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Volumn 12, Issue 10, 2013, Pages 1569-1577

Cdk9 phosphorylates Pirh2 protein and prevents degradation of p53 protein

Author keywords

Cdk9; HIV 1; P53; Pirh2; Transcription

Indexed keywords

CYCLIN DEPENDENT KINASE 9; PIRH2 PROTEIN; PROTEIN MDM2; PROTEIN P53; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; MDM2 PROTEIN, HUMAN; RCHY1 PROTEIN, HUMAN; SMALL INTERFERING RNA;

EID: 84877991350     PISSN: 15384101     EISSN: 15514005     Source Type: Journal    
DOI: 10.4161/cc.24733     Document Type: Article
Times cited : (17)

References (36)
  • 1
    • 0028216325 scopus 로고
    • PITALRE, a nuclear CDC2-related protein kinase that phosphorylates the retinoblastoma protein in vitro
    • PMID:8170997
    • Graña X, De Luca A, Sang N, Fu Y, Claudio PP, Rosenblatt J, et al. PITALRE, a nuclear CDC2-related protein kinase that phosphorylates the retinoblastoma protein in vitro. Proc Natl Acad Sci USA 1994; 91:3834-8; PMID:8170997; http://dx.doi.org/10.1073/pnas.91.9.3834
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3834-3838
    • Graña, X.1    De Luca, A.2    Sang, N.3    Fu, Y.4    Claudio, P.P.5    Rosenblatt, J.6
  • 2
    • 0028923566 scopus 로고
    • Chromosomal mapping of members of the cdc2 family of protein kinases, cdk3, cdk6, PISSLRE, and PITALRE, and a cdk inhibitor, p27Kip1, to regions involved in human cancer
    • PMID:7882308
    • Bullrich F, MacLachlan TK, Sang NL, Druck T, Veronese ML, Allen SL, et al. Chromosomal mapping of members of the cdc2 family of protein kinases, cdk3, cdk6, PISSLRE, and PITALRE, and a cdk inhibitor, p27Kip1, to regions involved in human cancer. Cancer Res 1995; 55:1199-205; PMID:7882308
    • (1995) Cancer Res , vol.55 , pp. 1199-1205
    • Bullrich, F.1    MacLachlan, T.K.2    Sang, N.L.3    Druck, T.4    Veronese, M.L.5    Allen, S.L.6
  • 3
    • 0032548918 scopus 로고    scopus 로고
    • A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA
    • PMID:9491887
    • Wei P, Garber ME, Fang SM, Fischer WH, Jones KA. A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 1998; 92:451-62; PMID:9491887; http://dx.doi.org/10.1016/S0092-8674(00)80939-3
    • (1998) Cell , vol.92 , pp. 451-462
    • Wei, P.1    Garber, M.E.2    Fang, S.M.3    Fischer, W.H.4    Jones, K.A.5
  • 4
    • 0035891288 scopus 로고    scopus 로고
    • 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes
    • PMID:11713533
    • Nguyen VT, Kiss TS, Michels AA, Bensaude O. 7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes. Nature 2001; 414:322-5; PMID:11713533; http://dx.doi.org/10.1038/35104581
    • (2001) Nature , vol.414 , pp. 322-325
    • Nguyen, V.T.1    Kiss, T.S.2    Michels, A.A.3    Bensaude, O.4
  • 5
    • 33746555497 scopus 로고    scopus 로고
    • Cdk9 phosphorylates p53 on serine 392 independently of CKII
    • PMID:16741955
    • Claudio PP, Cui J, Ghafouri M, Mariano C, White MK, Safak M, et al. Cdk9 phosphorylates p53 on serine 392 independently of CKII. J Cell Physiol 2006; 208:602-12; PMID:16741955; http://dx.doi.org/10.1002/jcp.20698
