메뉴 건너뛰기




Volumn 34, Issue 3, 2012, Pages 165-175

Caspase control: Protagonists of cancer cell apoptosis

Author keywords

Apoptosis; Caspase 8; Proteasome inhibitors

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; ABEXINOSTAT; ABIRATERONE; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; BEVACIZUMAB; BORTEZOMIB; CALISTOGA; CASPASE; CASPASE 8; CURCUMIN; DOCETAXEL; DOXORUBICIN; ENZALUTAMIDE; EPOXOMICIN; ETOPOSIDE; IDELALISIB; LACTACYSTIN; MITOMYCIN; PACLITAXEL; PERIFOSINE; PHOSPHATIDYLINOSITOL 3 KINASE INHIBITOR; RAPAMYCIN; RAPAMYCIN DERIVATIVE; RECOMBINANT TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; STAUROSPORINE; TAXANE DERIVATIVE; TEMSIROLIMUS; UNCLASSIFIED DRUG; WORTMANNIN;

EID: 84872445303     PISSN: 18129269     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (237)

References (150)
  • 1
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000; 100: 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 2
    • 0038052805 scopus 로고    scopus 로고
    • The cell cycle: A review of regulation, deregulation and therapeutic targets in cancer
    • Vermeulen K, van Bockstaele DR, Berneman ZN. The cell cycle: a review of regulation, deregulation and therapeutic targets in cancer. Cell Prolif 2003; 36: 131-49.
    • (2003) Cell Prolif , vol.36 , pp. 131-149
    • Vermeulen, K.1    Van Bockstaele, D.R.2    Berneman, Z.N.3
  • 3
    • 60749109846 scopus 로고    scopus 로고
    • Cell cycle, CDKs and cancer: A changing paradigm
    • Malumbres M, Barbacid M. Cell cycle, CDKs and cancer: a changing paradigm. Nat Rev Cancer 2009; 9: 153-66.
    • (2009) Nat Rev Cancer , vol.9 , pp. 153-166
    • Malumbres, M.1    Barbacid, M.2
  • 4
    • 79851505114 scopus 로고    scopus 로고
    • Selective depletion of mutant p53 by cancer chemopreventive isothiocyanates and their structure-activity relationships
    • Wang X, Di Pasqua AJ, Govind S, et al. Selective depletion of mutant p53 by cancer chemopreventive isothiocyanates and their structure-activity relationships. J Med Chem 2011; 54: 809-16.
    • (2011) J Med Chem , vol.54 , pp. 809-816
    • Wang, X.1    Di Pasqua, A.J.2    Govind, S.3
  • 5
    • 0033580435 scopus 로고    scopus 로고
    • p53 mediated death of cells overexpressing MDM2 by an inhibitor of MDM2 interaction with p53
    • Wasylyk C, Salvi R, Argentini M, et al. p53 mediated death of cells overexpressing MDM2 by an inhibitor of MDM2 interaction with p53. Oncogene 1999; 18: 1921-34.
    • (1999) Oncogene , vol.18 , pp. 1921-1934
    • Wasylyk, C.1    Salvi, R.2    Argentini, M.3
  • 6
    • 0242610835 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib stabilizes a novel active form of p53 in human LNCaP-Pro5 prostate cancer cells
    • Williams SA, McConkey DJ. The proteasome inhibitor bortezomib stabilizes a novel active form of p53 in human LNCaP-Pro5 prostate cancer cells. Cancer Res 2003; 63: 7338-44.
    • (2003) Cancer Res , vol.63 , pp. 7338-7344
    • Williams, S.A.1    McConkey, D.J.2
  • 7
    • 0141619285 scopus 로고    scopus 로고
    • Role of GRP58 in mitomycin C-induced DNA cross-linking
    • Celli CM, Jaiswal AK. Role of GRP58 in mitomycin C-induced DNA cross-linking. Cancer Res 2003; 63: 6016-25.
    • (2003) Cancer Res , vol.63 , pp. 6016-6025
    • Celli, C.M.1    Jaiswal, A.K.2
  • 8
    • 79959594483 scopus 로고    scopus 로고
    • Uncoupling protein downregulation in doxorubicin-induced heart failure improves mitochondrial coupling but increases reactive oxygen species generation
    • Bugger H, Guzman C, Zechner C, et al. Uncoupling protein downregulation in doxorubicin-induced heart failure improves mitochondrial coupling but increases reactive oxygen species generation. Cancer Chemother Pharmacol 2011; 67: 1381-8.
    • (2011) Cancer Chemother Pharmacol , vol.67 , pp. 1381-1388
    • Bugger, H.1    Guzman, C.2    Zechner, C.3
  • 9
    • 70450273190 scopus 로고    scopus 로고
    • Mitomycin C induces bystander killing in homogeneous and heterogeneous hepatoma cellular models
    • Kumari R, Sharma A, Ajay AK, Bhat MK. Mitomycin C induces bystander killing in homogeneous and heterogeneous hepatoma cellular models. Mol Cancer 2009; 8: 87.
    • (2009) Mol Cancer , vol.8 , pp. 87
    • Kumari, R.1    Sharma, A.2    Ajay, A.K.3    Bhat, M.K.4
  • 10
    • 71049152019 scopus 로고    scopus 로고
    • Curcumin reduced the side effects of mitomycin C by inhibiting GRP58-mediated DNA cross-linking in MCF-7 breast cancer xenografts
    • Zhou QM, Zhang H, Lu YY, et al. Curcumin reduced the side effects of mitomycin C by inhibiting GRP58-mediated DNA cross-linking in MCF-7 breast cancer xenografts. Cancer Sci 2009; 100: 2040-5.
    • (2009) Cancer Sci , vol.100 , pp. 2040-2045
    • Zhou, Q.M.1    Zhang, H.2    Lu, Y.Y.3
  • 11
    • 84864771065 scopus 로고    scopus 로고
    • Anticancer efficacy enhancement and attenuation of side effects of doxorubicin with titanium dioxide nanoparticles
    • Chen Y, Wan Y, Wang Y, et al. Anticancer efficacy enhancement and attenuation of side effects of doxorubicin with titanium dioxide nanoparticles. Int J Nanomedicine 2011; 6: 2321-6.
    • (2011) Int J Nanomedicine , vol.6 , pp. 2321-2326
    • Chen, Y.1    Wan, Y.2    Wang, Y.3
  • 12
    • 32044466838 scopus 로고    scopus 로고
    • Exploiting the PI3K/AKT pathway for cancer drug discovery
    • Hennessy BT, Smith DL, Ram PT, et al. Exploiting the PI3K/AKT pathway for cancer drug discovery. Nat Rev Drug Discov 2005; 4: 988-1004.
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 988-1004
    • Hennessy, B.T.1    Smith, D.L.2    Ram, P.T.3
  • 13
    • 4344602002 scopus 로고    scopus 로고
    • The biology and clinical relevance of the PTEN tumor suppressor pathway
    • Sansal I, Sellers WR. The biology and clinical relevance of the PTEN tumor suppressor pathway. J Clin Oncol 2004; 22: 2954-63.
    • (2004) J Clin Oncol , vol.22 , pp. 2954-2963
    • Sansal, I.1    Sellers, W.R.2
  • 14
    • 33749430399 scopus 로고    scopus 로고
    • Akt deficiency impairs normal cell proliferation and suppresses oncogenesis in a p53-independent and mTORC1-dependent manner
    • Skeen JE, Bhaskar PT, Chen CC, et al. Akt deficiency impairs normal cell proliferation and suppresses oncogenesis in a p53-independent and mTORC1-dependent manner. Cancer Cell 2006; 10: 269-80.
    • (2006) Cancer Cell , vol.10 , pp. 269-280
    • Skeen, J.E.1    Bhaskar, P.T.2    Chen, C.C.3
  • 15
    • 14144252004 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic
    • Kang S, Bader AG, Vogt PK. Phosphatidylinositol 3-kinase mutations identified in human cancer are oncogenic. Proc Natl Acad Sci USA 2005; 102: 802-7.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 802-807
    • Kang, S.1    Bader, A.G.2    Vogt, P.K.3
  • 16
    • 53849132331 scopus 로고    scopus 로고
    • A novel AKT3 mutation in melanoma tumours and cell lines
    • Davies MA, Stemke-Hale K, Tellez C, et al. A novel AKT3 mutation in melanoma tumours and cell lines. Br J Cancer 2008; 99: 1265-8.
    • (2008) Br J Cancer , vol.99 , pp. 1265-1268
    • Davies, M.A.1    Stemke-Hale, K.2    Tellez, C.3
  • 18
    • 31544448600 scopus 로고    scopus 로고
    • Phase II study of perifosine in previously untreated patients with metastatic melanoma
    • Ernst DS, Eisenhauer E, Wainman N, et al. Phase II study of perifosine in previously untreated patients with metastatic melanoma. Invest New Drugs 2005; 23: 569-75.
