메뉴 건너뛰기




Volumn , Issue , 2005, Pages 1-28

Disfunction of the apoptotic pathway in cancer cells

Author keywords

Apoptosis resistance; apoptosis signal defects; apoptotic signal pathway; human cancer cell

Indexed keywords


EID: 80054699437     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/1-4020-3302-8_1     Document Type: Chapter
Times cited : (3)

References (208)
  • 1
    • 0023084725 scopus 로고
    • Apoptosis: Cell death under homeostatic control
    • Wyllie AH. Apoptosis: cell death under homeostatic control. Arch Toxicol Suppl 1987; 11: 3-10.
    • (1987) Arch Toxicol Suppl , vol.11 , pp. 3-10
    • Wyllie, A.H.1
  • 2
    • 0034641963 scopus 로고    scopus 로고
    • Defying death after DNA damage
    • Rich T, Allen RL, Wyllie AH. Defying death after DNA damage. Nature 2000; 407: 777-783.
    • (2000) Nature , vol.407 , pp. 777-783
    • Rich, T.1    Allen, R.L.2    Wyllie, A.H.3
  • 3
    • 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
  • 4
    • 0036204110 scopus 로고    scopus 로고
    • The regulation of APAF1 expression during development and tumourigenesis
    • Hickman ES, Helin K. The regulation of APAF1 expression during development and tumourigenesis. Apoptosis 2002; 7: 167-171.
    • (2002) Apoptosis , vol.7 , pp. 167-171
    • Hickman, E.S.1    Helin, K.2
  • 5
    • 0032796715 scopus 로고    scopus 로고
    • Apoptosis and carcinogenesis
    • Wyllie AH et al. Apoptosis and carcinogenesis. Br J Cancer 1999; 80 Suppl 1: 34-37.
    • (1999) Br J Cancer , vol.80 , Issue.SUPPL. 1 , pp. 34-37
    • Wyllie, A.H.1
  • 6
    • 0033026714 scopus 로고    scopus 로고
    • Mechanisms of apoptosis avoidance in cancer
    • Reed JC. Mechanisms of apoptosis avoidance in cancer. Curr Opin Oncol 1999; 11: 68-75.
    • (1999) Curr Opin Oncol , vol.11 , pp. 68-75
    • Reed, J.C.1
  • 7
    • 0034905394 scopus 로고    scopus 로고
    • XIAP: Apoptotic brake and promising therapeutic target
    • Holcik M, Gibson H, Korneluk RG. XIAP: apoptotic brake and promising therapeutic target. Apoptosis 2001; 6: 253-261.
    • (2001) Apoptosis , vol.6 , pp. 253-261
    • Holcik, M.1    Gibson, H.2    Korneluk, R.G.3
  • 8
    • 0036547417 scopus 로고    scopus 로고
    • Death and anti-death: Tumour resistance to apoptosis
    • Igney FH, Krammer PH. Death and anti-death: tumour resistance to apoptosis. Nat Rev Cancer 2002; 2: 277-288.
    • (2002) Nat Rev Cancer , vol.2 , pp. 277-288
    • Igney, F.H.1    Krammer, P.H.2
  • 9
    • 0037233327 scopus 로고    scopus 로고
    • Survivin and apoptosis control
    • Altieri DC. Survivin and apoptosis control. Adv Cancer Res 2003; 88: 31-52.
    • (2003) Adv Cancer Res , vol.88 , pp. 31-52
    • Altieri, D.C.1
  • 12
    • 0037020196 scopus 로고    scopus 로고
    • The role of apoptosis in creating and maintaining luminal space within normal and oncogene-expressing mammary acini
    • Debnath J et al. The role of apoptosis in creating and maintaining luminal space within normal and oncogene-expressing mammary acini. Cell 2002; 111: 29-40.
    • (2002) Cell , vol.111 , pp. 29-40
    • Debnath, J.1
  • 13
    • 0031720975 scopus 로고    scopus 로고
    • Apoptosis in the mammary gland and breast cancer
    • Hahm HaD, NE. Apoptosis in the mammary gland and breast cancer. Endocrine-Related Cancer 1998; 5: 199-211.
    • (1998) Endocrine-Related Cancer , vol.5 , pp. 199-211
    • Hahm, D.1    Ha, N.E.2
  • 14
    • 0029056951 scopus 로고
    • Potential roles of apoptosis in viral pathogenesis
    • Collins M. Potential roles of apoptosis in viral pathogenesis. Am J Respir Crit Care Med 1995; 152: S20-24.
    • (1995) Am J Respir Crit Care Med , vol.152
    • Collins, M.1
  • 15
    • 0030790430 scopus 로고    scopus 로고
    • Cell death in the regulation of immune responses
    • Winoto A. Cell death in the regulation of immune responses. Curr Opin Immunol 1997; 9: 365-370.
    • (1997) Curr Opin Immunol , vol.9 , pp. 365-370
    • Winoto, A.1
  • 16
    • 0033873788 scopus 로고    scopus 로고
    • UV-induced apoptosis in resistant HeLa cells
    • Kamarajan P, Chao CC. UV-induced apoptosis in resistant HeLa cells. Biosci Rep 2000; 20: 99-108.
    • (2000) Biosci Rep , vol.20 , pp. 99-108
    • Kamarajan, P.1    Chao, C.C.2
  • 17
    • 0642375738 scopus 로고    scopus 로고
    • Ionizing radiation and nitric oxide donor sensitize Fas-induced apoptosis via up-regulation of Fas in human cervical cancer cells
    • Park IC et al. Ionizing radiation and nitric oxide donor sensitize Fas-induced apoptosis via up-regulation of Fas in human cervical cancer cells. Oncol Rep 2003; 10: 629-633.
    • (2003) Oncol Rep , vol.10 , pp. 629-633
    • Park, I.C.1
  • 18
    • 0034630167 scopus 로고    scopus 로고
    • Induction of apoptosis by cancer chemotherapy
    • Kaufmann SH, Earnshaw WC. Induction of apoptosis by cancer chemotherapy. Exp Cell Res 2000; 256: 42-49.
    • (2000) Exp Cell Res , vol.256 , pp. 42-49
    • Kaufmann, S.H.1    Earnshaw, W.C.2
  • 19
    • 0034320568 scopus 로고    scopus 로고
    • Mechanisms of apoptosis
    • Reed JC. Mechanisms of apoptosis. Am J Pathol 2000; 157: 1415-1430.
    • (2000) Am J Pathol , vol.157 , pp. 1415-1430
    • Reed, J.C.1
  • 20
    • 0032910361 scopus 로고    scopus 로고
    • Mitochondrial regulation of cell death: Mitochondria are essential for procaspase 3-p21 complex formation to resist Fas-mediated cell death
    • Suzuki A et al. Mitochondrial regulation of cell death: mitochondria are essential for procaspase 3-p21 complex formation to resist Fas-mediated cell death. Mol Cell Biol 1999; 19: 3842-3847.
    • (1999) Mol Cell Biol , vol.19 , pp. 3842-3847
    • Suzuki, A.1
  • 21
    • 2442460088 scopus 로고    scopus 로고
    • Role of mitochondrial membrane permeabilization in apoptosis and cancer
    • Henry-Mowatt J, Dive C, Martinou JC, James D. Role of mitochondrial membrane permeabilization in apoptosis and cancer. Oncogene 2004; 23: 2850-2860.
    • (2004) Oncogene , vol.23 , pp. 2850-2860
    • Henry-Mowatt, J.1    Dive, C.2    Martinou, J.C.3    James, D.4
  • 22
    • 0033280669 scopus 로고    scopus 로고
    • Biochemical pathways of caspase activation during apoptosis
    • Budihardjo I et al. Biochemical pathways of caspase activation during apoptosis. Annu Rev Cell Dev Biol 1999; 15: 269-290.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 269-290
    • Budihardjo, I.1
  • 23
    • 0032416062 scopus 로고    scopus 로고
    • Death by a thousand cuts: An ever increasing list of caspase substrates
    • Stroh C, Schulze-Osthoff K. Death by a thousand cuts: an ever increasing list of caspase substrates. Cell Death Differ 1998; 5: 997-1000.
    • (1998) Cell Death Differ , vol.5 , pp. 997-1000
    • Stroh, C.1    Schulze-Osthoff, K.2
  • 24
    • 0037276437 scopus 로고    scopus 로고
    • The CD95(APO-1/Fas) DISC and beyond
    • Peter ME, Krammer PH. The CD95(APO-1/Fas) DISC and beyond. Cell Death Differ 2003; 10: 26-35.
    • (2003) Cell Death Differ , vol.10 , pp. 26-35
    • Peter, M.E.1    Krammer, P.H.2
  • 25
    • 4143108125 scopus 로고    scopus 로고
    • CD95 ligand induces motility and invasiveness of apoptosis-resistant tumor cells
    • Barnhart BC et al. CD95 ligand induces motility and invasiveness of apoptosis-resistant tumor cells. Embo J 2004; 23: 3175-3185.
    • (2004) Embo J , vol.23 , pp. 3175-3185
    • Barnhart, B.C.1
  • 26
    • 0034856368 scopus 로고    scopus 로고
    • CD95 antigen mutations in hematopoietic malignancies
    • Landowski TH et al. CD95 antigen mutations in hematopoietic malignancies. Leuk Lymphoma 2001; 42: 835-846.
    • (2001) Leuk Lymphoma , vol.42 , pp. 835-846
    • Landowski, T.H.1
  • 27
    • 0032525198 scopus 로고    scopus 로고
    • CD95 (APO-1/Fas) mutations in childhood T-lineage acute lymphoblastic leukemia
    • Beltinger C et al. CD95 (APO-1/Fas) mutations in childhood T-lineage acute lymphoblastic leukemia. Blood 1998; 91: 3943-3951.
    • (1998) Blood , vol.91 , pp. 3943-3951
    • Beltinger, C.1
  • 28
    • 0033600179 scopus 로고    scopus 로고
    • Alterations of Fas (Apo-1/CD95) gene in non-small cell lung cancer
    • Lee SH et al. Alterations of Fas (Apo-1/CD95) gene in non-small cell lung cancer. Oncogene 1999; 18: 3754-3760.
    • (1999) Oncogene , vol.18 , pp. 3754-3760
    • Lee, S.H.1
  • 29
    • 0036133858 scopus 로고    scopus 로고
    • Identification of Fas (APO-1/CD95) and p53 gene mutations in non-small cell lung cancer
    • Boldrini L et al. Identification of Fas (APO-1/CD95) and p53 gene mutations in non-small cell lung cancer. Int J Oncol 2002; 20: 155-159.
