메뉴 건너뛰기




Volumn 66, Issue 3, 2006, Pages 1730-1739

Resistance of cancers to immunologic cytotoxicity and adoptive immunotherapy via X-linked inhibitor of apoptosis protein expression and coexisting defects in mitochondrial death signaling

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; CASPASE 7; GAMMA INTERFERON; GRANZYME B; PROTEIN BAX; PROTEIN BCL XL; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND; X LINKED INHIBITOR OF APOPTOSIS;

EID: 32944467254     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-3377     Document Type: Article
Times cited : (41)

References (51)
  • 1
    • 0037404069 scopus 로고    scopus 로고
    • Immunotherapy of hematologic malignancies and metastatic solid tumors in experimental animals and man
    • Slavin S, Morecki S, Weiss L, Or R. Immunotherapy of hematologic malignancies and metastatic solid tumors in experimental animals and man. Crit Rev Oncol Hematol 2003;46:139-63.
    • (2003) Crit Rev Oncol Hematol , vol.46 , pp. 139-163
    • Slavin, S.1    Morecki, S.2    Weiss, L.3    Or, R.4
  • 2
    • 4644324025 scopus 로고    scopus 로고
    • Cancer immunotherapy: Moving beyond current vaccines
    • Rosenberg SA, Yang JC, Restifo NP. Cancer immunotherapy: moving beyond current vaccines. Nat Med 2004;10:909-15.
    • (2004) Nat Med , vol.10 , pp. 909-915
    • Rosenberg, S.A.1    Yang, J.C.2    Restifo, N.P.3
  • 3
    • 0033991158 scopus 로고    scopus 로고
    • Escape of human solid tumors from T-cell recognition: Molecular mechanisms and functional significance
    • Marincola FM, Jaffee EM, Hicklin DJ, Ferrone S. Escape of human solid tumors from T-cell recognition: molecular mechanisms and functional significance. Adv Immunol 2000;74:181-273.
    • (2000) Adv Immunol , vol.74 , pp. 181-273
    • Marincola, F.M.1    Jaffee, E.M.2    Hicklin, D.J.3    Ferrone, S.4
  • 4
    • 0036779576 scopus 로고    scopus 로고
    • Functional significance of the perforin/granzyme cell death pathway
    • Trapani JA, Smyth MJ. Functional significance of the perforin/granzyme cell death pathway. Nat Rev Immunol 2002;2:735-47.
    • (2002) Nat Rev Immunol , vol.2 , pp. 735-747
    • Trapani, J.A.1    Smyth, M.J.2
  • 5
    • 0028219791 scopus 로고
    • Cytotoxicity mediated by T cells and natural killer cells is greatly impaired in perforin-deficient mice
    • Kagi D, Ledermann B, Burki K, et al. Cytotoxicity mediated by T cells and natural killer cells is greatly impaired in perforin-deficient mice. Nature 1994;369:31-7.
    • (1994) Nature , vol.369 , pp. 31-37
    • Kagi, D.1    Ledermann, B.2    Burki, K.3
  • 6
    • 0028110928 scopus 로고
    • Fas and perform pathways as major mechanisms of T cell-mediated cytotoxicity
    • Kagi D, Vignaux F, Ledermann B, et al. Fas and perform pathways as major mechanisms of T cell-mediated cytotoxicity. Science 1994;265:528-30.
    • (1994) Science , vol.265 , pp. 528-530
    • Kagi, D.1    Vignaux, F.2    Ledermann, B.3
  • 7
    • 0036598992 scopus 로고    scopus 로고
    • Targeting death and decoy receptors of the tumour-necrosis factor superfamily
    • Ashkenazi A. Targeting death and decoy receptors of the tumour-necrosis factor superfamily. Nat Rev Cancer 2002;2:420-30.
    • (2002) Nat Rev Cancer , vol.2 , pp. 420-430
    • Ashkenazi, A.1
  • 8
    • 0037240850 scopus 로고    scopus 로고
    • Nature's TRAIL-on a path to cancer immunotherapy
    • Smyth MJ, Takeda K, Hayakawa Y, et al. Nature's TRAIL-on a path to cancer immunotherapy. Immunity 2003;18:1-6.