    • (2006) J Cell Physiol , vol.208 , pp. 602-612
    • Claudio, P.P.1    Cui, J.2    Ghafouri, M.3    Mariano, C.4    White, M.K.5    Safak, M.6
  • 6
    • 37349085275 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus K-cyclin interacts with Cdk9 and stimulates Cdk9-mediated phosphorylation of p53 tumor suppressor
    • PMID:17942552
    • Chang PC, Li M. Kaposi's sarcoma-associated herpesvirus K-cyclin interacts with Cdk9 and stimulates Cdk9-mediated phosphorylation of p53 tumor suppressor. J Virol 2008; 82:278-90; PMID:17942552; http://dx.doi.org/10.1128/ JVI.01552-07
    • (2008) J Virol , vol.82 , pp. 278-290
    • Chang, P.C.1    Li, M.2
  • 7
    • 0034614455 scopus 로고    scopus 로고
    • Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription
    • PMID:10617616
    • O'Keeffe B, Fong Y, Chen D, Zhou S, Zhou Q. Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription. J Biol Chem 2000; 275:279-87; PMID:10617616; http://dx.doi.org/ 10.1074/jbc.275.1.279
    • (2000) J Biol Chem , vol.275 , pp. 279-287
    • O'Keeffe, B.1    Fong, Y.2    Chen, D.3    Zhou, S.4    Zhou, Q.5
  • 8
    • 0033521094 scopus 로고    scopus 로고
    • Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription
    • PMID:10574912
    • Fu TJ, Peng JM, Lee G, Price DH, Flores O. Cyclin K functions as a CDK9 regulatory subunit and participates in RNA polymerase II transcription. J Biol Chem 1999; 274:34527-30; PMID:10574912; http://dx.doi.org/10.1074/jbc.274.49. 34527
    • (1999) J Biol Chem , vol.274 , pp. 34527-34530
    • Fu, T.J.1    Peng, J.M.2    Lee, G.3    Price, D.H.4    Flores, O.5
  • 9
    • 0032858138 scopus 로고    scopus 로고
    • The CDK9-associated cyclins T1 and T2 exert opposite effects on HIV-1 Tat activity
    • PMID:10465067
    • Napolitano G, Licciardo P, Gallo P, Majello B, Giordano A, Lania L. The CDK9-associated cyclins T1 and T2 exert opposite effects on HIV-1 Tat activity. AIDS 1999; 13:1453-9; PMID:10465067; http://dx.doi.org/10.1097/00002030- 199908200-00003
    • (1999) AIDS , vol.13 , pp. 1453-1459
    • Napolitano, G.1    Licciardo, P.2    Gallo, P.3    Majello, B.4    Giordano, A.5    Lania, L.6
  • 10
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • PMID:9153396
    • Kubbutat MHG, Jones SN, Vousden KH. Regulation of p53 stability by Mdm2. Nature 1997; 387:299-303; PMID:9153396; http://dx.doi.org/10.1038/387299a0
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.G.1    Jones, S.N.2    Vousden, K.H.3
  • 11
    • 0037459377 scopus 로고    scopus 로고
    • Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation
    • PMID:12654245
    • Leng RP, Lin YP, Ma WL, Wu H, Lemmers B, Chung S, et al. Pirh2, a p53-induced ubiquitin-protein ligase, promotes p53 degradation. Cell 2003; 112:779-91; PMID:12654245; http://dx.doi.org/10.1016/S0092-8674(03)00193-4
    • (2003) Cell , vol.112 , pp. 779-791
    • Leng, R.P.1    Lin, Y.P.2    Ma, W.L.3    Wu, H.4    Lemmers, B.5    Chung, S.6
  • 12
    • 2342447397 scopus 로고    scopus 로고
    • The ubiquitin ligase COP1 is a critical negative regulator of p53
    • PMID:15103385
