메뉴 건너뛰기




Volumn 49, Issue 50, 2010, Pages 10728-10736

Dynamic origins of differential RNA binding function in two dsRBDs from the miRNA "Microprocessor" complex

Author keywords

[No Author keywords available]

Indexed keywords

BASE PAIRING; BINDING DOMAIN; BINDING MECHANISMS; CELLULAR HOMEOSTASIS; DYNAMIC FEATURES; ELECTROPHORETIC MOBILITY SHIFT ASSAY; GENE REGULATIONS; MD SIMULATION; MICRORNAS; RNA BINDING; SOLUTION DYNAMICS; SOLUTION STRUCTURES; SPIN RELAXATION;

EID: 78650396433     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1015716     Document Type: Article
Times cited : (21)

References (68)
  • 1
    • 58249088751 scopus 로고    scopus 로고
    • MicroRNAs: Target recognition and regulatory functions
    • Bartel, D. P. (2009) MicroRNAs: target recognition and regulatory functions Cell 136, 215-230
    • (2009) Cell , vol.136 , pp. 215-230
    • Bartel, D.P.1
  • 2
    • 34147149312 scopus 로고    scopus 로고
    • A developmental view of microRNA function
    • Zhao, Y. and Srivastava, D. (2007) A developmental view of microRNA function Trends Biochem. Sci. 32, 189-197
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 189-197
    • Zhao, Y.1    Srivastava, D.2
  • 3
    • 60149095444 scopus 로고    scopus 로고
    • Most mammalian mRNAs are conserved targets of microRNAs
    • Friedman, R. C., Farh, K. K. H., Burge, C. B., and Bartel, D. P. (2009) Most mammalian mRNAs are conserved targets of microRNAs Genome Res. 19, 92-105
    • (2009) Genome Res. , vol.19 , pp. 92-105
    • Friedman, R.C.1    Farh, K.K.H.2    Burge, C.B.3    Bartel, D.P.4
  • 4
    • 52449117077 scopus 로고    scopus 로고
    • MicroRNA epigenetic alterations: Predicting biomarkers and therapeutic targets in human diseases
    • Wang, Y., Liang, Y., and Lu, Q. (2008) MicroRNA epigenetic alterations: predicting biomarkers and therapeutic targets in human diseases Clin. Genet. 74, 307-315
    • (2008) Clin. Genet. , vol.74 , pp. 307-315
    • Wang, Y.1    Liang, Y.2    Lu, Q.3
  • 5
    • 34250841756 scopus 로고    scopus 로고
    • MicroRNAs in human cancer: From research to therapy
    • Negrini, M., Ferracin, M., Sabbioni, S., and Croce, C. M. (2007) MicroRNAs in human cancer: from research to therapy J. Cell Sci. 120, 1833-1840
    • (2007) J. Cell Sci. , vol.120 , pp. 1833-1840
    • Negrini, M.1    Ferracin, M.2    Sabbioni, S.3    Croce, C.M.4
  • 6
    • 38749095507 scopus 로고    scopus 로고
    • The expression of microRNA miR-107 decreases early in Alzheimer's disease and may accelerate disease progression through regulation of beta-site amyloid precursor protein-cleaving enzyme 1
    • Wang, W. X., Rajeev, B. W., Stromberg, A. J., Ren, N., Tang, G. L., Huang, Q. W., Rigoutsos, I., and Nelson, P. T. (2008) The expression of microRNA miR-107 decreases early in Alzheimer's disease and may accelerate disease progression through regulation of beta-site amyloid precursor protein-cleaving enzyme 1 J. Neurosci. 28, 1213-1223
    • (2008) J. Neurosci. , vol.28 , pp. 1213-1223
    • Wang, W.X.1    Rajeev, B.W.2    Stromberg, A.J.3    Ren, N.4    Tang, G.L.5    Huang, Q.W.6    Rigoutsos, I.7    Nelson, P.T.8
  • 7
    • 58149143288 scopus 로고    scopus 로고
    • The emerging role of microRNAs in cardiac remodeling and heart failure
    • Divakaran, V. and Mann, D. L. (2008) The emerging role of microRNAs in cardiac remodeling and heart failure Circ. Res. 103, 1072-1083
    • (2008) Circ. Res. , vol.103 , pp. 1072-1083
    • Divakaran, V.1    Mann, D.L.2
  • 8
  • 9
    • 58749113430 scopus 로고    scopus 로고
    • A three-dimensional view of the molecular machinery of RNA interference
    • Jinek, M. and Doudna, J. A. (2009) A three-dimensional view of the molecular machinery of RNA interference Nature 457, 405-412
    • (2009) Nature , vol.457 , pp. 405-412
    • Jinek, M.1    Doudna, J.A.2
  • 10
    • 0031860374 scopus 로고    scopus 로고
    • RNA recognition by RNP proteins during RNA processing