    • (2005) Invest New Drugs , vol.23 , pp. 569-575
    • Ernst, D.S.1    Eisenhauer, E.2    Wainman, N.3
  • 19
    • 15944406971 scopus 로고    scopus 로고
    • Coadministration of histone deacetylase inhibitors and perifosine synergistically induces apoptosis in human leukemia cells through Akt and ERK1/2 inactivation and the generation of ceramide and reactive oxygen species
    • Rahmani M, Reese E, Dai Y, et al. Coadministration of histone deacetylase inhibitors and perifosine synergistically induces apoptosis in human leukemia cells through Akt and ERK1/2 inactivation and the generation of ceramide and reactive oxygen species. Cancer Res 2005; 65: 2422-32.
    • (2005) Cancer Res , vol.65 , pp. 2422-2432
    • Rahmani, M.1    Reese, E.2    Dai, Y.3
  • 20
    • 33746637660 scopus 로고    scopus 로고
    • Current development of mTOR inhibitors as anticancer agents
    • Faivre S, Kroemer G, Raymond E. Current development of mTOR inhibitors as anticancer agents. Nat Rev Drug Discov 2006; 5: 671-88.
    • (2006) Nat Rev Drug Discov , vol.5 , pp. 671-688
    • Faivre, S.1    Kroemer, G.2    Raymond, E.3
  • 22
    • 77953439691 scopus 로고    scopus 로고
    • Discovery of novel anticancer therapeutics targeting the PI3K/Akt/mTOR pathway
    • Maira SM, Furet P, Stauffer F. Discovery of novel anticancer therapeutics targeting the PI3K/Akt/mTOR pathway. Future Med Chem 2009; 1: 137-55.
    • (2009) Future Med Chem , vol.1 , pp. 137-155
    • Maira, S.M.1    Furet, P.2    Stauffer, F.3
  • 24
    • 0035966127 scopus 로고    scopus 로고
    • Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex
    • Vazquez F, Grossman SR, Takahashi Y, et al. Phosphorylation of the PTEN tail acts as an inhibitory switch by preventing its recruitment into a protein complex. J Biol Chem 2001; 276: 48627-30.
    • (2001) J Biol Chem , vol.276 , pp. 48627-48630
    • Vazquez, F.1    Grossman, S.R.2    Takahashi, Y.3
  • 25
    • 0038243115 scopus 로고    scopus 로고
    • Loss of PTEN promotes tumor development in malignant melanoma
    • Stahl JM, Cheung M, Sharma A, et al. Loss of PTEN promotes tumor development in malignant melanoma. Cancer Res 2003; 63: 2881-90.
    • (2003) Cancer Res , vol.63 , pp. 2881-2890
    • Stahl, J.M.1    Cheung, M.2    Sharma, A.3
  • 26
    • 84862817081 scopus 로고    scopus 로고
    • Interactions and relationships of PTEN, ERG, SPINK1 and AR in castration-resistant prostate cancer
    • Bismar TA, Yoshimoto M, Duan Q, et al. Interactions and relationships of PTEN, ERG, SPINK1 and AR in castration-resistant prostate cancer. Histopathology 2012; 60: 645-52.
    • (2012) Histopathology , vol.60 , pp. 645-652
    • Bismar, T.A.1    Yoshimoto, M.2    Duan, Q.3
  • 27
    • 83055176408 scopus 로고    scopus 로고
    • PTEN genomic deletions that characterize aggressive prostate cancer originate close to segmental duplications
    • Yoshimoto M, Ludkovski O, DeGrace D, et al. PTEN genomic deletions that characterize aggressive prostate cancer originate close to segmental duplications. Genes Chromosomes Cancer 2012; 51: 149-60.
    • (2012) Genes Chromosomes Cancer , vol.51 , pp. 149-160
    • Yoshimoto, M.1    Ludkovski, O.2    DeGrace, D.3
  • 28
    • 0032126505 scopus 로고    scopus 로고
    • Frequent inactivation of PTEN in prostate cancer cell lines and xenografts
    • Vlietstra RJ, van Alewijk DC, Hermans KG, et al. Frequent inactivation of PTEN in prostate cancer cell lines and xenografts. Cancer Res 1998; 58: 2720-3.
    • (1998) Cancer Res , vol.58 , pp. 2720-2723
    • Vlietstra, R.J.1    Van Alewijk, D.C.2    Hermans, K.G.3
  • 30
    • 0036793098 scopus 로고    scopus 로고
    • The roles of androgen receptors and androgen-binding proteins in nongenomic androgen actions
    • Heinlein CA, Chang C. The roles of androgen receptors and androgen-binding proteins in nongenomic androgen actions. Mol Endocrinol 2002; 16: 2181-7.
    • (2002) Mol Endocrinol , vol.16 , pp. 2181-2187
    • Heinlein, C.A.1    Chang, C.2
  • 31
    • 84855669062 scopus 로고    scopus 로고
    • Emerging treatment options for patients with castration-resistant prostate cancer
    • George D, Moul JW. Emerging treatment options for patients with castration-resistant prostate cancer. Prostate 2012; 72: 338-49.
    • (2012) Prostate , vol.72 , pp. 338-349
    • George, D.1    Moul, J.W.2
  • 32
    • 33645056171 scopus 로고    scopus 로고
    • Increased expression of genes converting adrenal androgens to testosterone in androgen-independent prostate cancer
    • Stanbrough M, Bubley GJ, Ross K, et al. Increased expression of genes converting adrenal androgens to testosterone in androgen-independent prostate cancer. Cancer Res 2006; 66: 2815-25.
    • (2006) Cancer Res , vol.66 , pp. 2815-2825
    • Stanbrough, M.1    Bubley, G.J.2    Ross, K.3
  • 33
    • 79960074439 scopus 로고    scopus 로고
    • Beefing up prostate cancer therapy with performance-enhancing (anti-) steroids
    • Nelson WG, Haffner MC, Yegnasubramanian S. Beefing up prostate cancer therapy with performance-enhancing (anti-) steroids. Cancer Cell 2011; 20: 7-9.
    • (2011) Cancer Cell , vol.20 , pp. 7-9
    • Nelson, W.G.1    Haffner, M.C.2    Yegnasubramanian, S.3
  • 34
    • 77952105685 scopus 로고    scopus 로고
    • Antitumour activity of MDV3100 in castration-resistant prostate cancer: A phase 1-2 study
    • Scher HI, Beer TM, Higano CS, et al. Antitumour activity of MDV3100 in castration-resistant prostate cancer: a phase 1-2 study. Lancet 2010; 375: 1437-46.
    • (2010) Lancet , vol.375 , pp. 1437-1446
    • Scher, H.I.1    Beer, T.M.2    Higano, C.S.3
  • 35
    • 44949105206 scopus 로고    scopus 로고
    • Proteasome inhibitors induce apoptosis of prostate cancer cells by inducing nuclear translocation of IkappaBalpha
    • Vu HY, Juvekar A, Ghosh C, et al. Proteasome inhibitors induce apoptosis of prostate cancer cells by inducing nuclear translocation of IkappaBalpha. Arch Biochem Biophys 2008; 475: 156-63.
    • (2008) Arch Biochem Biophys , vol.475 , pp. 156-163
    • Vu, H.Y.1    Juvekar, A.2    Ghosh, C.3
  • 36
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: A novel target for cancer chemotherapy
    • Almond JB, Cohen GM. The proteasome: a novel target for cancer chemotherapy. Leukemia 2002; 16: 433-43.
    • (2002) Leukemia , vol.16 , pp. 433-443
    • Almond, J.B.1    Cohen, G.M.2
  • 37
    • 33947206642 scopus 로고    scopus 로고
    • MG-132 sensitizes TRAIL-resistant prostate cancer cells by activating c-Fos/c-Jun heterodimers and repressing c-FLIP(L)
    • Li W, Zhang X, Olumi AF. MG-132 sensitizes TRAIL-resistant prostate cancer cells by activating c-Fos/c-Jun heterodimers and repressing c-FLIP(L). Cancer Res 2007; 67: 2247-55.
    • (2007) Cancer Res , vol.67 , pp. 2247-2255
    • Li, W.1    Zhang, X.2    Olumi, A.F.3
  • 38
    • 33745728140 scopus 로고    scopus 로고
    • Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132
    • Crawford LJ, Walker B, Ovaa H, et al. Comparative selectivity and specificity of the proteasome inhibitors BzLLLCOCHO, PS-341, and MG-132. Cancer Res 2006; 66: 6379-86.
    • (2006) Cancer Res , vol.66 , pp. 6379-6386
    • Crawford, L.J.1    Walker, B.2    Ovaa, H.3
  • 39
    • 18244406798 scopus 로고    scopus 로고
    • Activity probe for in vivo profiling of the specificity of proteasome inhibitor bortezomib
    • Berkers CR, Verdoes M, Lichtman E, et al. Activity probe for in vivo profiling of the specificity of proteasome inhibitor bortezomib. Nat Methods 2005; 2: 357-62.