    • (2003) Immunity , vol.18 , pp. 1-6
    • Smyth, M.J.1    Takeda, K.2    Hayakawa, Y.3
  • 9
    • 0035911242 scopus 로고    scopus 로고
    • Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) contributes to interferon γ-dependent natural killer cell protection from tumor metastasis
    • Smyth MJ, Cretney E, Takeda K, et al. Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) contributes to interferon γ-dependent natural killer cell protection from tumor metastasis. J Exp Med 2001;193:661-70.
    • (2001) J Exp Med , vol.193 , pp. 661-670
    • Smyth, M.J.1    Cretney, E.2    Takeda, K.3
  • 10
    • 0033519303 scopus 로고    scopus 로고
    • Type I interferons (IFNs) regulate tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) expression on human T cells: A novel mechanism for the antitumor effects of type I IFNs
    • Kayagaki N, Yamaguchi N, Nakayama M, et al. Type I interferons (IFNs) regulate tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) expression on human T cells: a novel mechanism for the antitumor effects of type I IFNs. J Exp Med 1999;189:1451-60.
    • (1999) J Exp Med , vol.189 , pp. 1451-1460
    • Kayagaki, N.1    Yamaguchi, N.2    Nakayama, M.3
  • 11
    • 0035137696 scopus 로고    scopus 로고
    • Involvement of tumor necrosis factor-related apoptosis-inducing ligand in surveillance of tumor metastasis by liver natural killer cells
    • Takeda K, Hayakawa Y, Smyth MJ, et al. Involvement of tumor necrosis factor-related apoptosis-inducing ligand in surveillance of tumor metastasis by liver natural killer cells. Nat Med 2001;7:94-100.
    • (2001) Nat Med , vol.7 , pp. 94-100
    • Takeda, K.1    Hayakawa, Y.2    Smyth, M.J.3
  • 12
    • 0036467427 scopus 로고    scopus 로고
    • Increased susceptibility to tumor initiation and metastasis in TNF-related apoptosis-inducing ligand-deficient mice
    • Cretney E, Takeda K, Yagita H, et al. Increased susceptibility to tumor initiation and metastasis in TNF-related apoptosis-inducing ligand-deficient mice. J Immunol 2002;168:1356-61.
    • (2002) J Immunol , vol.168 , pp. 1356-1361
    • Cretney, E.1    Takeda, K.2    Yagita, H.3
  • 13
    • 0036914180 scopus 로고    scopus 로고
    • T cells require TRAIL for optimal graft-versus-tumor activity
    • Schmaltz C, Alpdogan O, Kappel BJ, et al. T cells require TRAIL for optimal graft-versus-tumor activity. Nat Med 2002;8:1433-37.
    • (2002) Nat Med , vol.8 , pp. 1433-1437
    • Schmaltz, C.1    Alpdogan, O.2    Kappel, B.J.3
  • 14
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
    • Darmon AJ, Nicholson DW, Bleackley RC. Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B. Nature 1995;377:446-8.
    • (1995) Nature , vol.377 , pp. 446-448
    • Darmon, A.J.1    Nicholson, D.W.2    Bleackley, R.C.3
  • 15
    • 0032545286 scopus 로고    scopus 로고
    • Granzyme B mimics apical caspases. Description of a unified pathway for trans-activation of executioner caspase-3 and -7
    • Yang X, Stennicke HR, Wang B, et al. Granzyme B mimics apical caspases. Description of a unified pathway for trans-activation of executioner caspase-3 and -7. J Biol Chem 1998;273:34278-83.
    • (1998) J Biol Chem , vol.273 , pp. 34278-34283
    • Yang, X.1    Stennicke, H.R.2    Wang, B.3
  • 16
    • 0034694091 scopus 로고    scopus 로고
    • Initiation of apoptosis by granzyme B requires direct cleavage of bid, but not direct granzyme B-mediated caspase activation
    • Sutton VR, Davis JE, Cancilla M, et al. Initiation of apoptosis by granzyme B requires direct cleavage of bid, but not direct granzyme B-mediated caspase activation. J Exp Med 2000;192:1403-14.
