-independent component in TRAIL/Apo-2L-induced cell death in human rhabdomyosarcoma cells. Cell Death Differ 2003;10:729-39.
    • (2003) Cell Death Differ , vol.10 , pp. 729-739
    • Petak, I.1    Vernes, R.2    Szucs, K.S.3
  • 15
    • 0025281150 scopus 로고
    • Isolation, sequencing, and disruption of the yeast CKA2 gene: Casein kinase II is essential for viability in Saccharomyces cerevisiae
    • Padmanabha R, Chen-Wu JL, Hanna DE, et al. Isolation, sequencing, and disruption of the yeast CKA2 gene: casein kinase II is essential for viability in Saccharomyces cerevisiae. Mol Cell Biol 1990;10:4089-99.
    • (1990) Mol Cell Biol , vol.10 , pp. 4089-4099
    • Padmanabha, R.1    Chen-Wu, J.L.2    Hanna, D.E.3
  • 16
    • 0026453351 scopus 로고
    • Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle
    • Kikkawa U, Mann SK, Firtel RA, et al. Molecular cloning of casein kinase II alpha subunit from Dictyostelium discoideum and its expression in the life cycle. Mol Cell Biol 1992;12:5711-23.
    • (1992) Mol Cell Biol , vol.12 , pp. 5711-5723
    • Kikkawa, U.1    Mann, S.K.2    Firtel, R.A.3
  • 17
    • 0028909420 scopus 로고
    • Protein kinases. 4. Protein kinase CK2: An enzyme with multiple substrates and a puzzling regulation
    • Allende JE, Allende CC. Protein kinases. 4. Protein kinase CK2: an enzyme with multiple substrates and a puzzling regulation. FASEB J 1995;9:313-23.
    • (1995) FASEB J , vol.9 , pp. 313-323
    • Allende, J.E.1    Allende, C.C.2
  • 18
    • 0025239619 scopus 로고
    • Casein kinase II is elevated in solid human tumours and rapidly proliferating non-neoplastic tissue
    • Munstermann U, Fritz G, Seitz G, et al. Casein kinase II is elevated in solid human tumours and rapidly proliferating non-neoplastic tissue. Eur J Biochem 1990;189:251-7.
    • (1990) Eur J Biochem , vol.189 , pp. 251-257
    • Munstermann, U.1    Fritz, G.2    Seitz, G.3
  • 19
    • 0034978002 scopus 로고    scopus 로고
    • Protein kinase CK2 in mammary gland tumorigenesis
    • Landesman-Bollag E, Romieu-Mourez R, Song DH, et al. Protein kinase CK2 in mammary gland tumorigenesis. Oncogene 2001;20: 3247-57.
    • (2001) Oncogene , vol.20 , pp. 3247-3257
    • Landesman-Bollag, E.1    Romieu-Mourez, R.2    Song, D.H.3
  • 20
    • 0032871379 scopus 로고    scopus 로고
    • Subcellular immunolocalization of protein kinase CK2 in normal and carcinoma cells
    • Faust RA, Niehans G, Gapany M, et al. Subcellular immunolocalization of protein kinase CK2 in normal and carcinoma cells. Int J Biochem Cell Biol 1999;31:941-9.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 941-949
    • Faust, R.A.1    Niehans, G.2    Gapany, M.3
  • 21
    • 0036568813 scopus 로고    scopus 로고
    • Joining the cell survival squad: An emerging role for protein kinase CK2
    • Ahmed K, Gerber DA, Cochet C. Joining the cell survival squad: an emerging role for protein kinase CK2. Trends Cell Biol 2002;12:226-30.
    • (2002) Trends Cell Biol , vol.12 , pp. 226-230
    • Ahmed, K.1    Gerber, D.A.2    Cochet, C.3
  • 22
    • 0035884195 scopus 로고    scopus 로고
    • Targeting of the transcription factor Max during apoptosis: Phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1
    • Krippner-Heidenreich A, Talanian RV, Sekul R, et al. Targeting of the transcription factor Max during apoptosis: phosphorylation-regulated cleavage by caspase-5 at an unusual glutamic acid residue in position P1. Biochem J 2001;358:705-15.
