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Volumn 19, Issue 3, 2013, Pages 295-305

Phosphorylation at intrinsically disordered regions of PAM2 motif-containing proteins modulates their interactions with PABPC1 and influences mRNA fate

Author keywords

Deadenylation; GW182; Intrinsically disordered region; MiRNA function; MRNA turnover; PABP; PAM2 motif; Protein phosphorylation; Translation

Indexed keywords

CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN; CYTOPLASMIC POLYADENYLATION ELEMENT BINDING PROTEIN C1; MESSENGER RNA; NUCLEIC ACID BINDING PROTEIN; NUCLEIC ACID BINDING PROTEIN PAN3; NUCLEIC ACID BINDING PROTEIN TNRC6C; NUCLEIC ACID BINDING PROTEIN TOB2; SERINE; THREONINE; UNCLASSIFIED DRUG;

EID: 84874312261     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.037317.112     Document Type: Article
Times cited : (35)

References (64)
  • 2
    • 80053580757 scopus 로고    scopus 로고
    • GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets
    • Braun JE, Huntzinger E, Fauser M, Izaurralde E. 2011. GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets. Mol Cell 44: 120-133.
    • (2011) Mol Cell , vol.44 , pp. 120-133
    • Braun, J.E.1    Huntzinger, E.2    Fauser, M.3    Izaurralde, E.4
  • 3
    • 84872779494 scopus 로고    scopus 로고
    • Protein Ser/Thr phosphatases-The ugly ducklings of cell signalling
    • doi: 10.1111/j.1742-4658.2012.08609.x
    • Brautigan DL. 2012. Protein Ser/Thr phosphatases-the ugly ducklings of cell signalling. FEBS J doi: 10.1111/j.1742-4658.2012.08609.x.
    • (2012) FEBS J
    • Brautigan, D.L.1
  • 4
    • 84864393412 scopus 로고    scopus 로고
    • The role of mammalian poly(A)-binding proteins in co-ordinating mRNA turnover
    • Brook M, Gray NK. 2012. The role of mammalian poly(A)-binding proteins in co-ordinating mRNA turnover. Biochem Soc Trans 40: 856-864.
    • (2012) Biochem Soc Trans , vol.40 , pp. 856-864
    • Brook, M.1    Gray, N.K.2
  • 5
    • 84855911694 scopus 로고    scopus 로고
    • The multifunctional poly(A)-binding protein (PABP) 1 is subject to extensive dynamic post-translational modification, which molecular modelling suggests plays an important role in co-ordinating its activities
    • Brook M, McCracken L, Reddington JP, Lu ZÄ, Morrice NA, Gray NK. 2012. The multifunctional poly(A)-binding protein (PABP) 1 is subject to extensive dynamic post-translational modification, which molecular modelling suggests plays an important role in co-ordinating its activities. Biochem J 441: 803-812.
    • (2012) Biochem J , vol.441 , pp. 803-812
    • Brook, M.1    McCracken, L.2    Reddington, J.P.3    Lu, Z.A.4    Morrice, N.A.5    Gray, N.K.6
  • 9
    • 84858442444 scopus 로고    scopus 로고
    • Mechanisms of deadenylation-dependent decay
    • Chen CYA, Shyu AB. 2011. Mechanisms of deadenylation-dependent decay. Wiley Interdiscip Rev RNA 2: 167-183.
    • (2011) Wiley Interdiscip Rev RNA , vol.2 , pp. 167-183
    • Chen, C.Y.A.1    Shyu, A.B.2
  • 10
    • 70350780068 scopus 로고    scopus 로고
    • Ago-TNRC6 triggers microRNA-mediated decay by promoting two deadenylation steps
    • Chen C-YA, Zheng D, Xia Z, Shyu A-B. 2009. Ago-TNRC6 triggers microRNA-mediated decay by promoting two deadenylation steps. Nat Struct Mol Biol 16: 1160-1166.