    • Varani, G. and Nagai, K. (1998) RNA recognition by RNP proteins during RNA processing Annu. Rev. Biophys. Biomol. 27, 407-445
    • (1998) Annu. Rev. Biophys. Biomol. , vol.27 , pp. 407-445
    • Varani, G.1    Nagai, K.2
  • 11
    • 66649131084 scopus 로고    scopus 로고
    • Structural and functional modules in RNA interference
    • Nowotny, M. and Yang, W. (2009) Structural and functional modules in RNA interference Curr. Opin. Biol. 19, 286-293
    • (2009) Curr. Opin. Biol. , vol.19 , pp. 286-293
    • Nowotny, M.1    Yang, W.2
  • 12
    • 77951964981 scopus 로고    scopus 로고
    • Posttranscriptional regulation of microRNA biogenesis in animals
    • Siomi, H. and Siomi, M. C. (2010) Posttranscriptional regulation of microRNA biogenesis in animals Mol. Cell 38, 323-332
    • (2010) Mol. Cell , vol.38 , pp. 323-332
    • Siomi, H.1    Siomi, M.C.2
  • 13
    • 0032535613 scopus 로고    scopus 로고
    • Molecular basis of double-stranded RNA-protein interactions: Structure of a dsRNA-binding domain complexed with dsRNA
    • Ryter, J. M. and Schultz, S. C. (1998) Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA EMBO J. 17, 7505-7513
    • (1998) EMBO J. , vol.17 , pp. 7505-7513
    • Ryter, J.M.1    Schultz, S.C.2
  • 16
    • 0037711199 scopus 로고    scopus 로고
    • The dsRNA binding protein family: Critical roles, diverse cellular functions
    • Saunders, L. R. and Barber, G. N. (2003) The dsRNA binding protein family: critical roles, diverse cellular functions FASEB J. 17, 961-983
    • (2003) FASEB J. , vol.17 , pp. 961-983
    • Saunders, L.R.1    Barber, G.N.2
  • 17
    • 0029782652 scopus 로고    scopus 로고
    • Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR
    • Bevilacqua, P. C. and Cech, T. R. (1996) Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR Biochemistry 35, 9983-9994
    • (1996) Biochemistry , vol.35 , pp. 9983-9994
    • Bevilacqua, P.C.1    Cech, T.R.2
  • 18
    • 0026713151 scopus 로고
    • Interactions between double-stranded RNA regulators and the protein kinase DAI
    • Manche, L., Green, S. R., Schmedt, C., and Mathews, M. B. (1992) Interactions between double-stranded RNA regulators and the protein kinase DAI Mol. Cell. Biol. 12, 5238-5248
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 5238-5248
    • Manche, L.1    Green, S.R.2    Schmedt, C.3    Mathews, M.B.4
  • 20
    • 18444380595 scopus 로고    scopus 로고
    • The double-stranded RNA-binding motif, a versatile macromolecular docking platform
    • Chang, K. Y. and Ramos, A. (2005) The double-stranded RNA-binding motif, a versatile macromolecular docking platform FEBS J. 272, 2109-2117
    • (2005) FEBS J. , vol.272 , pp. 2109-2117
    • Chang, K.Y.1    Ramos, A.2
  • 21
    • 0042838304 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA by proteins and small molecules
    • Carlson, C. B., Stephens, O. M., and Beal, P. A. (2003) Recognition of double-stranded RNA by proteins and small molecules Biopolymers 70, 86-102
    • (2003) Biopolymers , vol.70 , pp. 86-102
    • Carlson, C.B.1    Stephens, O.M.2    Beal, P.A.3
  • 23
    • 0036382941 scopus 로고    scopus 로고
    • A functional role for correlated motion in the N-terminal RNA-binding domain of human U1A protein
    • Showalter, S. A. and Hall, K. B. (2002) A functional role for correlated motion in the N-terminal RNA-binding domain of human U1A protein J. Mol. Biol. 322, 533-542
    • (2002) J. Mol. Biol. , vol.322 , pp. 533-542
    • Showalter, S.A.1    Hall, K.B.2
  • 24
    • 0346366805 scopus 로고    scopus 로고
    • Altering the RNA-binding mode of the U1A RBD1 protein
    • Showalter, S. A. and Hall, K. B. (2004) Altering the RNA-binding mode of the U1A RBD1 protein J. Mol. Biol. 335, 465-480
    • (2004) J. Mol. Biol. , vol.335 , pp. 465-480
    • Showalter, S.A.1    Hall, K.B.2
  • 26
    • 0034675856 scopus 로고    scopus 로고
    • A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR
