메뉴 건너뛰기




Volumn 110, Issue 2, 2003, Pages 217-224

Apoptosis induction by interleukin-2-activated cytotoxic lymphocytes in a squamous cell carcinoma cell line and Daudi cells - Involvement of reactive oxygen species-dependent cytochrome c and reactive oxygen species-independent apoptosis-inducing factors

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS INDUCING FACTOR; CASPASE 3; CYTOCHROME C; DNA FRAGMENT; FAS ANTIGEN; GRANZYME B; INTERLEUKIN 2; MONOCLONAL ANTIBODY; NEUTRALIZING ANTIBODY; PROTEIN INHIBITOR; REACTIVE OXYGEN METABOLITE; SCAVENGER;

EID: 0141992087     PISSN: 00192805     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2567.2003.01703.x     Document Type: Article
Times cited : (7)

References (52)
  • 1
    • 0028483262 scopus 로고
    • Lymphocyte-mediated cytotoxicity: Two pathways and multiple effector molecules
    • Henkart PA, Lymphocyte-mediated cytotoxicity: two pathways and multiple effector molecules. Immunity 1994; 1:343-6.
    • (1994) Immunity , vol.1 , pp. 343-346
    • Henkart, P.A.1
  • 2
    • 0031952224 scopus 로고    scopus 로고
    • Lymphocyte granule-mediated apoptosis: Matters of viral mimicry and deadly proteases
    • Froelich CJ, Dixit VM, Yang X. Lymphocyte granule-mediated apoptosis: matters of viral mimicry and deadly proteases. Immunol Today 1998; 19:30-6.
    • (1998) Immunol Today , vol.19 , pp. 30-36
    • Froelich, C.J.1    Dixit, V.M.2    Yang, X.3
  • 3
    • 0034630330 scopus 로고    scopus 로고
    • Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis
    • Bratton SB, MacFarlane M, Cain K, Cohen GM. Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis. Exp Cell Res 2000; 256:27-33.
    • (2000) Exp Cell Res , vol.256 , pp. 27-33
    • Bratton, S.B.1    MacFarlane, M.2    Cain, K.3    Cohen, G.M.4
  • 4
    • 0033614347 scopus 로고    scopus 로고
    • The CED-4-homologous protein FLASH is involved in Fas-mediated activation of caspase-8 during apoptosis
    • Imai Y, Kimura T, Murakami A, Yajima N, Sakamaki K, Yonehara S. The CED-4-homologous protein FLASH is involved in Fas-mediated activation of caspase-8 during apoptosis. Nature 1999; 398:777-85.
    • (1999) Nature , vol.398 , pp. 777-785
    • Imai, Y.1    Kimura, T.2    Murakami, A.3    Yajima, N.4    Sakamaki, K.5    Yonehara, S.6
  • 5
    • 0030931876 scopus 로고    scopus 로고
    • Caspases: The executioners of apoptosis
    • Cohen GM. Caspases: the executioners of apoptosis. Biochem J 1997; 326:1-16.
    • (1997) Biochem J , vol.326 , pp. 1-16
    • Cohen, G.M.1
  • 6
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M, Sakahira H, Yokoyama H, Okawa K, Iwamatsu A, Nagata S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 1998; 391:43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 7
    • 0029099845 scopus 로고
    • Activation of the apoptotic protease CPP32 by cytotoxic T-cell derived granzyme B
    • Darmon AJ, Nicolson DW, Bleakley RC. Activation of the apoptotic protease CPP32 by cytotoxic T-cell derived granzyme B. Nature 1995; 277:446-8.
    • (1995) Nature , vol.277 , pp. 446-448
    • Darmon, A.J.1    Nicolson, D.W.2    Bleakley, R.C.3
  • 8
    • 0029891838 scopus 로고    scopus 로고
    • The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A
    • Orth K, Chinnaiyan AM, Garg M, Froelich CJ, Dixit VM. The CED-3/ICE-like protease Mch2 is activated during apoptosis and cleaves the death substrate lamin A. J Biol Chem 1996; 271:16443-6.
