메뉴 건너뛰기




Volumn 203, Issue 1, 2010, Pages 177-184

Interresidue carbonyl-carbonyl polarization transfer experiments in uniformly 13C,15N-labeled peptides and proteins

Author keywords

Chemical shift anisotropy; Chemical shift correlation spectroscopy; Homonuclear recoupling; Magic angle spinning

Indexed keywords

[CARBONYL; AVERAGE HAMILTONIAN THEORY; BINDING DOMAIN; CHEMICAL SHIFT ANISOTROPY; CORRELATION SPECTROSCOPY; DIPOLAR INTERACTION; DIRECT TRANSFER; HOMONUCLEAR; HOMONUCLEAR RECOUPLING; MAGIC ANGLE SPINNING; MODEL PEPTIDES; POLARIZATION TRANSFER; POSSIBLE FUTURES; RADIO FREQUENCIES; RADIO FREQUENCY FIELDS; RECOUPLING; SPINNING FREQUENCY; VARIABLE AMPLITUDES;

EID: 75749091094     PISSN: 10907807     EISSN: 10960856     Source Type: Journal    
DOI: 10.1016/j.jmr.2009.12.014     Document Type: Article
Times cited : (3)

References (52)
  • 1
    • 0027360175 scopus 로고
    • High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR
    • Ketchem R.R., Hu W., and Cross T.A. High-resolution conformation of gramicidin A in a lipid bilayer by solid-state NMR. Science 261 (1993) 1457-1460
    • (1993) Science , vol.261 , pp. 1457-1460
    • Ketchem, R.R.1    Hu, W.2    Cross, T.A.3
  • 3
    • 0141645622 scopus 로고    scopus 로고
    • Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1
    • Park S.H., Mrse A.A., Nevzorov A.A., Mesleh M.F., Oblatt-Montal M., Montal M., and Opella S.J. Three-dimensional structure of the channel-forming trans-membrane domain of virus protein "u" (Vpu) from HIV-1. J. Mol. Biol. 333 (2003) 409-424
    • (2003) J. Mol. Biol. , vol.333 , pp. 409-424
    • Park, S.H.1    Mrse, A.A.2    Nevzorov, A.A.3    Mesleh, M.F.4    Oblatt-Montal, M.5    Montal, M.6    Opella, S.J.7
  • 4
    • 69549104773 scopus 로고    scopus 로고
    • Conformational heterogeneity of the M2 proton channel and a structural model for channel activation
    • Yi M., Cross T.A., and Zhou H.X. Conformational heterogeneity of the M2 proton channel and a structural model for channel activation. Proc. Natl. Acad. Sci. USA 106 (2009) 13311-13316
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13311-13316
    • Yi, M.1    Cross, T.A.2    Zhou, H.X.3
  • 5
    • 33749049148 scopus 로고    scopus 로고
    • Molecular interactions investigated by multi-dimensional solid-state NMR
    • Baldus M. Molecular interactions investigated by multi-dimensional solid-state NMR. Curr. Opin. Struct. Biol. 16 (2006) 618-623
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 618-623
    • Baldus, M.1
  • 6
    • 34548812858 scopus 로고    scopus 로고
    • Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy
    • Hong M. Structure, topology, and dynamics of membrane peptides and proteins from solid-state NMR spectroscopy. J. Phys. Chem. B 111 (2007) 10340-10351
    • (2007) J. Phys. Chem. B , vol.111 , pp. 10340-10351
    • Hong, M.1
  • 7
    • 67650285019 scopus 로고    scopus 로고
    • Solid state NMR studies of enzymes and membrane proteins
    • McDermott A. Solid state NMR studies of enzymes and membrane proteins. Annu. Rev. Biophys. 38 (2009) 385-403
    • (2009) Annu. Rev. Biophys. , vol.38 , pp. 385-403
    • McDermott, A.1
  • 8
    • 67249096746 scopus 로고    scopus 로고
    • Functional and shunt states of bacteriorhodopsin resolved by 250 GHz dynamic nuclear polarization-enhanced solid-state NMR
    • Bajaj V.S., Mak-Jurkauskas M.L., Belenky M., Herzfeld J., and Griffin R.G. Functional and shunt states of bacteriorhodopsin resolved by 250 GHz dynamic nuclear polarization-enhanced solid-state NMR. Proc. Natl. Acad. Sci. USA (2009)
    • (2009) Proc. Natl. Acad. Sci. USA
    • Bajaj, V.S.1    Mak-Jurkauskas, M.L.2    Belenky, M.3    Herzfeld, J.4    Griffin, R.G.5
  • 9
    • 60149086516 scopus 로고    scopus 로고
    • Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump - structural insights