    • (2001) Biochem J , vol.358 , pp. 705-715
    • Krippner-Heidenreich, A.1    Talanian, R.V.2    Sekul, R.3
  • 23
    • 0034799401 scopus 로고    scopus 로고
    • Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8
    • Desagher S, Osen-Sand A, Montessuit S, et al. Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. Mol Cell 2001;8:601-11.
    • (2001) Mol Cell , vol.8 , pp. 601-611
    • Desagher, S.1    Osen-Sand, A.2    Montessuit, S.3
  • 24
    • 0035750836 scopus 로고    scopus 로고
    • Regulation of lens connexin 45.6 by apoptotic protease, caspase-3
    • Yin X, Gu S, Jiang JX. Regulation of lens connexin 45.6 by apoptotic protease, caspase-3. Cell Commun Adhes 2001;8:373-6.
    • (2001) Cell Commun Adhes , vol.8 , pp. 373-376
    • Yin, X.1    Gu, S.2    Jiang, J.X.3
  • 25
    • 0036671304 scopus 로고    scopus 로고
    • Phosphorylation by protein kinase CK2: A signaling switch for the caspase-inhibiting protein ARC
    • Li PF, Li J, Muller EC, et al. Phosphorylation by protein kinase CK2: a signaling switch for the caspase-inhibiting protein ARC. Mol Cell 2002;10:247-58.
    • (2002) Mol Cell , vol.10 , pp. 247-258
    • Li, P.F.1    Li, J.2    Muller, E.C.3
  • 26
    • 0035937168 scopus 로고    scopus 로고
    • A potential role of nuclear matrix-associated protein kinase CK2 in protection against drug-induced apoptosis in cancer cells
    • Guo C, Yu S, Davis AT, et al. A potential role of nuclear matrix-associated protein kinase CK2 in protection against drug-induced apoptosis in cancer cells. J Biol Chem 2001;276:5992-9.
    • (2001) J Biol Chem , vol.276 , pp. 5992-5999
    • Guo, C.1    Yu, S.2    Davis, A.T.3
  • 27
    • 0037093352 scopus 로고    scopus 로고
    • Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells
    • Ruzzene M, Penzo D, Pinna LA. Protein kinase CK2 inhibitor 4,5,6,7-tetrabromobenzotriazole (TBB) induces apoptosis and caspase-dependent degradation of haematopoietic lineage cell-specific protein 1 (HS1) in Jurkat cells. Biochem J 2002;364:41-7.
    • (2002) Biochem J , vol.364 , pp. 41-47
    • Ruzzene, M.1    Penzo, D.2    Pinna, L.A.3
  • 28
    • 0036682276 scopus 로고    scopus 로고
    • Sensitization of tumor cells to Apo2 ligand/ TRAIL-induced apoptosis by inhibition of casein kinase II
    • Ravi R, Bedi A. Sensitization of tumor cells to Apo2 ligand/ TRAIL-induced apoptosis by inhibition of casein kinase II. Cancer Res 2002;62:4180-5.
    • (2002) Cancer Res , vol.62 , pp. 4180-4185
    • Ravi, R.1    Bedi, A.2
  • 29
    • 0034096356 scopus 로고    scopus 로고
    • Antisense oligonucleotides against protein kinase CK2-alpha inhibit growth of squamous cell carcinoma of the head and neck in vitro
    • Faust RA, Tawfic S, Davis AT, et al. Antisense oligonucleotides against protein kinase CK2-alpha inhibit growth of squamous cell carcinoma of the head and neck in vitro. Head Neck 2000;22:341-6.
    • (2000) Head Neck , vol.22 , pp. 341-346
    • Faust, R.A.1    Tawfic, S.2    Davis, A.T.3
  • 30
    • 0037269847 scopus 로고    scopus 로고
    • Protein kinase CK2: Structure, regulation and role in cellular decisions of life and death
    • Litchfield DW. Protein kinase CK2: structure, regulation and role in cellular decisions of life and death. Biochem J 2003;369:1-15.
    • (2003) Biochem J , vol.369 , pp. 1-15
    • Litchfield, D.W.1
  • 31
    • 0033861106 scopus 로고    scopus 로고
    • P53 mutation and MDM2 amplification frequency in pediatric rhabdomyosarcoma tumors and cell lines
    • Taylor AC, Shu L, Danks MK, et al. P53 mutation and MDM2 amplification frequency in pediatric rhabdomyosarcoma tumors and cell lines. Med Pediatr Oncol 2000;35:96-103.