    • Dornan D, Wertz I, Shimizu H, Arnott D, Frantz GD, Dowd P, et al. The ubiquitin ligase COP1 is a critical negative regulator of p53. Nature 2004; 429:86-92; PMID:15103385; http://dx.doi.org/10.1038/nature02514
    • (2004) Nature , vol.429 , pp. 86-92
    • Dornan, D.1    Wertz, I.2    Shimizu, H.3    Arnott, D.4    Frantz, G.D.5    Dowd, P.6
  • 13
    • 21244451434 scopus 로고    scopus 로고
    • ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
    • PMID:15989956
    • Chen DL, Kon N, Li MY, Zhang WZ, Qin J, Gu W. ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 2005; 121:1071-83; PMID:15989956; http://dx.doi.org/10.1016/j.cell.2005.03.037
    • (2005) Cell , vol.121 , pp. 1071-1083
    • Chen, D.L.1    Kon, N.2    Li, M.Y.3    Zhang, W.Z.4    Qin, J.5    Gu, W.6
  • 14
    • 75749108557 scopus 로고    scopus 로고
    • Pirh2 E3 ubiquitin ligase targets DNA polymerase eta for 20S proteasomal degradation
    • PMID:20008555
    • Jung YS, Liu G, Chen X. Pirh2 E3 ubiquitin ligase targets DNA polymerase eta for 20S proteasomal degradation. Mol Cell Biol 2010; 30:1041-8; PMID:20008555; http://dx.doi.org/10.1128/MCB.01198-09
    • (2010) Mol Cell Biol , vol.30 , pp. 1041-1048
    • Jung, Y.S.1    Liu, G.2    Chen, X.3
  • 15
    • 34447308810 scopus 로고    scopus 로고
    • Phosphorylation of Pirh2 by calmodulin-dependent kinase II impairs its ability to ubiquitinate p53
    • PMID:17568776
    • Duan S, Yao Z, Hou D, Wu Z, Zhu WG, Wu M. Phosphorylation of Pirh2 by calmodulin-dependent kinase II impairs its ability to ubiquitinate p53. EMBO J 2007; 26:3062-74; PMID:17568776; http://dx.doi.org/10.1038/sj.emboj.7601749
    • (2007) EMBO J , vol.26 , pp. 3062-3074
    • Duan, S.1    Yao, Z.2    Hou, D.3    Wu, Z.4    Zhu, W.G.5    Wu, M.6
  • 16
    • 78649834513 scopus 로고    scopus 로고
    • Transcriptional regulation of HIV-1 gene expression by p53
    • PMID:21088492
    • Mukerjee R, Claudio PP, Chang JR, Del Valle L, Sawaya BE. Transcriptional regulation of HIV-1 gene expression by p53. Cell Cycle 2010; 9:4569-78; PMID:21088492; http://dx.doi.org/10.4161/cc.9.22.13836
    • (2010) Cell Cycle , vol.9 , pp. 4569-4578
    • Mukerjee, R.1    Claudio, P.P.2    Chang, J.R.3    Del Valle, L.4    Sawaya, B.E.5
  • 17
    • 77954383344 scopus 로고    scopus 로고
    • RNA-mediated displacement of an inhibitory snRNP complex activates transcription elongation
    • PMID:20562857
    • D'Orso I, Frankel AD. RNA-mediated displacement of an inhibitory snRNP complex activates transcription elongation. Nat Struct Mol Biol 2010; 17:815-21; PMID:20562857; http://dx.doi.org/10.1038/nsmb.1827
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 815-821
    • D'Orso, I.1    Frankel, A.D.2
  • 18
    • 33751526281 scopus 로고    scopus 로고
    • Inhibition of HIV-1 replication by RNA interference of p53 expression
    • PMID:16844765
    • Pauls E, Senserrich J, Clotet B, Esté JA. Inhibition of HIV-1 replication by RNA interference of p53 expression. J Leukoc Biol 2006; 80:659-67; PMID:16844765; http://dx.doi.org/10.1189/jlb.0306189
    • (2006) J Leukoc Biol , vol.80 , pp. 659-667