    • (2002) Int J Oncol , vol.20 , pp. 155-159
    • Boldrini, L.1
  • 30
    • 0035999095 scopus 로고    scopus 로고
    • Frequent downregulation of Fas (CD95) expression and function in melanoma
    • Bullani RR et al. Frequent downregulation of Fas (CD95) expression and function in melanoma. Melanoma Res 2002; 12: 263-270.
    • (2002) Melanoma Res , vol.12 , pp. 263-270
    • Bullani, R.R.1
  • 31
    • 0035079863 scopus 로고    scopus 로고
    • Expression of Fas and Fas-related molecules in human hepatocellular carcinoma
    • Lee SH et al. Expression of Fas and Fas-related molecules in human hepatocellular carcinoma. Hum Pathol 2001; 32: 250-256.
    • (2001) Hum Pathol , vol.32 , pp. 250-256
    • Lee, S.H.1
  • 32
    • 0032032577 scopus 로고    scopus 로고
    • Lack of cell surface Fas/APO-1 expression in pulmonary adenocarcinomas
    • Nambu Y et al. Lack of cell surface Fas/APO-1 expression in pulmonary adenocarcinomas. J Clin Invest 1998; 101: 1102-1110.
    • (1998) J Clin Invest , vol.101 , pp. 1102-1110
    • Nambu, Y.1
  • 33
    • 0141926700 scopus 로고    scopus 로고
    • Frequent loss of Fas expression and function in human lung tumours with overexpression of FasL in small cell lung carcinoma
    • Viard-Leveugle I et al. Frequent loss of Fas expression and function in human lung tumours with overexpression of FasL in small cell lung carcinoma. J Pathol 2003; 201: 268-277.
    • (2003) J Pathol , vol.201 , pp. 268-277
    • Viard-Leveugle, I.1
  • 34
    • 0033054108 scopus 로고    scopus 로고
    • In vivo expression of soluble Fas and FAP-1: Possible mechanisms of Fas resistance in human hepatoblastomas
    • Lee SH et al. In vivo expression of soluble Fas and FAP-1: possible mechanisms of Fas resistance in human hepatoblastomas. J Pathol 1999; 188: 207-212.
    • (1999) J Pathol , vol.188 , pp. 207-212
    • Lee, S.H.1
  • 35
    • 0037103302 scopus 로고    scopus 로고
    • Blockade of Fas-dependent apoptosis by soluble Fas in LGL leukemia
    • Liu JH et al. Blockade of Fas-dependent apoptosis by soluble Fas in LGL leukemia. Blood 2002; 100: 1449-1453.
    • (2002) Blood , vol.100 , pp. 1449-1453
    • Liu, J.H.1
  • 36
    • 0035258678 scopus 로고    scopus 로고
    • Human pancreatic cancer cells disable function of Fas receptors at several levels in Fas signal transduction pathway
    • Elnemr A et al. Human pancreatic cancer cells disable function of Fas receptors at several levels in Fas signal transduction pathway. Int J Oncol 2001; 18: 311-316.
    • (2001) Int J Oncol , vol.18 , pp. 311-316
    • Elnemr, A.1
  • 37
    • 19244376868 scopus 로고    scopus 로고
    • Resistance to CD95 (APO-1/Fas)-mediated apoptosis in human renal cell carcinomas: An important factor for evasion from negative growth control
    • Gerharz CD et al. Resistance to CD95 (APO-1/Fas)-mediated apoptosis in human renal cell carcinomas: an important factor for evasion from negative growth control. Lab Invest 1999; 79: 1521-1534.
    • (1999) Lab Invest , vol.79 , pp. 1521-1534
    • Gerharz, C.D.1
  • 38
    • 0035871978 scopus 로고    scopus 로고
    • Resistance to CD95-mediated apoptosis in breast cancer is not due to somatic mutation of the CD95 gene
    • Muschen M et al. Resistance to CD95-mediated apoptosis in breast cancer is not due to somatic mutation of the CD95 gene. Int J Cancer 2001; 92: 309-310.
    • (2001) Int J Cancer , vol.92 , pp. 309-310
    • Muschen, M.1
  • 39
    • 0029817663 scopus 로고    scopus 로고
    • Fas expression and function in normal and malignant breast cell lines
    • Keane MM et al. Fas expression and function in normal and malignant breast cell lines. Cancer Res 1996; 56: 4791-4798.
    • (1996) Cancer Res , vol.56 , pp. 4791-4798
    • Keane, M.M.1
  • 40
    • 0032522848 scopus 로고    scopus 로고
    • Human pancreatic adenocarcinomas express Fas and Fas ligand yet are resistant to Fas-mediated apoptosis
    • Ungefroren H et al. Human pancreatic adenocarcinomas express Fas and Fas ligand yet are resistant to Fas-mediated apoptosis. Cancer Res 1998; 58: 1741-1749.
    • (1998) Cancer Res , vol.58 , pp. 1741-1749
    • Ungefroren, H.1
  • 41
    • 0027145632 scopus 로고
    • Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family
    • Suda T, Takahashi T, Golstein P, Nagata S. Molecular cloning and expression of the Fas ligand, a novel member of the tumor necrosis factor family. Cell 1993; 75: 1169-1178.
    • (1993) Cell , vol.75 , pp. 1169-1178
    • Suda, T.1    Takahashi, T.2    Golstein, P.3    Nagata, S.4
  • 42
    • 0028864778 scopus 로고
    • A role for CD95 ligand in preventing graft rejection
    • Bellgrau D et al. A role for CD95 ligand in preventing graft rejection. Nature 1995; 377: 630-632.
    • (1995) Nature , vol.377 , pp. 630-632
    • Bellgrau, D.1
  • 43
    • 0342979787 scopus 로고    scopus 로고
    • Fas ligand is expressed in normal breast epithelial cells and is frequently up-regulated in breast cancer
    • Mullauer L et al. Fas ligand is expressed in normal breast epithelial cells and is frequently up-regulated in breast cancer. J Pathol 2000; 190: 20-30.
    • (2000) J Pathol , vol.190 , pp. 20-30
    • Mullauer, L.1
  • 44
    • 0041411313 scopus 로고    scopus 로고
    • The Fas/Fas ligand system and cancer: Immune privilege and apoptosis
    • Abrahams VM, Kamsteeg M, Mor G. The Fas/Fas ligand system and cancer: immune privilege and apoptosis. Mol Biotechnol 2003; 25: 19-30.
    • (2003) Mol Biotechnol , vol.25 , pp. 19-30
    • Abrahams, V.M.1    Kamsteeg, M.2    Mor, G.3
  • 45
    • 0034881170 scopus 로고    scopus 로고
    • Fas ligand upregulation is an early event in colonic carcinogenesis
    • Bennett MW et al. Fas ligand upregulation is an early event in colonic carcinogenesis. J Clin Pathol 2001; 54: 598-604.
    • (2001) J Clin Pathol , vol.54 , pp. 598-604
    • Bennett, M.W.1
  • 46
    • 0034036052 scopus 로고    scopus 로고
    • Expression of the apoptosis-inducing ligands FasL and TRAIL in malignant and benign human breast tumors
    • Herrnring C et al. Expression of the apoptosis-inducing ligands FasL and TRAIL in malignant and benign human breast tumors. Histochem Cell Biol 2000; 113: 189-194.
    • (2000) Histochem Cell Biol , vol.113 , pp. 189-194
    • Herrnring, C.1
  • 47
    • 0242584489 scopus 로고    scopus 로고
    • Prognostic relevance of Fas (APO-1/CD95) ligand in human colorectal cancer
    • Sheehan KM et al. Prognostic relevance of Fas (APO-1/CD95) ligand in human colorectal cancer. Eur J Gastroenterol Hepatol 2003; 15: 375-380.
    • (2003) Eur J Gastroenterol Hepatol , vol.15 , pp. 375-380
    • Sheehan, K.M.1
  • 48
    • 0001646169 scopus 로고    scopus 로고
    • Common regulation of apoptosis signaling induced by CD95 and the DNA-damaging stimuli etoposide and gamma-radiation downstream from caspase-8 activation
    • Boesen-de Cock JG et al. Common regulation of apoptosis signaling induced by CD95 and the DNA-damaging stimuli etoposide and gamma-radiation downstream from caspase-8 activation. J Biol Chem 1999; 274: 14255-14261.
    • (1999) J Biol Chem , vol.274 , pp. 14255-14261
    • Boesen-De Cock, J.G.1
  • 49
    • 0030752603 scopus 로고    scopus 로고
    • The CD95 (APO-1/Fas) system mediates drug-induced apoptosis in neuroblastoma cells
    • Fulda S et al. The CD95 (APO-1/Fas) system mediates drug-induced apoptosis in neuroblastoma cells. Cancer Res 1997; 57: 3823-3829.
    • (1997) Cancer Res , vol.57 , pp. 3823-3829
    • Fulda, S.1
  • 50
    • 0030897001 scopus 로고    scopus 로고
    • Selection for drug resistance results in resistance to Fas-mediated apoptosis
    • Landowski TH, Gleason-Guzman MC, Dalton WS. Selection for drug resistance results in resistance to Fas-mediated apoptosis. Blood 1997; 89: 1854-1861.
    • (1997) Blood , vol.89 , pp. 1854-1861
    • Landowski, T.H.1    Gleason-Guzman, M.C.2    Dalton, W.S.3
  • 51
    • 0346792725 scopus 로고    scopus 로고
    • TRAIL and apoptosis induction by TNF-family death receptors
    • Wang S, El-Deiry WS. TRAIL and apoptosis induction by TNF-family death receptors. Oncogene 2003; 22: 8628-8633.
    • (2003) Oncogene , vol.22 , pp. 8628-8633
    • Wang, S.1    El-Deiry, W.S.2
  • 52
    • 3342894130 scopus 로고    scopus 로고
    • Targeting death receptors in cancer with Apo2L/TRAIL
    • Kelley SK, Ashkenazi A. Targeting death receptors in cancer with Apo2L/TRAIL. Curr Opin Pharmacol 2004; 4: 333-339.
    • (2004) Curr Opin Pharmacol , vol.4 , pp. 333-339
    • Kelley, S.K.1    Ashkenazi, A.2
  • 53
    • 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
  • 55
    • 0032910169 scopus 로고    scopus 로고
    • Apoptosis control by death and decoy receptors
    • Ashkenazi A, Dixit VM. Apoptosis control by death and decoy receptors. Curr Opin Cell Biol 1999; 11: 255-260.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 255-260
    • Ashkenazi, A.1    Dixit, V.M.2
  • 56
    • 0034956807 scopus 로고    scopus 로고
    • Pancreatic adenocarcinoma cell lines show variable susceptibility to TRAIL-mediated cell death
    • Ibrahim SM et al. Pancreatic adenocarcinoma cell lines show variable susceptibility to TRAIL-mediated cell death. Pancreas 2001; 23: 72-79.