    • (2005) Nat Methods , vol.2 , pp. 357-362
    • Berkers, C.R.1    Verdoes, M.2    Lichtman, E.3
  • 40
    • 1842861723 scopus 로고    scopus 로고
    • The hierarchical relationship between MAPK signaling and ROS generation in human leukemia cells undergoing apoptosis in response to the proteasome inhibitor Bortezomib
    • Yu C, Rahmani M, Dent P, Grant S. The hierarchical relationship between MAPK signaling and ROS generation in human leukemia cells undergoing apoptosis in response to the proteasome inhibitor Bortezomib. Exp Cell Res 2004; 295: 555-66.
    • (2004) Exp Cell Res , vol.295 , pp. 555-566
    • Yu, C.1    Rahmani, M.2    Dent, P.3    Grant, S.4
  • 41
    • 0038240386 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 sensitizes neoplastic cells to TRAIL-mediated apoptosis by reducing levels of c-FLIP
    • Sayers TJ, Brooks AD, Koh CY, et al. The proteasome inhibitor PS-341 sensitizes neoplastic cells to TRAIL-mediated apoptosis by reducing levels of c-FLIP. Blood 2003; 102: 303-10.
    • (2003) Blood , vol.102 , pp. 303-310
    • Sayers, T.J.1    Brooks, A.D.2    Koh, C.Y.3
  • 42
    • 59749083936 scopus 로고    scopus 로고
    • Cooperation between Apo2L/TRAIL and bortezomib in multiple myeloma apoptosis
    • Balsas P, Lopez-Royuela N, Galan-Malo P, et al. Cooperation between Apo2L/TRAIL and bortezomib in multiple myeloma apoptosis. Biochem Pharmacol 2009; 77: 804-12.
    • (2009) Biochem Pharmacol , vol.77 , pp. 804-812
    • Balsas, P.1    Lopez-Royuela, N.2    Galan-Malo, P.3
  • 43
    • 20144388905 scopus 로고    scopus 로고
    • Evidence for a protective role of Mcl-1 in proteasome inhibitor-induced apoptosis
    • Nencioni A, Hua F, Dillon CP, et al. Evidence for a protective role of Mcl-1 in proteasome inhibitor-induced apoptosis. Blood 2005; 105: 3255-62.
    • (2005) Blood , vol.105 , pp. 3255-3262
    • Nencioni, A.1    Hua, F.2    Dillon, C.P.3
  • 44
    • 66249124267 scopus 로고    scopus 로고
    • PCI-24781 induces caspase and reactive oxygen species-dependent apoptosis through NF-kappaB mechanisms and is synergistic with bortezomib in lymphoma cells
    • Bhalla S, Balasubramanian S, David K, et al. PCI-24781 induces caspase and reactive oxygen species-dependent apoptosis through NF-kappaB mechanisms and is synergistic with bortezomib in lymphoma cells. Clin Cancer Res 2009; 15: 3354-65.
    • (2009) Clin Cancer Res , vol.15 , pp. 3354-3365
    • Bhalla, S.1    Balasubramanian, S.2    David, K.3
  • 45
    • 0037443551 scopus 로고    scopus 로고
    • The proteasome inhibitor PS-341 potentiates sensitivity of multiple myeloma cells to conventional chemotherapeutic agents: Therapeutic applications
    • Mitsiades N, Mitsiades CS, Richardson PG, et al. The proteasome inhibitor PS-341 potentiates sensitivity of multiple myeloma cells to conventional chemotherapeutic agents: therapeutic applications. Blood 2003; 101: 2377-80.
    • (2003) Blood , vol.101 , pp. 2377-2380
    • Mitsiades, N.1    Mitsiades, C.S.2    Richardson, P.G.3
  • 46
    • 38749133727 scopus 로고    scopus 로고
    • Proteasome inhibition blocks caspase-8 degradation and sensitizes prostate cancer cells to death receptor-mediated apoptosis
    • Thorpe JA, Christian PA, Schwarze SR. Proteasome inhibition blocks caspase-8 degradation and sensitizes prostate cancer cells to death receptor-mediated apoptosis. Prostate 2008; 68: 200-9.
    • (2008) Prostate , vol.68 , pp. 200-209
    • Thorpe, J.A.1    Christian, P.A.2    Schwarze, S.R.3
  • 47
    • 66149126567 scopus 로고    scopus 로고
    • Velcade sensitizes prostate cancer cells to TRAIL induced apoptosis and suppresses tumor growth in vivo
    • Christian PA, Thorpe JA, Schwarze SR. Velcade sensitizes prostate cancer cells to TRAIL induced apoptosis and suppresses tumor growth in vivo. Cancer Biol Ther 2009; 8: 73-80.
    • (2009) Cancer Biol Ther , vol.8 , pp. 73-80
    • Christian, P.A.1    Thorpe, J.A.2    Schwarze, S.R.3
  • 48
    • 70249146895 scopus 로고    scopus 로고
    • Single-agent bortezomib in previously untreated multiple myeloma: Efficacy, characterization of peripheral neuropathy, and molecular correlations with response and neuropathy
    • Richardson PG, Xie W, Mitsiades C, et al. Single-agent bortezomib in previously untreated multiple myeloma: efficacy, characterization of peripheral neuropathy, and molecular correlations with response and neuropathy. J Clin Oncol 2009; 27: 3518-25.
    • (2009) J Clin Oncol , vol.27 , pp. 3518-3525
    • Richardson, P.G.1    Xie, W.2    Mitsiades, C.3
  • 49
    • 12944277104 scopus 로고    scopus 로고
    • A common pharmacophore for epothilone and taxanes: Molecular basis for drug resistance conferred by tubulin mutations in human cancer cells
    • Giannakakou P, Gussio R, Nogales E, et al. A common pharmacophore for epothilone and taxanes: molecular basis for drug resistance conferred by tubulin mutations in human cancer cells. Proc Natl Acad Sci USA 2000; 97: 2904-9.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2904-2909
    • Giannakakou, P.1    Gussio, R.2    Nogales, E.3
  • 50
    • 79959194682 scopus 로고    scopus 로고
    • Overcoming chemotherapy resistance in prostate cancer
    • Madan RA, Pal SK, Sartor O, Dahut WL. Overcoming chemotherapy resistance in prostate cancer. Clin Cancer Res 2011; 17: 3892-902.
    • (2011) Clin Cancer Res , vol.17 , pp. 3892-3902
    • Madan, R.A.1    Pal, S.K.2    Sartor, O.3    Dahut, W.L.4
  • 51
    • 27944468179 scopus 로고    scopus 로고
    • Cell death induced by taxanes in breast cancer cells: Cytochrome C is released in resistant but not in sensitive cells
    • Ehrlichova M, Koc M, Truksa J, et al. Cell death induced by taxanes in breast cancer cells: cytochrome C is released in resistant but not in sensitive cells. Anticancer Res 2005; 25: 4215-24.
    • (2005) Anticancer Res , vol.25 , pp. 4215-4224
    • Ehrlichova, M.1    Koc, M.2    Truksa, J.3
  • 52
    • 0036927127 scopus 로고    scopus 로고
    • Taxanes for advanced non-small cell lung cancer
    • Ramalingam S, Belani CP. Taxanes for advanced non-small cell lung cancer. Exp Opin Pharmacother 2002; 3: 1693-709.
    • (2002) Exp Opin Pharmacother , vol.3 , pp. 1693-1709
    • Ramalingam, S.1    Belani, C.P.2
  • 53
  • 56
    • 0029940289 scopus 로고    scopus 로고
    • Rapid onset of apoptosis in vitro follows disruption of beta 1-integrin/matrix interactions in human colonic crypt cells
    • Strater J, Wedding U, Barth TF, et al. Rapid onset of apoptosis in vitro follows disruption of beta 1-integrin/matrix interactions in human colonic crypt cells. Gastroenterology 1996; 110: 1776-84.
    • (1996) Gastroenterology , vol.110 , pp. 1776-1784
    • Strater, J.1    Wedding, U.2    Barth, T.F.3
  • 57
    • 0030030021 scopus 로고    scopus 로고
    • Two distinct phases of apoptosis in mammary gland involution: Proteinase-independent and -dependent pathways
    • Lund LR, Romer J, Thomasset N, et al. Two distinct phases of apoptosis in mammary gland involution: proteinase-independent and -dependent pathways. Development 1996; 122: 181-93.
    • (1996) Development , vol.122 , pp. 181-193
    • Lund, L.R.1    Romer, J.2    Thomasset, N.3
  • 58
    • 77951169413 scopus 로고    scopus 로고
    • ErbB2 requires integrin alpha5 for anoikis resistance via Src regulation of receptor activity in human mammary epithelial cells
    • Haenssen KK, Caldwell SA, Shahriari KS, et al. ErbB2 requires integrin alpha5 for anoikis resistance via Src regulation of receptor activity in human mammary epithelial cells. J Cell Sci 2010; 123: 1373-82.