    • (2000) Med Pediatr Oncol , vol.35 , pp. 96-103
    • Taylor, A.C.1    Shu, L.2    Danks, M.K.3
  • 32
    • 0033760404 scopus 로고    scopus 로고
    • Pediatric rhabdomyosarcoma cell lines are resistant to Fas-induced apoptosis and highly sensitive to TRAIL-induced apoptosis
    • Petak I, Douglas L, Tillman DM, et al. Pediatric rhabdomyosarcoma cell lines are resistant to Fas-induced apoptosis and highly sensitive to TRAIL-induced apoptosis. Clin Cancer Res 2000;6:4119-27.
    • (2000) Clin Cancer Res , vol.6 , pp. 4119-4127
    • Petak, I.1    Douglas, L.2    Tillman, D.M.3
  • 33
    • 0024417111 scopus 로고
    • Kinetics of inhibition by 5,6-dichloro-1-beta-D- ribofuranosylbenzimidazole on calf thymus casein kinase II
    • Zandomeni RO. Kinetics of inhibition by 5,6-dichloro-1-beta-D- ribofuranosylbenzimidazole on calf thymus casein kinase II. Biochem J 1989;262:469-73.
    • (1989) Biochem J , vol.262 , pp. 469-473
    • Zandomeni, R.O.1
  • 34
    • 0030947347 scopus 로고    scopus 로고
    • Casein kinase II is a selective target of HIV-1 transcriptional inhibitors
    • Critchfield JW, Coligan JE, Folks TM, et al. Casein kinase II is a selective target of HIV-1 transcriptional inhibitors. Proc Natl Acad Sci USA 1997;94:6110-5.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6110-6115
    • Critchfield, J.W.1    Coligan, J.E.2    Folks, T.M.3
  • 35
    • 0043016254 scopus 로고    scopus 로고
    • Rottlerin sensitizes colon carcinoma cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis via uncoupling of the mitochondria independent of protein kinase C
    • Tillman DM, Izeradjene K, Szucs KS, et al. Rottlerin sensitizes colon carcinoma cells to tumor necrosis factor-related apoptosis-inducing ligand-induced apoptosis via uncoupling of the mitochondria independent of protein kinase C. Cancer Res 2003;63:5118-25.
    • (2003) Cancer Res , vol.63 , pp. 5118-5125
    • Tillman, D.M.1    Izeradjene, K.2    Szucs, K.S.3
  • 36
    • 0032919402 scopus 로고    scopus 로고
    • Toxic bile salts induce rodent hepatocyte apoptosis via direct activation of Fas
    • Faubion WA, Guicciardi ME, Miyoshi H, et al. Toxic bile salts induce rodent hepatocyte apoptosis via direct activation of Fas. J Clin Investig 1999;103:137-45.
    • (1999) J Clin Investig , vol.103 , pp. 137-145
    • Faubion, W.A.1    Guicciardi, M.E.2    Miyoshi, H.3
  • 37
    • 0038339094 scopus 로고    scopus 로고
    • TRAIL induced survival and proliferation in cancer cells resistant towards TRAIL-induced apoptosis mediated by NF-kappaB
    • Ehrhardt H, Fulda S, Schmid I, et al. TRAIL induced survival and proliferation in cancer cells resistant towards TRAIL-induced apoptosis mediated by NF-kappaB. Oncogene 2003;22:3842-52.
    • (2003) Oncogene , vol.22 , pp. 3842-3852
    • Ehrhardt, H.1    Fulda, S.2    Schmid, I.3
  • 38
    • 0031870398 scopus 로고    scopus 로고
    • Expression of genes that regulate Fas signalling and Fas-mediated apoptosis in colon carcinoma cells
    • Tillman DM, Harwood FG, Gibson AA, et al. Expression of genes that regulate Fas signalling and Fas-mediated apoptosis in colon carcinoma cells. Cell Death Differ 1998;5:450-7.
    • (1998) Cell Death Differ , vol.5 , pp. 450-457
    • Tillman, D.M.1    Harwood, F.G.2    Gibson, A.A.3
  • 39
    • 0033555811 scopus 로고    scopus 로고
    • Enforced expression of the GATA-2 transcription factor blocks normal hematopoiesis
    • Persons DA, Allay JA, Allay ER, et al. Enforced expression of the GATA-2 transcription factor blocks normal hematopoiesis. Blood 1999; 93:488-99.