    • Nanduri, S., Rahman, F., Williams, B. R. G., and Qin, J. (2000) A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR EMBO J. 19, 5567-5574
    • (2000) EMBO J. , vol.19 , pp. 5567-5574
    • Nanduri, S.1    Rahman, F.2    Williams, B.R.G.3    Qin, J.4
  • 27
    • 0029058994 scopus 로고
    • Structure of the dsRNA binding domain of E. coli RNase III
    • Kharrat, A., Macias, M., Gibson, T. J., Nilges, M., and Pastore, A. (1995) Structure of the dsRNA binding domain of E. coli RNase III EMBO J. 14, 3572-3584
    • (1995) EMBO J. , vol.14 , pp. 3572-3584
    • Kharrat, A.1    MacIas, M.2    Gibson, T.J.3    Nilges, M.4    Pastore, A.5
  • 28
    • 0035846580 scopus 로고    scopus 로고
    • Intrinsic double-stranded-RNA processing activity of Escherichia coli ribonuclease III lacking the dsRNA-binding domain
    • Sun, W. M., Jun, E., and Nicholson, A. W. (2001) Intrinsic double-stranded-RNA processing activity of Escherichia coli ribonuclease III lacking the dsRNA-binding domain Biochemistry 40, 14976-14984
    • (2001) Biochemistry , vol.40 , pp. 14976-14984
    • Sun, W.M.1    Jun, E.2    Nicholson, A.W.3
  • 29
    • 3142613181 scopus 로고    scopus 로고
    • Single processing center models for human dicer and bacterial RNase III
    • Zhang, H. D., Kolb, F. A., Jaskiewicz, L., Westhof, E., and Filipowicz, W. (2004) Single processing center models for human dicer and bacterial RNase III Cell 118, 57-68
    • (2004) Cell , vol.118 , pp. 57-68
    • Zhang, H.D.1    Kolb, F.A.2    Jaskiewicz, L.3    Westhof, E.4    Filipowicz, W.5
  • 31
    • 40649086065 scopus 로고    scopus 로고
    • Structural and biochemical insights into the dicing mechanism of mouse Dicer: A conserved lysine is critical for dsRNA cleavage
    • Du, Z., Lee, J. K., Tjhen, R., Stroud, R. M., and James, T. L. (2008) Structural and biochemical insights into the dicing mechanism of mouse Dicer: a conserved lysine is critical for dsRNA cleavage Proc. Natl. Acad. Sci. U.S.A. 105, 2391-2396
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 2391-2396
    • Du, Z.1    Lee, J.K.2    Tjhen, R.3    Stroud, R.M.4    James, T.L.5
  • 33
    • 31044448524 scopus 로고    scopus 로고
    • Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III
    • Gan, J. H., Tropea, J. E., Austin, B. P., Court, D. L., Waugh, D. S., and Ji, X. H. (2006) Structural insight into the mechanism of double-stranded RNA processing by ribonuclease III Cell 124, 355-366
    • (2006) Cell , vol.124 , pp. 355-366
    • Gan, J.H.1    Tropea, J.E.2    Austin, B.P.3    Court, D.L.4    Waugh, D.S.5    Ji, X.H.6
  • 35
    • 10644234841 scopus 로고    scopus 로고
    • The Drosha-DGCR8 complex in primary microRNA processing
    • Han, J. J., Lee, Y., Yeom, K. H., Kim, Y. K., Jin, H., and Kim, V. N. (2004) The Drosha-DGCR8 complex in primary microRNA processing Genes Dev. 18, 3016-3027
    • (2004) Genes Dev. , vol.18 , pp. 3016-3027
    • Han, J.J.1    Lee, Y.2    Yeom, K.H.3    Kim, Y.K.4    Jin, H.5    Kim, V.N.6
  • 36
    • 0037273432 scopus 로고    scopus 로고
    • Sequence requirements for micro RNA processing and function in human cells
    • Zeng, Y. and Cullen, B. R. (2003) Sequence requirements for micro RNA processing and function in human cells RNA 9, 112-123
    • (2003) RNA , vol.9 , pp. 112-123
    • Zeng, Y.1    Cullen, B.R.2
  • 37
    • 12544255565 scopus 로고    scopus 로고
    • Recognition and cleavage of primary microRNA precursors by the nuclear processing enzyme Drosha
    • Zeng, Y., Yi, R., and Cullen, B. R. (2005) Recognition and cleavage of primary microRNA precursors by the nuclear processing enzyme Drosha EMBO J. 24, 138-148
    • (2005) EMBO J. , vol.24 , pp. 138-148
    • Zeng, Y.1    Yi, R.2    Cullen, B.R.3
  • 38
    • 33749984008 scopus 로고    scopus 로고
    • Characterization of DGCR8/Pasha, the essential cofactor for Drosha in primary miRNA processing