    • (1996) J Biol Chem , vol.271 , pp. 16443-16446
    • Orth, K.1    Chinnaiyan, A.M.2    Garg, M.3    Froelich, C.J.4    Dixit, V.M.5
  • 10
    • 0031459164 scopus 로고    scopus 로고
    • Cleavage of FLICE (caspase 8) by granzyme B during cytotoxic T lymphocyte induced apoptosis
    • Madema JP, Toe REM, Scaffidi C et al. Cleavage of FLICE (caspase 8) by granzyme B during cytotoxic T lymphocyte induced apoptosis. Eur J Immunol 1997; 27:3492-8.
    • (1997) Eur J Immunol , vol.27 , pp. 3492-3498
    • Madema, J.P.1    Toe, R.E.M.2    Scaffidi, C.3
  • 11
    • 0030008812 scopus 로고    scopus 로고
    • ICE-LAP6, a novel member of the ICE/CED3 gene family, is activated by the cytotoxic T cell protease granzyme B
    • Duan H, Orth K, Chinnaiyan AM, Poier GG, Froelich CJ, He W-W, Dixit VM. ICE-LAP6, a novel member of the ICE/CED3 gene family, is activated by the cytotoxic T cell protease granzyme B. J Biol Chem 1996; 271:16720-4.
    • (1996) J Biol Chem , vol.271 , pp. 16720-16724
    • Duan, H.1    Orth, K.2    Chinnaiyan, A.M.3    Poier, G.G.4    Froelich, C.J.5    He, W.-W.6    Dixit, V.M.7
  • 12
    • 0344053451 scopus 로고    scopus 로고
    • In vitro activation of CPP32 and Mch3 by Mch4, a novel human apototic cystein protease containing two FADD-like domains
    • Fernandes-Alnemri T, Armstrong RC, Krebs J et al. In vitro activation of CPP32 and Mch3 by Mch4, a novel human apototic cystein protease containing two FADD-like domains. Proc Natl Acad Sci U S A 1996; 93:7464-9.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7464-7469
    • Fernandes-Alnemri, T.1    Armstrong, R.C.2    Krebs, J.3
  • 13
    • 0032055097 scopus 로고    scopus 로고
    • Granzyme B directly and efficiently cleaves several downstream caspase substrates: Implication for CTL-induced apoptosis
    • Andrade F, Roy S, Nicholson D, Thornberry N, Rosen A, Casciola-Rosen L. Granzyme B directly and efficiently cleaves several downstream caspase substrates: implication for CTL-induced apoptosis. Immunity 1998; 8:451-60.
    • (1998) Immunity , vol.8 , pp. 451-460
    • Andrade, F.1    Roy, S.2    Nicholson, D.3    Thornberry, N.4    Rosen, A.5    Casciola-Rosen, L.6
  • 14
    • 17844365555 scopus 로고    scopus 로고
    • Direct cleavage of the human DNA fragmentation factor-45 by granzyme B induces caspase-activated DNase release and DNA fragmentation
    • Sharif-Askari E, Alam A, Rhéaume E et al Direct cleavage of the human DNA fragmentation factor-45 by granzyme B induces caspase-activated DNase release and DNA fragmentation. EMBO J 2001; 20:3101-13.
    • (2001) EMBO J , vol.20 , pp. 3101-3113
    • Sharif-Askari, E.1    Alam, A.2    Rhéaume, E.3
  • 17
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281:1309-12.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 18
    • 0033565557 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore and its role in cell death
    • Crompton M. The mitochondrial permeability transition pore and its role in cell death. Biochem J 1999; 341:233-49.
    • (1999) Biochem J , vol.341 , pp. 233-249
    • Crompton, M.1
  • 19
    • 0034730884 scopus 로고    scopus 로고
    • Mitochondria: Execution central
    • Gottlieb RA. Mitochondria: execution central. FEBS Lett 2000; 482:6-12.
    • (2000) FEBS Lett , vol.482 , pp. 6-12
    • Gottlieb, R.A.1
  • 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, Srinivasula SM, Ahmad M, Alnemri ES, Wang X. 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    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 21
    • 0033521741 scopus 로고    scopus 로고
    • Molecular characterization of mitochondrial apoptosis-inducing factor
    • Susin SA, Lorenzo HK, Zamzami N et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 1999; 397: 441-6.