    • (2001) Pancreas , vol.23 , pp. 72-79
    • Ibrahim, S.M.1
  • 57
    • 0141705424 scopus 로고    scopus 로고
    • Synergistic interactions of chemotherapeutic drugs and tumor necrosis factor-related apoptosis-inducing ligand/Apo-2 ligand on apoptosis and on regression of breast carcinoma in vivo
    • Singh TR et al. Synergistic interactions of chemotherapeutic drugs and tumor necrosis factor-related apoptosis-inducing ligand/Apo-2 ligand on apoptosis and on regression of breast carcinoma in vivo. Cancer Res 2003; 63: 5390-5400.
    • (2003) Cancer Res , vol.63 , pp. 5390-5400
    • Singh, T.R.1
  • 58
    • 9944263245 scopus 로고    scopus 로고
    • Deficient TRAIL death receptor transport to the cell surface in human colon cancer cells selected for resistance to TRAIL-induced apoptosis
    • Jin Z, McDonald ER, 3rd, Dicker DT, El-Deiry WS. Deficient TRAIL death receptor transport to the cell surface in human colon cancer cells selected for resistance to TRAIL-induced apoptosis. J Biol Chem 2004.
    • (2004) J Biol Chem
    • Jin, Z.1    McDonald, E.R.2    Dicker III, D.T.3    El-Deiry, W.S.4
  • 59
    • 0036466842 scopus 로고    scopus 로고
    • TRAIL, FasL and a blocking anti-DR5 antibody augment paclitaxel-induced apoptosis in human non-small-cell lung cancer
    • Odoux C et al. TRAIL, FasL and a blocking anti-DR5 antibody augment paclitaxel-induced apoptosis in human non-small-cell lung cancer. Int J Cancer 2002; 97: 458-465.
    • (2002) Int J Cancer , vol.97 , pp. 458-465
    • Odoux, C.1
  • 60
    • 2942565827 scopus 로고    scopus 로고
    • Enhancement of therapeutic potential of TRAIL by cancer chemotherapy and irradiation: Mechanisms and clinical implications
    • Shankar S, Srivastava RK. Enhancement of therapeutic potential of TRAIL by cancer chemotherapy and irradiation: mechanisms and clinical implications. Drug Resist Updat 2004; 7: 139-156.
    • (2004) Drug Resist Updat , vol.7 , pp. 139-156
    • Shankar, S.1    Srivastava, R.K.2
  • 61
    • 0032575714 scopus 로고    scopus 로고
    • Death receptors: Signaling and modulation
    • Ashkenazi A, Dixit VM. Death receptors: signaling and modulation. Science 1998; 281: 1305-1308.
    • (1998) Science , vol.281 , pp. 1305-1308
    • Ashkenazi, A.1    Dixit, V.M.2
  • 62
    • 0037054549 scopus 로고    scopus 로고
    • Nuclear and cytoplasmic shuttling of TRADD induces apoptosis via different mechanisms
    • Morgan M, Thorburn J, Pandolfi PP, Thorburn A. Nuclear and cytoplasmic shuttling of TRADD induces apoptosis via different mechanisms. J Cell Biol 2002; 157: 975-984.
    • (2002) J Cell Biol , vol.157 , pp. 975-984
    • Morgan, M.1    Thorburn, J.2    Pandolfi, P.P.3    Thorburn, A.4
  • 63
    • 1342285692 scopus 로고    scopus 로고
    • Tumor necrosis factor: An apoptosis JuNKie?
    • Varfolomeev EE, Ashkenazi A. Tumor necrosis factor: an apoptosis JuNKie? Cell 2004; 116: 491-497.
    • (2004) Cell , vol.116 , pp. 491-497
    • Varfolomeev, E.E.1    Ashkenazi, A.2
  • 64
    • 0034743199 scopus 로고    scopus 로고
    • NF-kappaB signals induce the expression of c-FLIP
    • Micheau O et al. NF-kappaB signals induce the expression of c-FLIP. Mol Cell Biol 2001; 21: 5299-5305.
    • (2001) Mol Cell Biol , vol.21 , pp. 5299-5305
    • Micheau, O.1
  • 65
    • 0034983077 scopus 로고    scopus 로고
    • Expression of the tumour necrosis factor receptor-associated factors 1 and 2 in Hodgkin's disease
    • Murray PG et al. Expression of the tumour necrosis factor receptor-associated factors 1 and 2 in Hodgkin's disease. J Pathol 2001; 194: 158-164.
    • (2001) J Pathol , vol.194 , pp. 158-164
    • Murray, P.G.1
  • 66
    • 0034326624 scopus 로고    scopus 로고
    • TNFR-associated factor family protein expression in normal tissues and lymphoid malignancies
    • Zapata JM et al. TNFR-associated factor family protein expression in normal tissues and lymphoid malignancies. J Immunol 2000; 165: 5084-5096.
    • (2000) J Immunol , vol.165 , pp. 5084-5096
    • Zapata, J.M.1
  • 67
    • 0037621450 scopus 로고    scopus 로고
    • Silencing of death receptor and caspase-8 expression in small cell lung carcinoma cell lines and tumors by DNA methylation
    • Hopkins-Donaldson S et al. Silencing of death receptor and caspase-8 expression in small cell lung carcinoma cell lines and tumors by DNA methylation. Cell Death Differ 2003; 10: 356-364.
    • (2003) Cell Death Differ , vol.10 , pp. 356-364
    • Hopkins-Donaldson, S.1
  • 68
    • 0141453653 scopus 로고    scopus 로고
    • Caspase 3 and 8 deficiency in human neuroblastoma
    • Iolascon A et al. Caspase 3 and 8 deficiency in human neuroblastoma. Cancer Genet Cytogenet 2003; 146: 41-47.
    • (2003) Cancer Genet Cytogenet , vol.146 , pp. 41-47
    • Iolascon, A.1
  • 69
    • 0034066405 scopus 로고    scopus 로고
    • Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN
    • Teitz T et al. Caspase 8 is deleted or silenced preferentially in childhood neuroblastomas with amplification of MYCN. Nat Med 2000; 6: 529-535.
    • (2000) Nat Med , vol.6 , pp. 529-535
    • Teitz, T.1
  • 70
    • 0033890808 scopus 로고    scopus 로고
    • Reduced expression of ICE/caspase1 and CPP32/caspase3 in human hepatocellular carcinoma
    • Fujikawa K et al. Reduced expression of ICE/caspase1 and CPP32/caspase3 in human hepatocellular carcinoma. Anticancer Res 2000; 20: 1927-1932.
    • (2000) Anticancer Res , vol.20 , pp. 1927-1932
    • Fujikawa, K.1
  • 71
    • 0033564103 scopus 로고    scopus 로고
    • Dead or dying: Necrosis versus apoptosis in caspase-deficient human renal cell carcinoma
    • Kolenko V et al. Dead or dying: necrosis versus apoptosis in caspase-deficient human renal cell carcinoma. Cancer Res 1999; 59: 2838-2842.
    • (1999) Cancer Res , vol.59 , pp. 2838-2842
    • Kolenko, V.1
  • 72
    • 0034990676 scopus 로고    scopus 로고
    • Caspase 7 downregulation as an immunohistochemical marker of colonic carcinoma
    • Palmerini F et al. Caspase 7 downregulation as an immunohistochemical marker of colonic carcinoma. Hum Pathol 2001; 32: 461-467.
    • (2001) Hum Pathol , vol.32 , pp. 461-467
    • Palmerini, F.1
  • 73
    • 0035937797 scopus 로고    scopus 로고
    • A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis
    • Chu ZL et al. A novel enhancer of the Apaf1 apoptosome involved in cytochrome c-dependent caspase activation and apoptosis. J Biol Chem 2001; 276: 9239-9245.
    • (2001) J Biol Chem , vol.276 , pp. 9239-9245
    • Chu, Z.L.1
  • 74
    • 0035843169 scopus 로고    scopus 로고
    • Inactivation of the apoptosis effector Apaf-1 in malignant melanoma
    • Soengas MS et al. Inactivation of the apoptosis effector Apaf-1 in malignant melanoma. Nature 2001; 409: 207-211.
    • (2001) Nature , vol.409 , pp. 207-211
    • Soengas, M.S.1
  • 75
    • 0035744678 scopus 로고    scopus 로고
    • Immunohistochemical expression of caspase-3 as an adverse indicator of the clinical outcome in human breast cancer
    • Nakopoulou L et al. Immunohistochemical expression of caspase-3 as an adverse indicator of the clinical outcome in human breast cancer. Pathobiology 2001; 69: 266-273.
    • (2001) Pathobiology , vol.69 , pp. 266-273
    • Nakopoulou, L.1
  • 76
    • 0032881750 scopus 로고    scopus 로고
    • Expression of caspases 3, 6 and 8 is increased in parallel with apoptosis and histological aggressiveness of the breast lesion
    • Vakkala M, Paakko P, Soini Y. Expression of caspases 3, 6 and 8 is increased in parallel with apoptosis and histological aggressiveness of the breast lesion. Br J Cancer 1999; 81: 592-599.
    • (1999) Br J Cancer , vol.81 , pp. 592-599
    • Vakkala, M.1    Paakko, P.2    Soini, Y.3
  • 77
    • 0035992283 scopus 로고    scopus 로고
    • Coordinate expression of apoptosis-associated proteins in human breast cancer before and during chemotherapy
    • Parton M et al. Coordinate Expression of Apoptosis-associated Proteins in Human Breast Cancer before and during Chemotherapy. Clin Cancer Res 2002; 8: 2100-2108.
    • (2002) Clin Cancer Res , vol.8 , pp. 2100-2108
    • Parton, M.1
  • 78
    • 0037312545 scopus 로고    scopus 로고
    • Caspase 3 in breast cancer
    • O'Donovan N et al. Caspase 3 in breast cancer. Clin Cancer Res 2003; 9: 738-742.
    • (2003) Clin Cancer Res , vol.9 , pp. 738-742
    • O'Donovan, N.1
  • 79
    • 0142188706 scopus 로고    scopus 로고
    • Coexistence of high levels of apoptotic signaling and inhibitor of apoptosis proteins in human tumor cells: Implication for cancer specific therapy
    • Yang L, Cao Z, Yan H, Wood WC. Coexistence of high levels of apoptotic signaling and inhibitor of apoptosis proteins in human tumor cells: implication for cancer specific therapy. Cancer Res 2003; 63: 6815-6824.