    • Yeom, K. H., Lee, Y., Han, J. J., Suh, M. R., and Kim, V. N. (2006) Characterization of DGCR8/Pasha, the essential cofactor for Drosha in primary miRNA processing Nucleic Acids Res. 34, 4622-4629
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4622-4629
    • Yeom, K.H.1    Lee, Y.2    Han, J.J.3    Suh, M.R.4    Kim, V.N.5
  • 41
    • 0032530310 scopus 로고    scopus 로고
    • Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation
    • Nanduri, S., Carpick, B. W., Yang, Y. W., Williams, B. R. G., and Qin, J. (1998) Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation EMBO J. 17, 5458-5465
    • (1998) EMBO J. , vol.17 , pp. 5458-5465
    • Nanduri, S.1    Carpick, B.W.2    Yang, Y.W.3    Williams, B.R.G.4    Qin, J.5
  • 42
    • 77954378538 scopus 로고    scopus 로고
    • MD simulations of the dsRBP DGCR8 reveal correlated motions that may aid pri-miRNA binding
    • Wostenberg, C., Noid, W. G., and Showalter, S. A. (2010) MD simulations of the dsRBP DGCR8 reveal correlated motions that may aid pri-miRNA binding Biophys. J. 99, 248-256
    • (2010) Biophys. J. , vol.99 , pp. 248-256
    • Wostenberg, C.1    Noid, W.G.2    Showalter, S.A.3
  • 43
    • 14844361989 scopus 로고    scopus 로고
    • NMR studies of protein structure and dynamics
    • Kay, L. E. (2005) NMR studies of protein structure and dynamics J. Magn. Reson. 173, 193-207
    • (2005) J. Magn. Reson. , vol.173 , pp. 193-207
    • Kay, L.E.1
  • 44
    • 0036189601 scopus 로고    scopus 로고
    • Multidimensional NMR methods for protein structure determination
    • Kanelis, V., Forman-Kay, J. D., and Kay, L. E. (2001) Multidimensional NMR methods for protein structure determination IUBMB Life 52, 291-302
    • (2001) IUBMB Life , vol.52 , pp. 291-302
    • Kanelis, V.1    Forman-Kay, J.D.2    Kay, L.E.3
  • 45
    • 4243155782 scopus 로고    scopus 로고
    • NMR characterization of the dynamics of biomacromolecules
    • Palmer, A. G. (2004) NMR characterization of the dynamics of biomacromolecules Chem. Rev. 104, 3623-3640
    • (2004) Chem. Rev. , vol.104 , pp. 3623-3640
    • Palmer, A.G.1
  • 46
    • 33646911358 scopus 로고    scopus 로고
    • Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences
    • Jarymowycz, V. A. and Stone, M. J. (2006) Fast time scale dynamics of protein backbones: NMR relaxation methods, applications, and functional consequences Chem. Rev. 106, 1624-1671
    • (2006) Chem. Rev. , vol.106 , pp. 1624-1671
    • Jarymowycz, V.A.1    Stone, M.J.2
  • 47
    • 0028941877 scopus 로고
    • Backbone dynamics in Escherichia coli ribonuclease HI correlations with structure and function in an active enzyme
    • Mandel, A. M., Akke, M., and Palmer, A. G. (1995) Backbone dynamics in Escherichia coli ribonuclease HI correlations with structure and function in an active enzyme J. Mol. Biol. 246, 144-163
    • (1995) J. Mol. Biol. , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 48
    • 0029029566 scopus 로고
    • Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
    • Bruschweiler, R., Liao, X. B., and Wright, P. E. (1995) Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling Science 268, 886-889
    • (1995) Science , vol.268 , pp. 886-889
    • Bruschweiler, R.1    Liao, X.B.2    Wright, P.E.3
  • 51
    • 32244437816 scopus 로고    scopus 로고
    • HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations
    • Hornak, V., Okur, A., Rizzo, R. C., and Simmerling, C. (2006) HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations Proc. Natl. Acad. Sci. U.S.A. 103, 915-920
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 915-920
    • Hornak, V.1    Okur, A.2    Rizzo, R.C.3    Simmerling, C.4
  • 54
    • 33846823909 scopus 로고
    • Particle mesh Ewald - an N.Log(N) method for Ewald sums in large systems
    • Darden, T., York, D., and Pedersen, L. (1993) Particle mesh Ewald - an N.Log(N) method for Ewald sums in large systems J. Chem. Phys. 98, 10089-10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 55