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 1160-1166
    • Chen, C.-Y.A.1    Zheng, D.2    Xia, Z.3    Shyu, A.-B.4
  • 11
    • 3943051423 scopus 로고    scopus 로고
    • Eukaryotic mRNA decapping
    • DOI 10.1146/annurev.biochem.73.011303.074032
    • Coller J, Parker R. 2004. Eukaryotic mRNA decapping. Annu Rev Biochem 74: 861-890. (Pubitemid 39050388)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 861-890
    • Coller, J.1    Parker, R.2
  • 13
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson HJ, Wright PE. 2005. Intrinsically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6: 197-208. (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 14
    • 0141856112 scopus 로고    scopus 로고
    • The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies
    • DOI 10.1261/rna.5810203
    • Eystathioy T, Jakymiw A, Chan EKL, Seraphin B, Cougot N, Fritzler MJ. 2003. The GW182 protein colocalizes with mRNA degradation associated proteins hDcp1 and hLSm4 in cytoplasmic GW bodies. RNA 9: 1171-1173. (Pubitemid 37151671)
    • (2003) RNA , vol.9 , Issue.10 , pp. 1171-1173
    • Eystathioy, T.1    Jakymiw, A.2    Chan, E.K.L.3    Seraphin, B.4    Cougot, N.5    Fritzler, M.J.6
  • 15
    • 36049016095 scopus 로고    scopus 로고
    • Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation
    • DOI 10.1128/MCB.01254-07
    • Ezzeddine N, Chang T-C, Zhu W, Yamashita A, Chen C-YA, Zhong Z, Yamashita Y, Zheng D, Shyu A-B. 2007. Human TOB, an antiproliferative transcription factor, is a poly(A)-binding protein-dependent positive regulator of cytoplasmic mRNA deadenylation. Mol Cell Biol 27: 7791-7801. (Pubitemid 350086413)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.22 , pp. 7791-7801
    • Ezzeddine, N.1    Chang, T.-C.2    Zhu, W.3    Yamashita, A.4    Chen, C.-Y.A.5    Zhong, Z.6    Yamashita, Y.7    Zheng, D.8    Shyu, A.-B.9
  • 18
    • 36849079370 scopus 로고    scopus 로고
    • Mechanism of mRNA deadenylation: Evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases
    • DOI 10.1101/gad.1597707
    • Funakoshi Y, Doi Y, Hosoda N, Uchida N, Osawa M, Shimada I, Tsujimoto M, Suzuki T, Katada T, Hoshino S. 2007. Mechanism of mRNA deadenylation: Evidence for a molecular interplay between translation termination factor eRF3 and mRNA deadenylases. Genes Dev 21: 3135-3148. (Pubitemid 350223530)
    • (2007) Genes and Development , vol.21 , Issue.23 , pp. 3135-3148
    • Funakoshi, Y.1    Doi, Y.2    Hosoda, N.3    Uchida, N.4    Osawa, M.5    Shimada, I.6    Tsujimoto, M.7    Suzuki, T.8    Katada, T.9    Hoshino, S.-I.10
  • 19
    • 78651277460 scopus 로고    scopus 로고
    • PHOSIDA 2011: The posttranslational modification database
    • Gnad F, Gunawardena J, Mann M. 2011. PHOSIDA 2011: The posttranslational modification database. Nucleic Acids Res 39: D253-D260.
    • (2011) Nucleic Acids Res , vol.39
    • Gnad, F.1    Gunawardena, J.2    Mann, M.3
  • 20
    • 0033546405 scopus 로고    scopus 로고
    • The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein
    • Hoshino S, Imai M, Kobayashi T, Uchida N, Katada T. 1999. The eukaryotic polypeptide chain releasing factor (eRF3/GSPT) carrying the translation termination signal to the 3'-Poly(A) tail of mRNA. Direct association of erf3/GSPT with polyadenylate-binding protein. J Biol Chem 274: 16677-16680.
    • (1999) J Biol Chem , vol.274 , pp. 16677-16680
    • Hoshino, S.1    Imai, M.2    Kobayashi, T.3    Uchida, N.4    Katada, T.5
  • 21
    • 36749010218 scopus 로고    scopus 로고
    • The age of crosstalk: Phosphorylation, ubiquitination, and beyond
    • DOI 10.1016/j.molcel.2007.11.019, PII S1097276507007988
    • Hunter T. 2007. The age of crosstalk: Phosphorylation, ubiquitination, and beyond. Mol Cell 28: 730-738. (Pubitemid 350217067)
    • (2007) Molecular Cell , vol.28 , Issue.5 , pp. 730-738
    • Hunter, T.1
  • 22
    • 78650258635 scopus 로고    scopus 로고
    • Two PABPC1-binding sites in GW182 proteins promote miRNA-mediated gene silencing
    • Huntzinger E, Braun JE, Heimstadt S, Zekri L, Izaurralde E. 2010. Two PABPC1-binding sites in GW182 proteins promote miRNA-mediated gene silencing. EMBO J 29: 4146-4160.
