메뉴 건너뛰기




Volumn 12, Issue 9, 2005, Pages 1240-1254

Caspase activation and apoptosis in response to proteasome inhibitors

Author keywords

Caspase; Chemotherapy; GFP; IAP; Mitochondria; Time lapse; TMRM

Indexed keywords

APOPTOSOME; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CASPASE; CASPASE 3; CASPASE 7; CASPASE 9; CISPLATIN; COLCHICINE; CYTARABINE; CYTOCHROME C; DAUNORUBICIN; DOXORUBICIN; EPIRUBICIN; ETOPOSIDE; FLUDARABINE; GEMCITABINE; IRINOTECAN; PACLITAXEL; PROTEASOME; PROTEASOME INHIBITOR; PROTEIN BCL 2; RALTITREXED; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; TOPOTECAN; TRICHOSANTHIN; VINBLASTINE; VINCRISTINE;

EID: 23944483498     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401729     Document Type: Article
Times cited : (47)

References (64)
  • 1
    • 0034654326 scopus 로고    scopus 로고
    • Activation of apoptosis pathways by anticancer treatment
    • Debatin K (2000) Activation of apoptosis pathways by anticancer treatment. Toxicol Lett. 112-113: 41-48
    • (2000) Toxicol. Lett. , vol.112-113 , pp. 41-48
    • Debatin, K.1
  • 2
    • 0035500410 scopus 로고    scopus 로고
    • Apoptosis and cancer chemotherapy
    • Makin G and Dive C (2001) Apoptosis and cancer chemotherapy. Trends Cell Biol. 11: S22-S26
    • (2001) Trends Cell Biol. , vol.11
    • Makin, G.1    Dive, C.2
  • 3
    • 2642689658 scopus 로고    scopus 로고
    • Proteases to die for
    • Cryns V and Yuan J (1998) Proteases to die for. Genes Dev. 12: 1551-1570
    • (1998) Genes Dev. , vol.12 , pp. 1551-1570
    • Cryns, V.1    Yuan, J.2
  • 5
    • 2942746419 scopus 로고    scopus 로고
    • Caspase activation: Revisiting the induced proximity model
    • Shi Y (2004) Caspase activation: revisiting the induced proximity model. Cell 117: 855-858
    • (2004) Cell , vol.117 , pp. 855-858
    • Shi, Y.1
  • 6
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: A comprehensive update of caspase substrates
    • Fischer U, Janicke RU and Schulze-Osthoff K (2003) Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 10: 76-100
    • (2003) Cell Death Differ. , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 7
    • 3943071150 scopus 로고    scopus 로고
    • Cytochrome C-mediated apoptosis
    • Jiang X and Wang X (2004) Cytochrome C-mediated apoptosis. Annu. Rev. Biochem. 73: 87-106
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 87-106
    • Jiang, X.1    Wang, X.2
  • 8
    • 0142117313 scopus 로고    scopus 로고
    • The Bcl-2 family: Roles in cell survival and oncogenesis
    • Cory S, Huang DC and Adams JM (2003) The Bcl-2 family: roles in cell survival and oncogenesis. Oncogene 22: 8590-8607
    • (2003) Oncogene , vol.22 , pp. 8590-8607
    • Cory, S.1    Huang, D.C.2    Adams, J.M.3
  • 9
    • 0037427412 scopus 로고    scopus 로고
    • Mechanisms of cytochrome c release by proapoptotic BCL-2 family members
    • Scorrano L and Korsmeyer SJ (2003) Mechanisms of cytochrome c release by proapoptotic BCL-2 family members. Biochem. Biophys. Res. Commun. 304: 437-444
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 437-444
    • Scorrano, L.1    Korsmeyer, S.J.2
  • 10
  • 11
    • 0037069929 scopus 로고    scopus 로고
    • Chemotherapy: Targeting the mitochondrial cell death pathway
    • Debatin KM, Poncet D and Kroemer G (2002) Chemotherapy: targeting the mitochondrial cell death pathway. Oncogene 21: 8786-8803
    • (2002) Oncogene , vol.21 , pp. 8786-8803
    • Debatin, K.M.1    Poncet, D.2    Kroemer, G.3
  • 12
    • 0032544449 scopus 로고    scopus 로고
    • Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development
    • Cecconi F, Alvarez-Bolado G, Meyer BI, Roth KA and Gruss P (1998) Apaf1 (CED-4 homolog) regulates programmed cell death in mammalian development. Cell 94: 727-733