    • (2000) J Exp Med , vol.192 , pp. 1403-1414
    • Sutton, V.R.1    Davis, J.E.2    Cancilla, M.3
  • 17
    • 0034694083 scopus 로고    scopus 로고
    • Granzyme B-mediated cytochrome c release is regulated by the Bcl-2 family members bid and Bax
    • Heibein JA, Goping IS, Barry M, et al. Granzyme B-mediated cytochrome c release is regulated by the Bcl-2 family members bid and Bax. J Exp Med 2000;192:1391-402.
    • (2000) J Exp Med , vol.192 , pp. 1391-1402
    • Heibein, J.A.1    Goping, I.S.2    Barry, M.3
  • 18
    • 0035158920 scopus 로고    scopus 로고
    • Resistance to granzyme B-mediated cytochrome c release in Bak-deficient cells
    • Wang GQ, Wieckowski E, Goldstein LA, et al. Resistance to granzyme B-mediated cytochrome c release in Bak-deficient cells. J Exp Med 2001;194:1325-37.
    • (2001) J Exp Med , vol.194 , pp. 1325-1337
    • Wang, G.Q.1    Wieckowski, E.2    Goldstein, L.A.3
  • 19
    • 0033521626 scopus 로고    scopus 로고
    • Mitochondria-dependent and -independent regulation of Granzyme B-induced apoptosis
    • MacDonald G, Shi L, Vande VC, Lieberman J, Greenberg AH. Mitochondria-dependent and -independent regulation of Granzyme B-induced apoptosis. J Exp Med 1999;189:131-44.
    • (1999) J Exp Med , vol.189 , pp. 131-144
    • MacDonald, G.1    Shi, L.2    Vande, V.C.3    Lieberman, J.4    Greenberg, A.H.5
  • 20
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997;91:479-89.
    • (1997) Cell , vol.91 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3
  • 21
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 1997;275:1132-36.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 22
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K, et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 1997;275:1129-32.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 23
    • 0034616945 scopus 로고    scopus 로고
    • Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
    • Du C, Fang M, Li Y, Li L, Wang X. 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    Fang, M.2    Li, Y.3    Li, L.4    Wang, X.5
  • 24
    • 0034616942 scopus 로고    scopus 로고
    • Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
    • Verhagen AM, Ekert PG, Pakusch M, et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 2000;102:43-53.
    • (2000) Cell , vol.102 , pp. 43-53
    • Verhagen, A.M.1    Ekert, P.G.2    Pakusch, M.3
  • 25
    • 0035282570 scopus 로고    scopus 로고
    • A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis
    • Srinivasula SM, Hegde R, Saleh A, et al. A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis. Nature 2001;410:112-6.
    • (2001) Nature , vol.410 , pp. 112-116
    • Srinivasula, S.M.1    Hegde, R.2    Saleh, A.3
  • 26
    • 0035831019 scopus 로고    scopus 로고
    • Structural basis for the inhibition of caspase-3 by XIAP
    • Riedl SJ, Renatus M, Schwarzenbacher R, et al. Structural basis for the inhibition of caspase-3 by XIAP. Cell 2001;104:791-800.
    • (2001) Cell , vol.104 , pp. 791-800
    • Riedl, S.J.1    Renatus, M.2    Schwarzenbacher, R.3
  • 27
    • 0035831021 scopus 로고    scopus 로고
    • Structural basis of caspase-7 inhibition by XIAP
    • Chai J, Shiozaki E, Srinavasula SM, et al. Structural basis of caspase-7 inhibition by XIAP. Cell 2001;104:769-80.
