메뉴 건너뛰기




Volumn 3, Issue 6, 2012, Pages

Novel phosphorylations of IKKγ/NEMO

Author keywords

[No Author keywords available]

Indexed keywords

FLICE INHIBITORY PROTEIN; I KAPPA B KINASE GAMMA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 6; PROTEIN KINASE FGR; PROTEIN KINASE FYN; PROTEIN KINASE LYN; PROTEIN TYROSINE KINASE; TUMOR NECROSIS FACTOR ALPHA; TYROSINE; UNCLASSIFIED DRUG;

EID: 84872124759     PISSN: 21612129     EISSN: 21507511     Source Type: Journal    
DOI: 10.1128/mBio.00411-12     Document Type: Article
Times cited : (16)

References (48)
  • 1
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKKrelated kinases
    • Häcker H, Karin M. 2006. Regulation and function of IKK and IKKrelated kinases. Sci. STKE 2006:re13. http://dx.doi.org/10.1126/stke.3572006re13.
    • (2006) Sci. STKE , pp. 13
    • Häcker, H.1    Karin, M.2
  • 2
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NFkappaB transcription factors in the immune system
    • Vallabhapurapu S, Karin M. 2009. Regulation and function of NFkappaB transcription factors in the immune system. Annu. Rev. Immunol. 27:693-733.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 3
    • 77957252647 scopus 로고    scopus 로고
    • The IKK complex, a central regulator of NF-kappaB activation
    • Israël A. 2010. The IKK complex, a central regulator of NF-kappaB activation. Cold Spring Harbor Perspect. Biol. 2:a000158. http://dx.doi.org/10.1101/cshperspect.a000158.
    • (2010) Cold Spring Harbor Perspect. Biol. , vol.2
    • Israël, A.1
  • 4
    • 80051982064 scopus 로고    scopus 로고
    • Return to homeostasis: Downregulation of NF-kappaB responses
    • Ruland J. 2011. Return to homeostasis: downregulation of NF-kappaB responses. Nat. Immunol. 12:709-714.
    • (2011) Nat. Immunol. , vol.12 , pp. 709-714
    • Ruland, J.1
  • 5
    • 0035174615 scopus 로고    scopus 로고
    • Series introduction: The transcription factor NFkappaB and human disease
    • Baldwin AS, Jr. 2001. Series introduction: the transcription factor NFkappaB and human disease. J. Clin. Invest. 107:3-6.
    • (2001) J. Clin. Invest. , vol.107 , pp. 3-6
    • Baldwin, A.S.1
  • 6
    • 33750312876 scopus 로고    scopus 로고
    • Posttranslational modifications ofNEMOand its partners in NF-kappaB signaling
    • Sebban H, Yamaoka S, Courtois G. 2006. Posttranslational modifications ofNEMOand its partners in NF-kappaB signaling. Trends Cell Biol. 16:569-577.
    • (2006) Trends Cell Biol. , vol.16 , pp. 569-577
    • Sebban, H.1    Yamaoka, S.2    Courtois, G.3
  • 7
    • 33750457370 scopus 로고    scopus 로고
    • Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway
    • Perkins ND. 2006. Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway. Oncogene 25: 6717-6730.
    • (2006) Oncogene , vol.25 , pp. 6717-6730
    • Perkins, N.D.1
  • 8
    • 78650915536 scopus 로고    scopus 로고
    • Structural studies of NF-kappaB signaling
    • Zheng C, Yin Q, Wu H. 2011. Structural studies of NF-kappaB signaling. Cell Res. 21:183-195.
    • (2011) Cell Res. , vol.21 , pp. 183-195
    • Zheng, C.1    Yin, Q.2    Wu, H.3
  • 9
    • 0345826149 scopus 로고    scopus 로고
    • Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO
    • Zhou H, et al. 2004. Bcl10 activates the NF-kappaB pathway through ubiquitination of NEMO. Nature 427:167-171.
    • (2004) Nature , vol.427 , pp. 167-171
    • Zhou, H.1
  • 10
    • 33747615237 scopus 로고    scopus 로고
    • Key function for the Ubc13 E2 ubiquitinconjugating enzyme in immune receptor signaling
    • Yamamoto M, et al. 2006. Key function for the Ubc13 E2 ubiquitinconjugating enzyme in immune receptor signaling. Nat. Immunol. 7:962-970.