    • (1999) Nature , vol.397 , pp. 441-446
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3
  • 22
    • 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
  • 23
    • 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
  • 24
    • 0033579810 scopus 로고    scopus 로고
    • Mitochondrial release of caspase-2 and -9 during the apoptotic process
    • Susin SA, Lorenzo HK, Zamzami N et al. Mitochondrial release of caspase-2 and -9 during the apoptotic process. J Exp Med 1999; 189:381-94.
    • (1999) J Exp Med , vol.189 , pp. 381-394
    • Susin, S.A.1    Lorenzo, H.K.2    Zamzami, N.3
  • 25
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G, Reed JC. Mitochondrial control of cell death. Nat Med 2000; 6:513-9.
    • (2000) Nat Med , vol.6 , pp. 513-519
    • Kroemer, G.1    Reed, J.C.2
  • 26
    • 0035896592 scopus 로고    scopus 로고
    • Pro-caspase-8 is predominantly localized in mitochondria and released into cytoplasm upon apoptotic stimulation
    • Quin Z-H, Wang Y, Kikly KK, Sapp E, Kegel KB, Aronin N, DiFiglia M. Pro-caspase-8 is predominantly localized in mitochondria and released into cytoplasm upon apoptotic stimulation. J Biol Chem 2001; 276:8079-86.
    • (2001) J Biol Chem , vol.276 , pp. 8079-8086
    • Quin, Z.-H.1    Wang, Y.2    Kikly, K.K.3    Sapp, E.4    Kegel, K.B.5    Aronin, N.6    Difiglia, M.7
  • 27
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti M, Szabo I. The mitochondrial permeability transition. Biochim Biophys Acta 1995; 1241:139-76.
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabo, I.2
  • 28
    • 0030051609 scopus 로고    scopus 로고
    • Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, a cyclosporin A-sensitive channel
    • Nicolli A, Basso E, Petronilli V, Wenger RM, Bernardi P. Interactions of cyclophilin with the mitochondrial inner membrane and regulation of the permeability transition pore, a cyclosporin A-sensitive channel. J Biol Chem 1996; 271:2185-92.
    • (1996) J Biol Chem , vol.271 , pp. 2185-2192
    • Nicolli, A.1    Basso, E.2    Petronilli, V.3    Wenger, R.M.4    Bernardi, P.5
  • 29
    • 0034617449 scopus 로고    scopus 로고
    • Apoptosis-inducing factor (AIF): A ubiquitous mitochondrial oxidoreductase involved in apoptosis
    • Daugas E, Nochy D, Ravagnan L, Loeffler M, Susin SA, Zamzami N, Kroemer G. Apoptosis-inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis. FEBS Lett 2000; 476:118-23.
    • (2000) FEBS Lett , vol.476 , pp. 118-123
    • Daugas, E.1    Nochy, D.2    Ravagnan, L.3    Loeffler, M.4    Susin, S.A.5    Zamzami, N.6    Kroemer, G.7
  • 30
    • 0032959345 scopus 로고    scopus 로고
    • Reactive oxygen intermediates as mediators of programmed cell death in plants and animals
    • Jabs T. Reactive oxygen intermediates as mediators of programmed cell death in plants and animals. Biochem Pharmacol 1999; 57: 231-45.
    • (1999) Biochem Pharmacol , vol.57 , pp. 231-245
    • Jabs, T.1
  • 31
    • 0032422488 scopus 로고    scopus 로고
    • Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria
    • Narita M, Shimizu S, Ito T, Chittenden T, Lutz RJ, Matsuda H, Tsujimoto Y. Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci U S A 1998; 95: 14681-6.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 14681-14686
    • Narita, M.1    Shimizu, S.2    Ito, T.3    Chittenden, T.4    Lutz, R.J.5    Matsuda, H.6    Tsujimoto, Y.7
  • 32
    • 0033519705 scopus 로고    scopus 로고
    • Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC
    • Shimizu S, Narita M, Tsujimoto Y. Bcl-2 family proteins regulate the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 1999; 399:483-7.
    • (1999) Nature , vol.399 , pp. 483-487
    • Shimizu, S.1    Narita, M.2    Tsujimoto, Y.3
  • 33
    • 0034001070 scopus 로고    scopus 로고
    • Activation of apoptosis signal-regulating kinase 1 (ASK-1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin
    • Liu H, Nishitoh H, Ichijo H, Kyriakis JM. Activation of apoptosis signal-regulating kinase 1 (ASK-1) by tumor necrosis factor receptor-associated factor 2 requires prior dissociation of the ASK1 inhibitor thioredoxin. Mol Cell Biol 2000; 20:2198-208.