    • Shi L., Ahmed M.A.M., Zhang W., Whited G., Brown L.S., and Ladizhansky V. Three-dimensional solid-state NMR study of a seven-helical integral membrane proton pump - structural insights. J. Mol. Biol. 386 (2009) 1078-1093
    • (2009) J. Mol. Biol. , vol.386 , pp. 1078-1093
    • Shi, L.1    Ahmed, M.A.M.2    Zhang, W.3    Whited, G.4    Brown, L.S.5    Ladizhansky, V.6
  • 10
    • 71749093086 scopus 로고    scopus 로고
    • Solid-state NMR study of proteorhodopsin in the lipid environment: secondary structure and dynamics
    • Shi L., Lake E.M., Ahmed M.A., Brown L.S., and Ladizhansky V. Solid-state NMR study of proteorhodopsin in the lipid environment: secondary structure and dynamics. Biochim. Biophys. Acta 1788 (2009) 2563-2574
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 2563-2574
    • Shi, L.1    Lake, E.M.2    Ahmed, M.A.3    Brown, L.S.4    Ladizhansky, V.5
  • 12
  • 15
    • 38649130606 scopus 로고    scopus 로고
    • Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy
    • Li Y., Berthold D.A., Gennis R.B., and Rienstra C.M. Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy. Protein Sci. 17 (2008) 199-204
    • (2008) Protein Sci. , vol.17 , pp. 199-204
    • Li, Y.1    Berthold, D.A.2    Gennis, R.B.3    Rienstra, C.M.4
  • 16
    • 85056069017 scopus 로고    scopus 로고
    • Spectral assignment of (membrane) proteins under magic angle spinning
    • Ramamoorthy A. (Ed), Taylor & Francis Group, LLC, Boca Raton, FL
    • Baldus M. Spectral assignment of (membrane) proteins under magic angle spinning. In: Ramamoorthy A. (Ed). NMR Spectroscopy of Biological Solids (2006), Taylor & Francis Group, LLC, Boca Raton, FL 39-56
    • (2006) NMR Spectroscopy of Biological Solids , pp. 39-56
    • Baldus, M.1
  • 17
    • 0035795429 scopus 로고    scopus 로고
    • Backbone and side-chain C-13 and N-15 signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 tesla
    • Pauli J., Baldus M., van Rossum B., de Groot H., and Oschkinat H. Backbone and side-chain C-13 and N-15 signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 tesla. ChemBioChem 2 (2001) 272-281
    • (2001) ChemBioChem , vol.2 , pp. 272-281
    • Pauli, J.1    Baldus, M.2    van Rossum, B.3    de Groot, H.4    Oschkinat, H.5
  • 18
    • 34548504572 scopus 로고    scopus 로고
    • Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins
    • Franks W.T., Kloepper K.D., Wylie B.J., and Rienstra C.M. Four-dimensional heteronuclear correlation experiments for chemical shift assignment of solid proteins. J. Biomol. NMR 39 (2007) 107-131
    • (2007) J. Biomol. NMR , vol.39 , pp. 107-131
    • Franks, W.T.1    Kloepper, K.D.2    Wylie, B.J.3    Rienstra, C.M.4
  • 19
    • 33846430490 scopus 로고    scopus 로고
    • Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy
    • Etzkorn M., Martell S., Andronesi O.C., Seidel K., Engelhard M., and Baldus M. Secondary structure, dynamics, and topology of a seven-helix receptor in native membranes, studied by solid-state NMR spectroscopy. Angew. Chem. Int. Ed. 46 (2007) 459-462
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 459-462
    • Etzkorn, M.1    Martell, S.2    Andronesi, O.C.3    Seidel, K.4    Engelhard, M.5    Baldus, M.6
  • 20
    • 0033121307 scopus 로고    scopus 로고
    • Selective and extensive C-13 labeling of a membrane protein for solid-state NMR investigations
    • Hong M., and Jakes K. Selective and extensive C-13 labeling of a membrane protein for solid-state NMR investigations. J. Biomol. NMR 14 (1999) 71-74
    • (1999) J. Biomol. NMR , vol.14 , pp. 71-74
    • Hong, M.1    Jakes, K.2
  • 21
    • 68349098894 scopus 로고    scopus 로고
    • Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins
    • Higman V.A., Flinders J., Hiller M., Jehle S., Markovic S., Fiedler S., van Rossum B.J., and Oschkinat H. Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins. J. Biomol. NMR 44 (2009) 245-260
    • (2009) J. Biomol. NMR , vol.44 , pp. 245-260