    • (2006) Nat. Immunol. , vol.7 , pp. 962-970
    • Yamamoto, M.1
  • 11
    • 0141621240 scopus 로고    scopus 로고
    • A role for NF-kappaB essential modifier/IkappaB kinase-gamma (NEMO/IKKgamma) ubiquitination in the activation of the IkappaB kinase complex by tumor necrosis factor-alpha
    • Tang ED, Wang CY, Xiong Y, Guan KL. 2003. A role for NF-kappaB essential modifier/IkappaB kinase-gamma (NEMO/IKKgamma) ubiquitination in the activation of the IkappaB kinase complex by tumor necrosis factor-alpha. J. Biol. Chem. 278:37297-37305.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37297-37305
    • Tang, E.D.1    Wang, C.Y.2    Xiong, Y.3    Guan, K.L.4
  • 12
    • 11144289688 scopus 로고    scopus 로고
    • The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO
    • Abbott DW, Wilkins A, Asara JM, Cantley LC. 2004. The Crohn's disease protein, NOD2, requires RIP2 in order to induce ubiquitinylation of a novel site on NEMO. Curr. Biol. 14:2217-2227.
    • (2004) Curr. Biol. , vol.14 , pp. 2217-2227
    • Abbott, D.W.1    Wilkins, A.2    Asara, J.M.3    Cantley, L.C.4
  • 13
    • 33644538632 scopus 로고    scopus 로고
    • Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli
    • Wu ZH, Shi Y, Tibbetts RS, Miyamoto S. 2006. Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli. Science 311:1141-1146.
    • (2006) Science , vol.311 , pp. 1141-1146
    • Wu, Z.H.1    Shi, Y.2    Tibbetts, R.S.3    Miyamoto, S.4
  • 14
    • 0344305376 scopus 로고    scopus 로고
    • Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress
    • Huang TT, Wuerzberger-Davis SM, Wu ZH, Miyamoto S. 2003. Sequential modification of NEMO/IKKgamma by SUMO-1 and ubiquitin mediates NF-kappaB activation by genotoxic stress. Cell 115:565-576.
    • (2003) Cell , vol.115 , pp. 565-576
    • Huang, T.T.1    Wuerzberger-Davis, S.M.2    Wu, Z.H.3    Miyamoto, S.4
  • 15
    • 63649144413 scopus 로고    scopus 로고
    • Principles of ubiquitin and Sumo modifications in DNA repair
    • Bergink S, Jentsch S. 2009. Principles of ubiquitin and Sumo modifications in DNA repair. Nature 458:461-467.
    • (2009) Nature , vol.458 , pp. 461-467
    • Bergink, S.1    Jentsch, S.2
  • 16
    • 0034806402 scopus 로고    scopus 로고
    • Sites on FIP-3 (NEMO/IKKgamma) essential for its phosphorylation and NF-kappaB modulating activity
    • Tarassishin L, Horwitz MS. 2001. Sites on FIP-3 (NEMO/IKKgamma) essential for its phosphorylation and NF-kappaB modulating activity. Biochem. Biophys. Res. Commun. 285:555-560.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 555-560
    • Tarassishin, L.1    Horwitz, M.S.2
  • 17
    • 0037024696 scopus 로고    scopus 로고
    • Regulation of Ikappa B kinase (IKK-)gamma /NEMO function by IKKbeta-mediated phosphorylation
    • Prajapati S, Gaynor RB. 2002. Regulation of Ikappa B kinase (IKK-)gamma /NEMO function by IKKbeta-mediated phosphorylation. J. Biol. Chem. 277:24331-24339.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24331-24339
    • Prajapati, S.1    Gaynor, R.B.2
  • 18
    • 0038143356 scopus 로고    scopus 로고
    • In vivo identification of inducible phosphoacceptors in the IKKgamma/NEMO subunit of human IkappaB kinase
    • Carter RS, Pennington KN, Ungurait BJ, Ballard DW. 2003. In vivo identification of inducible phosphoacceptors in the IKKgamma/NEMO subunit of human IkappaB kinase. J. Biol. Chem. 278:19642-19648.
    • (2003) J. Biol. Chem. , vol.278 , pp. 19642-19648
    • Carter, R.S.1    Pennington, K.N.2    Ungurait, B.J.3    Ballard, D.W.4
  • 19
    • 0035913278 scopus 로고    scopus 로고
    • TAK1 is a ubiquitin-dependent kinase of MKK and IKK
    • Wang C, et al. 2001. TAK1 is a ubiquitin-dependent kinase of MKK and IKK. Nature 412:346-351.