    • (2003) Cancer Res , vol.63 , pp. 6815-6824
    • Yang, L.1    Cao, Z.2    Yan, H.3    Wood, W.C.4
  • 80
    • 0035878930 scopus 로고    scopus 로고
    • Expression of survivin is correlated with cancer cell apoptosis and is involved in the development of human pancreatic duct cell tumors
    • Satoh K et al. Expression of survivin is correlated with cancer cell apoptosis and is involved in the development of human pancreatic duct cell tumors. Cancer 2001; 92: 271-278.
    • (2001) Cancer , vol.92 , pp. 271-278
    • Satoh, K.1
  • 81
    • 0036876248 scopus 로고    scopus 로고
    • Stomach cancer highly expresses both initiator and effector caspases; An immunohistochemical study
    • Yoo NJ et al. Stomach cancer highly expresses both initiator and effector caspases; an immunohistochemical study. Apmis 2002; 110: 825-832.
    • (2002) Apmis , vol.110 , pp. 825-832
    • Yoo, N.J.1
  • 82
    • 0033386808 scopus 로고    scopus 로고
    • Caspase activation is required for T cell proliferation
    • Kennedy NJ, Kataoka T, Tschopp J, Budd RC. Caspase activation is required for T cell proliferation. J Exp Med 1999; 190: 1891-1896.
    • (1999) J Exp Med , vol.190 , pp. 1891-1896
    • Kennedy, N.J.1    Kataoka, T.2    Tschopp, J.3    Budd, R.C.4
  • 83
    • 0036824646 scopus 로고    scopus 로고
    • Differential modulation of interleukin-2-and interleukin-4-mediated early activation of normal human B lymphocytes by the caspase inhibitor zVAD-fmk
    • Mouhamad S et al. Differential modulation of interleukin-2-and interleukin-4-mediated early activation of normal human B lymphocytes by the caspase inhibitor zVAD-fmk. Eur Cytokine Netw 2002; 13: 439-445.
    • (2002) Eur Cytokine Netw , vol.13 , pp. 439-445
    • Mouhamad, S.1
  • 84
    • 0036446885 scopus 로고    scopus 로고
    • Caspase-14 expression by epidermal keratinocytes is regulated by retinoids in a differentiation-associated manner
    • Rendl M et al. Caspase-14 expression by epidermal keratinocytes is regulated by retinoids in a differentiation-associated manner. J Invest Dermatol 2002; 119: 1150-1155.
    • (2002) J Invest Dermatol , vol.119 , pp. 1150-1155
    • Rendl, M.1
  • 85
    • 0036377840 scopus 로고    scopus 로고
    • The biological role of the Fas/FasL system during tumor formation and progression
    • Reichmann E. The biological role of the Fas/FasL system during tumor formation and progression. Semin Cancer Biol 2002; 12: 309-315.
    • (2002) Semin Cancer Biol , vol.12 , pp. 309-315
    • Reichmann, E.1
  • 86
    • 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: 1541-1548.
    • (1999) J Biol Chem , vol.274 , pp. 1541-1548
    • Scaffidi, C.1    Schmitz, I.2    Krammer, P.H.3    Peter, M.E.4
  • 87
    • 4844220794 scopus 로고    scopus 로고
    • Possible role of FLICE-like inhibitory protein (FLIP) in chemoresistant ovarian cancer cells in vitro
    • Abedini MR, Qiu Q, Yan X, Tsang BK. Possible role of FLICE-like inhibitory protein (FLIP) in chemoresistant ovarian cancer cells in vitro. Oncogene 2004.
    • (2004) Oncogene
    • Abedini, M.R.1    Qiu, Q.2    Yan, X.3    Tsang, B.K.4
  • 88
    • 0038556793 scopus 로고    scopus 로고
    • Increased expression of FLIP, an inhibitor of Fas-mediated apoptosis, in stomach cancer
    • Lee SH et al. Increased expression of FLIP, an inhibitor of Fas-mediated apoptosis, in stomach cancer. Apmis 2003; 111: 309-314.
    • (2003) Apmis , vol.111 , pp. 309-314
    • Lee, S.H.1
  • 89
    • 0032530612 scopus 로고    scopus 로고
    • Intracellular regulation of TRAIL-induced apoptosis in human melanoma cells
    • Griffith TS et al. Intracellular regulation of TRAIL-induced apoptosis in human melanoma cells. J Immunol 1998; 161: 2833-2840.
    • (1998) J Immunol , vol.161 , pp. 2833-2840
    • Griffith, T.S.1
  • 90
    • 0344393606 scopus 로고    scopus 로고
    • Up-regulation of FLIP in cisplatin-selected HeLa cells causes cross-resistance to CD95/Fas death signalling
    • Kamarajan P, Sun NK, Chao CC. Up-regulation of FLIP in cisplatin-selected HeLa cells causes cross-resistance to CD95/Fas death signalling. Biochem J 2003; 376: 253-260.
    • (2003) Biochem J , vol.376 , pp. 253-260
    • Kamarajan, P.1    Sun, N.K.2    Chao, C.C.3
  • 91
    • 0032409781 scopus 로고    scopus 로고
    • Bcl-2 family proteins
    • Reed JC. Bcl-2 family proteins. Oncogene 1998; 17: 3225-3236.
    • (1998) Oncogene , vol.17 , pp. 3225-3236
    • Reed, J.C.1
  • 92
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: Roles in cell survival and oncogenesis
    • Cory S, Huang DC, Adams JM. The Bcl-2 family: roles in cell survival and oncogenesis. Oncogene 2003; 22: 8590-8607.
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.2    Adams, J.M.3
  • 93
    • 0028958030 scopus 로고
    • Bcl-2: Prevention of apoptosis as a mechanism of drug resistance
    • Reed JC. Bcl-2: prevention of apoptosis as a mechanism of drug resistance. Hematol Oncol Clin North Am 1995; 9: 451-473.
    • (1995) Hematol Oncol Clin North Am , vol.9 , pp. 451-473
    • Reed, J.C.1
  • 94
    • 0027970798 scopus 로고
    • Immunocytochemical localization of BCL-2 protein in human breast cancers and its relationship to a series of prognostic markers and response to endocrine therapy
    • Gee JM et al. Immunocytochemical localization of BCL-2 protein in human breast cancers and its relationship to a series of prognostic markers and response to endocrine therapy. Int J Cancer 1994; 59: 619-628.
    • (1994) Int J Cancer , vol.59 , pp. 619-628
    • Gee, J.M.1
  • 95
    • 0029794419 scopus 로고    scopus 로고
    • Upregulated expression of BCL-2 in multiple myeloma cells induced by exposure to doxorubicin, etoposide, and hydrogen peroxide
    • Tu Y et al. Upregulated expression of BCL-2 in multiple myeloma cells induced by exposure to doxorubicin, etoposide, and hydrogen peroxide. Blood 1996; 88: 1805-1812.
    • (1996) Blood , vol.88 , pp. 1805-1812
    • Tu, Y.1
  • 96
    • 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: 2283-2294.
    • (2002) Oncogene , vol.21 , pp. 2283-2294
    • Fulda, S.1    Meyer, E.2    Debatin, K.M.3
  • 97
    • 0242721548 scopus 로고    scopus 로고
    • Targeting Bcl-2 and Bcl-XL with nonpeptidic small-molecule antagonists
    • Wang S, Yang D, Lippman ME. Targeting Bcl-2 and Bcl-XL with nonpeptidic small-molecule antagonists. Semin Oncol 2003; 30: 133-142.
    • (2003) Semin Oncol , vol.30 , pp. 133-142
    • Wang, S.1    Yang, D.2    Lippman, M.E.3
  • 98
    • 0031575073 scopus 로고    scopus 로고
    • Promise and problems of Bcl-2 antisense therapy
    • Reed JC. Promise and problems of Bcl-2 antisense therapy. J Natl Cancer Inst 1997; 89: 988-990.
    • (1997) J Natl Cancer Inst , vol.89 , pp. 988-990
    • Reed, J.C.1
  • 99
    • 0036463649 scopus 로고    scopus 로고
    • Apoptosis-based therapies
    • Reed JC. Apoptosis-based therapies. Nat Rev Drug Discov 2002; 1: 111-121.
    • (2002) Nat Rev Drug Discov , vol.1 , pp. 111-121
    • Reed, J.C.1
  • 100
    • 0032943691 scopus 로고    scopus 로고
    • Prognostic significance of apoptosis regulators in breast cancer
    • Krajewski S et al. Prognostic significance of apoptosis regulators in breast cancer. Endocr Relat Cancer 1999; 6: 29-40.
    • (1999) Endocr Relat Cancer , vol.6 , pp. 29-40
    • Krajewski, S.1
  • 101
    • 0033973291 scopus 로고    scopus 로고
    • Immunohistochemical analysis of Bcl-2 and Bax expression in relation to cell turnover and epithelial differentiation markers in the non-lactating human mammary gland epithelium
    • Feuerhake F et al. Immunohistochemical analysis of Bcl-2 and Bax expression in relation to cell turnover and epithelial differentiation markers in the non-lactating human mammary gland epithelium. Cell Tissue Res 2000; 299: 47-58.
    • (2000) Cell Tissue Res , vol.299 , pp. 47-58
    • Feuerhake, F.1
  • 102
    • 0027944957 scopus 로고
    • Bcl-2 protein expression and long-term survival in breast cancer
    • Joensuu H, Pylkkanen L, Toikkanen S. Bcl-2 protein expression and long-term survival in breast cancer. Am J Pathol 1994; 145: 1191-1198.
    • (1994) Am J Pathol , vol.145 , pp. 1191-1198
    • Joensuu, H.1    Pylkkanen, L.2    Toikkanen, S.3
  • 103
    • 0031927561 scopus 로고    scopus 로고
    • Apoptotic index correlates to bcl-2 and p53 protein expression, histological grade and prognosis in invasive breast cancers
    • Zhang GJ et al. Apoptotic index correlates to bcl-2 and p53 protein expression, histological grade and prognosis in invasive breast cancers. Anticancer Res 1998; 18: 1989-1998.
    • (1998) Anticancer Res , vol.18 , pp. 1989-1998
    • Zhang, G.J.1
  • 104
    • 0035080860 scopus 로고    scopus 로고
    • Bcl-2 Expression and apoptosis in primary and metastatic breast carcinomas
    • Villar E et al. bcl-2 Expression and apoptosis in primary and metastatic breast carcinomas. Tumour Biol 2001; 22: 137-145.