    • (2010) J Cell Sci , vol.123 , pp. 1373-1382
    • Haenssen, K.K.1    Caldwell, S.A.2    Shahriari, K.S.3
  • 59
    • 84857477485 scopus 로고    scopus 로고
    • Integrin signaling, cell survival, and anoikis: Distinctions, differences, and differentiation
    • Vachon PH. Integrin signaling, cell survival, and anoikis: distinctions, differences, and differentiation. J Signal Transduct 2011; 2011: 738137.
    • (2011) J Signal Transduct , vol.2011 , pp. 738137
    • Vachon, P.H.1
  • 60
    • 29244478619 scopus 로고    scopus 로고
    • Anoikis and survival connections in the tumor microenvironment: Is there a role in prostate cancer metastasis?
    • Rennebeck G, Martelli M, Kyprianou N. Anoikis and survival connections in the tumor microenvironment: is there a role in prostate cancer metastasis? Cancer Res 2005; 65: 11230-5.
    • (2005) Cancer Res , vol.65 , pp. 11230-11235
    • Rennebeck, G.1    Martelli, M.2    Kyprianou, N.3
  • 61
    • 40049087549 scopus 로고    scopus 로고
    • Bax-mediated mitochondrial outer membrane permeabilization (MOMP), distinct from the mitochondrial permeability transition, is a key mechanism in diclofenac-induced hepatocyte injury: Multiple protective roles of cyclosporin A
    • Siu WP, Pun PB, Latchoumycandane C, Boelsterli UA. Bax-mediated mitochondrial outer membrane permeabilization (MOMP), distinct from the mitochondrial permeability transition, is a key mechanism in diclofenac-induced hepatocyte injury: Multiple protective roles of cyclosporin A. Toxicol Appl Pharmacol 2008; 227: 451-61.
    • (2008) Toxicol Appl Pharmacol , vol.227 , pp. 451-461
    • Siu, W.P.1    Pun, P.B.2    Latchoumycandane, C.3    Boelsterli, U.A.4
  • 62
    • 0037417134 scopus 로고    scopus 로고
    • Synergistic induction of tumor cell apoptosis by death receptor antibody and chemotherapy agent through JNK/p38 and mitochondrial death pathway
    • Ohtsuka T, Buchsbaum D, Oliver P, et al. Synergistic induction of tumor cell apoptosis by death receptor antibody and chemotherapy agent through JNK/p38 and mitochondrial death pathway. Oncogene 2003; 22: 2034-44.
    • (2003) Oncogene , vol.22 , pp. 2034-2044
    • Ohtsuka, T.1    Buchsbaum, D.2    Oliver, P.3
  • 63
    • 34250308322 scopus 로고    scopus 로고
    • Apoptosis: A review of programmed cell death
    • Elmore S. Apoptosis: a review of programmed cell death. Toxicol Pathol 2007; 35: 495-516.
    • (2007) Toxicol Pathol , vol.35 , pp. 495-516
    • Elmore, S.1
  • 64
    • 77956095537 scopus 로고    scopus 로고
    • Mitochondria and cell death: Outer membrane permeabilization and beyond
    • Tait SW, Green DR. Mitochondria and cell death: outer membrane permeabilization and beyond. Nat Rev Mol Cell Biol 2010; 11: 621-32.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 621-632
    • Tait, S.W.1    Green, D.R.2
  • 65
    • 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
  • 66
    • 50049110244 scopus 로고    scopus 로고
    • Regulation of apoptosis by XIAP ubiquitin-ligase activity
    • Schile AJ, Garcia-Fernandez M, Steller H. Regulation of apoptosis by XIAP ubiquitin-ligase activity. Genes Dev 2008; 22: 2256-66.
    • (2008) Genes Dev , vol.22 , pp. 2256-2266
    • Schile, A.J.1    Garcia-Fernandez, M.2    Steller, H.3
  • 67
    • 0033104331 scopus 로고    scopus 로고
    • Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis
    • Srinivasula SM, Ahmad M, Guo Y, et al. Identification of an endogenous dominant-negative short isoform of caspase-9 that can regulate apoptosis. Cancer Res 1999; 59: 999-1002.
    • (1999) Cancer Res , vol.59 , pp. 999-1002
    • Srinivasula, S.M.1    Ahmad, M.2    Guo, Y.3
  • 68
    • 33745634880 scopus 로고    scopus 로고
    • Caspase 9 promoter polymorphisms and risk of primary lung cancer
    • Park JY, Park JM, Jang JS, et al. Caspase 9 promoter polymorphisms and risk of primary lung cancer. Hum Mol Genet 2006; 15: 1963-71.
    • (2006) Hum Mol Genet , vol.15 , pp. 1963-1971
    • Park, J.Y.1    Park, J.M.2    Jang, J.S.3
  • 69
    • 70349956567 scopus 로고    scopus 로고
    • Apoptosis and autophagy: Regulation of caspase-9 by phosphorylation
    • Allan LA, Clarke PR. Apoptosis and autophagy: Regulation of caspase-9 by phosphorylation. FEBS J 2009; 276: 6063-73.
    • (2009) FEBS J , vol.276 , pp. 6063-6073
    • Allan, L.A.1    Clarke, P.R.2
  • 70
    • 36348971785 scopus 로고    scopus 로고
    • Apaf-1 and caspase-9 deficiency prevents apoptosis in a Bax-controlled pathway and promotes clonogenic survival during paclitaxel treatment
    • Janssen K, Pohlmann S, Janicke RU, et al. Apaf-1 and caspase-9 deficiency prevents apoptosis in a Bax-controlled pathway and promotes clonogenic survival during paclitaxel treatment. Blood 2007; 110: 3662-72.
    • (2007) Blood , vol.110 , pp. 3662-3672
    • Janssen, K.1    Pohlmann, S.2    Janicke, R.U.3
  • 71
    • 77956908962 scopus 로고    scopus 로고
    • Regulation of the Apaf-1-caspase-9 apoptosome
    • Bratton SB, Salvesen GS. Regulation of the Apaf-1-caspase-9 apoptosome. J Cell Sci 2010; 123: 3209-14.
    • (2010) J Cell Sci , vol.123 , pp. 3209-3214
    • Bratton, S.B.1    Salvesen, G.S.2
  • 72
    • 52149086177 scopus 로고    scopus 로고
    • The extrinsic cell death pathway and the elan mortel
    • Wallach D, Kang TB, Kovalenko A. The extrinsic cell death pathway and the elan mortel. Cell Death Differ 2008; 15: 1533-41.
    • (2008) Cell Death Differ , vol.15 , pp. 1533-1541
    • Wallach, D.1    Kang, T.B.2    Kovalenko, A.3
  • 74
    • 79952498248 scopus 로고    scopus 로고
    • TNFR1-induced activation of the classical NF-kappaB pathway
    • Wajant H, Scheurich P. TNFR1-induced activation of the classical NF-kappaB pathway. FEBS J 2011; 278: 862-76.
    • (2011) FEBS J , vol.278 , pp. 862-876
    • Wajant, H.1    Scheurich, P.2
  • 75
    • 43049152912 scopus 로고    scopus 로고
    • TNF-alpha induces two distinct caspase-8 activation pathways
    • Wang L, Du F, Wang X. TNF-alpha induces two distinct caspase-8 activation pathways. Cell 2008; 133: 693-703.
    • (2008) Cell , vol.133 , pp. 693-703
    • Wang, L.1    Du, F.2    Wang, X.3
  • 76
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-kappaB pathway
    • Chen ZJ. Ubiquitin signalling in the NF-kappaB pathway. Nat Cell Biol 2005; 7: 758-65.
    • (2005) Nat Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 77
    • 20044387665 scopus 로고    scopus 로고
    • TNF-alpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination
    • Wu CJ, Conze DB, Li X, et al. TNF-alpha induced c-IAP1/TRAF2 complex translocation to a Ubc6-containing compartment and TRAF2 ubiquitination. EMBO J 2005; 24: 1886-98.
    • (2005) EMBO J , vol.24 , pp. 1886-1898
    • Wu, C.J.1    Conze, D.B.2    Li, X.3
  • 78
    • 58149301485 scopus 로고    scopus 로고
    • PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and K63-linked polyubiquitination
    • Li S, Wang L, Dorf ME. PKC phosphorylation of TRAF2 mediates IKKalpha/beta recruitment and K63-linked polyubiquitination. Mol Cell 2009; 33: 30-42.
    • (2009) Mol Cell , vol.33 , pp. 30-42
    • Li, S.1    Wang, L.2    Dorf, M.E.3
  • 79
    • 1542380581 scopus 로고    scopus 로고
    • Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB
    • Habelhah H, Takahashi S, Cho SG, et al. Ubiquitination and translocation of TRAF2 is required for activation of JNK but not of p38 or NF-kappaB. EMBO J 2004; 23: 322-32.