    • Higman, V.A.1    Flinders, J.2    Hiller, M.3    Jehle, S.4    Markovic, S.5    Fiedler, S.6    van Rossum, B.J.7    Oschkinat, H.8
  • 23
    • 11444258696 scopus 로고    scopus 로고
    • Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. Resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation
    • Marulanda D., Tasayco M.L., McDermott A., Cataldi M., Arriaran V., and Polenova T. Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. Resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation. J. Am. Chem. Soc. 126 (2004) 16608-16620
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 16608-16620
    • Marulanda, D.1    Tasayco, M.L.2    McDermott, A.3    Cataldi, M.4    Arriaran, V.5    Polenova, T.6
  • 24
    • 33644942810 scopus 로고    scopus 로고
    • Backbone conformational constraints in a microcrystalline U-N-15-labeled protein by 3D dipolar-shift solid-state NMR spectroscopy
    • Franks W.T., Wylie B.J., Stellfox S.A., and Rienstra C.M. Backbone conformational constraints in a microcrystalline U-N-15-labeled protein by 3D dipolar-shift solid-state NMR spectroscopy. J. Am. Chem. Soc. 128 (2006) 3154-3155
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3154-3155
    • Franks, W.T.1    Wylie, B.J.2    Stellfox, S.A.3    Rienstra, C.M.4
  • 25
    • 0034700129 scopus 로고    scopus 로고
    • Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils
    • Antzutkin O.N., Balbach J.J., Leapman R.D., Rizzo N.W., Reed J., and Tycko R. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils. Proc. Natl. Acad. Sci. USA 97 (2000) 13045-13050
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13045-13050
    • Antzutkin, O.N.1    Balbach, J.J.2    Leapman, R.D.3    Rizzo, N.W.4    Reed, J.5    Tycko, R.6
  • 27
    • 39549090438 scopus 로고    scopus 로고
    • Determination of peptide backbone torsion angles using double-quantum dipolar recoupling solid-state NMR spectroscopy
    • Mehta M.A., Eddy M.T., McNeill S.A., Mills F.D., and Long J.R. Determination of peptide backbone torsion angles using double-quantum dipolar recoupling solid-state NMR spectroscopy. J. Am. Chem. Soc. 130 (2008) 2202-2212
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 2202-2212
    • Mehta, M.A.1    Eddy, M.T.2    McNeill, S.A.3    Mills, F.D.4    Long, J.R.5
  • 28
    • 0035872678 scopus 로고    scopus 로고
    • C-13-C-13 dipolar recoupling under very fast magic angle spinning in solid-state nuclear magnetic resonance: applications to distance measurements, spectral assignments, and high-throughput secondary-structure determination
    • Ishii Y. C-13-C-13 dipolar recoupling under very fast magic angle spinning in solid-state nuclear magnetic resonance: applications to distance measurements, spectral assignments, and high-throughput secondary-structure determination. J. Chem. Phys. 114 (2001) 8473-8483
    • (2001) J. Chem. Phys. , vol.114 , pp. 8473-8483
    • Ishii, Y.1
  • 29
    • 38849105584 scopus 로고    scopus 로고
    • Investigation of finite-pulse radiofrequency-driven recoupling methods for measurement of intercarbonyl distances in polycrystalline and membrane-associated HIV fusion peptide samples
    • Zheng Z., Qiang W., and Weliky D.P. Investigation of finite-pulse radiofrequency-driven recoupling methods for measurement of intercarbonyl distances in polycrystalline and membrane-associated HIV fusion peptide samples. Magn. Reson. Chem. 45 (2007) S247-S260
    • (2007) Magn. Reson. Chem. , vol.45
    • Zheng, Z.1    Qiang, W.2    Weliky, D.P.3
  • 30
    • 0000069148 scopus 로고
    • Double-quantum homonuclear rotary resonance - efficient dipolar recovery in magic-angle-spinning nuclear-magnetic-resonance
    • Nielsen N.C., Bildsoe H., Jakobsen H.J., and Levitt M.H. Double-quantum homonuclear rotary resonance - efficient dipolar recovery in magic-angle-spinning nuclear-magnetic-resonance. J. Chem. Phys. 101 (1994) 1805-1812