    • (2001) Tumour Biol , vol.22 , pp. 137-145
    • Villar, E.1
  • 105
    • 0344938137 scopus 로고    scopus 로고
    • Bax is frequently compromised in Burkitt's lymphomas with irreversible resistance to Fas-induced apoptosis
    • Gutierrez MI et al. Bax is frequently compromised in Burkitt's lymphomas with irreversible resistance to Fas-induced apoptosis. Cancer Res 1999; 59: 696-703.
    • (1999) Cancer Res , vol.59 , pp. 696-703
    • Gutierrez, M.I.1
  • 107
    • 0031018674 scopus 로고    scopus 로고
    • Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype
    • Rampino N et al. Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype. Science 1997; 275: 967-969.
    • (1997) Science , vol.275 , pp. 967-969
    • Rampino, N.1
  • 108
    • 0028944271 scopus 로고
    • Expression of the bcl-2 gene family in normal and malignant breast tissue: Low bax-alpha expression in tumor cells correlates with resistance towards apoptosis
    • Bargou RC et al. Expression of the bcl-2 gene family in normal and malignant breast tissue: low bax-alpha expression in tumor cells correlates with resistance towards apoptosis. Int J Cancer 1995; 60: 854-859.
    • (1995) Int J Cancer , vol.60 , pp. 854-859
    • Bargou, R.C.1
  • 109
    • 0029045784 scopus 로고
    • Reduced expression of proapoptotic gene BAX is associated with poor response rates to combination chemotherapy and shorter survival in women with metastatic breast adenocarcinoma
    • Krajewski S et al. Reduced expression of proapoptotic gene BAX is associated with poor response rates to combination chemotherapy and shorter survival in women with metastatic breast adenocarcinoma. Cancer Res 1995; 55: 4471-4478.
    • (1995) Cancer Res , vol.55 , pp. 4471-4478
    • Krajewski, S.1
  • 110
    • 0037570803 scopus 로고    scopus 로고
    • Expression of bax and p53 proteins in the tumorigenesis and progression of breast carcinomas
    • Redondo M et al. Expression of bax and p53 proteins in the tumorigenesis and progression of breast carcinomas. Tumour Biol 2003; 24: 23-31.
    • (2003) Tumour Biol , vol.24 , pp. 23-31
    • Redondo, M.1
  • 111
    • 0030698127 scopus 로고    scopus 로고
    • The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases
    • Roy N et al. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. Embo J 1997; 16: 6914-6925.
    • (1997) Embo J , vol.16 , pp. 6914-6925
    • Roy, N.1
  • 112
    • 0035920126 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and-7 in distinct modes
    • Suzuki Y et al. X-linked inhibitor of apoptosis protein (XIAP) inhibits caspase-3 and-7 in distinct modes. J Biol Chem 2001; 276: 27058-27063.
    • (2001) J Biol Chem , vol.276 , pp. 27058-27063
    • Suzuki, Y.1
  • 113
    • 0035793557 scopus 로고    scopus 로고
    • Livin, a novel inhibitor of apoptosis protein family member
    • Kasof GM, Gomes BC. Livin, a novel inhibitor of apoptosis protein family member. J Biol Chem 2001; 276: 3238-3246.
    • (2001) J Biol Chem , vol.276 , pp. 3238-3246
    • Kasof, G.M.1    Gomes, B.C.2
  • 114
    • 1942534018 scopus 로고    scopus 로고
    • Regulation of apoptosis proteins in cancer cells by ubiquitin
    • Zhang HG et al. Regulation of apoptosis proteins in cancer cells by ubiquitin. Oncogene 2004; 23: 2009-2015.
    • (2004) Oncogene , vol.23 , pp. 2009-2015
    • Zhang, H.G.1
  • 115
    • 0032403126 scopus 로고    scopus 로고
    • IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs
    • Tamm I et al. IAP-family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD95), Bax, caspases, and anticancer drugs. Cancer Res 1998; 58: 5315-5320.
    • (1998) Cancer Res , vol.58 , pp. 5315-5320
    • Tamm, I.1
  • 116
    • 4544261227 scopus 로고    scopus 로고
    • An IAP-IAP complex inhibits apoptosis
    • Dohi T et al. An IAP-IAP complex inhibits apoptosis. J Biol Chem 2004; 279: 34087-34090.
    • (2004) J Biol Chem , vol.279 , pp. 34087-34090
    • Dohi, T.1
  • 117
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C et al. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 2000; 102: 33-42.
    • (2000) Cell , vol.102 , pp. 33-42
    • Du, C.1
  • 118
    • 0034700495 scopus 로고    scopus 로고
    • Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
    • Liu Z et al. Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain. Nature 2000; 408: 1004-1008.
    • (2000) Nature , vol.408 , pp. 1004-1008
    • Liu, Z.1
  • 119
    • 0035156848 scopus 로고    scopus 로고
    • Identification of XAF1 as an antagonist of XIAP anti-Caspase activity
    • Liston P et al. Identification of XAF1 as an antagonist of XIAP anti-Caspase activity. Nat Cell Biol 2001; 3: 128-133.
    • (2001) Nat Cell Biol , vol.3 , pp. 128-133
    • Liston, P.1
  • 120
    • 0034672506 scopus 로고    scopus 로고
    • Expression and genetic analysis of XIAP-associated factor 1 (XAF1) in cancer cell lines
    • Fong WG et al. Expression and genetic analysis of XIAP-associated factor 1 (XAF1) in cancer cell lines. Genomics 2000; 70: 113-122.
    • (2000) Genomics , vol.70 , pp. 113-122
    • Fong, W.G.1
  • 121
    • 0242442595 scopus 로고    scopus 로고
    • Hypermethylation of XIAP-associated factor 1, a putative tumor suppressor gene from the 17p13.2 locus, in human gastric adenocarcinomas
    • Byun DS et al. Hypermethylation of XIAP-associated factor 1, a putative tumor suppressor gene from the 17p13.2 locus, in human gastric adenocarcinomas. Cancer Res 2003; 63: 7068-7075.
    • (2003) Cancer Res , vol.63 , pp. 7068-7075
    • Byun, D.S.1
  • 122
    • 0031984247 scopus 로고    scopus 로고
    • Developmentally regulated expression of the novel cancer anti-apoptosis gene survivin in human and mouse differentiation
    • Adida C et al. Developmentally regulated expression of the novel cancer anti-apoptosis gene survivin in human and mouse differentiation. Am J Pathol 1998; 152: 43-49.
    • (1998) Am J Pathol , vol.152 , pp. 43-49
    • Adida, C.1
  • 123
    • 0346250160 scopus 로고    scopus 로고
    • Survivin, versatile modulation of cell division and apoptosis in cancer
    • Altieri DC. Survivin, versatile modulation of cell division and apoptosis in cancer. Oncogene 2003; 22: 8581-8589.
    • (2003) Oncogene , vol.22 , pp. 8581-8589
    • Altieri, D.C.1
  • 124
    • 0030746636 scopus 로고    scopus 로고
    • A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma
    • Ambrosini G, Adida C, Altieri DC. A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma. Nat Med 1997; 3: 917-921.
    • (1997) Nat Med , vol.3 , pp. 917-921
    • Ambrosini, G.1    Adida, C.2    Altieri, D.C.3
  • 125
    • 0141595100 scopus 로고    scopus 로고
    • Survivin study: What is the next wave?
    • Li F. Survivin study: what is the next wave? J Cell Physiol 2003; 197: 8-29.
    • (2003) J Cell Physiol , vol.197 , pp. 8-29
    • Li, F.1
  • 126
    • 0033980409 scopus 로고    scopus 로고
    • Expression of survivin and its relationship to loss of apoptosis in breast carcinomas
    • Tanaka K et al. Expression of survivin and its relationship to loss of apoptosis in breast carcinomas. Clin Cancer Res 2000; 6: 127-134.
    • (2000) Clin Cancer Res , vol.6 , pp. 127-134
    • Tanaka, K.1
  • 127
    • 0037128687 scopus 로고    scopus 로고
    • Expression of survivin, a novel inhibitor of apoptosis and cell cycle regulatory protein, in pancreatic adenocarcinoma
    • Sarela AI et al. Expression of survivin, a novel inhibitor of apoptosis and cell cycle regulatory protein, in pancreatic adenocarcinoma. Br J Cancer 2002; 86: 886-892.
    • (2002) Br J Cancer , vol.86 , pp. 886-892
    • Sarela, A.I.1
  • 128
    • 0033661699 scopus 로고    scopus 로고
    • Role of survivin, whose gene is mapped to 17q25, in human neuroblastoma and identification of a novel dominant-negative isoform, survivin-beta/2B
    • Islam A et al. Role of survivin, whose gene is mapped to 17q25, in human neuroblastoma and identification of a novel dominant-negative isoform, survivin-beta/2B. Med Pediatr Oncol 2000; 35: 550-553.
    • (2000) Med Pediatr Oncol , vol.35 , pp. 550-553
    • Islam, A.1
  • 129
    • 0035964487 scopus 로고    scopus 로고
    • DNA demethylase is expressed in ovarian cancers and the expression correlates with demethylation of CpG sites in the promoter region of c-erbB-2 and survivin genes
    • Hattori M, Sakamoto H, Satoh K, Yamamoto T. DNA demethylase is expressed in ovarian cancers and the expression correlates with demethylation of CpG sites in the promoter region of c-erbB-2 and survivin genes. Cancer Lett 2001; 169: 155-164.
    • (2001) Cancer Lett , vol.169 , pp. 155-164
    • Hattori, M.1    Sakamoto, H.2    Satoh, K.3    Yamamoto, T.4
  • 130
    • 0037012343 scopus 로고    scopus 로고
    • Activation of cancer-specific gene expression by the survivin promoter
    • Bao R et al. Activation of cancer-specific gene expression by the survivin promoter. J Natl Cancer Inst 2002; 94: 522-528.
    • (2002) J Natl Cancer Inst , vol.94 , pp. 522-528
    • Bao, R.1
  • 131
    • 0036479115 scopus 로고    scopus 로고
    • Transcriptional repression of the anti-apoptotic survivin gene by wild type p53
    • Hoffman WH et al. Transcriptional repression of the anti-apoptotic survivin gene by wild type p53. J Biol Chem 2002; 277: 3247-3257.
    • (2002) J Biol Chem , vol.277 , pp. 3247-3257
    • Hoffman, W.H.1
  • 132
    • 0036747409 scopus 로고    scopus 로고
    • A role for survivin in radioresistance of pancreatic cancer cells
    • Asanuma K et al. A role for survivin in radioresistance of pancreatic cancer cells. Jpn J Cancer Res 2002; 93: 1057-1062.