    • (2001) Cell , vol.104 , pp. 769-780
    • Chai, J.1    Shiozaki, E.2    Srinavasula, S.M.3
  • 28
    • 0037341354 scopus 로고    scopus 로고
    • Caspase activation by granzyme B is indirect, and caspase autoprocessing requires the release of proapoptotic mitochondrial factors
    • Sutton VR, Wowk ME, Cancilla M, Trapani JA. Caspase activation by granzyme B is indirect, and caspase autoprocessing requires the release of proapoptotic mitochondrial factors. Immunity 2003;18:319-29.
    • (2003) Immunity , vol.18 , pp. 319-329
    • Sutton, V.R.1    Wowk, M.E.2    Cancilla, M.3    Trapani, J.A.4
  • 29
    • 0037343068 scopus 로고    scopus 로고
    • Granzyme B-induced apoptosis requires both direct caspase activation and relief of caspase inhibition
    • Goping IS, Barry M, Liston P, et al. Granzyme B-induced apoptosis requires both direct caspase activation and relief of caspase inhibition. Immunity 2003;18:355-65.
    • (2003) Immunity , vol.18 , pp. 355-365
    • Goping, I.S.1    Barry, M.2    Liston, P.3
  • 30
    • 0030810926 scopus 로고    scopus 로고
    • X-linked IAP is a direct inhibitor of cell-death proteases
    • Deveraux QL, Takahashi R, Salvesen GS, Reed JC. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 1997;388:300-4.
    • (1997) Nature , vol.388 , pp. 300-304
    • Deveraux, Q.L.1    Takahashi, R.2    Salvesen, G.S.3    Reed, J.C.4
  • 31
    • 0036141029 scopus 로고    scopus 로고
    • TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO
    • Deng Y, Lin Y, Wu X. TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO. Genes Dev 2002;16:33-45.
    • (2002) Genes Dev , vol.16 , pp. 33-45
    • Deng, Y.1    Lin, Y.2    Wu, X.3
  • 32
    • 2542448011 scopus 로고    scopus 로고
    • Granzyme M mediates a novel form of perforin-dependent cell death
    • Kelly JM, Waterhouse NJ, Cretney E, et al. Granzyme M mediates a novel form of perforin-dependent cell death. J Biol Chem 2004;279:22236-42.
    • (2004) J Biol Chem , vol.279 , pp. 22236-22242
    • Kelly, J.M.1    Waterhouse, N.J.2    Cretney, E.3
  • 34
    • 0034602188 scopus 로고    scopus 로고
    • Role of BAX in the apoptotic response to anticancer agents
    • Zhang L, Yu J, Park BH, Kinzler KW, Vogelstein B. Role of BAX in the apoptotic response to anticancer agents. Science 2000;290:989-92.
    • (2000) Science , vol.290 , pp. 989-992
    • Zhang, L.1    Yu, J.2    Park, B.H.3    Kinzler, K.W.4    Vogelstein, B.5
  • 35
    • 10044265235 scopus 로고    scopus 로고
    • SMAC/Diablo-dependent apoptosis induced by nonsteroidal antiinflammatory drugs (NSAIDs) in colon cancer cells
    • Kohli M, Yu J, Seaman C, et al. SMAC/Diablo-dependent apoptosis induced by nonsteroidal antiinflammatory drugs (NSAIDs) in colon cancer cells. Proc Natl Acad Sci U S A 2004;101:16897-902.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16897-16902
    • Kohli, M.1    Yu, J.2    Seaman, C.3
  • 36
    • 2342615480 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein (XIAP) is a nonredundant modulator of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-mediated apoptosis in human cancer cells
    • Cummins JM, Kohli M, Rago C, et al. X-linked inhibitor of apoptosis protein (XIAP) is a nonredundant modulator of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-mediated apoptosis in human cancer cells. Cancer Res 2004;64:3006-8.
    • (2004) Cancer Res , vol.64 , pp. 3006-3008
    • Cummins, J.M.1    Kohli, M.2    Rago, C.3
  • 37
    • 0030800070 scopus 로고    scopus 로고
    • Inhibition of death receptor signals by cellular FLIP
    • Irmler M, Thome M, Hahne M, et al. Inhibition of death receptor signals by cellular FLIP. Nature 1997;388:190-5.