    • (2010) EMBO J , vol.29 , pp. 4146-4160
    • Huntzinger, E.1    Braun, J.E.2    Heimstadt, S.3    Zekri, L.4    Izaurralde, E.5
  • 24
    • 0033539924 scopus 로고    scopus 로고
    • Tob2, a novel anti-proliferative Tob/BTG1 family member, associates with a component of the CCR4 transcriptional regulatory complex capable of binding cyclin-dependent kinases
    • Ikematsu N, Yoshida Y, Kawamura-Tsuzuku J, Ohsugi M, Onda M, Hirai M, Fujimoto J, Yamamoto T. 1999. Tob2, a novel anti-proliferative Tob/BTG1 family member, associates with a component of the CCR4 transcriptional regulatory complex capable of binding cyclin-dependent kinases. Oncogene 18: 7432-7441. (Pubitemid 30035044)
    • (1999) Oncogene , vol.18 , Issue.52 , pp. 7432-7441
    • Ikematsu, N.1    Yoshida, Y.2    Kawamura-Tsuzuku, J.3    Ohsugi, M.4    Onda, M.5    Hirai, M.6    Fujimoto, J.7    Yamamoto, T.8
  • 25
    • 0002799007 scopus 로고    scopus 로고
    • Poly(A) metabolism and translation: The closed-loop model
    • (ed. JWB Hershey et al.),. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Jacobson A. 1996. Poly(A) metabolism and translation: The closed-loop model. In Translational control (ed. JWB Hershey et al.), pp. 451-480. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1996) Translational Control , pp. 451-480
    • Jacobson, A.1
  • 26
    • 76349104822 scopus 로고    scopus 로고
    • Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation
    • Jinek M, Fabian MR, Coyle SM, Sonenberg N, Doudna JA. 2010. Structural insights into the human GW182-PABC interaction in microRNA-mediated deadenylation. Nat Struct Mol Biol 17: 238-240.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 238-240
    • Jinek, M.1    Fabian, M.R.2    Coyle, S.M.3    Sonenberg, N.4    Doudna, J.A.5
  • 27
    • 0035413607 scopus 로고    scopus 로고
    • Structural basis for control by phosphorylation
    • DOI 10.1021/cr000225s
    • Johnson LN, Lewis RJ. 2001. Structural basis for control by phosphorylation. Chem Rev 101: 2209-2242. (Pubitemid 35373017)
    • (2001) Chemical Reviews , vol.101 , Issue.8 , pp. 2209-2242
    • Johnson, L.N.1    Lewis, R.J.2
  • 29
    • 77956319461 scopus 로고    scopus 로고
    • Molecular basis of eRF3 recognition by the MLLE domain of Poly(A)-binding protein
    • Kozlov G, Gehring K. 2010. Molecular basis of eRF3 recognition by the MLLE domain of Poly(A)-binding protein. PLoS One 5: E10169.
    • (2010) PLoS One , vol.5
    • Kozlov, G.1    Gehring, K.2
  • 32
    • 0042622240 scopus 로고    scopus 로고
    • GlobPlot: Exploring protein sequences for globularity and disorder
    • DOI 10.1093/nar/gkg519
    • Linding R, Russell RB, Neduva V, Gibson TJ. 2003. GlobPlot: Exploring protein sequences for globularity and disorder. Nucleic Acids Res 31: 3701-3708. (Pubitemid 37442227)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3701-3708
    • Linding, R.1    Russell, R.B.2    Neduva, V.3    Gibson, T.J.4
  • 33
    • 0027250384 scopus 로고
    • 3'-end labeling of RNA with recombinant yeast poly(A) polymerase
    • Lingner J, Keller W. 1993. 3'-end labeling of RNA with recombinant yeast poly(A) polymerase. Nucleic Acids Res 21: 2917-2920. (Pubitemid 23220445)
    • (1993) Nucleic Acids Research , vol.21 , Issue.12 , pp. 2917-2920
    • Lingner, J.1    Keller, W.2
  • 35
    • 0038487811 scopus 로고    scopus 로고
    • Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression
    • Mangus DA, Evans MC, Jacobson A. 2003. Poly(A)-binding proteins: Multifunctional scaffolds for the post-transcriptional control of gene expression. Genome Biol 4: 233.