    • (2002) Jpn J Cancer Res , vol.93 , pp. 1057-1062
    • Asanuma, K.1
  • 133
    • 0032533494 scopus 로고    scopus 로고
    • Inhibition of apoptosis by survivin predicts shorter survival rates in colorectal cancer
    • Kawasaki H et al. Inhibition of apoptosis by survivin predicts shorter survival rates in colorectal cancer. Cancer Res 1998; 58: 5071-5074.
    • (1998) Cancer Res , vol.58 , pp. 5071-5074
    • Kawasaki, H.1
  • 134
    • 3843099444 scopus 로고    scopus 로고
    • Survivin expression is a prognostic marker in pancreatic cancer patients
    • Kami K et al. Survivin expression is a prognostic marker in pancreatic cancer patients. Surgery 2004; 136: 443-448.
    • (2004) Surgery , vol.136 , pp. 443-448
    • Kami, K.1
  • 135
    • 0034795822 scopus 로고    scopus 로고
    • Transgenic expression of survivin in keratinocytes counteracts UVB-induced apoptosis and cooperates with loss of p53
    • Grossman D et al. Transgenic expression of survivin in keratinocytes counteracts UVB-induced apoptosis and cooperates with loss of p53. J Clin Invest 2001; 108: 991-999.
    • (2001) J Clin Invest , vol.108 , pp. 991-999
    • Grossman, D.1
  • 136
    • 0034789355 scopus 로고    scopus 로고
    • Cancer gene therapy using a survivin mutant adenovirus
    • Mesri M et al. Cancer gene therapy using a survivin mutant adenovirus. J Clin Invest 2001; 108: 981-990.
    • (2001) J Clin Invest , vol.108 , pp. 981-990
    • Mesri, M.1
  • 137
    • 1342332363 scopus 로고    scopus 로고
    • Antisense to apoptosis inhibitors facilitates chemotherapy and TRAIL-induced death signaling
    • Zangemeister-Wittke U. Antisense to apoptosis inhibitors facilitates chemotherapy and TRAIL-induced death signaling. Ann N Y Acad Sci 2003; 1002: 90-94.
    • (2003) Ann N y Acad Sci , vol.1002 , pp. 90-94
    • Zangemeister-Wittke, U.1
  • 138
    • 0033258543 scopus 로고    scopus 로고
    • Pleiotropic cell-division defects and apoptosis induced by interference with survivin function
    • Li F et al. Pleiotropic cell-division defects and apoptosis induced by interference with survivin function. Nat Cell Biol 1999; 1: 461-466.
    • (1999) Nat Cell Biol , vol.1 , pp. 461-466
    • Li, F.1
  • 139
    • 0026669469 scopus 로고
    • Kinzler KW. p53 function and dysfunction
    • Vogelstein B, Kinzler KW. p53 function and dysfunction. Cell 1992; 70: 523-526.
    • (1992) Cell , vol.70 , pp. 523-526
    • Vogelstein, B.1
  • 141
    • 0030930366 scopus 로고    scopus 로고
    • A model for p53-induced apoptosis
    • Polyak K et al. A model for p53-induced apoptosis. Nature 1997; 389: 300-305.
    • (1997) Nature , vol.389 , pp. 300-305
    • Polyak, K.1
  • 142
    • 0031743648 scopus 로고    scopus 로고
    • P53 activates the CD95 (APO-1/Fas) gene in response to DNA damage by anticancer drugs
    • Muller M et al. p53 activates the CD95 (APO-1/Fas) gene in response to DNA damage by anticancer drugs. J Exp Med 1998; 188: 2033-2045.
    • (1998) J Exp Med , vol.188 , pp. 2033-2045
    • Muller, M.1
  • 143
    • 0031038137 scopus 로고    scopus 로고
    • Bax suppresses tumorigenesis and stimulates apoptosis in vivo
    • Yin C, Knudson CM, Korsmeyer SJ, Van Dyke T. Bax suppresses tumorigenesis and stimulates apoptosis in vivo. Nature 1997; 385: 637-640.
    • (1997) Nature , vol.385 , pp. 637-640
    • Yin, C.1    Knudson, C.M.2    Korsmeyer, S.J.3    Van Dyke, T.4
  • 144
    • 0037452759 scopus 로고    scopus 로고
    • PUMA mediates the apoptotic response to p53 in colorectal cancer cells
    • Yu J et al. PUMA mediates the apoptotic response to p53 in colorectal cancer cells. Proc Natl Acad Sci USA 2003; 100: 1931-1936.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1931-1936
    • Yu, J.1
  • 145
    • 0034717014 scopus 로고    scopus 로고
    • Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling
    • Marchenko ND, Zaika A, Moll UM. Death signal-induced localization of p53 protein to mitochondria. A potential role in apoptotic signaling. J Biol Chem 2000; 275: 16202-16212.
    • (2000) J Biol Chem , vol.275 , pp. 16202-16212
    • Marchenko, N.D.1    Zaika, A.2    Moll, U.M.3
  • 146
    • 0037349289 scopus 로고    scopus 로고
    • P53 has a direct apoptogenic role at the mitochondria
    • Mihara M et al. p53 has a direct apoptogenic role at the mitochondria. Mol Cell 2003; 11: 577-590.
    • (2003) Mol Cell , vol.11 , pp. 577-590
    • Mihara, M.1
  • 147
    • 0036287040 scopus 로고    scopus 로고
    • The EGF/ErbB receptor family and apoptosis
    • Danielsen AJ, Maihle NJ. The EGF/ErbB receptor family and apoptosis. Growth Factors 2002; 20: 1-15.
    • (2002) Growth Factors , vol.20 , pp. 1-15
    • Danielsen, A.J.1    Maihle, N.J.2
  • 148
    • 0029824114 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase recruitment by p185erbB-2 and erbB-3 is potently induced by neu differentiation factor/heregulin during mitogenesis and is constitutively elevated in growth factor-independent breast carcinoma cells with c-erbB-2 gene amplification
    • Ram TG, Ethier SP. Phosphatidylinositol 3-kinase recruitment by p185erbB-2 and erbB-3 is potently induced by neu differentiation factor/heregulin during mitogenesis and is constitutively elevated in growth factor-independent breast carcinoma cells with c-erbB-2 gene amplification. Cell Growth Differ 1996; 7: 551-561.
    • (1996) Cell Growth Differ , vol.7 , pp. 551-561
    • Ram, T.G.1    Ethier, S.P.2
  • 149
    • 0034708482 scopus 로고    scopus 로고
    • Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
    • Toker A, Newton AC. Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site. J Biol Chem 2000; 275: 8271-8274.
    • (2000) J Biol Chem , vol.275 , pp. 8271-8274
    • Toker, A.1    Newton, A.C.2
  • 150
    • 0030702123 scopus 로고    scopus 로고
    • Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery
    • Datta SR et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell 1997; 91: 231-241.
    • (1997) Cell , vol.91 , pp. 231-241
    • Datta, S.R.1
  • 151
    • 0033588217 scopus 로고    scopus 로고
    • Phosphoinositide 3-OH kinase (PI3K) and PKB/Akt delay the onset of p53-mediated, transcriptionally dependent apoptosis
    • Sabbatini P, McCormick F. Phosphoinositide 3-OH kinase (PI3K) and PKB/Akt delay the onset of p53-mediated, transcriptionally dependent apoptosis. J Biol Chem 1999; 274: 24263-24269.
    • (1999) J Biol Chem , vol.274 , pp. 24263-24269
    • Sabbatini, P.1    McCormick, F.2
  • 152
    • 1242317030 scopus 로고    scopus 로고
    • Akt phosphorylation and stabilization of X-linked inhibitor of apoptosis protein (XIAP)
    • Dan HC et al. Akt phosphorylation and stabilization of X-linked inhibitor of apoptosis protein (XIAP). J Biol Chem 2004; 279: 5405-5412.
    • (2004) J Biol Chem , vol.279 , pp. 5405-5412
    • Dan, H.C.1
  • 153
    • 0033517840 scopus 로고    scopus 로고
    • Marked induction of the IAP family antiapoptotic proteins survivin and XIAP by VEGF in vascular endothelial cells
    • Tran J et al. Marked induction of the IAP family antiapoptotic proteins survivin and XIAP by VEGF in vascular endothelial cells. Biochem Biophys Res Commun 1999; 264: 781-788.
    • (1999) Biochem Biophys Res Commun , vol.264 , pp. 781-788
    • Tran, J.1
  • 154
    • 0034841661 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase signalling in breast cancer: How big a role might it play?
    • Fry MJ. Phosphoinositide 3-kinase signalling in breast cancer: how big a role might it play? Breast Cancer Res 2001; 3: 304-312.
    • (2001) Breast Cancer Res , vol.3 , pp. 304-312
    • Fry, M.J.1
  • 155
    • 0035008874 scopus 로고    scopus 로고
    • Activation of Akt (protein kinase B) in mammary epithelium provides a critical cell survival signal required for tumor progression
    • Hutchinson J et al. Activation of Akt (protein kinase B) in mammary epithelium provides a critical cell survival signal required for tumor progression. Mol Cell Biol 2001; 21: 2203-2212.
    • (2001) Mol Cell Biol , vol.21 , pp. 2203-2212
    • Hutchinson, J.1
  • 156
    • 0034907425 scopus 로고    scopus 로고
    • Inhibition of PI3-kinase sensitises HL60 human leukaemia cells to both chemotherapeutic drug-and Fas-induced apoptosis by a JNK independent pathway
    • O'Gorman DM, McKenna SL, McGahon AJ, Cotter TG. Inhibition of PI3-kinase sensitises HL60 human leukaemia cells to both chemotherapeutic drug-and Fas-induced apoptosis by a JNK independent pathway. Leuk Res 2001; 25: 801-811.
    • (2001) Leuk Res , vol.25 , pp. 801-811
    • O'Gorman, D.M.1    McKenna, S.L.2    McGahon, A.J.3    Cotter, T.G.4
  • 157
    • 0032558822 scopus 로고    scopus 로고
    • Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC
    • Haas-Kogan D et al. Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC. Curr Biol 1998; 8: 1195-1198.
    • (1998) Curr Biol , vol.8 , pp. 1195-1198
    • Haas-Kogan, D.1
  • 158
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa] B activity
    • Karin M, Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol 2000; 18: 621-663.