    • (2004) EMBO J , vol.23 , pp. 322-332
    • Habelhah, H.1    Takahashi, S.2    Cho, S.G.3
  • 80
    • 65049086930 scopus 로고    scopus 로고
    • Tumor necrosis factor receptor-associated factor-1 enhances proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2 cooperation
    • Wicovsky A, Henkler F, Salzmann S, et al. Tumor necrosis factor receptor-associated factor-1 enhances proinflammatory TNF receptor-2 signaling and modifies TNFR1-TNFR2 cooperation. Oncogene 2009; 28: 1769-81.
    • (2009) Oncogene , vol.28 , pp. 1769-1781
    • Wicovsky, A.1    Henkler, F.2    Salzmann, S.3
  • 81
    • 79952831701 scopus 로고    scopus 로고
    • Emerging complexity of protein ubiquitination in the NF-kappaB pathway
    • Habelhah H. Emerging complexity of protein ubiquitination in the NF-kappaB pathway. Genes Cancer 2010; 1: 735-47.
    • (2010) Genes Cancer , vol.1 , pp. 735-747
    • Habelhah, H.1
  • 82
    • 33646034316 scopus 로고    scopus 로고
    • Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO
    • Ea CK, Deng L, Xia ZP, et al. Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO. Mol Cell 2006; 22: 245-57.
    • (2006) Mol Cell , vol.22 , pp. 245-257
    • Ea, C.K.1    Deng, L.2    Xia, Z.P.3
  • 83
    • 43249110701 scopus 로고    scopus 로고
    • NF-kappaB dictates the degradation pathway of IkappaBalpha
    • Mathes E, O'Dea EL, Hoffmann A, Ghosh G. NF-kappaB dictates the degradation pathway of IkappaBalpha. EMBO J 2008; 27: 1357-67.
    • (2008) EMBO J , vol.27 , pp. 1357-1367
    • Mathes, E.1    O'Dea, E.L.2    Hoffmann, A.3    Ghosh, G.4
  • 84
    • 33645983982 scopus 로고    scopus 로고
    • The NF-kappaB-mediated control of the JNK cascade in the antagonism of programmed cell death in health and disease
    • Papa S, Bubici C, Zazzeroni F, et al. The NF-kappaB-mediated control of the JNK cascade in the antagonism of programmed cell death in health and disease. Cell Death Differ 2006; 13: 712-29.
    • (2006) Cell Death Differ , vol.13 , pp. 712-729
    • Papa, S.1    Bubici, C.2    Zazzeroni, F.3
  • 85
    • 0035830885 scopus 로고    scopus 로고
    • Role of IKKgamma/nemo in assembly of the Ikappa B kinase complex
    • Li XH, Fang X, Gaynor RB. Role of IKKgamma/nemo in assembly of the Ikappa B kinase complex. J Biol Chem 2001; 276: 4494-500.
    • (2001) J Biol Chem , vol.276 , pp. 4494-4500
    • Li, X.H.1    Fang, X.2    Gaynor, R.B.3
  • 86
    • 34547564902 scopus 로고    scopus 로고
    • Survival and apoptotic pathways initiated by TNF-alpha: Modeling and predictions
    • Rangamani P, Sirovich L. Survival and apoptotic pathways initiated by TNF-alpha: modeling and predictions. Biotechnol Bioeng 2007; 97: 1216-29.
    • (2007) Biotechnol Bioeng , vol.97 , pp. 1216-1229
    • Rangamani, P.1    Sirovich, L.2
  • 87
    • 79953282304 scopus 로고    scopus 로고
    • NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-alpha feedforward signaling
    • Biton S, Ashkenazi A. NEMO and RIP1 control cell fate in response to extensive DNA damage via TNF-alpha feedforward signaling. Cell 2011; 145: 92-103.
    • (2011) Cell , vol.145 , pp. 92-103
    • Biton, S.1    Ashkenazi, A.2
  • 88
    • 78649901091 scopus 로고    scopus 로고
    • Alternative cell death mechanisms in development and beyond
    • Yuan J, Kroemer G. Alternative cell death mechanisms in development and beyond. Genes Dev 2010; 24: 2592-602.
    • (2010) Genes Dev , vol.24 , pp. 2592-2602
    • Yuan, J.1    Kroemer, G.2
  • 89
    • 79960921946 scopus 로고    scopus 로고
    • The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs
    • Tenev T, Bianchi K, Darding M, et al. The Ripoptosome, a signaling platform that assembles in response to genotoxic stress and loss of IAPs. Mol Cell 2011; 43: 432-48.
    • (2011) Mol Cell , vol.43 , pp. 432-448
    • Tenev, T.1    Bianchi, K.2    Darding, M.3
  • 90
    • 79960895769 scopus 로고    scopus 로고
    • The Ripoptosome: Death decision in the cytosol
    • Bertrand MJ, Vandenabeele P. The Ripoptosome: death decision in the cytosol. Mol Cell 2011; 43: 323-5.
    • (2011) Mol Cell , vol.43 , pp. 323-325
    • Bertrand, M.J.1    Vandenabeele, P.2
  • 91
    • 83455245162 scopus 로고    scopus 로고
    • Ripoptosome: A novel IAP-regulated cell death-signalling platform
    • Imre G, Larisch S, Rajalingam K. Ripoptosome: a novel IAP-regulated cell death-signalling platform. J Mol Cell Biol 2011; 3: 324-6.
    • (2011) J Mol Cell Biol , vol.3 , pp. 324-326
    • Imre, G.1    Larisch, S.2    Rajalingam, K.3
  • 92
    • 79960922705 scopus 로고    scopus 로고
    • cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms
    • Feoktistova M, Geserick P, Kellert B, et al. cIAPs block Ripoptosome formation, a RIP1/caspase-8 containing intracellular cell death complex differentially regulated by cFLIP isoforms. Mol Cell 2011; 43: 449-63.
    • (2011) Mol Cell , vol.43 , pp. 449-463
    • Feoktistova, M.1    Geserick, P.2    Kellert, B.3
  • 93
    • 84863124281 scopus 로고    scopus 로고
    • Metastatic cells can escape the proapoptotic effects of TNF-alpha through increased autocrine IL-6/STAT3 signaling
    • Li S, Wang N, Brodt P. Metastatic cells can escape the proapoptotic effects of TNF-alpha through increased autocrine IL-6/STAT3 signaling. Cancer Res 2012; 72: 865-75.
    • (2012) Cancer Res , vol.72 , pp. 865-875
    • Li, S.1    Wang, N.2    Brodt, P.3
  • 94
    • 34547123570 scopus 로고    scopus 로고
    • Lipid rafts and nonrafts mediate tumor necrosis factor related apoptosis-inducing ligand induced apoptotic and nonapoptotic signals in non small cell lung carcinoma cells
    • Song JH, Tse MC, Bellail A, et al. Lipid rafts and nonrafts mediate tumor necrosis factor related apoptosis-inducing ligand induced apoptotic and nonapoptotic signals in non small cell lung carcinoma cells. Cancer Res 2007; 67: 6946-55.
    • (2007) Cancer Res , vol.67 , pp. 6946-6955
    • Song, J.H.1    Tse, M.C.2    Bellail, A.3
  • 95
    • 50349095215 scopus 로고    scopus 로고
    • Caspase-8 cleaves histone deacetylase 7 and abolishes its transcription repressor function
    • Scott FL, Fuchs GJ, Boyd SE, et al. Caspase-8 cleaves histone deacetylase 7 and abolishes its transcription repressor function. J Biol Chem 2008; 283: 19499-510.
    • (2008) J Biol Chem , vol.283 , pp. 19499-19510
    • Scott, F.L.1    Fuchs, G.J.2    Boyd, S.E.3
  • 96
    • 42149095910 scopus 로고    scopus 로고
    • NF-kappaB inhibition reveals differential mechanisms of TNF versus TRAIL-induced apoptosis upstream or at the level of caspase-8 activation independent of cIAP2
    • Diessenbacher P, Hupe M, Sprick MR, et al. NF-kappaB inhibition reveals differential mechanisms of TNF versus TRAIL-induced apoptosis upstream or at the level of caspase-8 activation independent of cIAP2. J Invest Dermatol 2008; 128: 1134-47.
    • (2008) J Invest Dermatol , vol.128 , pp. 1134-1147
    • Diessenbacher, P.1    Hupe, M.2    Sprick, M.R.3
  • 97
    • 13744263743 scopus 로고    scopus 로고
    • Resistance to Apo2 ligand (Apo2L)/tumor necrosis factor-related apoptosis- Inducing ligand (TRAIL)-mediated apoptosis and constitutive expression of Apo2L/TRAIL in human T-cell leukemia virus type 1-infected T-cell lines
    • Matsuda T, Almasan A, Tomita M, et al. Resistance to Apo2 ligand (Apo2L)/tumor necrosis factor-related apoptosis- inducing ligand (TRAIL)-mediated apoptosis and constitutive expression of Apo2L/TRAIL in human T-cell leukemia virus type 1-infected T-cell lines. J Virol 2005; 79: 1367-78.