    • (1998) Cell , vol.94 , pp. 727-733
    • Cecconi, F.1    Alvarez-Bolado, G.2    Meyer, B.I.3    Roth, K.A.4    Gruss, P.5
  • 15
    • 0037162833 scopus 로고    scopus 로고
    • Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization
    • Lassus P, Opitz-Araya X and Lazebnik Y (2002) Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science 297: 1352-1354
    • (2002) Science , vol.297 , pp. 1352-1354
    • Lassus, P.1    Opitz-Araya, X.2    Lazebnik, Y.3
  • 18
    • 0038485588 scopus 로고    scopus 로고
    • Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA)
    • Henderson C, Mizzau M, Paroni G, Maestro R, Schneider C and Brancolini C (2003) Role of caspases, Bid, and p53 in the apoptotic response triggered by histone deacetylase inhibitors trichostatin-A (TSA) and suberoylanilide hydroxamic acid (SAHA). J. Biol. Chem. 278: 12579-12589
    • (2003) J. Biol. Chem. , vol.278 , pp. 12579-12589
    • Henderson, C.1    Mizzau, M.2    Paroni, G.3    Maestro, R.4    Schneider, C.5    Brancolini, C.6
  • 20
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee DH and Goldberg AL (1998) Proteasome inhibitors: valuable new tools for cell biologists. Trends Cell Biol. 8: 397-403
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 22
    • 3042592579 scopus 로고    scopus 로고
    • Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9
    • Marsden VS, Ekert PG, Van Delft M, Vaux DL, Adams JM and Strasser A (2004) Bcl-2-regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9. J. Cell Biol. 165: 775-780
    • (2004) J. Cell Biol. , vol.165 , pp. 775-780
    • Marsden, V.S.1    Ekert, P.G.2    Van Delft, M.3    Vaux, D.L.4    Adams, J.M.5    Strasser, A.6
  • 26
    • 0037879052 scopus 로고    scopus 로고
    • The mitochondrial membrane potential (deltapsi(m)) in apoptosis; an update
    • Ly JD, Grubb DR and Lawen A (2003) The mitochondrial membrane potential (deltapsi(m)) in apoptosis; an update. Apoptosis 8: 115-128
    • (2003) Apoptosis , vol.8 , pp. 115-128
    • Ly, J.D.1    Grubb, D.R.2    Lawen, A.3
  • 27
    • 0033605376 scopus 로고    scopus 로고
    • Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells
    • Heiskanen KM, Bhat MB, Wang HM, Ma J and Nieminen AL (1999) Mitochondrial depolarization accompanies cytochrome c release during apoptosis in PC6 cells. J. Biol. Chem. 26: 5654-5658
    • (1999) J. Biol. Chem. , vol.26 , pp. 5654-5658
    • Heiskanen, K.M.1    Bhat, M.B.2    Wang, H.M.3    Ma, J.4    Nieminen, A.L.5
  • 28
  • 29
    • 0033529712 scopus 로고    scopus 로고
    • Commitment to apoptosis by GD3 ganglioside depends on opening of the mitochondrial permeability transition pore
    • Scorrano L, Petronilli V, Di Lisa F and Bernardi P (1999) Commitment to apoptosis by GD3 ganglioside depends on opening of the mitochondrial permeability transition pore. J. Biol. Chem. 274: 22581-22585
    • (1999) J. Biol. Chem. , vol.274 , pp. 22581-22585
    • Scorrano, L.1    Petronilli, V.2    Di Lisa, F.3    Bernardi, P.4
  • 30
    • 0037326590 scopus 로고    scopus 로고
    • Outer mitochondrial membrane permeabilization during apoptosis triggers caspase-independent mitochondrial and caspase-dependent plasma membrane potential depolarization: A single-cell analysis
    • Dussmann H, Rehm M, Kogel D and Prehn JH (2003) Outer mitochondrial membrane permeabilization during apoptosis triggers caspase-independent mitochondrial and caspase-dependent plasma membrane potential depolarization: a single-cell analysis. J. Cell Sci. 116: 525-536
    • (2003) J. Cell Sci. , vol.116 , pp. 525-536
    • Dussmann, H.1    Rehm, M.2    Kogel, D.3    Prehn, J.H.4
  • 31
    • 0141768255 scopus 로고    scopus 로고
    • Real-time single cell analysis of Smac/DIABLO release during apoptosis