    • (2003) Genome Biol , vol.4 , pp. 233
    • Mangus, D.A.1    Evans, M.C.2    Jacobson, A.3
  • 37
    • 41949099124 scopus 로고    scopus 로고
    • The BTG2 protein is a general activator of mRNA deadenylation
    • DOI 10.1038/emboj.2008.43, PII EMBOJ200843
    • Mauxion F, Faux C, Seraphin B. 2008. The BTG2 protein is a general activator of mRNA deadenylation. EMBO J 27: 1039-1048. (Pubitemid 351508153)
    • (2008) EMBO Journal , vol.27 , Issue.7 , pp. 1039-1048
    • Mauxion, F.1    Faux, C.2    Seraphin, B.3
  • 39
    • 84861839851 scopus 로고    scopus 로고
    • PABP and the poly(A) tail augment microRNA repression by facilitated MiRISC binding
    • Moretti F, Kaiser C, Zdanowicz-Specht A, HentzeMW. 2012. PABP and the poly(A) tail augment microRNA repression by facilitated miRISC binding. Nat Struct Mol Biol 19: 603-608.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 603-608
    • Moretti, F.1    Kaiser, C.2    Zdanowicz-Specht, A.3    Hentze, M.W.4
  • 40
    • 14244256765 scopus 로고    scopus 로고
    • Interaction of anti-proliferative protein Tob with poly(A)-binding protein and inducible poly(A)-binding protein: Implication of Tob in translational control
    • DOI 10.1111/j.1365-2443.2005.00826.x
    • Okochi K, Suzuki T, Inoue J, Matsuda S, Yamamoto T. 2005. Interaction of anti-proliferative protein Tob with poly(A)-binding protein and inducible poly(A)-binding protein: Implication of Tob in translational control. Genes Cells 10: 151-163. (Pubitemid 40287518)
    • (2005) Genes to Cells , vol.10 , Issue.2 , pp. 151-163
    • Okochi, K.1    Suzuki, T.2    Inoue, J.-I.3    Matsuda, S.4    Yamamoto, T.5
  • 41
    • 4644310115 scopus 로고    scopus 로고
    • Tethering of human Ago proteins to mRNA mimics the miRNA-mediated repression of protein synthesis
    • DOI 10.1261/rna.7131604
    • Pillai RS, Artus CG, Filipowicz W. 2004. Tethering of human Ago proteins to mRNA mimics the miRNA-mediated repression of protein synthesis. RNA 10: 1518-1525. (Pubitemid 39288186)
    • (2004) RNA , vol.10 , Issue.10 , pp. 1518-1525
    • Pillai, R.S.1    Artus, C.G.2    Filipowicz, W.3
  • 44
    • 22744437069 scopus 로고    scopus 로고
    • Natively disordered proteins: Functions and predictions
    • DOI 10.2165/00822942-200403020-00005
    • Romero P, Obradovic Z, Dunker AK. 2004. Natively disordered proteins: Functions and predictions. Appl Bioinformatics 3: 105-113. (Pubitemid 41032063)
    • (2004) Applied Bioinformatics , vol.3 , Issue.2-3 , pp. 105-113
    • Romero, P.1    Obradovic, Z.2    Dunker, A.K.3
  • 45
    • 0017382248 scopus 로고
    • Specific inhibition of chromatin associated poly(A) synthesis in vitro by cordycepin 5' triphosphate
    • Rose KM, Bell LE, Jacob ST. 1977. Specific inhibition of chromatin-associated poly(A) synthesis in vitro by cordycepin 5'-triphosphate. Nature 267: 178-180. (Pubitemid 8093499)
    • (1977) Nature , vol.267 , Issue.5607 , pp. 178-180
    • Rose, K.M.1    Bell, L.E.2    Jacob, S.T.3
  • 47
    • 0002411516 scopus 로고    scopus 로고
    • Physical and functional interactions between the mRNA cap structure and the poly(A) tail
    • (ed. N Sonenberg et al.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sachs AB. 2000. Physical and functional interactions between the mRNA cap structure and the poly(A) tail. In Translational control of gene expression (ed. N Sonenberg et al.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (2000) Translational Control of Gene Expression
    • Sachs, A.B.1
  • 49
    • 38949195105 scopus 로고    scopus 로고
    • Messenger RNA regulation: To translate or to degrade
    • DOI 10.1038/sj.emboj.7601977, PII 7601977
    • Shyu AB, Wilkinson MF, van Hoof A. 2008. Messenger RNA regulation: To translate or to degrade. EMBO J 27: 471-481. (Pubitemid 351225677)
    • (2008) EMBO Journal , vol.27 , Issue.3 , pp. 471-481
    • Shyu, A.-B.1    Wilkinson, M.F.2    Van Hoof, A.3
  • 50
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: Mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG. 2009. Regulation of translation initiation in eukaryotes: Mechanisms and biological targets. Cell 136: 731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 53
    • 42249086071 scopus 로고    scopus 로고
    • Integrated analytical strategies for the study of phosphorylation and glycosylation in proteins
    • DOI 10.1002/mas.20164
    • Temporini C, Calleri E, Massolini G, Caccialanza G. 2008. Integrated analytical strategies for the study of phosphorylation and glycosylation in proteins. Mass Spectrom Rev 27: 207-236. (Pubitemid 351547982)
    • (2008) Mass Spectrometry Reviews , vol.27 , Issue.3 , pp. 207-236
    • Temporini, C.1    Calleri, E.2    Massolini, G.3    Caccialanza, G.4
  • 54
    • 78649758708 scopus 로고    scopus 로고
    • Molecular mechanisms of phosphorylation-regulated TTP (tristetraprolin) action and screening for further TTP-interacting proteins
    • Tiedje C, Kotlyarov A, Gaestel M. 2010. Molecular mechanisms of phosphorylation-regulated TTP (tristetraprolin) action and screening for further TTP-interacting proteins. Biochem Soc Trans 38: 1632-1637.