    • (2005) J Virol , vol.79 , pp. 1367-1378
    • Matsuda, T.1    Almasan, A.2    Tomita, M.3
  • 98
    • 0037273848 scopus 로고    scopus 로고
    • Apo2L/TRAIL and its death and decoy receptors
    • LeBlanc HN, Ashkenazi A. Apo2L/TRAIL and its death and decoy receptors. Cell Death Differ 2003; 10: 66-75.
    • (2003) Cell Death Differ , vol.10 , pp. 66-75
    • LeBlanc, H.N.1    Ashkenazi, A.2
  • 99
    • 0034676268 scopus 로고    scopus 로고
    • Bcl-xL protects pancreatic adenocarcinoma cells against CD95- And TRAIL-receptor-mediated apoptosis
    • Hinz S, Trauzold A, Boenicke L, et al. Bcl-xL protects pancreatic adenocarcinoma cells against CD95- and TRAIL-receptor-mediated apoptosis. Oncogene 2000; 19: 5477-86.
    • (2000) Oncogene , vol.19 , pp. 5477-5486
    • Hinz, S.1    Trauzold, A.2    Boenicke, L.3
  • 100
    • 0037018277 scopus 로고    scopus 로고
    • Inhibition of TRAIL-induced apoptosis by Bcl-2 overexpression
    • Fulda S, Meyer E, Debatin KM. Inhibition of TRAIL-induced apoptosis by Bcl-2 overexpression. Oncogene 2002; 21: 2283-94.
    • (2002) Oncogene , vol.21 , pp. 2283-2294
    • Fulda, S.1    Meyer, E.2    Debatin, K.M.3
  • 101
    • 0035437171 scopus 로고    scopus 로고
    • TRAIL/Apo2L ligand selectively induces apoptosis and overcomes drug resistance in multiple myeloma: Therapeutic applications
    • Mitsiades CS, Treon SP, Mitsiades N, et al. TRAIL/Apo2L ligand selectively induces apoptosis and overcomes drug resistance in multiple myeloma: therapeutic applications. Blood 2001; 98: 795-804.
    • (2001) Blood , vol.98 , pp. 795-804
    • Mitsiades, C.S.1    Treon, S.P.2    Mitsiades, N.3
  • 102
    • 37249013515 scopus 로고    scopus 로고
    • Human agonistic TRAIL receptor antibodies Mapatumumab and Lexatumumab induce apoptosis in malignant mesothelioma and act synergistically with cisplatin
    • Belyanskaya LL, Marti TM, Hopkins-Donaldson S, et al. Human agonistic TRAIL receptor antibodies Mapatumumab and Lexatumumab induce apoptosis in malignant mesothelioma and act synergistically with cisplatin. Mol Cancer 2007; 6: 66.
    • (2007) Mol Cancer , vol.6 , pp. 66
    • Belyanskaya, L.L.1    Marti, T.M.2    Hopkins-Donaldson, S.3
  • 103
    • 60849086467 scopus 로고    scopus 로고
    • Mapatumumab and lexatumumab induce apoptosis in TRAIL-R1 and TRAIL-R2 antibody-resistant NSCLC cell lines when treated in combination with bortezomib
    • Luster TA, Carrell JA, McCormick K, et al. Mapatumumab and lexatumumab induce apoptosis in TRAIL-R1 and TRAIL-R2 antibody-resistant NSCLC cell lines when treated in combination with bortezomib. Mol Cancer Ther 2009; 8: 292-302.
    • (2009) Mol Cancer Ther , vol.8 , pp. 292-302
    • Luster, T.A.1    Carrell, J.A.2    McCormick, K.3
  • 104
    • 38749147839 scopus 로고    scopus 로고
    • Phytosphingosine in combination with TRAIL sensitizes cancer cells to TRAIL through synergistic up-regulation of DR4 and DR5
    • Choi SY, Kim MJ, Chung HY, et al. Phytosphingosine in combination with TRAIL sensitizes cancer cells to TRAIL through synergistic up-regulation of DR4 and DR5. Oncol Rep 2007; 17: 175-84.
    • (2007) Oncol Rep , vol.17 , pp. 175-184
    • Choi, S.Y.1    Kim, M.J.2    Chung, H.Y.3
  • 105
    • 79960926267 scopus 로고    scopus 로고
    • TRAIL and doxorubicin combination enhances anti-glioblastoma effect based on passive tumor targeting of liposomes
    • Guo L, Fan L, Pang Z, et al. TRAIL and doxorubicin combination enhances anti-glioblastoma effect based on passive tumor targeting of liposomes. J Control Release 2011; 154: 93-102.
    • (2011) J Control Release , vol.154 , pp. 93-102
    • Guo, L.1    Fan, L.2    Pang, Z.3
  • 106
    • 50249095026 scopus 로고    scopus 로고
    • Pretreatment of docetaxel enhances TRAIL-mediated apoptosis in prostate cancer cells
    • Yoo J, Park SS, Lee YJ. Pretreatment of docetaxel enhances TRAIL-mediated apoptosis in prostate cancer cells. J Cell Biochem 2008; 104: 1636-46.
    • (2008) J Cell Biochem , vol.104 , pp. 1636-1646
    • Yoo, J.1    Park, S.S.2    Lee, Y.J.3
  • 107
    • 70349974226 scopus 로고    scopus 로고
    • Paclitaxel promotes a caspase 8-mediated apoptosis through death effector domain association with microtubules
    • Mielgo A, Torres VA, Clair K, et al. Paclitaxel promotes a caspase 8-mediated apoptosis through death effector domain association with microtubules. Oncogene 2009; 28: 3551-62.
    • (2009) Oncogene , vol.28 , pp. 3551-3562
    • Mielgo, A.1    Torres, V.A.2    Clair, K.3
  • 108
    • 50849119416 scopus 로고    scopus 로고
    • The caspase-1 inflammasome: A pilot of innate immune responses
    • Yu HB, Finlay BB. The caspase-1 inflammasome: a pilot of innate immune responses. Cell Host Microbe 2008; 4: 198-208.
    • (2008) Cell Host Microbe , vol.4 , pp. 198-208
    • Yu, H.B.1    Finlay, B.B.2
  • 109
    • 84855383301 scopus 로고    scopus 로고
    • Expression and functional roles of caspase-5 in inflammatory responses of human retinal pigment epithelial cells
    • Bian ZM, Elner SG, Khanna H, et al. Expression and functional roles of caspase-5 in inflammatory responses of human retinal pigment epithelial cells. Invest Ophthalmol Vis Sci 2011; 52: 8646-56.
    • (2011) Invest Ophthalmol Vis Sci , vol.52 , pp. 8646-8656
    • Bian, Z.M.1    Elner, S.G.2    Khanna, H.3
  • 110
    • 38549103628 scopus 로고    scopus 로고
    • Protein quality control in the early secretory pathway
    • Anelli T, Sitia R. Protein quality control in the early secretory pathway. EMBO J 2008; 27: 315-27.
    • (2008) EMBO J , vol.27 , pp. 315-327
    • Anelli, T.1    Sitia, R.2
  • 111
    • 0038216621 scopus 로고    scopus 로고
    • Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: A possible involvement of the ER stress pathway in hepatocarcinogenesis
    • Shuda M, Kondoh N, Imazeki N, et al. Activation of the ATF6, XBP1 and grp78 genes in human hepatocellular carcinoma: a possible involvement of the ER stress pathway in hepatocarcinogenesis. J Hepatol 2003; 38: 605-14.
    • (2003) J Hepatol , vol.38 , pp. 605-614
    • Shuda, M.1    Kondoh, N.2    Imazeki, N.3
  • 112
    • 34447527676 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress: Signaling the unfolded protein response
    • Bethesda
    • Lai E, Teodoro T, Volchuk A. Endoplasmic reticulum stress: signaling the unfolded protein response. Physiology (Bethesda) 2007; 22: 193-201.
    • (2007) Physiology , vol.22 , pp. 193-201
    • Lai, E.1    Teodoro, T.2    Volchuk, A.3
  • 113
    • 73349101516 scopus 로고    scopus 로고
    • Dual involvement of caspase-4 in inflammatory and ER stress-induced apoptotic responses in human retinal pigment epithelial cells
    • Bian ZM, Elner SG, Elner VM. Dual involvement of caspase-4 in inflammatory and ER stress-induced apoptotic responses in human retinal pigment epithelial cells. Invest Ophthalmol Vis Sci 2009; 50: 6006-14.