    • (1994) J. Chem. Phys. , vol.101 , pp. 1805-1812
    • Nielsen, N.C.1    Bildsoe, H.2    Jakobsen, H.J.3    Levitt, M.H.4
  • 32
    • 0042367594 scopus 로고    scopus 로고
    • Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy
    • Ulmer T.S., Ramirez B.E., Delaglio F., and Bax A. Evaluation of backbone proton positions and dynamics in a small protein by liquid crystal NMR spectroscopy. J. Am. Chem. Soc. 125 (2003) 9179-9191
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9179-9191
    • Ulmer, T.S.1    Ramirez, B.E.2    Delaglio, F.3    Bax, A.4
  • 33
    • 24644462659 scopus 로고    scopus 로고
    • Magic-angle spinning solid-state NMR spectroscopy of the beta 1 immunoglobulin binding domain of protein G (GB1): N-15 and C-13 chemical shift assignments and conformational analysis
    • Franks W.T., Zhou D.H., Wylie B.J., Money B.G., Graesser D.T., Frericks H.L., Sahota G., and Rienstra C.M. Magic-angle spinning solid-state NMR spectroscopy of the beta 1 immunoglobulin binding domain of protein G (GB1): N-15 and C-13 chemical shift assignments and conformational analysis. J. Am. Chem. Soc. 127 (2005) 12291-12305
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12291-12305
    • Franks, W.T.1    Zhou, D.H.2    Wylie, B.J.3    Money, B.G.4    Graesser, D.T.5    Frericks, H.L.6    Sahota, G.7    Rienstra, C.M.8
  • 34
    • 42649089356 scopus 로고    scopus 로고
    • C-13 and N-15 chemical shift assignments and secondary structure of the B3 immunoglobulin-binding domain of streptococcal protein G by magic-angle spinning solid-state NMR spectroscopy
    • Nadaud P.S., Helmus J.J., and Jaroniec C.P. C-13 and N-15 chemical shift assignments and secondary structure of the B3 immunoglobulin-binding domain of streptococcal protein G by magic-angle spinning solid-state NMR spectroscopy. Biomol. NMR Assignments 1 (2007) 117-120
    • (2007) Biomol. NMR Assignments , vol.1 , pp. 117-120
    • Nadaud, P.S.1    Helmus, J.J.2    Jaroniec, C.P.3
  • 35
    • 37849004188 scopus 로고    scopus 로고
    • Isotropic chemical shifts in magic-angle spinning NMR spectra of proteins
    • Wylie B.J., Sperling L.J., and Rienstra C.M. Isotropic chemical shifts in magic-angle spinning NMR spectra of proteins. Phys. Chem. Chem. Phys. 10 (2008) 405-413
    • (2008) Phys. Chem. Chem. Phys. , vol.10 , pp. 405-413
    • Wylie, B.J.1    Sperling, L.J.2    Rienstra, C.M.3
  • 36
    • 36849106840 scopus 로고
    • Proton-enhanced NMR of dilute spins in solids
    • Pines A., Gibby M.G., and Waugh J.S. Proton-enhanced NMR of dilute spins in solids. J. Chem. Phys. 59 (1973) 569-590
    • (1973) J. Chem. Phys. , vol.59 , pp. 569-590
    • Pines, A.1    Gibby, M.G.2    Waugh, J.S.3
  • 38
    • 0033629304 scopus 로고    scopus 로고
    • An improved broadband decoupling sequence for liquid crystals and solids
    • Fung B.M., Khitrin A.K., and Ermolaev K. An improved broadband decoupling sequence for liquid crystals and solids. J. Magn. Reson. 142 (2000) 97-101
    • (2000) J. Magn. Reson. , vol.142 , pp. 97-101
    • Fung, B.M.1    Khitrin, A.K.2    Ermolaev, K.3
  • 39
    • 36149026370 scopus 로고
    • Nuclear double resonance in the rotating frame
    • Hartmann S.R., and Hahn E.L. Nuclear double resonance in the rotating frame. Phys. Rev. 128 (1962) 2042-2053
    • (1962) Phys. Rev. , vol.128 , pp. 2042-2053
    • Hartmann, S.R.1    Hahn, E.L.2
  • 40
    • 0000368822 scopus 로고    scopus 로고
    • Cross polarization in the tilted frame: assignment and spectral simplification in heteronuclear spin systems
    • Baldus M., Petkova A.T., Herzfeld J., and Griffin R.G. Cross polarization in the tilted frame: assignment and spectral simplification in heteronuclear spin systems. Mol. Phys. 95 (1998) 1197-1207
    • (1998) Mol. Phys. , vol.95 , pp. 1197-1207
    • Baldus, M.1    Petkova, A.T.2    Herzfeld, J.3    Griffin, R.G.4
  • 41
    • 43649102166 scopus 로고    scopus 로고