    • (2001) Nature , vol.412 , pp. 346-351
    • Wang, C.1
  • 20
    • 17944378526 scopus 로고    scopus 로고
    • Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway
    • Senftleben U, et al. 2001. Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway. Science 293:1495-1499.
    • (2001) Science , vol.293 , pp. 1495-1499
    • Senftleben, U.1
  • 21
    • 0032583947 scopus 로고    scopus 로고
    • NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of ser-176
    • U. S. A
    • Ling L, Cao Z, Goeddel DV. 1998. NF-kappaB-inducing kinase activates IKK-alpha by phosphorylation of ser-176. Proc. Natl. Acad. Sci. U. S. A. 95:3792-3797.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 3792-3797
    • Ling, L.1    Cao, Z.2    Goeddel, D.V.3
  • 22
    • 0033537719 scopus 로고    scopus 로고
    • Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation
    • Delhase M, Hayakawa M, Chen Y, Karin M. 1999. Positive and negative regulation of IkappaB kinase activity through IKKbeta subunit phosphorylation. Science 284:309-313.
    • (1999) Science , vol.284 , pp. 309-313
    • Delhase, M.1    Hayakawa, M.2    Chen, Y.3    Karin, M.4
  • 23
    • 33750433585 scopus 로고    scopus 로고
    • Manipulation of the nuclear factor-kappaB pathway and the innate immune response by viruses
    • Hiscott J, Nguyen TL, Arguello M, Nakhaei P, Paz S. 2006. Manipulation of the nuclear factor-kappaB pathway and the innate immune response by viruses. Oncogene 25:6844-6867.
    • (2006) Oncogene , vol.25 , pp. 6844-6867
    • Hiscott, J.1    Nguyen, T.L.2    Arguello, M.3    Nakhaei, P.4    Paz, S.5
  • 24
    • 77951192990 scopus 로고    scopus 로고
    • KSHV and the pathogenesis of Kaposi sarcoma: Listening to human biology and medicine
    • Ganem D. 2010. KSHV and the pathogenesis of Kaposi sarcoma: listening to human biology and medicine. J. Clin. Invest. 120:939-949.
    • (2010) J. Clin. Invest. , vol.120 , pp. 939-949
    • Ganem, D.1
  • 25
    • 0030970013 scopus 로고    scopus 로고
    • Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors
    • Thome M, et al. 1997. Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors. Nature 386:517-521.
    • (1997) Nature , vol.386 , pp. 517-521
    • Thome, M.1
  • 26
    • 0030950228 scopus 로고    scopus 로고
    • A novel family of viral death effector domain-containing molecules that inhibit both CD-95- and tumor necrosis factor receptor-1-induced apoptosis
    • Hu S, Vincenz C, Buller M, Dixit VM. 1997. A novel family of viral death effector domain-containing molecules that inhibit both CD-95- and tumor necrosis factor receptor-1-induced apoptosis. J. Biol. Chem. 272: 9621-9624.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9621-9624
    • Hu, S.1    Vincenz, C.2    Buller, M.3    Dixit, V.M.4
  • 27
    • 12644286556 scopus 로고    scopus 로고
    • Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis
    • U. S. A
    • Bertin J, et al. 1997. Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis. Proc. Natl. Acad. Sci. U. S. A. 94:1172-1176.
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 1172-1176
    • Bertin, J.1
  • 28
    • 0346101776 scopus 로고    scopus 로고
    • The human herpes virus 8-encoded viral FLICE-inhibitory protein induces cellular transformation via NF-kappaB activation
    • Sun Q, Zachariah S, Chaudhary PM. 2003. The human herpes virus 8-encoded viral FLICE-inhibitory protein induces cellular transformation via NF-kappaB activation. J. Biol. Chem. 278:52437-52445.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52437-52445
    • Sun, Q.1    Zachariah, S.2    Chaudhary, P.M.3
  • 29
    • 0037134478 scopus 로고    scopus 로고
    • The human herpes virus 8-encoded viral FLICE inhibitory protein physically associates with and persistently activates the Ikappa B kinase complex
    • Liu L, et al. 2002. The human herpes virus 8-encoded viral FLICE inhibitory protein physically associates with and persistently activates the Ikappa B kinase complex. J. Biol. Chem. 277:13745-13751.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13745-13751
    • Liu, L.1
  • 30
    • 0141502126 scopus 로고    scopus 로고
    • KSHV vFLIP binds to IKK-gamma to activate IKK
    • Field N, et al. 2003. KSHV vFLIP binds to IKK-gamma to activate IKK. J. Cell Sci. 116:3721-3728.