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 159
    • 0036719081 scopus 로고    scopus 로고
    • Propapoptotic effects of NF-kappaB in LNCaP prostate cancer cells lead to serine protease activation
    • Kimura K, Gelmann EP. Propapoptotic effects of NF-kappaB in LNCaP prostate cancer cells lead to serine protease activation. Cell Death Differ 2002; 9: 972-980.
    • (2002) Cell Death Differ , vol.9 , pp. 972-980
    • Kimura, K.1    Gelmann, E.P.2
  • 160
    • 0032588794 scopus 로고    scopus 로고
    • NF-kappaB regulates Fas/APO-1/CD95-and TCR-mediated apoptosis of T lymphocytes
    • Dudley E et al. NF-kappaB regulates Fas/APO-1/CD95-and TCR-mediated apoptosis of T lymphocytes. Eur J Immunol 1999; 29: 878-886.
    • (1999) Eur J Immunol , vol.29 , pp. 878-886
    • Dudley, E.1
  • 161
    • 0036546501 scopus 로고    scopus 로고
    • NF-kappaB in cancer: From innocent bystander to major culprit
    • Karin M, Cao Y, Greten FR, Li ZW. NF-kappaB in cancer: from innocent bystander to major culprit. Nat Rev Cancer 2002; 2: 301-310.
    • (2002) Nat Rev Cancer , vol.2 , pp. 301-310
    • Karin, M.1    Cao, Y.2    Greten, F.R.3    Li, Z.W.4
  • 162
    • 1642553460 scopus 로고    scopus 로고
    • To be, or not to be: NF-kappaB is the answer-role of Rel/NF-kappaB in the regulation of apoptosis
    • Kucharczak J, Simmons MJ, Fan Y, Gelinas C. To be, or not to be: NF-kappaB is the answer-role of Rel/NF-kappaB in the regulation of apoptosis. Oncogene 2003; 22: 8961-8982.
    • (2003) Oncogene , vol.22 , pp. 8961-8982
    • Kucharczak, J.1    Simmons, M.J.2    Fan, Y.3    Gelinas, C.4
  • 163
    • 0041853690 scopus 로고    scopus 로고
    • Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
    • Micheau O, Tschopp J. Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes. Cell 2003; 114: 181-190.
    • (2003) Cell , vol.114 , pp. 181-190
    • Micheau, O.1    Tschopp, J.2
  • 164
    • 0033557805 scopus 로고    scopus 로고
    • Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis
    • Grumont RJ, Rourke IJ, Gerondakis S. Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis. Genes Dev 1999; 13: 400-411.
    • (1999) Genes Dev , vol.13 , pp. 400-411
    • Grumont, R.J.1    Rourke, I.J.2    Gerondakis, S.3
  • 165
    • 0038103154 scopus 로고    scopus 로고
    • NF-kappa B2/p100 induces Bcl-2 expression
    • Viatour P et al. NF-kappa B2/p100 induces Bcl-2 expression. Leukemia 2003; 17: 1349-1356.
    • (2003) Leukemia , vol.17 , pp. 1349-1356
    • Viatour, P.1
  • 166
    • 2342426324 scopus 로고    scopus 로고
    • Expression of the IAPs in multidrug resistant tumor cells
    • Notarbartolo M et al. Expression of the IAPs in multidrug resistant tumor cells. Oncol Rep 2004; 11: 133-136.
    • (2004) Oncol Rep , vol.11 , pp. 133-136
    • Notarbartolo, M.1
  • 167
    • 0346435107 scopus 로고    scopus 로고
    • Induction of cIAP-2 in human colon cancer cells through PKC delta/NF-kappa B
    • Wang Q, Wang X, Evers BM. Induction of cIAP-2 in human colon cancer cells through PKC delta/NF-kappa B. J Biol Chem 2003; 278: 51091-51099.
    • (2003) J Biol Chem , vol.278 , pp. 51091-51099
    • Wang, Q.1    Wang, X.2    Evers, B.M.3
  • 168
    • 0034616122 scopus 로고    scopus 로고
    • Regulation of FasL by NF-kappaB and AP-1 in Fas-dependent thymineless death of human colon carcinoma cells
    • Harwood FG et al. Regulation of FasL by NF-kappaB and AP-1 in Fas-dependent thymineless death of human colon carcinoma cells. J Biol Chem 2000; 275: 10023-10029.
    • (2000) J Biol Chem , vol.275 , pp. 10023-10029
    • Harwood, F.G.1
  • 169
    • 0037376895 scopus 로고    scopus 로고
    • NF-kappaB in cancer: A marked target
    • Lin A, Karin M. NF-kappaB in cancer: a marked target. Semin Cancer Biol 2003; 13: 107-114.
    • (2003) Semin Cancer Biol , vol.13 , pp. 107-114
    • Lin, A.1    Karin, M.2
  • 170
    • 1542644825 scopus 로고    scopus 로고
    • NF-kappaB in mammary gland development and breast cancer
    • Cao Y, Karin M. NF-kappaB in mammary gland development and breast cancer. J Mammary Gland Biol Neoplasia 2003; 8: 215-223.
    • (2003) J Mammary Gland Biol Neoplasia , vol.8 , pp. 215-223
    • Cao, Y.1    Karin, M.2
  • 171
    • 0036651553 scopus 로고    scopus 로고
    • Reduced response of prostate cancer cells to TRAIL is modulated by NFkappaB-mediated inhibition of caspases and Bid activation
    • Eid MA, Lewis RW, Abdel-Mageed AB, Kumar MV. Reduced response of prostate cancer cells to TRAIL is modulated by NFkappaB-mediated inhibition of caspases and Bid activation. Int J Oncol 2002; 21: 111-117.
    • (2002) Int J Oncol , vol.21 , pp. 111-117
    • Eid, M.A.1    Lewis, R.W.2    Abdel-Mageed, A.B.3    Kumar, M.V.4
  • 172
    • 1342284288 scopus 로고    scopus 로고
    • NF-kappaB inhibition restores sensitivity to Fas-mediated apoptosis in lymphoma cell lines
    • Meli M et al. NF-kappaB inhibition restores sensitivity to Fas-mediated apoptosis in lymphoma cell lines. Ann N Y Acad Sci 2003; 1010: 232-236.
    • (2003) Ann N y Acad Sci , vol.1010 , pp. 232-236
    • Meli, M.1
  • 173
    • 0036122242 scopus 로고    scopus 로고
    • Involvement of hypoxia-inducible factor 1 in human cancer
    • Semenza GL. Involvement of hypoxia-inducible factor 1 in human cancer. Intern Med 2002; 41: 79-83.
    • (2002) Intern Med , vol.41 , pp. 79-83
    • Semenza, G.L.1
  • 174
    • 0842333201 scopus 로고    scopus 로고
    • Prognostic significance of HIF-1 alpha overexpression in human pancreatic cancer
    • Shibaji T et al. Prognostic significance of HIF-1 alpha overexpression in human pancreatic cancer. Anticancer Res 2003; 23: 4721-4727.
    • (2003) Anticancer Res , vol.23 , pp. 4721-4727
    • Shibaji, T.1
  • 175
    • 0035418621 scopus 로고    scopus 로고
    • Constitutive expression of hypoxia-inducible factor-1alpha renders pancreatic cancer cells resistant to apoptosis induced by hypoxia and nutrient deprivation
    • Akakura N et al. Constitutive expression of hypoxia-inducible factor-1alpha renders pancreatic cancer cells resistant to apoptosis induced by hypoxia and nutrient deprivation. Cancer Res 2001; 61: 6548-6554.
    • (2001) Cancer Res , vol.61 , pp. 6548-6554
    • Akakura, N.1
  • 176
    • 1542344522 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1 and oncogenic signalling
    • Bardos JI, Ashcroft M. Hypoxia-inducible factor-1 and oncogenic signalling. Bioessays 2004; 26: 262-269.
    • (2004) Bioessays , vol.26 , pp. 262-269
    • Bardos, J.I.1    Ashcroft, M.2
  • 177
    • 1542408478 scopus 로고    scopus 로고
    • Tumour hypoxia: Impact on biology, prognosis and treatment of solid malignant tumours
    • Weinmann M, Belka C, Plasswilm L. Tumour hypoxia: impact on biology, prognosis and treatment of solid malignant tumours. Onkologie 2004; 27: 83-90.
    • (2004) Onkologie , vol.27 , pp. 83-90
    • Weinmann, M.1    Belka, C.2    Plasswilm, L.3
  • 179
    • 2342588053 scopus 로고    scopus 로고
    • Molecular ordering of hypoxia-induced apoptosis: Critical involvement of the mitochondrial death pathway in a FADD/caspase-8 independent manner
    • Weinmann M et al. Molecular ordering of hypoxia-induced apoptosis: critical involvement of the mitochondrial death pathway in a FADD/caspase-8 independent manner. Oncogene 2004; 23: 3757-3769.
    • (2004) Oncogene , vol.23 , pp. 3757-3769
    • Weinmann, M.1
  • 180
    • 1842861767 scopus 로고    scopus 로고
    • Hypoxia and CoCl2 protect HepG2 cells against serum deprivation-and t-BHP-induced apoptosis: A possible anti-apoptotic role for HIF-1
    • Piret JP et al. Hypoxia and CoCl2 protect HepG2 cells against serum deprivation-and t-BHP-induced apoptosis: a possible anti-apoptotic role for HIF-1. Exp Cell Res 2004; 295: 340-349.
    • (2004) Exp Cell Res , vol.295 , pp. 340-349
    • Piret, J.P.1
  • 181
    • 0042845994 scopus 로고    scopus 로고
    • Apoptosis-resistance of hypoxic cells: Multiple factors involved and a role for IAP-2
    • Dong Z, Wang JZ, Yu F, Venkatachalam MA. Apoptosis-resistance of hypoxic cells: multiple factors involved and a role for IAP-2. Am J Pathol 2003; 163: 663-671.
    • (2003) Am J Pathol , vol.163 , pp. 663-671
    • Dong, Z.1    Wang, J.Z.2    Yu, F.3    Venkatachalam, M.A.4
  • 182
    • 1542305379 scopus 로고    scopus 로고
    • Hypoxia selection of death-resistant cells. A role for Bcl-X(L)
    • Dong Z, Wang J. Hypoxia selection of death-resistant cells. A role for Bcl-X(L). J Biol Chem 2004; 279: 9215-9221.
    • (2004) J Biol Chem , vol.279 , pp. 9215-9221
    • Dong, Z.1    Wang, J.2
  • 183
    • 1842583652 scopus 로고    scopus 로고
    • Hypoxia increases resistance of human pancreatic cancer cells to apoptosis induced by gemcitabine
    • Yokoi K, Fidler IJ. Hypoxia increases resistance of human pancreatic cancer cells to apoptosis induced by gemcitabine. Clin Cancer Res 2004; 10: 2299-2306.