    • Resolution enhancement by homonuclear J-decoupling: application to three-dimensional solid-state magic angle spinning NMR spectroscopy
    • Shi L., Peng X., Ahmed M.A., Edwards D.A., Brown L.S., and Ladizhansky V. Resolution enhancement by homonuclear J-decoupling: application to three-dimensional solid-state magic angle spinning NMR spectroscopy. J. Biomol. NMR 41 (2008) 9-15
    • (2008) J. Biomol. NMR , vol.41 , pp. 9-15
    • Shi, L.1    Peng, X.2    Ahmed, M.A.3    Edwards, D.A.4    Brown, L.S.5    Ladizhansky, V.6
  • 44
    • 0042995329 scopus 로고    scopus 로고
    • Chemical shift referencing in MAS solid state NMR
    • Morcombe C.R., and Zilm K.W. Chemical shift referencing in MAS solid state NMR. J. Magn. Reson. 162 (2003) 479-486
    • (2003) J. Magn. Reson. , vol.162 , pp. 479-486
    • Morcombe, C.R.1    Zilm, K.W.2
  • 45
    • 0032063320 scopus 로고    scopus 로고
    • A homonuclear spin-pair filter for solid-state NMR based on adiabatic-passage techniques
    • Verel R., Baldus M., Ernst M., and Meier B.H. A homonuclear spin-pair filter for solid-state NMR based on adiabatic-passage techniques. Chem. Phys. Lett. 287 (1998) 421-428
    • (1998) Chem. Phys. Lett. , vol.287 , pp. 421-428
    • Verel, R.1    Baldus, M.2    Ernst, M.3    Meier, B.H.4
  • 46
    • 0035743161 scopus 로고    scopus 로고
    • Adiabatic dipolar recoupling in solid-state NMR: the DREAM scheme
    • Verel R., Ernst M., and Meier B.H. Adiabatic dipolar recoupling in solid-state NMR: the DREAM scheme. J. Magn. Reson. 150 (2001) 81-99
    • (2001) J. Magn. Reson. , vol.150 , pp. 81-99
    • Verel, R.1    Ernst, M.2    Meier, B.H.3
  • 47
    • 36049055838 scopus 로고
    • Coherent averaging effects in magnetic resonance
    • Haeberlen U., and Waugh J.S. Coherent averaging effects in magnetic resonance. Phys. Rev. 175 (1968) 453-467
    • (1968) Phys. Rev. , vol.175 , pp. 453-467
    • Haeberlen, U.1    Waugh, J.S.2
  • 48
    • 0009580266 scopus 로고    scopus 로고
    • Dipolar recoupling under magic-angle spinning conditions
    • Dusold S., and Sebald A. Dipolar recoupling under magic-angle spinning conditions. Annu. Rep. NMR Spectrosc. 41 (2000) 185-264
    • (2000) Annu. Rep. NMR Spectrosc. , vol.41 , pp. 185-264
    • Dusold, S.1    Sebald, A.2
  • 49
    • 0000462578 scopus 로고
    • Selective excitation and detection in multilevel spin systems: application of single transition operators
    • Wokaun A., and Ernst R.R. Selective excitation and detection in multilevel spin systems: application of single transition operators. J. Chem. Phys. 67 (1977) 1752-1758
    • (1977) J. Chem. Phys. , vol.67 , pp. 1752-1758
    • Wokaun, A.1    Ernst, R.R.2
  • 50
    • 36749113303 scopus 로고
    • Fictitious spin 1/2 operator formalism for multiple quantum NMR
    • Vega S. Fictitious spin 1/2 operator formalism for multiple quantum NMR. J. Chem. Phys. 68 (1978) 5518-5527
    • (1978) J. Chem. Phys. , vol.68 , pp. 5518-5527
    • Vega, S.1
  • 51
    • 0030607947 scopus 로고    scopus 로고
    • NMR chemical shift anisotropy measurements by RF driven rotary resonance
    • Gan Z.H., Grant D.M., and Ernst R.R. NMR chemical shift anisotropy measurements by RF driven rotary resonance. Chem. Phys. Lett. 254 (1996) 349-357
    • (1996) Chem. Phys. Lett. , vol.254 , pp. 349-357
    • Gan, Z.H.1    Grant, D.M.2    Ernst, R.R.3
  • 52
    • 0028080176 scopus 로고
    • The third IgG-binding domain from streptococcal protein G. An analysis by X-ray crystallography of the structure alone and in a complex with Fab
    • Derrick J.P., and Wigley D.B. The third IgG-binding domain from streptococcal protein G. An analysis by X-ray crystallography of the structure alone and in a complex with Fab. J. Mol. Biol. 243 (1994) 906-918
    • (1994) J. Mol. Biol. , vol.243 , pp. 906-918
    • Derrick, J.P.1    Wigley, D.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.