    • (2003) J. Cell Sci. , vol.116 , pp. 3721-3728
    • Field, N.1
  • 31
    • 0033554648 scopus 로고    scopus 로고
    • Modulation of the NF-kappa B pathway by virally encoded death effector domainscontaining proteins
    • Chaudhary PM, Jasmin A, Eby MT, Hood L. 1999. Modulation of the NF-kappa B pathway by virally encoded death effector domainscontaining proteins. Oncogene 18:5738-5746.
    • (1999) Oncogene , vol.18 , pp. 5738-5746
    • Chaudhary, P.M.1    Jasmin, A.2    Eby, M.T.3    Hood, L.4
  • 32
    • 70549086229 scopus 로고    scopus 로고
    • Large-scale proteomics analysis of the human kinome
    • Oppermann FS, et al. 2009. Large-scale proteomics analysis of the human kinome. Mol. Cell. Proteomics 8:1751-1764.
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 1751-1764
    • Oppermann, F.S.1
  • 33
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • Zandi E, Rothwarf DM, Delhase M, Hayakawa M, Karin M. 1997. The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 91:243-252.
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1    Rothwarf, D.M.2    Delhase, M.3    Hayakawa, M.4    Karin, M.5
  • 34
    • 0032541657 scopus 로고    scopus 로고
    • IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex
    • Rothwarf DM, Zandi E, Natoli G, Karin M. 1998. IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex. Nature 395: 297-300.
    • (1998) Nature , vol.395 , pp. 297-300
    • Rothwarf, D.M.1    Zandi, E.2    Natoli, G.3    Karin, M.4
  • 35
    • 42949159409 scopus 로고    scopus 로고
    • Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site
    • Rushe M, et al. 2008. Structure of a NEMO/IKK-associating domain reveals architecture of the interaction site. Structure 16:798-808.
    • (2008) Structure , vol.16 , pp. 798-808
    • Rushe, M.1
  • 36
    • 0034284715 scopus 로고    scopus 로고
    • Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex
    • May MJ, et al. 2000. Selective inhibition of NF-kappaB activation by a peptide that blocks the interaction of NEMO with the IkappaB kinase complex. Science 289:1550-1554.
    • (2000) Science , vol.289 , pp. 1550-1554
    • May, M.J.1
  • 37
    • 0037332580 scopus 로고    scopus 로고
    • Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation
    • Tegethoff S, Behlke J, Scheidereit C. 2003. Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation. Mol. Cell. Biol. 23:2029-2041.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2029-2041
    • Tegethoff, S.1    Behlke, J.2    Scheidereit, C.3
  • 38
    • 0037124036 scopus 로고    scopus 로고
    • NEMO trimerizes through its coiled-coil C-terminal domain
    • Agou F, et al. 2002. NEMO trimerizes through its coiled-coil C-terminal domain. J. Biol. Chem. 277:17464-17475.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17464-17475
    • Agou, F.1
  • 39
    • 49449085504 scopus 로고    scopus 로고
    • A quantitative atlas of mitotic phosphorylation
    • U. S. A
    • Dephoure N, et al. 2008. A quantitative atlas of mitotic phosphorylation. Proc. Natl. Acad. Sci. U. S. A. 105:10762-10767.
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , pp. 10762-10767
    • Dephoure, N.1
  • 40
    • 1642528831 scopus 로고    scopus 로고
    • Post-translational modifications and their biological functions: Proteomic analysis and systematic approaches
    • Seo J, Lee KJ. 2004. Post-translational modifications and their biological functions: proteomic analysis and systematic approaches. J. Biochem. Mol. Biol. 37:35-44.
    • (2004) J. Biochem. Mol. Biol. , vol.37 , pp. 35-44
    • Seo, J.1    Lee, K.J.2
  • 41
    • 0034718693 scopus 로고    scopus 로고
    • Activation of IKKalpha and IKKbeta through their fusion with HTLV-I tax protein
    • Xiao G, Sun SC. 2000. Activation of IKKalpha and IKKbeta through their fusion with HTLV-I tax protein. Oncogene 19:5198-5203.