    • Rehm M, Dussmann H and Prehn JH (2003) Real-time single cell analysis of Smac/DIABLO release during apoptosis. J. Cell Biol. 162: 1031-1043
    • (2003) J. Cell Biol. , vol.162 , pp. 1031-1043
    • Rehm, M.1    Dussmann, H.2    Prehn, J.H.3
  • 32
    • 0035897408 scopus 로고    scopus 로고
    • Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process
    • Waterhouse NJ, JGoldstein JC, von Ahsen O, Schuler M, Newmeyer DD and Green DR (2001) Cytochrome c maintains mitochondrial transmembrane potential and ATP generation after outer mitochondrial membrane permeabilization during the apoptotic process. J. Cell Biol. 153: 319-328
    • (2001) J. Cell Biol. , vol.153 , pp. 319-328
    • Waterhouse, N.J.1    JGoldstein, J.C.2    von Ahsen, O.3    Schuler, M.4    Newmeyer, D.D.5    Green, D.R.6
  • 34
    • 0037184113 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro
    • MacFarlane M, Merrison W, Bratton SB and Cohen GM (2002) Proteasome-mediated degradation of Smac during apoptosis: XIAP promotes Smac ubiquitination in vitro. J. Biol. Chem. 277: 36611-36616
    • (2002) J. Biol. Chem. , vol.277 , pp. 36611-36616
    • MacFarlane, M.1    Merrison, W.2    Bratton, S.B.3    Cohen, G.M.4
  • 35
    • 2942674780 scopus 로고    scopus 로고
    • Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase
    • Bartke T, Pohl C, Pyrowolakis G and Jentsch S (2004) Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3 ubiquitin ligase. Mol Cell 14: 801-811
    • (2004) Mol. Cell , vol.14 , pp. 801-811
    • Bartke, T.1    Pohl, C.2    Pyrowolakis, G.3    Jentsch, S.4
  • 36
    • 0037855783 scopus 로고    scopus 로고
    • Cellular inhibitor of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO
    • Hu S and Yang X (2003) Cellular inhibitor of apoptosis 1 and 2 are ubiquitin ligases for the apoptosis inducer Smac/DIABLO. J. Biol. Chem. 278: 10055-10060
    • (2003) J. Biol. Chem. , vol.278 , pp. 10055-10060
    • Hu, S.1    Yang, X.2
  • 37
    • 12844258128 scopus 로고    scopus 로고
    • The membrane-associated inhibitor of apoptosis protein, BRUCE/Apollon, antagonizes both the precursor and mature forms of Smac and caspase-9
    • Qiu XB and Goldberg AL (2005) The membrane-associated inhibitor of apoptosis protein, BRUCE/Apollon, antagonizes both the precursor and mature forms of Smac and caspase-9. J. Biol. Chem. 280: 174-182
    • (2005) J. Biol. Chem. , vol.280 , pp. 174-182
    • Qiu, X.B.1    Goldberg, A.L.2
  • 38
    • 10944247878 scopus 로고    scopus 로고
    • Neutralization of Smac/Diablo by inhibitors of apoptosis (IAPs): A caspase-independent mechanism for apoptotic inhibition
    • Wilkinson JC, Wilkinson AS, Scott FL, Csomos RA, Salvesen GS and Duckett CS (2004) Neutralization of Smac/Diablo by inhibitors of apoptosis (IAPs): a caspase-independent mechanism for apoptotic inhibition. J. Biol. Chem. 279: 51082-51090
    • (2004) J. Biol. Chem. , vol.279 , pp. 51082-51090
    • Wilkinson, J.C.1    Wilkinson, A.S.2    Scott, F.L.3    Csomos, R.A.4    Salvesen, G.S.5    Duckett, C.S.6
  • 39
    • 0037470027 scopus 로고    scopus 로고
    • A novel ubiquitin fusion system bypasses the mitochondria and generates biologically active Smac/DIABLO
    • Hunter AM, Kottachchi D, Lewis J, Duckett CS, Korneluk RG and Liston P (2003) A novel ubiquitin fusion system bypasses the mitochondria and generates biologically active Smac/DIABLO. J. Biol. Chem. 278: 7494-7499
    • (2003) J. Biol. Chem. , vol.278 , pp. 7494-7499
    • Hunter, A.M.1    Kottachchi, D.2    Lewis, J.3    Duckett, C.S.4    Korneluk, R.G.5    Liston, P.6
  • 40
    • 0034710649 scopus 로고    scopus 로고
    • Structural and biochemical basis of apoptotic activation by Smac/DIABLO
    • Chai J, Du C, Wu JW, Kyin S, Wang X and Shi Y (2000) Structural and biochemical basis of apoptotic activation by Smac/DIABLO. Nature 406: 855-862