    • (2000) Mol Cell Biol , vol.20 , pp. 2198-2208
    • Liu, H.1    Nishitoh, H.2    Ichijo, H.3    Kyriakis, J.M.4
  • 34
    • 0032504189 scopus 로고    scopus 로고
    • Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-α signal transduction
    • Gotoh Y, Cooper JA. Reactive oxygen species- and dimerization-induced activation of apoptosis signal-regulating kinase 1 in tumor necrosis factor-α signal transduction. J Biol Chem 1998; 273: 17477-82.
    • (1998) J Biol Chem , vol.273 , pp. 17477-17482
    • Gotoh, Y.1    Cooper, J.A.2
  • 35
    • 0029990552 scopus 로고    scopus 로고
    • Role of oxidants and antioxidants in the induction of AP-1, NF-κB, and glutathione 5-transferase gene expression
    • Pinkus R, Weiner LM, Daniel V. Role of oxidants and antioxidants in the induction of AP-1, NF-κB, and glutathione 5-transferase gene expression. J Biol Chem 1996; 271:13422-9.
    • (1996) J Biol Chem , vol.271 , pp. 13422-13429
    • Pinkus, R.1    Weiner, L.M.2    Daniel, V.3
  • 36
    • 0032955276 scopus 로고    scopus 로고
    • NSAIDs and butyrate sensitize a human colorectal cancer cell line to TNF-α and Fas ligation: The role of reactive oxygen species
    • Giardina C, Boulares H, Inan MS. NSAIDs and butyrate sensitize a human colorectal cancer cell line to TNF-α and Fas ligation: the role of reactive oxygen species. Biochim Biophys Acta 1999; 1448:425-38.
    • (1999) Biochim Biophys Acta , vol.1448 , pp. 425-438
    • Giardina, C.1    Boulares, H.2    Inan, M.S.3
  • 37
    • 0033805442 scopus 로고    scopus 로고
    • Oxidative stress and apoptosis
    • Kannan K, Jain SK. Oxidative stress and apoptosis. Pathophysiology 2000; 7:153-63.
    • (2000) Pathophysiology , vol.7 , pp. 153-163
    • Kannan, K.1    Jain, S.K.2
  • 38
    • 0024428198 scopus 로고
    • Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor
    • Wong GH, Elwell JH, Oberley LW, Goeddel DV. Manganous superoxide dismutase is essential for cellular resistance to cytotoxicity of tumor necrosis factor. Cell 1989; 58:923-31.
    • (1989) Cell , vol.58 , pp. 923-931
    • Wong, G.H.1    Elwell, J.H.2    Oberley, L.W.3    Goeddel, D.V.4
  • 39
    • 0030610962 scopus 로고    scopus 로고
    • Role of Bcl-xL as an inhibitor of cytosolic cytochrome c accumulation in DNA damage-induced apoptosis
    • Kharbanda S, Pandey P, Schefield L et al. Role of Bcl-xL as an inhibitor of cytosolic cytochrome c accumulation in DNA damage-induced apoptosis. Proc Natl Acad Sci U S A 1997; 94:6939-42.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6939-6942
    • Kharbanda, S.1    Pandey, P.2    Schefield, L.3
  • 40
    • 0034493914 scopus 로고    scopus 로고
    • Mechanisms of biological S-nitrosation and its measurement
    • Akaike T. Mechanisms of biological S-nitrosation and its measurement. Free Radic Res 2000; 33:461-9.
    • (2000) Free Radic Res , vol.33 , pp. 461-469
    • Akaike, T.1
  • 41
    • 0033025146 scopus 로고    scopus 로고
    • Manganese superoxide dismutase negatively regulates the induction of apoptosis by 5-fluorouracil, peplomycin and gamma-rays in squamous cell carcinoma cells
    • Ueta E, Yoneda K, Yamamoto T, Osaki T. Manganese superoxide dismutase negatively regulates the induction of apoptosis by 5-fluorouracil, peplomycin and gamma-rays in squamous cell carcinoma cells. Jpn J Cancer Res 1999; 90:555-64.