    • (1997) Nature , vol.388 , pp. 190-195
    • Irmler, M.1    Thome, M.2    Hahne, M.3
  • 38
    • 0037085935 scopus 로고    scopus 로고
    • Requirement of BAX for TRAIL/Apo2L-induced apoptosis of colorectal cancers: Synergism with Sulindac-mediated inhibition of Bcl-x(L)
    • Ravi R, Bedi A. Requirement of BAX for TRAIL/Apo2L-induced apoptosis of colorectal cancers: synergism with Sulindac-mediated inhibition of Bcl-x(L). Cancer Res 2002;62:1583-7.
    • (2002) Cancer Res , vol.62 , pp. 1583-1587
    • Ravi, R.1    Bedi, A.2
  • 39
    • 0347895102 scopus 로고    scopus 로고
    • Synthetic Smac/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAP1 in situ
    • Arnt CR, Chiorean MV, Heldebrant MP, Gores GJ, Kaufmann SH. Synthetic Smac/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAP1 in situ. J Biol Chem 2002;277:44236-43.
    • (2002) J Biol Chem , vol.277 , pp. 44236-44243
    • Arnt, C.R.1    Chiorean, M.V.2    Heldebrant, M.P.3    Gores, G.J.4    Kaufmann, S.H.5
  • 40
    • 10844223742 scopus 로고    scopus 로고
    • Elimination of hepatic metastases of colon cancer cells via p53-independent cross-talk between irinotecan and Apo2 ligand/TRAIL
    • Ravi R, Jain AJ, Schulick RD, et al. Elimination of hepatic metastases of colon cancer cells via p53-independent cross-talk between irinotecan and Apo2 ligand/TRAIL. Cancer Res 2004;64:9105-14.
    • (2004) Cancer Res , vol.64 , pp. 9105-9114
    • Ravi, R.1    Jain, A.J.2    Schulick, R.D.3
  • 41
    • 3543060047 scopus 로고    scopus 로고
    • Mesothelin-specific CD8(+) T cell responses provide evidence of in vivo cross-priming by antigen-presenting cells in vaccinated pancreatic cancer patients
    • Thomas AM, Santarsiero LM, Lutz ER, et al. Mesothelin-specific CD8(+) T cell responses provide evidence of in vivo cross-priming by antigen-presenting cells in vaccinated pancreatic cancer patients. J Exp Med 2004;200:297-306.
    • (2004) J Exp Med , vol.200 , pp. 297-306
    • Thomas, A.M.1    Santarsiero, L.M.2    Lutz, E.R.3
  • 42
    • 0034786019 scopus 로고    scopus 로고
    • BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis
    • Cheng EH, Wei MC, Weiler S, et al. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell 2001;8:705-11.
    • (2001) Mol Cell , vol.8 , pp. 705-711
    • Cheng, E.H.1    Wei, M.C.2    Weiler, S.3
  • 43
    • 0032490670 scopus 로고    scopus 로고
    • Nuclear factor (NF)-KB-regulated X-chromosome-linked iap gene expression protects endothelial cells from tumor necrosis factor alpha-induced apoptosis
    • Stehlik C, de Martin R, Kumabashiri I, et al. Nuclear factor (NF)-KB-regulated X-chromosome-linked iap gene expression protects endothelial cells from tumor necrosis factor alpha-induced apoptosis. J Exp Med 1998;188:211-6.
    • (1998) J Exp Med , vol.188 , pp. 211-216
    • Stehlik, C.1    De Martin, R.2    Kumabashiri, I.3
  • 44
    • 0031018674 scopus 로고    scopus 로고
    • Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype
    • Rampino N, Yamamoto H, Ionov Y, et al. Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype. Science 1997;275:967-9.
    • (1997) Science , vol.275 , pp. 967-969
    • Rampino, N.1    Yamamoto, H.2    Ionov, Y.3
  • 45
    • 0032422475 scopus 로고    scopus 로고
    • Apoptosis inhibiting factor Bcl-xL might be the crucial member of the Bcl-2 gene family in colorectal cancer
    • Maurer CA, Friess H, Buhler SS, et al. Apoptosis inhibiting factor Bcl-xL might be the crucial member of the Bcl-2 gene family in colorectal cancer. Dig Dis Sci 1998;43:2641-8.