    • (2000) Nature , vol.406 , pp. 855-862
    • Chai, J.1    Du, C.2    Wu, J.W.3    Kyin, S.4    Wang, X.5    Shi, Y.6
  • 41
    • 0034680876 scopus 로고    scopus 로고
    • Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway
    • Srinivasula SM, Datta P, Fan XJ, Fernandes-Alnemri F, Huang Z and Alnemri ES (2000) Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway. J. Biol. Chem. 275: 36152-36157
    • (2000) J. Biol. Chem. , vol.275 , pp. 36152-36157
    • Srinivasula, S.M.1    Datta, P.2    Fan, X.J.3    Fernandes-Alnemri, F.4    Huang, Z.5    Alnemri, E.S.6
  • 43
  • 45
    • 0036240701 scopus 로고    scopus 로고
    • The proteasome: A novel target for cancer chemotherapy
    • Almond JB and Cohen GM (2002) The proteasome: a novel target for cancer chemotherapy. Leukemia 16: 433-443
    • (2002) Leukemia , vol.16 , pp. 433-443
    • Almond, J.B.1    Cohen, G.M.2
  • 46
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • Adams J (2004) The proteasome: a suitable antineoplastic target. Nat. Rev. Cancer 4: 349-360
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 48
    • 0030962262 scopus 로고    scopus 로고
    • p53-dependent induction of apoptosis by proteasome inhibitors
    • Lopes UG, Erhardt P, Yao R and Cooper GM (1997) p53-dependent induction of apoptosis by proteasome inhibitors. J. Biol. Chem. 272: 12893-12896
    • (1997) J. Biol. Chem. , vol.272 , pp. 12893-12896
    • Lopes, U.G.1    Erhardt, P.2    Yao, R.3    Cooper, G.M.4
  • 49
    • 0035284812 scopus 로고    scopus 로고
    • Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells
    • Marshansky V, Wang X, Bertrand R, Luo H, Duguid W, Chinnadurai G, Kanaan N, Vu N and Wu J (2001) Proteasomes modulate balance among proapoptotic and antiapoptotic Bcl-2 family members and compromise functioning of the electron transport chain in leukemic cells. J. Immunol. 166: 3130-3142
    • (2001) J. Immunol. , vol.166 , pp. 3130-3142
    • Marshansky, V.1    Wang, X.2    Bertrand, R.3    Luo, H.4    Duguid, W.5    Chinnadurai, G.6    Kanaan, N.7    Vu, N.8    Wu, J.9
  • 50
    • 0033773607 scopus 로고    scopus 로고
    • Proteasome inhibitor-induced apoptosis of glioma cells involves the processing of multiple caspases and cytochrome c release
    • Wagenknecht B, Hermisson M, Groscurth P, Liston P, Krammer PH and Weller M (2000) Proteasome inhibitor-induced apoptosis of glioma cells involves the processing of multiple caspases and cytochrome c release. J. Neurochem. 75: 2288-2297
    • (2000) J. Neurochem. , vol.75 , pp. 2288-2297
    • Wagenknecht, B.1    Hermisson, M.2    Groscurth, P.3    Liston, P.4    Krammer, P.H.5    Weller, M.6
  • 51
    • 0037516876 scopus 로고    scopus 로고
    • Conformational change and mitochondrial translocation of Bax accompany proteasome inhibitor-induced apoptosis of chronic lymphocytic leukemic cells
    • Dewson G, Snowden RT, Almond JB, Dyer MJ and Cohen GM (2003) Conformational change and mitochondrial translocation of Bax accompany proteasome inhibitor-induced apoptosis of chronic lymphocytic leukemic cells. Oncogene 22: 2643-2654
    • (2003) Oncogene , vol.22 , pp. 2643-2654
    • Dewson, G.1    Snowden, R.T.2    Almond, J.B.3    Dyer, M.J.4    Cohen, G.M.5
  • 52
    • 1642564603 scopus 로고    scopus 로고
    • Inhibition of proteasomal function by curcumin induces apoptosis through mitochondrial pathway
    • Jana NR, Dikshit P, Goswami A and Nukina N (2004) Inhibition of proteasomal function by curcumin induces apoptosis through mitochondrial pathway. J. Biol. Chem. 279: 11680-11685
    • (2004) J. Biol. Chem. , vol.279 , pp. 11680-11685
    • Jana, N.R.1    Dikshit, P.2    Goswami, A.3    Nukina, N.4
  • 54
    • 7644242953 scopus 로고    scopus 로고
    • Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells