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , pp. 6006-6014
    • Bian, Z.M.1    Elner, S.G.2    Elner, V.M.3
  • 114
    • 84855597540 scopus 로고    scopus 로고
    • ER stress and apoptosis: A new mechanism for retinal cell death
    • Jing G, Wang JJ, Zhang SX. ER stress and apoptosis: a new mechanism for retinal cell death. Exp Diabetes Res 2012; 2012: 589589.
    • (2012) Exp Diabetes Res , vol.2012 , pp. 589589
    • Jing, G.1    Wang, J.J.2    Zhang, S.X.3
  • 115
    • 0037077254 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway
    • Rao RV, Castro-Obregon S, Frankowski H, et al. Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway. J Biol Chem 2002; 277: 21836-42.
    • (2002) J Biol Chem , vol.277 , pp. 21836-21842
    • Rao, R.V.1    Castro-Obregon, S.2    Frankowski, H.3
  • 116
    • 2442453730 scopus 로고    scopus 로고
    • The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress
    • Tinel A, Tschopp J. The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress. Science 2004; 304: 843-6.
    • (2004) Science , vol.304 , pp. 843-846
    • Tinel, A.1    Tschopp, J.2
  • 117
    • 77955947900 scopus 로고    scopus 로고
    • Linking ER stress to autophagy: Potential implications for cancer therapy
    • Verfaillie T, Salazar M, Velasco G, Agostinis P. Linking ER stress to autophagy: potential implications for cancer therapy. Int J Cell Biol 2010; 2010:930509.
    • (2010) Int J Cell Biol , vol.2010 , pp. 930509
    • Verfaillie, T.1    Salazar, M.2    Velasco, G.3    Agostinis, P.4
  • 118
    • 68449096176 scopus 로고    scopus 로고
    • Dysregulation of unfolded protein response partially underlies proapoptotic activity of bortezomib in multiple myeloma cells
    • Dong H, Chen L, Chen X, et al. Dysregulation of unfolded protein response partially underlies proapoptotic activity of bortezomib in multiple myeloma cells. Leuk Lymphoma 2009; 50: 974-84.
    • (2009) Leuk Lymphoma , vol.50 , pp. 974-984
    • Dong, H.1    Chen, L.2    Chen, X.3
  • 119
    • 20844435806 scopus 로고    scopus 로고
    • Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma
    • Hideshima T, Bradner JE, Wong J, et al. Small-molecule inhibition of proteasome and aggresome function induces synergistic antitumor activity in multiple myeloma. Proc Natl Acad Sci USA 2005; 102: 8567-72.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8567-8572
    • Hideshima, T.1    Bradner, J.E.2    Wong, J.3
  • 120
    • 0033573020 scopus 로고    scopus 로고
    • Caspase-9 and APAF-1 form an active holoenzyme
    • Rodriguez J, Lazebnik Y. Caspase-9 and APAF-1 form an active holoenzyme. Genes Dev 1999; 13: 3179-84.
    • (1999) Genes Dev , vol.13 , pp. 3179-3184
    • Rodriguez, J.1    Lazebnik, Y.2
  • 121
    • 0037291737 scopus 로고    scopus 로고
    • Mechanism of XIAP-mediated inhibition of caspase-9
    • Shiozaki EN, Chai J, Rigotti DJ, et al. Mechanism of XIAP-mediated inhibition of caspase-9. Mol Cell 2003; 11: 519-27.
    • (2003) Mol Cell , vol.11 , pp. 519-527
    • Shiozaki, E.N.1    Chai, J.2    Rigotti, D.J.3
  • 122
    • 33646507051 scopus 로고    scopus 로고
    • Mutational analysis of proapoptotic caspase-9 gene in common human carcinomas
    • Soung YH, Lee JW, Kim SY, et al. Mutational analysis of proapoptotic caspase-9 gene in common human carcinomas. APMIS 2006; 114: 292-7.
    • (2006) APMIS , vol.114 , pp. 292-297
    • Soung, Y.H.1    Lee, J.W.2    Kim, S.Y.3
  • 123
    • 77749298000 scopus 로고    scopus 로고
    • Caspase 3/caspase-activated DNase promote cell differentiation by inducing DNA strand breaks
    • Larsen BD, Rampalli S, Burns LE, et al. Caspase 3/caspase-activated DNase promote cell differentiation by inducing DNA strand breaks. Proc Natl Acad Sci USA 2010; 107: 4230-5.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4230-4235
    • Larsen, B.D.1    Rampalli, S.2    Burns, L.E.3
  • 124
    • 0035036133 scopus 로고    scopus 로고
    • Caspase-9 processing by caspase-3 via a feedback amplification loop in vivo
    • Fujita E, Egashira J, Urase K, et al. Caspase-9 processing by caspase-3 via a feedback amplification loop in vivo. Cell Death Differ 2001; 8: 335-44.
    • (2001) Cell Death Differ , vol.8 , pp. 335-344
    • Fujita, E.1    Egashira, J.2    Urase, K.3
  • 125
    • 0037069938 scopus 로고    scopus 로고
    • Down-regulation of caspase 3 in breast cancer: A possible mechanism for chemoresistance
    • Devarajan E, Sahin AA, Chen JS, et al. Down-regulation of caspase 3 in breast cancer: a possible mechanism for chemoresistance. Oncogene 2002; 21: 8843-51.
    • (2002) Oncogene , vol.21 , pp. 8843-8851
    • Devarajan, E.1    Sahin, A.A.2    Chen, J.S.3
  • 126
    • 0034990676 scopus 로고    scopus 로고
    • Caspase 7 downregulation as an immunohistochemical marker of colonic carcinoma
    • Palmerini F, Devilard E, Jarry A, et al. Caspase 7 downregulation as an immunohistochemical marker of colonic carcinoma. Hum Pathol 2001; 32: 461-7.
    • (2001) Hum Pathol , vol.32 , pp. 461-467
    • Palmerini, F.1    Devilard, E.2    Jarry, A.3
  • 127
    • 0035824635 scopus 로고    scopus 로고
    • Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8
    • Kischkel FC, Lawrence DA, Tinel A, et al. Death receptor recruitment of endogenous caspase-10 and apoptosis initiation in the absence of caspase-8. J Biol Chem 2001; 276: 46639-46.
    • (2001) J Biol Chem , vol.276 , pp. 46639-46646
    • Kischkel, F.C.1    Lawrence, D.A.2    Tinel, A.3
  • 128
    • 0037009370 scopus 로고    scopus 로고
    • Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8
    • Sprick MR, Rieser E, Stahl H, et al. Caspase-10 is recruited to and activated at the native TRAIL and CD95 death-inducing signalling complexes in a FADD-dependent manner but can not functionally substitute caspase-8. EMBO J 2002; 21: 4520-30.
    • (2002) EMBO J , vol.21 , pp. 4520-4530
    • Sprick, M.R.1    Rieser, E.2    Stahl, H.3
  • 129
    • 65949097277 scopus 로고    scopus 로고
    • Caspase-8 association with the focal adhesion complex promotes tumor cell migration and metastasis
    • Barbero S, Mielgo A, Torres V, et al. Caspase-8 association with the focal adhesion complex promotes tumor cell migration and metastasis. Cancer Res 2009; 69: 3755-63.
    • (2009) Cancer Res , vol.69 , pp. 3755-3763
    • Barbero, S.1    Mielgo, A.2    Torres, V.3
  • 130
    • 30144434107 scopus 로고    scopus 로고
    • Potentiation of neuroblastoma metastasis by loss of caspase-8
    • Stupack DG, Teitz T, Potter MD, et al. Potentiation of neuroblastoma metastasis by loss of caspase-8. Nature 2006; 439: 95-9.
    • (2006) Nature , vol.439 , pp. 95-99
    • Stupack, D.G.1    Teitz, T.2    Potter, M.D.3
  • 131
    • 45149096045 scopus 로고    scopus 로고
    • Identification of a critical tyrosine residue in caspase 8 that promotes cell migration
    • Barbero S, Barila D, Mielgo A, et al. Identification of a critical tyrosine residue in caspase 8 that promotes cell migration. J Biol Chem 2008; 283: 13031-4.
    • (2008) J Biol Chem , vol.283 , pp. 13031-13034
    • Barbero, S.1    Barila, D.2    Mielgo, A.3
  • 132
    • 61349156806 scopus 로고    scopus 로고
    • Caspase 8 promotes peripheral localization and activation of Rab5
    • Torres VA, Mielgo A, Barila D, et al. Caspase 8 promotes peripheral localization and activation of Rab5. J Biol Chem 2008; 283: 36280-9.
    • (2008) J Biol Chem , vol.283 , pp. 36280-36289
    • Torres, V.A.1    Mielgo, A.2    Barila, D.3
  • 133
    • 0032834212 scopus 로고    scopus 로고
    • Rab5 induces Rac-independent lamellipodia formation and cell migration
    • Spaargaren M, Bos JL. Rab5 induces Rac-independent lamellipodia formation and cell migration. Mol Biol Cell 1999; 10: 3239-50.