    • (1999) Jpn J Cancer Res , vol.90 , pp. 555-564
    • Ueta, E.1    Yoneda, K.2    Yamamoto, T.3    Osaki, T.4
  • 42
    • 0035889658 scopus 로고    scopus 로고
    • Mn-SOD antisense upegulates in vitro apoptosis of squamous cell carcinoma cells by anticancer drugs and γ-rays regulating expression of the Bcl-2 family proteins, Cox-2 and p21
    • Ueta E, Yoneda K, Kimura T, Tatemoto Y, Doi S, Yamamoto T, Osaki T. Mn-SOD antisense upegulates in vitro apoptosis of squamous cell carcinoma cells by anticancer drugs and γ-rays regulating expression of the Bcl-2 family proteins, Cox-2 and p21. Int J Cancer 2001; 94:545-50.
    • (2001) Int J Cancer , vol.94 , pp. 545-550
    • Ueta, E.1    Yoneda, K.2    Kimura, T.3    Tatemoto, Y.4    Doi, S.5    Yamamoto, T.6    Osaki, T.7
  • 43
    • 0031918742 scopus 로고    scopus 로고
    • The mitochondrial death/life regulator in apoptosis and necrosis
    • Kroemer G, Dallaporta B, Resche-Rigon M. The mitochondrial death/life regulator in apoptosis and necrosis. Annu Rev Physiol 1998; 60:619-42.
    • (1998) Annu Rev Physiol , vol.60 , pp. 619-642
    • Kroemer, G.1    Dallaporta, B.2    Resche-Rigon, M.3
  • 45
    • 0034666197 scopus 로고    scopus 로고
    • Reactive oxidizing species produced near the plasma membrane induce apoptosis in bovine aorta endothelial cells
    • Lin CP, Lynch MC, Kochevar IE. Reactive oxidizing species produced near the plasma membrane induce apoptosis in bovine aorta endothelial cells. Exp Cell Res 2000; 29:351-9.
    • (2000) Exp Cell Res , vol.29 , pp. 351-359
    • Lin, C.P.1    Lynch, M.C.2    Kochevar, I.E.3
  • 46
    • 0030065418 scopus 로고    scopus 로고
    • Superoxide anion is a natural inhibitor of Fas-mediated cell death
    • Clément M-V, Stamenkovic I. Superoxide anion is a natural inhibitor of Fas-mediated cell death. EMBO J 1996; 15:216-25.
    • (1996) EMBO J , vol.15 , pp. 216-225
    • Clément, M.-V.1    Stamenkovic, I.2
  • 47
    • 0032570577 scopus 로고    scopus 로고
    • Cytochrome c in the apoptotic and antioxidant cascades
    • Skulachev VP. Cytochrome c in the apoptotic and antioxidant cascades. FEBS Lett 1998; 423:275-80.
    • (1998) FEBS Lett , vol.423 , pp. 275-280
    • Skulachev, V.P.1
  • 48
    • 0030856714 scopus 로고    scopus 로고
    • Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide
    • Gudz TI, Tserng KY, Hoppel CL. Direct inhibition of mitochondrial respiratory chain complex III by cell-permeable ceramide. J Biol Chem 1997; 272:24154-8.
    • (1997) J Biol Chem , vol.272 , pp. 24154-24158
    • Gudz, T.I.1    Tserng, K.Y.2    Hoppel, C.L.3
  • 50
    • 17844362452 scopus 로고    scopus 로고
    • Bid acts on the permeability transition pore complex to induce apoptosis
    • Zamzami N, Hamel EI, Maisse C et al. Bid acts on the permeability transition pore complex to induce apoptosis. Oncogene 2000; 19:6342-50.
    • (2000) Oncogene , vol.19 , pp. 6342-6350
    • Zamzami, N.1    Hamel, E.I.2    Maisse, C.3
  • 52
    • 0035421688 scopus 로고    scopus 로고
    • A role of the mitochondrial apoptosis-inducing factor in granulysis-induced apoptosis
    • Pardo J, Perez-Galan P, Gamen S et al. A role of the mitochondrial apoptosis-inducing factor in granulysis-induced apoptosis. J Immunol 2001; 167:1222-9.
    • (2001) J Immunol , vol.167 , pp. 1222-1229
    • Pardo, J.1    Perez-Galan, P.2    Gamen, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.