    • (2004) Clin Cancer Res , vol.10 , pp. 2299-2306
    • Yokoi, K.1    Fidler, I.J.2
  • 184
    • 4243182684 scopus 로고    scopus 로고
    • Tumor-specific gene expression using the survivin promoter is further increased by hypoxia
    • Yang L et al. Tumor-specific gene expression using the survivin promoter is further increased by hypoxia. Gene Ther 2004; 11: 1215-1223.
    • (2004) Gene Ther , vol.11 , pp. 1215-1223
    • Yang, L.1
  • 185
    • 0035884701 scopus 로고    scopus 로고
    • HIF-1-dependent regulation of hypoxic induction of the cell death factors BNIP3 and NIX in human tumors
    • Sowter HM et al. HIF-1-dependent regulation of hypoxic induction of the cell death factors BNIP3 and NIX in human tumors. Cancer Res 2001; 61: 6669-6673.
    • (2001) Cancer Res , vol.61 , pp. 6669-6673
    • Sowter, H.M.1
  • 186
    • 3442888541 scopus 로고    scopus 로고
    • Silencing of the hypoxia-inducible cell death protein BNIP3 in pancreatic cancer
    • Okami J, Simeone DM, Logsdon CD. Silencing of the hypoxia-inducible cell death protein BNIP3 in pancreatic cancer. Cancer Res 2004; 64: 5338-5346.
    • (2004) Cancer Res , vol.64 , pp. 5338-5346
    • Okami, J.1    Simeone, D.M.2    Logsdon, C.D.3
  • 187
    • 0032568150 scopus 로고    scopus 로고
    • Stabilization of wild-type p53 by hypoxia-inducible factor 1alpha
    • An WG et al. Stabilization of wild-type p53 by hypoxia-inducible factor 1alpha. Nature 1998; 392: 405-408.
    • (1998) Nature , vol.392 , pp. 405-408
    • An, W.G.1
  • 188
    • 0034988045 scopus 로고    scopus 로고
    • Induction of tumour cell apoptosis by matrix metalloproteinase inhibitors: New tricks from a (not so) old drug
    • Mitsiades N, Poulaki V, Mitsiades CS, Anderson KC. Induction of tumour cell apoptosis by matrix metalloproteinase inhibitors: new tricks from a (not so) old drug. Expert Opin Investig Drugs 2001; 10: 1075-1084.
    • (2001) Expert Opin Investig Drugs , vol.10 , pp. 1075-1084
    • Mitsiades, N.1    Poulaki, V.2    Mitsiades, C.S.3    Anderson, K.C.4
  • 189
    • 0033032317 scopus 로고    scopus 로고
    • Extracellular matrix proteins protect small cell lung cancer cells against apoptosis: A mechanism for small cell lung cancer growth and drug resistance in vivo
    • Sethi T et al. Extracellular matrix proteins protect small cell lung cancer cells against apoptosis: a mechanism for small cell lung cancer growth and drug resistance in vivo. Nat Med 1999; 5: 662-668.
    • (1999) Nat Med , vol.5 , pp. 662-668
    • Sethi, T.1
  • 191
    • 0347383715 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their tissue inhibitors direct cell fate during cancer development
    • Hojilla CV, Mohammed FF, Khokha R. Matrix metalloproteinases and their tissue inhibitors direct cell fate during cancer development. Br J Cancer 2003; 89: 1817-1821.
    • (2003) Br J Cancer , vol.89 , pp. 1817-1821
    • Hojilla, C.V.1    Mohammed, F.F.2    Khokha, R.3
  • 192
    • 0034467122 scopus 로고    scopus 로고
    • Metalloproteinases: Role in breast carcinogenesis, invasion and metastasis
    • Duffy MJ et al. Metalloproteinases: role in breast carcinogenesis, invasion and metastasis. Breast Cancer Res 2000; 2: 252-257.
    • (2000) Breast Cancer Res , vol.2 , pp. 252-257
    • Duffy, M.J.1
  • 193
    • 2442684321 scopus 로고    scopus 로고
    • Cleavage of CD95 by matrix metalloproteinase-7 induces apoptosis resistance in tumour cells
    • Strand S et al. Cleavage of CD95 by matrix metalloproteinase-7 induces apoptosis resistance in tumour cells. Oncogene 2004; 23: 3732-3736.
    • (2004) Oncogene , vol.23 , pp. 3732-3736
    • Strand, S.1
  • 194
    • 0035863471 scopus 로고    scopus 로고
    • Matrix metalloproteinase-7-mediated cleavage of Fas ligand protects tumor cells from chemotherapeutic drug cytotoxicity
    • Mitsiades N et al. Matrix metalloproteinase-7-mediated cleavage of Fas ligand protects tumor cells from chemotherapeutic drug cytotoxicity. Cancer Res 2001; 61: 577-581.
    • (2001) Cancer Res , vol.61 , pp. 577-581
    • Mitsiades, N.1
  • 195
    • 0036791136 scopus 로고    scopus 로고
    • Matrilysin (matrix metalloproteinase-7) selects for apoptosis-resistant mammary cells in vivo
    • Vargo-Gogola T, Fingleton B, Crawford HC, Matrisian LM. Matrilysin (matrix metalloproteinase-7) selects for apoptosis-resistant mammary cells in vivo. Cancer Res 2002; 62: 5559-5563.
    • (2002) Cancer Res , vol.62 , pp. 5559-5563
    • Vargo-Gogola, T.1    Fingleton, B.2    Crawford, H.C.3    Matrisian, L.M.4
  • 196
    • 0035899331 scopus 로고    scopus 로고
    • Integrin signaling inhibits paclitaxel-induced apoptosis in breast cancer cells
    • Aoudjit F, Vuori K. Integrin signaling inhibits paclitaxel-induced apoptosis in breast cancer cells. Oncogene 2001; 20: 4995-5004.
    • (2001) Oncogene , vol.20 , pp. 4995-5004
    • Aoudjit, F.1    Vuori, K.2
  • 197
    • 1542328956 scopus 로고    scopus 로고
    • A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors
    • Jan Y et al. A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors. Cell 2004; 116: 751-762.
    • (2004) Cell , vol.116 , pp. 751-762
    • Jan, Y.1
  • 198
    • 0033166087 scopus 로고    scopus 로고
    • Treatment of experimental glioma by administration of adenoviral vectors expressing Fas ligand
    • Ambar BB et al. Treatment of experimental glioma by administration of adenoviral vectors expressing Fas ligand. Hum Gene Ther 1999; 10: 1641-1648.
    • (1999) Hum Gene Ther , vol.10 , pp. 1641-1648
    • Ambar, B.B.1
  • 199
    • 0036288826 scopus 로고    scopus 로고
    • Caspase-8 gene therapy using the human telomerase reverse transcriptase promoter for malignant glioma cells
    • Komata T et al. Caspase-8 gene therapy using the human telomerase reverse transcriptase promoter for malignant glioma cells. Hum Gene Ther 2002; 13: 1015-1025.
    • (2002) Hum Gene Ther , vol.13 , pp. 1015-1025
    • Komata, T.1
  • 200
    • 0034674306 scopus 로고    scopus 로고
    • Transduction of Apaf-1 or caspase-9 induces apoptosis in A-172 cells that are resistant to p53-mediated apoptosis
    • Shinoura N et al. Transduction of Apaf-1 or caspase-9 induces apoptosis in A-172 cells that are resistant to p53-mediated apoptosis. Biochem Biophys Res Commun 2000; 272: 667-673.
    • (2000) Biochem Biophys Res Commun , vol.272 , pp. 667-673
    • Shinoura, N.1
  • 201
    • 0034194022 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of caspase-3 with Fas ligand induces drastic apoptosis in U-373MG glioma cells
    • Shinoura N et al. Adenovirus-mediated transfer of caspase-3 with Fas ligand induces drastic apoptosis in U-373MG glioma cells. Exp Cell Res 2000; 256: 423-433.
    • (2000) Exp Cell Res , vol.256 , pp. 423-433
    • Shinoura, N.1
  • 202
    • 0035136282 scopus 로고    scopus 로고
    • Adenovirus-mediated Bax overexpression for the induction of therapeutic apoptosis in prostate cancer
    • Li X et al. Adenovirus-mediated Bax overexpression for the induction of therapeutic apoptosis in prostate cancer. Cancer Res 2001; 61: 186-191.
    • (2001) Cancer Res , vol.61 , pp. 186-191
    • Li, X.1
  • 203
    • 0035144922 scopus 로고    scopus 로고
    • Adenovirus-mediated Bak gene transfer induces apoptosis in mesothelioma cell lines
    • Pataer A et al. Adenovirus-mediated Bak gene transfer induces apoptosis in mesothelioma cell lines. J Thorac Cardiovasc Surg 2001; 121: 61-67.
    • (2001) J Thorac Cardiovasc Surg , vol.121 , pp. 61-67
    • Pataer, A.1
  • 204
    • 0035147560 scopus 로고    scopus 로고
    • Somatic mutations in the death domain of the Fas (Apo-1/CD95) gene in gastric cancer
    • Park WS et al. Somatic mutations in the death domain of the Fas (Apo-1/CD95) gene in gastric cancer. J Pathol 2001; 193: 162-168.
    • (2001) J Pathol , vol.193 , pp. 162-168
    • Park, W.S.1
  • 205
    • 9144234685 scopus 로고    scopus 로고
    • Small-molecule antagonists of apoptosis suppressor XIAP exhibit broad antitumor activity
    • Schimmer AD et al. Small-molecule antagonists of apoptosis suppressor XIAP exhibit broad antitumor activity. Cancer Cell 2004; 5: 25-35.
    • (2004) Cancer Cell , vol.5 , pp. 25-35
    • Schimmer, A.D.1
  • 207
    • 0029915677 scopus 로고    scopus 로고
    • Extensive apoptosis in ductal carcinoma in situ of the breast
    • Bodis S et al. Extensive apoptosis in ductal carcinoma in situ of the breast. Cancer 1996; 77: 1831-1835.
    • (1996) Cancer , vol.77 , pp. 1831-1835
    • Bodis, S.1
  • 208
    • 0030065185 scopus 로고    scopus 로고
    • Quantitation of multistage carcinogenesis in rat liver
    • Pitot HC et al. Quantitation of multistage carcinogenesis in rat liver. Toxicol Pathol 1996; 24: 119-128.
    • (1996) Toxicol Pathol , vol.24 , pp. 119-128
    • Pitot, H.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.