    • (1999) Mol Biol Cell , vol.10 , pp. 3239-3250
    • Spaargaren, M.1    Bos, J.L.2
  • 134
    • 51449087302 scopus 로고    scopus 로고
    • Integrin trafficking regulated by Rab21 is necessary for cytokinesis
    • Pellinen T, Tuomi S, Arjonen A, et al. Integrin trafficking regulated by Rab21 is necessary for cytokinesis. Dev Cell 2008; 15: 371-85.
    • (2008) Dev Cell , vol.15 , pp. 371-385
    • Pellinen, T.1    Tuomi, S.2    Arjonen, A.3
  • 135
    • 37549060944 scopus 로고    scopus 로고
    • Novel noncatalytic role for caspase-8 in promoting SRC-mediated adhesion and Erk signaling in neuroblastoma cells
    • Finlay D, Vuori K. Novel noncatalytic role for caspase-8 in promoting SRC-mediated adhesion and Erk signaling in neuroblastoma cells. Cancer Res 2007; 67: 11704-11.
    • (2007) Cancer Res , vol.67 , pp. 11704-11711
    • Finlay, D.1    Vuori, K.2
  • 136
    • 49949110101 scopus 로고    scopus 로고
    • Caspase-8 deficiency facilitates cellular transformation in vitro
    • Krelin Y, Zhang L, Kang TB, et al. Caspase-8 deficiency facilitates cellular transformation in vitro. Cell Death Differ 2008; 15: 1350-5.
    • (2008) Cell Death Differ , vol.15 , pp. 1350-1355
    • Krelin, Y.1    Zhang, L.2    Kang, T.B.3
  • 137
    • 0034066405 scopus 로고    scopus 로고
    • Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN
    • Teitz T, Wei T, Valentine MB, et al. Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN. Nat Med 2000; 6: 529-35.
    • (2000) Nat Med , vol.6 , pp. 529-535
    • Teitz, T.1    Wei, T.2    Valentine, M.B.3
  • 138
    • 7744227335 scopus 로고    scopus 로고
    • Deletion and aberrant CpG island methylation of Caspase 8 gene in medulloblastoma
    • Gonzalez-Gomez P, Bello MJ, Inda MM, et al. Deletion and aberrant CpG island methylation of Caspase 8 gene in medulloblastoma. Oncol Rep 2004; 12: 663-6.
    • (2004) Oncol Rep , vol.12 , pp. 663-666
    • Gonzalez-Gomez, P.1    Bello, M.J.2    Inda, M.M.3
  • 139
    • 13444309090 scopus 로고    scopus 로고
    • CASPASE-8 gene is inactivated by somatic mutations in gastric carcinomas
    • Soung YH, Lee JW, Kim SY, et al. CASPASE-8 gene is inactivated by somatic mutations in gastric carcinomas. Cancer Res 2005; 65: 815-21.
    • (2005) Cancer Res , vol.65 , pp. 815-821
    • Soung, Y.H.1    Lee, J.W.2    Kim, S.Y.3
  • 140
    • 0030925774 scopus 로고    scopus 로고
    • FLICE is activated by association with the CD95 death-inducing signaling complex (DISC)
    • Medema JP, Scaffidi C, Kischkel FC, et al. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J 1997; 16: 2794-804.
    • (1997) EMBO J , vol.16 , pp. 2794-2804
    • Medema, J.P.1    Scaffidi, C.2    Kischkel, F.C.3
  • 141
    • 33846247103 scopus 로고    scopus 로고
    • Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling
    • Feig C, Tchikov V, Schutze S, Peter ME. Palmitoylation of CD95 facilitates formation of SDS-stable receptor aggregates that initiate apoptosis signaling. EMBO J 2007; 26: 221-31.
    • (2007) EMBO J , vol.26 , pp. 221-231
    • Feig, C.1    Tchikov, V.2    Schutze, S.3    Peter, M.E.4
  • 142
    • 4344607589 scopus 로고    scopus 로고
    • Enhanced caspase-8 recruitment to and activation at the DISC is critical for sensitisation of human hepatocellular carcinoma cells to TRAIL-induced apoptosis by chemotherapeutic drugs
    • Ganten TM, Haas TL, Sykora J, et al. Enhanced caspase-8 recruitment to and activation at the DISC is critical for sensitisation of human hepatocellular carcinoma cells to TRAIL-induced apoptosis by chemotherapeutic drugs. Cell Death Differ 2004; 11 Suppl 1: S86-96.
    • (2004) Cell Death Differ , vol.11 , Issue.SUPPL. 1
    • Ganten, T.M.1    Haas, T.L.2    Sykora, J.3
  • 143
    • 0032548842 scopus 로고    scopus 로고
    • Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal
    • Martin DA, Siegel RM, Zheng L, Lenardo MJ. Membrane oligomerization and cleavage activates the caspase-8 (FLICE/MACHalpha1) death signal. J Biol Chem 1998; 273: 4345-9.
    • (1998) J Biol Chem , vol.273 , pp. 4345-4349
    • Martin, D.A.1    Siegel, R.M.2    Zheng, L.3    Lenardo, M.J.4
  • 144
    • 0033556310 scopus 로고    scopus 로고
    • The role of c-FLIP in modulation of CD95-induced apoptosis
    • Scaffidi C, Schmitz I, Krammer PH, Peter ME. The role of c-FLIP in modulation of CD95-induced apoptosis. J Biol Chem 1999; 274: 1541-8.
    • (1999) J Biol Chem , vol.274 , pp. 1541-1548
    • Scaffidi, C.1    Schmitz, I.2    Krammer, P.H.3    Peter, M.E.4
  • 145
    • 79955761920 scopus 로고    scopus 로고
    • Cellular FLICE-inhibitory protein (cFLIP) isoforms block CD95- And TRAIL death receptor-induced gene induction irrespective of processing of caspase-8 or cFLIP in the death-inducing signaling complex
    • Kavuri SM, Geserick P, Berg D, et al. Cellular FLICE-inhibitory protein (cFLIP) isoforms block CD95- and TRAIL death receptor-induced gene induction irrespective of processing of caspase-8 or cFLIP in the death-inducing signaling complex. J Biol Chem 2011; 286: 16631-46.
    • (2011) J Biol Chem , vol.286 , pp. 16631-16646
    • Kavuri, S.M.1    Geserick, P.2    Berg, D.3
  • 146
    • 0033647484 scopus 로고    scopus 로고
    • Caspase-8 in apoptosis: The beginning of "the end"?
    • Kruidering M, Evan GI. Caspase-8 in apoptosis: the beginning of "the end"? IUBMB Life 2000; 50: 85-90.
    • (2000) IUBMB Life , vol.50 , pp. 85-90
    • Kruidering, M.1    Evan, G.I.2
  • 147
    • 65549085701 scopus 로고    scopus 로고
    • Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling
    • Jin Z, Li Y, Pitti R, et al. Cullin3-based polyubiquitination and p62-dependent aggregation of caspase-8 mediate extrinsic apoptosis signaling. Cell 2009; 137: 721-35.
    • (2009) Cell , vol.137 , pp. 721-735
    • Jin, Z.1    Li, Y.2    Pitti, R.3
  • 148
    • 79953214075 scopus 로고    scopus 로고
    • Phosphorylation of caspase-8 (Thr-263) by ribosomal S6 kinase 2 (RSK2) mediates caspase-8 ubiquitination and stability
    • Peng C, Cho YY, Zhu F, et al. Phosphorylation of caspase-8 (Thr-263) by ribosomal S6 kinase 2 (RSK2) mediates caspase-8 ubiquitination and stability. J Biol Chem 2011; 286: 6946-54.
    • (2011) J Biol Chem , vol.286 , pp. 6946-6954
    • Peng, C.1    Cho, Y.Y.2    Zhu, F.3
  • 149
    • 79958856296 scopus 로고    scopus 로고
    • Possible role of death receptor-mediated apoptosis by the E3 ubiquitin ligases Siah2 and POSH
    • Christian PA, Fiandalo MV, Schwarze SR. Possible role of death receptor-mediated apoptosis by the E3 ubiquitin ligases Siah2 and POSH. Mol Cancer 2011; 10: 57.
    • (2011) Mol Cancer , vol.10 , pp. 57
    • Christian, P.A.1    Fiandalo, M.V.2    Schwarze, S.R.3
  • 150
    • 77952944929 scopus 로고    scopus 로고
    • Bortezomib sensitizes human renal cell carcinomas to TRAIL apoptosis through increased activation of caspase-8 in the death-inducing signaling complex
    • Brooks AD, Jacobsen KM, Li W, et al. Bortezomib sensitizes human renal cell carcinomas to TRAIL apoptosis through increased activation of caspase-8 in the death-inducing signaling complex. Mol Cancer Res 2010; 8: 729-38.
    • (2010) Mol Cancer Res , vol.8 , pp. 729-738
    • Brooks, A.D.1    Jacobsen, K.M.2    Li, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.