    • (2000) Oncogene , vol.19 , pp. 5198-5203
    • Xiao, G.1    Sun, S.C.2
  • 42
    • 0033580931 scopus 로고    scopus 로고
    • Role of adapter function in oncoprotein-mediated activation of NF-kappaB. Human T-cell leukemia virus type I tax interacts directly with IkappaB kinase gamma
    • Jin DY, Giordano V, Kibler KV, Nakano H, Jeang KT. 1999. Role of adapter function in oncoprotein-mediated activation of NF-kappaB. Human T-cell leukemia virus type I tax interacts directly with IkappaB kinase gamma. J. Biol. Chem. 274:17402-17405.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17402-17405
    • Jin, D.Y.1    Giordano, V.2    Kibler, K.V.3    Nakano, H.4    Jeang, K.T.5
  • 43
    • 0347362814 scopus 로고    scopus 로고
    • Molecular genetic analysis of human herpes virus 8-encoded viral FLICE inhibitory proteininduced NF-kappaB activation
    • Matta H, Sun Q, Moses G, Chaudhary PM. 2003. Molecular genetic analysis of human herpes virus 8-encoded viral FLICE inhibitory proteininduced NF-kappaB activation. J. Biol. Chem. 278:52406-52411.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52406-52411
    • Matta, H.1    Sun, Q.2    Moses, G.3    Chaudhary, P.M.4
  • 44
    • 77951228086 scopus 로고    scopus 로고
    • Protein-protein interactions involving IKKgamma (NEMO) that promote the activation of NF-kappaB
    • Shifera AS. 2010. Protein-protein interactions involving IKKgamma (NEMO) that promote the activation of NF-kappaB. J. Cell. Physiol. 223: 558-561.
    • (2010) J. Cell. Physiol. , vol.223 , pp. 558-561
    • Shifera, A.S.1
  • 45
    • 77953026286 scopus 로고    scopus 로고
    • Proteins that bind to IKKgamma (NEMO) and downregulate the activation of NF-kappaB
    • Shifera AS. 2010. Proteins that bind to IKKgamma (NEMO) and downregulate the activation of NF-kappaB. Biochem. Biophys. Res. Commun. 396:585-589.
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 585-589
    • Shifera, A.S.1
  • 46
    • 3042689762 scopus 로고    scopus 로고
    • Activation of alternative NF-kappa B pathway by human herpes virus 8-encoded Fas-associated death domainlike IL-1 beta-converting enzyme inhibitory protein (vFLIP)
    • U. S. A
    • Matta H, Chaudhary PM. 2004. Activation of alternative NF-kappa B pathway by human herpes virus 8-encoded Fas-associated death domainlike IL-1 beta-converting enzyme inhibitory protein (vFLIP). Proc. Natl. Acad. Sci. U. S. A. 101:9399-9404.
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 9399-9404
    • Matta, H.1    Chaudhary, P.M.2
  • 47
    • 79960390341 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus vFLIP and human T cell lymphotropic virus type 1 tax oncogenic proteins activate IkappaB kinase subunit gamma by different mechanisms independent of the physiological cytokine-induced pathways
    • Shimizu A, et al. 2011. Kaposi's sarcoma-associated herpesvirus vFLIP and human T cell lymphotropic virus type 1 tax oncogenic proteins activate IkappaB kinase subunit gamma by different mechanisms independent of the physiological cytokine-induced pathways. J. Virol. 85: 7444-7448.
    • (2011) J. Virol. , vol.85 , pp. 7444-7448
    • Shimizu, A.1
  • 48
    • 33947418102 scopus 로고    scopus 로고
    • Herpesvirus saimiri STP-A oncoprotein utilizes Src family protein tyrosine kinase and tumor necrosis factor receptor-associated factors to elicit cellular signal transduction
    • Garcia MI, Kaserman J, Chung YH, Jung JU, Lee SH. 2007. Herpesvirus saimiri STP-A oncoprotein utilizes Src family protein tyrosine kinase and tumor necrosis factor receptor-associated factors to elicit cellular signal transduction. J. Virol. 81:2663-2674.
    • (2007) J. Virol. , vol.81 , pp. 2663-2674
    • Garcia, M.I.1    Kaserman, J.2    Chung, Y.H.3    Jung, J.U.4    Lee, S.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.