    • (2010) Biochem Soc Trans , vol.38 , pp. 1632-1637
    • Tiedje, C.1    Kotlyarov, A.2    Gaestel, M.3
  • 55
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • DOI 10.1096/fj.04-1584rev
    • Tompa P, Csermely P. 2004. The role of structural disorder in the function of RNA and protein chaperones. FASEB J 18: 1169-1175. (Pubitemid 39006878)
    • (2004) FASEB Journal , vol.18 , Issue.11 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 56
    • 77951622022 scopus 로고    scopus 로고
    • Role of GW182 proteins and PABPC1 in the miRNA pathway: A sense of déjà vu
    • Tritschler F, Huntzinger E, Izaurralde E. 2010. Role of GW182 proteins and PABPC1 in the miRNA pathway: A sense of déjà vu. Nat Rev Mol Cell Biol 11: 379-384.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 379-384
    • Tritschler, F.1    Huntzinger, E.2    Izaurralde, E.3
  • 57
    • 0347093310 scopus 로고    scopus 로고
    • Identification of a Human Cytoplasmic Poly(A) Nuclease Complex Stimulated by Poly(A)-binding Protein
    • DOI 10.1074/jbc.M309125200
    • Uchida N, Hoshino S, Katada T. 2004. Identification of a human cytoplasmic poly(A) nuclease complex stimulated by poly(A)-binding protein. J Biol Chem 279: 1383-1391. (Pubitemid 38082665)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.2 , pp. 1383-1391
    • Uchida, N.1    Hoshino, S.-I.2    Katada, T.3
  • 58
    • 79958741408 scopus 로고    scopus 로고
    • Intrinsically disordered proteins from A to Z
    • Uversky VN. 2011. Intrinsically disordered proteins from A to Z. Int J Biochem Cell Biol 43: 1090-1103.
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 1090-1103
    • Uversky, V.N.1
  • 59
    • 0032112017 scopus 로고    scopus 로고
    • Circularization of mRNA by eukaryotic translation initiation factors
    • Wells SE, Hillner PE, Vale RD, Sachs AB. 1998. Circularization of mRNA by eukaryotic translation initiation factors. Mol Cell 2: 135-140. (Pubitemid 128378975)
    • (1998) Molecular Cell , vol.2 , Issue.1 , pp. 135-140
    • Wells, S.E.1    Hillner, P.E.2    Vale, R.D.3    Sachs, A.B.4
  • 63
    • 71949121493 scopus 로고    scopus 로고
    • The silencing domain of GW182 interacts with PABPC1 to promote translational repression and degradation of microRNA targets and is required for target release
    • Zekri L, Huntzinger E, Heimstadt S, Izaurralde E. 2009. The silencing domain of GW182 interacts with PABPC1 to promote translational repression and degradation of microRNA targets and is required for target release. Mol Cell Biol 29: 6220-6231.
    • (2009) Mol Cell Biol , vol.29 , pp. 6220-6231
    • Zekri, L.1    Huntzinger, E.2    Heimstadt, S.3    Izaurralde, E.4
  • 64
    • 47549087539 scopus 로고    scopus 로고
    • Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells
    • DOI 10.1083/jcb.200801196
    • Zheng D, Ezzeddine N, Chen C-YA, Zhu W, He X, Shyu A-B. 2008. Deadenylation is prerequisite for P-body formation and mRNA decay in mammalian cells. J Cell Biol 182: 89-101. (Pubitemid 352008624)
    • (2008) Journal of Cell Biology , vol.182 , Issue.1 , pp. 89-101
    • Zheng, D.1    Ezzeddine, N.2    Chen, C.-Y.A.3    Zhu, W.4    He, X.5    Shyu, A.-B.6


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