    • Pauls, E.1    Senserrich, J.2    Clotet, B.3    Esté, J.A.4
  • 19
    • 0035339357 scopus 로고    scopus 로고
    • ATM-dependent phosphorylation of Mdm2 on serine 395: Role in p53 activation by DNA damage
    • PMID:11331603
    • Maya R, Balass M, Kim ST, Shkedy D, Leal JFM, Shifman O, et al. ATM-dependent phosphorylation of Mdm2 on serine 395: role in p53 activation by DNA damage. Genes Dev 2001; 15:1067-77; PMID:11331603; http://dx.doi.org/10. 1101/gad.886901
    • (2001) Genes Dev , vol.15 , pp. 1067-1077
    • Maya, R.1    Balass, M.2    Kim, S.T.3    Shkedy, D.4    Leal, J.F.M.5    Shifman, O.6
  • 20
    • 31544457877 scopus 로고    scopus 로고
    • p53 ubiquitination: Mdm2 and beyond
    • PMID:16455486
    • Brooks CL, Gu W. p53 ubiquitination: Mdm2 and beyond. Mol Cell 2006; 21:307-15; PMID:16455486; http://dx.doi.org/10.1016/j.molcel.2006.01.020
    • (2006) Mol Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 21
    • 80052728974 scopus 로고    scopus 로고
    • p53 regulation by ubiquitin
    • PMID:21624367
    • Brooks CL, Gu W. p53 regulation by ubiquitin. FEBS Lett 2011; 585:2803-9; PMID:21624367; http://dx.doi.org/10.1016/j.febslet.2011.05.022
    • (2011) FEBS Lett , vol.585 , pp. 2803-2809
    • Brooks, C.L.1    Gu, W.2
  • 22
    • 46949093191 scopus 로고    scopus 로고
    • The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation
    • PMID:18566585
    • Baumli S, Lolli G, Lowe ED, Troiani S, Rusconi L, Bullock AN, et al. The structure of P-TEFb (CDK9/cyclin T1), its complex with flavopiridol and regulation by phosphorylation. EMBO J 2008; 27:1907-18; PMID:18566585; http://dx.doi.org/10.1038/emboj.2008.121
    • (2008) EMBO J , vol.27 , pp. 1907-1918
    • Baumli, S.1    Lolli, G.2    Lowe, E.D.3    Troiani, S.4    Rusconi, L.5    Bullock, A.N.6
  • 23
    • 0029115575 scopus 로고
    • Establishment of human microglial cell lines after transfection of primary cultures of embryonic microglial cells with the SV40 large T antigen
    • PMID:7478261
    • Janabi N, Peudenier S, Héron B, Ng KH, Tardieu M. Establishment of human microglial cell lines after transfection of primary cultures of embryonic microglial cells with the SV40 large T antigen. Neurosci Lett 1995; 195:105-8; PMID:7478261; http://dx.doi.org/10.1016/0304-3940(94)11792-H
    • (1995) Neurosci Lett , vol.195 , pp. 105-108
    • Janabi, N.1    Peudenier, S.2    Héron, B.3    Ng, K.H.4    Tardieu, M.5
  • 24
    • 1642523726 scopus 로고    scopus 로고
    • Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome
    • PMID:14701804
    • Logan IR, Sapountzi V, Gaughan L, Neal DE, Robson CN. Control of human PIRH2 protein stability: involvement of TIP60 and the proteosome. J Biol Chem 2004; 279:11696-704; PMID:14701804; http://dx.doi.org/10.1074/jbc.M312712200
    • (2004) J Biol Chem , vol.279 , pp. 11696-11704
    • Logan, I.R.1    Sapountzi, V.2    Gaughan, L.3    Neal, D.E.4    Robson, C.N.5
  • 25
    • 23044476198 scopus 로고    scopus 로고
    • HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses
    • PMID:16001085