    • (1999) Blood , vol.93 , pp. 488-499
    • Persons, D.A.1    Allay, J.A.2    Allay, E.R.3
  • 40
    • 0036790423 scopus 로고    scopus 로고
    • Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: Absolute requirement for removal of caspase-6 prodomain
    • Cowling V, Downward J. Caspase-6 is the direct activator of caspase-8 in the cytochrome c-induced apoptosis pathway: absolute requirement for removal of caspase-6 prodomain. Cell Death Differ 2002;9:1046-56.
    • (2002) Cell Death Differ , vol.9 , pp. 1046-1056
    • Cowling, V.1    Downward, J.2
  • 41
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Lond
    • Deveraux QL, Takahashi R, Salvesen GS, Reed JC. X-linked IAP is a direct inhibitor of cell-death proteases. Nature (Lond) 1997;388: 300-4.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 42
    • 0032522738 scopus 로고    scopus 로고
    • IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases
    • Deveraux QL, Roy N, Stennicke HR, et al. IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases. EMBO J 1998;17:2215-23.
    • (1998) EMBO J , vol.17 , pp. 2215-2223
    • Deveraux, Q.L.1    Roy, N.2    Stennicke, H.R.3
  • 43
    • 10744228158 scopus 로고    scopus 로고
    • Regulation and targeting of antiapoptotic XIAP in acute myeloid leukemia
    • Baltimore
    • Carter BZ, Milella M, Tsao T, et al. Regulation and targeting of antiapoptotic XIAP in acute myeloid leukemia. Leukemia (Baltimore) 2003;17:2081-9.
    • (2003) Leukemia , vol.17 , pp. 2081-2089
    • Carter, B.Z.1    Milella, M.2    Tsao, T.3
  • 44
    • 0031961994 scopus 로고    scopus 로고
    • Human IAP-like protein regulates programmed cell death downstream of Bcl-xL and cytochrome c
    • Duckett CS, Li F, Wang Y, Tomaselli KJ, et al. Human IAP-like protein regulates programmed cell death downstream of Bcl-xL and cytochrome c. Mol Cell Biol 1998;18:608-15.
    • (1998) Mol Cell Biol , vol.18 , pp. 608-615
    • Duckett, C.S.1    Li, F.2    Wang, Y.3    Tomaselli, K.J.4
  • 45
    • 13344278692 scopus 로고    scopus 로고
    • Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes
    • Lond
    • Liston P, Roy N, Tamai K, et al. Suppression of apoptosis in mammalian cells by NAIP and a related family of IAP genes. Nature (Lond) 1996;379:349-53.
    • (1996) Nature , vol.379 , pp. 349-353
    • Liston, P.1    Roy, N.2    Tamai, K.3
  • 46
    • 0030849093 scopus 로고    scopus 로고
    • A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis
    • Thornberry NA, Rano TA, Peterson EP, et al. A combinatorial approach defines specificities of members of the caspase family and granzyme B. Functional relationships established for key mediators of apoptosis. J Biol Chem 1997;272:17907-11.
    • (1997) J Biol Chem , vol.272 , pp. 17907-17911
    • Thornberry, N.A.1    Rano, T.A.2    Peterson, E.P.3
  • 48
    • 0032555697 scopus 로고    scopus 로고
    • Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis
    • Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 1998;94:491-501.
    • (1998) Cell , vol.94 , pp. 491-501
    • Li, H.1    Zhu, H.2    Xu, C.J.3    Yuan, J.4
  • 49
    • 0033534446 scopus 로고    scopus 로고
    • Caspase cleaved BID targets mitochondria and is required for cytochrome C release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death
    • Gross A, Yin XM, Wang K, et al. Caspase cleaved BID targets mitochondria and is required for cytochrome C release, while BCL-XL prevents this release but not tumor necrosis factor-R1/Fas death. J Biol Chem 1999;274:1156-63.
    • (1999) J Biol Chem , vol.274 , pp. 1156-1163
    • Gross, A.1    Yin, X.M.2    Wang, K.3
  • 50
    • 0034663829 scopus 로고    scopus 로고
    • tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c
    • Wei MC, Lindsten T, Mootha VK, et al. tBID, a membrane-targeted death ligand, oligomerizes BAK to release cytochrome c. Genes Dev 2000;14:2060-71.