    • 35948943745 scopus 로고    scopus 로고
    • Validation of molecular dynamics simulations of biomolecules using NMR spin relaxation as benchmarks: Application to the AMBER99SB force field
    • Showalter, S. A. and Bruschweiler, R. (2007) Validation of molecular dynamics simulations of biomolecules using NMR spin relaxation as benchmarks: application to the AMBER99SB force field J. Chem. Theory Comput. 3, 961-975
    • (2007) J. Chem. Theory Comput. , vol.3 , pp. 961-975
    • Showalter, S.A.1    Bruschweiler, R.2
  • 57
    • 0037165750 scopus 로고    scopus 로고
    • General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation
    • Prompers, J. J. and Bruschweiler, R. (2002) General framework for studying the dynamics of folded and nonfolded proteins by NMR relaxation spectroscopy and MD simulation J. Am. Chem. Soc. 124, 4522-4534
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 4522-4534
    • Prompers, J.J.1    Bruschweiler, R.2
  • 58
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • Lipari, G. and Szabo, A. (1982) Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity J. Am. Chem. Soc. 104, 4546-4559
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 59
    • 33748619206 scopus 로고    scopus 로고
    • An NMR perspective on enzyme dynamics
    • Boehr, D. D., Dyson, H. J., and Wright, P. E. (2006) An NMR perspective on enzyme dynamics Chem. Rev. 106, 3055-3079
    • (2006) Chem. Rev. , vol.106 , pp. 3055-3079
    • Boehr, D.D.1    Dyson, H.J.2    Wright, P.E.3
  • 61
    • 0033117937 scopus 로고    scopus 로고
    • Investigating protein dynamics in collective coordinate space
    • Kitao, A. and Go, N. (1999) Investigating protein dynamics in collective coordinate space Curr. Opin. Struct. Biol. 9, 164-169
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 164-169
    • Kitao, A.1    Go, N.2
  • 64
    • 0034127361 scopus 로고    scopus 로고
    • Collective protein dynamics in relation to function
    • Berendsen, H. J. C. and Hayward, S. (2000) Collective protein dynamics in relation to function Curr. Opin. Struct. Biol. 10, 165-169
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 165-169
    • Berendsen, H.J.C.1    Hayward, S.2
  • 65
    • 33748614305 scopus 로고    scopus 로고
    • Computational and theoretical methods to explore the relation between enzyme dynamics and catalysis
    • Antoniou, D., Basner, J., Nunez, S., and Schwartz, S. D. (2006) Computational and theoretical methods to explore the relation between enzyme dynamics and catalysis Chem. Rev. 106, 3170-3187
    • (2006) Chem. Rev. , vol.106 , pp. 3170-3187
    • Antoniou, D.1    Basner, J.2    Nunez, S.3    Schwartz, S.D.4
  • 66
    • 56249098241 scopus 로고    scopus 로고
    • DsRNA binding properties of RDE-4 and TRBP reflect their distinct roles in RNAi
    • Parker, G. S., Maity, T. S., and Bass, B. L. (2008) dsRNA binding properties of RDE-4 and TRBP reflect their distinct roles in RNAi J. Mol. Biol. 384, 967-979
    • (2008) J. Mol. Biol. , vol.384 , pp. 967-979
    • Parker, G.S.1    Maity, T.S.2    Bass, B.L.3
  • 67
    • 33846700754 scopus 로고    scopus 로고
    • Activation of PKR: An open and shut case?
    • Cole, J. L. (2007) Activation of PKR: an open and shut case? Trends Biochem. Sci. 32, 57-62
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 57-62
    • Cole, J.L.1
  • 68
    • 33846077126 scopus 로고    scopus 로고
    • Mechanism of interaction of the double-stranded RNA (dsRNA) binding domain of protein kinase R with short dsRNA sequences
    • Ucci, J. W., Kobayashi, Y., Choi, G., Alexandrescu, A. T., and Cole, J. L. (2007) Mechanism of interaction of the double-stranded RNA (dsRNA) binding domain of protein kinase R with short dsRNA sequences Biochemistry 46, 55-65
    • (2007) Biochemistry , vol.46 , pp. 55-65
    • Ucci, J.W.1    Kobayashi, Y.2    Choi, G.3    Alexandrescu, A.T.4    Cole, J.L.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.