    • Col E, Caron C, Chable-Bessia C, Legube G, Gazzeri S, Komatsu Y, et al. HIV-1 Tat targets Tip60 to impair the apoptotic cell response to genotoxic stresses. EMBO J 2005; 24:2634-45; PMID:16001085; http://dx.doi.org/10.1038/sj. emboj.7600734
    • (2005) EMBO J , vol.24 , pp. 2634-2645
    • Col, E.1    Caron, C.2    Chable-Bessia, C.3    Legube, G.4    Gazzeri, S.5    Komatsu, Y.6
  • 26
    • 79955658113 scopus 로고    scopus 로고
    • TRIM29 negatively regulates p53 via inhibition of Tip60
    • PMID:21463657
    • Sho T, Tsukiyama T, Sato T, Kondo T, Cheng J, Saku T, et al. TRIM29 negatively regulates p53 via inhibition of Tip60. Biochim Biophys Acta 2011; 1813:1245-53; PMID:21463657; http://dx.doi.org/10.1016/j.bbamcr.2011.03.018
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 1245-1253
    • Sho, T.1    Tsukiyama, T.2    Sato, T.3    Kondo, T.4    Cheng, J.5    Saku, T.6
  • 27
    • 0035976987 scopus 로고    scopus 로고
    • TFIIH inhibits CDK9 phosphorylation during human immunodeficiency virus type 1 transcription
    • PMID:11572868
    • Zhou MS, Nekhai S, Bharucha DC, Kumar A, Ge H, Price DH, et al. TFIIH inhibits CDK9 phosphorylation during human immunodeficiency virus type 1 transcription. J Biol Chem 2001; 276:44633-40; PMID:11572868; http://dx.doi.org/10.1074/jbc.M107466200
    • (2001) J Biol Chem , vol.276 , pp. 44633-44640
    • Zhou, M.S.1    Nekhai, S.2    Bharucha, D.C.3    Kumar, A.4    Ge, H.5    Price, D.H.6
  • 28
    • 44649154972 scopus 로고    scopus 로고
    • The multi-tasking P-TEFb complex
    • PMID:18513937
    • Brès V, Yoh SM, Jones KA. The multi-tasking P-TEFb complex. Curr Opin Cell Biol 2008; 20:334-40; PMID:18513937; http://dx.doi.org/10.1016/j.ceb. 2008.04.008
    • (2008) Curr Opin Cell Biol , vol.20 , pp. 334-340
    • Brès, V.1    Yoh, S.M.2    Jones, K.A.3
  • 29
    • 33644758287 scopus 로고    scopus 로고
    • CDK9 phosphorylates p53 on serine residues 33, 315 and 392
    • PMID:16552184
    • Radhakrishnan SK, Gartel AL. CDK9 phosphorylates p53 on serine residues 33, 315 and 392. Cell Cycle 2006; 5:519-21; PMID:16552184; http://dx.doi.org/10. 4161/cc.5.5.2514
    • (2006) Cell Cycle , vol.5 , pp. 519-521
    • Radhakrishnan, S.K.1    Gartel, A.L.2
  • 30
    • 77956399689 scopus 로고    scopus 로고
    • P-TEFb kinase complex phosphorylates histone H1 to regulate expression of cellular and HIV-1 genes
    • PMID:20551309
    • O'Brien SK, Cao H, Nathans R, Ali A, Rana TM. P-TEFb kinase complex phosphorylates histone H1 to regulate expression of cellular and HIV-1 genes. J Biol Chem 2010; 285:29713-20; PMID:20551309; http://dx.doi.org/10.1074/jbc.M110. 125997
    • (2010) J Biol Chem , vol.285 , pp. 29713-29720
    • O'Brien, S.K.1    Cao, H.2    Nathans, R.3    Ali, A.4    Rana, T.M.5
  • 31
    • 9244247669 scopus 로고    scopus 로고
    • Regulation of p53 activity through lysine methylation
    • PMID:15525938
    • Chuikov S, Kurash JK, Wilson JR, Xiao B, Justin N, Ivanov GS, et al. Regulation of p53 activity through lysine methylation. Nature 2004; 432:353-60; PMID:15525938; http://dx.doi.org/10.1038/nature03117
    • (2004) Nature , vol.432 , pp. 353-360