    • (1998) Dig Dis Sci , vol.43 , pp. 2641-2648
    • Maurer, C.A.1    Friess, H.2    Buhler, S.S.3
  • 46
    • 0036548986 scopus 로고    scopus 로고
    • Spinning molecular immunology into successful immunotherapy
    • Pardoll DM. Spinning molecular immunology into successful immunotherapy. Nat Rev Immunol 2002;2:227-38.
    • (2002) Nat Rev Immunol , vol.2 , pp. 227-238
    • Pardoll, D.M.1
  • 47
    • 0037058993 scopus 로고    scopus 로고
    • Adoptive T cell therapy using antigen-specific CD8+ T cell clones for the treatment of patients with metastatic melanoma: In vivo persistence, migration, and antitumor effect of transferred T cells
    • Yee C, Thompson JA, Byrd D, et al. Adoptive T cell therapy using antigen-specific CD8+ T cell clones for the treatment of patients with metastatic melanoma: in vivo persistence, migration, and antitumor effect of transferred T cells. Proc Natl Acad Sci U S A 2002;99:16168-73.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 16168-16173
    • Yee, C.1    Thompson, J.A.2    Byrd, D.3
  • 48
    • 0037114621 scopus 로고    scopus 로고
    • Chemoresistant or aggressive lymphoma predicts for a poor outcome following reduced-intensity allogeneic progenitor cell transplantation: An analysis from the Lymphoma Working Party of the European Group for Blood and Bone Marrow Transplantation
    • Robinson SP, Goldstone AH, Mackinnon S, et al. Chemoresistant or aggressive lymphoma predicts for a poor outcome following reduced-intensity allogeneic progenitor cell transplantation: an analysis from the Lymphoma Working Party of the European Group for Blood and Bone Marrow Transplantation. Blood 2002;100:4310-6.
    • (2002) Blood , vol.100 , pp. 4310-4316
    • Robinson, S.P.1    Goldstone, A.H.2    Mackinnon, S.3
  • 49
    • 0032713075 scopus 로고    scopus 로고
    • Safety and antitumor activity of recombinant soluble Apo2 ligand
    • Ashkenazi A, Pai RC, Fong S, et al. Safety and antitumor activity of recombinant soluble Apo2 ligand. J Clin Invest 1999;104:155-62.
    • (1999) J Clin Invest , vol.104 , pp. 155-162
    • Ashkenazi, A.1    Pai, R.C.2    Fong, S.3
  • 50
    • 0035949570 scopus 로고    scopus 로고
    • Blockade of the granzyme B/perforin pathway through overexpression of the serine protease inhibitor PI-9/SPI-6 constitutes a mechanism for immune escape by tumors
    • Medema JP, de Jong J, Peltenburg LT, et al. Blockade of the granzyme B/perforin pathway through overexpression of the serine protease inhibitor PI-9/SPI-6 constitutes a mechanism for immune escape by tumors. Proc Natl Acad Sci U S A 2001;98:11515-20.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 11515-11520
    • Medema, J.P.1    De Jong, J.2    Peltenburg, L.T.3
  • 51
    • 23844496672 scopus 로고    scopus 로고
    • Reactive oxygen species regulate caspase activation in tumor necrosis factor-related apoptosis-inducing ligand-resistant human colon carcinoma cell lines
    • Izeradjene K, Douglas L, Tillman DM, Delaney AB, Houghton JA. Reactive oxygen species regulate caspase activation in tumor necrosis factor-related apoptosis-inducing ligand-resistant human colon carcinoma cell lines. Cancer Res 2005;65:7436-45.
    • (2005) Cancer Res , vol.65 , pp. 7436-7445
    • Izeradjene, K.1    Douglas, L.2    Tillman, D.M.3    Delaney, A.B.4    Houghton, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.