    • (2000) Genes Dev , vol.14 , pp. 2060-2071
    • Wei, M.C.1    Lindsten, T.2    Mootha, V.K.3
  • 51
    • 0035097350 scopus 로고    scopus 로고
    • Activation of protein kinase C inhibits TRAIL-induced caspases activation, mitochondrial events and apoptosis in a human leukemic T cell line
    • Sarker M, Ruiz-Ruiz C, Lopez-Rivas A. Activation of protein kinase C inhibits TRAIL-induced caspases activation, mitochondrial events and apoptosis in a human leukemic T cell line. Cell Death Differ 2001;8:172-81.
    • (2001) Cell Death Differ , vol.8 , pp. 172-181
    • Sarker, M.1    Ruiz-Ruiz, C.2    Lopez-Rivas, A.3
  • 52
    • 0035912060 scopus 로고    scopus 로고
    • Intracellular mechanisms of TRAIL: Apoptosis through mitochondrial- dependent and -independent pathways
    • Suliman A, Lam A, Datta R, et al. Intracellular mechanisms of TRAIL: apoptosis through mitochondrial-dependent and -independent pathways. Oncogene 2001;20:2122-33.
    • (2001) Oncogene , vol.20 , pp. 2122-2133
    • Suliman, A.1    Lam, A.2    Datta, R.3
  • 53
    • 0034811651 scopus 로고    scopus 로고
    • Trail-induced apoptosis in type I leukemic cells is not enhanced by overexpression of bax
    • Jia L, Patwari Y, Kelsey SM, et al. Trail-induced apoptosis in type I leukemic cells is not enhanced by overexpression of bax. Biochem Biophys Res Commun 2001;283:1037-45.
    • (2001) Biochem Biophys Res Commun , vol.283 , pp. 1037-1045
    • Jia, L.1    Patwari, Y.2    Kelsey, S.M.3
  • 54
    • 0034615860 scopus 로고    scopus 로고
    • Failure of Bcl-2 to block cytochrome c redistribution during TRAIL-induced apoptosis
    • Keogh SA, Walczak H, Bouchier-Hayes L, et al. Failure of Bcl-2 to block cytochrome c redistribution during TRAIL-induced apoptosis. FEBS Lett 2000;471:93-8.
    • (2000) FEBS Lett , vol.471 , pp. 93-98
    • Keogh, S.A.1    Walczak, H.2    Bouchier-Hayes, L.3
  • 55
    • 0034213248 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand retains its apoptosis-inducing capacity on Bcl-2- Or Bcl-xL-overexpressing chemotherapy-resistant tumor cells
    • Walczak H, Bouchon A, Stahl H, et al. Tumor necrosis factor-related apoptosis-inducing ligand retains its apoptosis-inducing capacity on Bcl-2- or Bcl-xL-overexpressing chemotherapy-resistant tumor cells. Cancer Res 2000;60:3051-7.
    • (2000) Cancer Res , vol.60 , pp. 3051-3057
    • Walczak, H.1    Bouchon, A.2    Stahl, H.3
  • 56
    • 0038320035 scopus 로고    scopus 로고
    • Apo2L/TRAIL: Apoptosis signaling, biology, and potential for cancer therapy
    • Almasan A, Ashkenazi A. Apo2L/TRAIL: apoptosis signaling, biology, and potential for cancer therapy. Cytokine Growth Factor Rev 2003;14:337-48.
    • (2003) Cytokine Growth Factor Rev , vol.14 , pp. 337-348
    • Almasan, A.1    Ashkenazi, A.2
  • 57
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Lond
    • Elbashi SM, Harborth J, Lendeckel W, et al. Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature (Lond) 2001;411:494-8.
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashi, S.M.1    Harborth, J.2    Lendeckel, W.3
  • 58
    • 0035670183 scopus 로고    scopus 로고
    • Response of cancer cells to molecular interruption of the CK2 signal
    • Wang H, Davis A, Yu S, et al. Response of cancer cells to molecular interruption of the CK2 signal. Mol Cell Biochem 2001;227:167-74.
    • (2001) Mol Cell Biochem , vol.227 , pp. 167-174
    • Wang, H.1    Davis, A.2    Yu, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.