    • Chuikov, S.1    Kurash, J.K.2    Wilson, J.R.3    Xiao, B.4    Justin, N.5    Ivanov, G.S.6
  • 32
    • 0032493627 scopus 로고    scopus 로고
    • Cooperative actions of HIV-1 Vpr and p53 modulate viral gene transcription
    • PMID:9685344
    • Sawaya BE, Khalili K, Mercer WE, Denisova L, Amini S. Cooperative actions of HIV-1 Vpr and p53 modulate viral gene transcription. J Biol Chem 1998; 273:20052-7; PMID:9685344; http://dx.doi.org/10.1074/jbc.273.32.20052
    • (1998) J Biol Chem , vol.273 , pp. 20052-20057
    • Sawaya, B.E.1    Khalili, K.2    Mercer, W.E.3    Denisova, L.4    Amini, S.5
  • 33
    • 0034634585 scopus 로고    scopus 로고
    • Cooperative interaction between HIV-1 regulatory proteins Tat and Vpr modulates transcription of the viral genome
    • PMID:10931842
    • Sawaya BE, Khalili K, Gordon J, Taube R, Amini S. Cooperative interaction between HIV-1 regulatory proteins Tat and Vpr modulates transcription of the viral genome. J Biol Chem 2000; 275:35209-14; PMID:10931842; http://dx.doi.org/10.1074/jbc.M005197200
    • (2000) J Biol Chem , vol.275 , pp. 35209-35214
    • Sawaya, B.E.1    Khalili, K.2    Gordon, J.3    Taube, R.4    Amini, S.5
  • 34
    • 0029813871 scopus 로고    scopus 로고
    • Chicken ovalbumin upstream promoter transcription factor, a transcriptional activator of HIV-1 gene expression in human brain cells
    • PMID:8798567
    • Sawaya BE, Rohr O, Aunis D, Schaeffer E. Chicken ovalbumin upstream promoter transcription factor, a transcriptional activator of HIV-1 gene expression in human brain cells. J Biol Chem 1996; 271:23572-6; PMID:8798567; http://dx.doi.org/10.1074/jbc.271.38.23572
    • (1996) J Biol Chem , vol.271 , pp. 23572-23576
    • Sawaya, B.E.1    Rohr, O.2    Aunis, D.3    Schaeffer, E.4
  • 35
    • 24344474152 scopus 로고    scopus 로고
    • p73 Interacts with human immunodeficiency virus type 1 Tat in astrocytic cells and prevents its acetylation on lysine 28
    • PMID:16135803
    • Amini S, Mameli G, Del Valle L, Skowronska A, Reiss K, Gelman BB, et al. p73 Interacts with human immunodeficiency virus type 1 Tat in astrocytic cells and prevents its acetylation on lysine 28. Mol Cell Biol 2005; 25:8126-38; PMID:16135803; http://dx.doi.org/10.1128/MCB.25.18.8126-8138.2005
    • (2005) Mol Cell Biol , vol.25 , pp. 8126-8138
    • Amini, S.1    Mameli, G.2    Del Valle, L.3    Skowronska, A.4    Reiss, K.5    Gelman, B.B.6
  • 36
    • 66449137818 scopus 로고    scopus 로고
    • Activation of the oxidative stress pathway by HIV-1 Vpr leads to induction of hypoxia-inducible factor 1alpha expression
    • PMID:19204000
    • Deshmane SL, Mukerjee R, Fan S, Del Valle L, Michiels C, Sweet T, et al. Activation of the oxidative stress pathway by HIV-1 Vpr leads to induction of hypoxia-inducible factor 1alpha expression. J Biol Chem 2009; 284:11364-73; PMID:19204000; http://dx.doi.org/10.1074/jbc.M809266200
    • (2009) J Biol Chem , vol.284 , pp. 11364-11373
    • Deshmane, S.L.1    Mukerjee, R.2    Fan, S.3    Del Valle, L.4    Michiels, C.5    Sweet, T.6


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