    • Fribley A, Zeng Q and Wang CY (2004) Proteasome inhibitor PS-341 induces apoptosis through induction of endoplasmic reticulum stress-reactive oxygen species in head and neck squamous cell carcinoma cells. Mol. Cell Biol. 24: 9695-9704
    • (2004) Mol. Cell Biol. , vol.24 , pp. 9695-9704
    • Fribley, A.1    Zeng, Q.2    Wang, C.Y.3
  • 55
    • 0141706672 scopus 로고    scopus 로고
    • Reactive oxygen species generation and mitochondrial dysfunction in the apoptotic response to Bortezomib, a novel proteasome inhibitor, in human H460 non-small cell lung cancer cells
    • Ling YH, Liebes L, Zou Y and Perez-Soler R (2003) Reactive oxygen species generation and mitochondrial dysfunction in the apoptotic response to Bortezomib, a novel proteasome inhibitor, in human H460 non-small cell lung cancer cells. J. Biol. Chem. 278: 33714-33723
    • (2003) J. Biol. Chem. , vol.278 , pp. 33714-33723
    • Ling, Y.H.1    Liebes, L.2    Zou, Y.3    Perez-Soler, R.4
  • 57
    • 1842861723 scopus 로고    scopus 로고
    • The hierarchical relationship between MAPK signaling and ROS generation in human leukemia cells undergoing apoptosis in response to the proteasome inhibitor Bortezomib
    • Yu C, Rahmani M, Dent P and Grant S (2004) The hierarchical relationship between MAPK signaling and ROS generation in human leukemia cells undergoing apoptosis in response to the proteasome inhibitor Bortezomib. Exp. Cell Res. 295: 555-566
    • (2004) Exp. Cell Res. , vol.295 , pp. 555-566
    • Yu, C.1    Rahmani, M.2    Dent, P.3    Grant, S.4
  • 58
    • 0043170892 scopus 로고    scopus 로고
    • BCL6 overexpression prevents increase in reactive oxygen species and inhibits apoptosis induced by chemotherapeutic reagents in B-cell lymphoma cells
    • Kurosu T, Fukuda T, Miki T and Miura O (2003) BCL6 overexpression prevents increase in reactive oxygen species and inhibits apoptosis induced by chemotherapeutic reagents in B-cell lymphoma cells. Oncogene 22: 4459-4468
    • (2003) Oncogene , vol.22 , pp. 4459-4468
    • Kurosu, T.1    Fukuda, T.2    Miki, T.3    Miura, O.4
  • 59
    • 1942534018 scopus 로고    scopus 로고
    • Regulation of apoptosis proteins in cancer cells by ubiquitin
    • Zhang HG, Wang J, Yang X, Hsu HC and Mountz JD (2004) Regulation of apoptosis proteins in cancer cells by ubiquitin. Oncogene 23: 2009-2015
    • (2004) Oncogene , vol.23 , pp. 2009-2015
    • Zhang, H.G.1    Wang, J.2    Yang, X.3    Hsu, H.C.4    Mountz, J.D.5
  • 62
    • 0035072535 scopus 로고    scopus 로고
    • Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors
    • Tenev T, Marani M, McNeish I and Lemoine NR (2001) Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors 8: 256-264
    • (2001) , vol.8 , pp. 256-264
    • Tenev, T.1    Marani, M.2    McNeish, I.3    Lemoine, N.R.4
  • 63
    • 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 and Wood WC (2003) Coexistence of high levels of apoptotic signaling and inhibitor of apoptosis proteins in human tumor cells: implication for cancer specific therapy. Cancer Res. 63: 6815-6824
    • (2003) Cancer Res. , vol.63 , pp. 6815-6824
    • Yang, L.1    Cao, Z.2    Yan, H.3    Wood, W.C.4
  • 64
    • 2542431137 scopus 로고    scopus 로고
    • Caspase-dependent regulation of histone deacetylase 4 nuclear-cytoplasmic shuttling promotes apoptosis
    • Paroni G, Mizzau M, Henderson C, Del Sal G, Schneider C and Brancolini C (2004) Caspase-dependent regulation of histone deacetylase 4 nuclear-cytoplasmic shuttling promotes apoptosis. Mol. Biol. Cell 15: 2804-2818
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2804-2818
    • Paroni, G.1    Mizzau, M.2    Henderson, C.3    Del Sal, G.4    Schneider, C.5    Brancolini, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.