메뉴 건너뛰기




Volumn 130, Issue 2, 1998, Pages 305-316

Magic Angle-Oriented Sample Spinning (MAOSS): A New Approach toward Biomembrane Studies

Author keywords

Lipids; MAS; Oriented membranes; Peptides; Solid state NMR

Indexed keywords

DIMYRISTOYLPHOSPHATIDYLCHOLINE;

EID: 0031993272     PISSN: 10907807     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmre.1997.1344     Document Type: Article
Times cited : (119)

References (69)
  • 1
    • 0030861070 scopus 로고    scopus 로고
    • NMR and membrane proteins
    • S. J. Opella, NMR and membrane proteins, Nature Struct. Biol. 4, 845-848 (1997).
    • (1997) Nature Struct. Biol. , vol.4 , pp. 845-848
    • Opella, S.J.1
  • 2
    • 0028025665 scopus 로고
    • Solid-state NMR structural studies of peptides and proteins in membranes
    • T. A. Cross and S. J. Opella, Solid-state NMR structural studies of peptides and proteins in membranes, Curr. Opinion Struct. Biol. 4, 574-581 (1994).
    • (1994) Curr. Opinion Struct. Biol. , vol.4 , pp. 574-581
    • Cross, T.A.1    Opella, S.J.2
  • 3
    • 0030437935 scopus 로고    scopus 로고
    • Magic angle spinning NMR spectroscopy of membrane proteins
    • S. O. Smith and M. Groesbeek, Magic angle spinning NMR spectroscopy of membrane proteins, Q. Rev. Biophys. 29, 395-449 (1996).
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 395-449
    • Smith, S.O.1    Groesbeek, M.2
  • 7
    • 0030253417 scopus 로고    scopus 로고
    • Prospects for resonance assignments in multidimensional solid-state NMR-spectra of uniformly labelled proteins
    • R. Tycko, Prospects for resonance assignments in multidimensional solid-state NMR-spectra of uniformly labelled proteins, J. Biomol. NMR 8, 239-251 (1996).
    • (1996) J. Biomol. NMR , vol.8 , pp. 239-251
    • Tycko, R.1
  • 10
    • 0023962259 scopus 로고
    • High-field, high-resolution proton magic-angle sample-spinning nuclear magnetic-resonance spectroscopy studies of gel and liquid-crystalline lipid bilayers and the effects of cholesterol
    • J. Forbes, C. Husted, and E. Oldfield, High-field, high-resolution proton magic-angle sample-spinning nuclear magnetic-resonance spectroscopy studies of gel and liquid-crystalline lipid bilayers and the effects of cholesterol, J. Am. Chem. Soc. 110, 1059-1065 (1988).
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 1059-1065
    • Forbes, J.1    Husted, C.2    Oldfield, E.3
  • 11
    • 0001501402 scopus 로고
    • Some new developments in solid-state nuclear magnetic-resonance spectroscopic studies of lipids and biological-membranes, including the effects of cholesterol in model and natural systems
    • J. Forbes, J. Bowers, X. Shan, L. Moran, E. Oldfield, and M. A. Moscarello, Some new developments in solid-state nuclear magnetic-resonance spectroscopic studies of lipids and biological-membranes, including the effects of cholesterol in model and natural systems, J. Chem. Soc. Faraday Trans. 84, 3821-3849 (1988).
    • (1988) J. Chem. Soc. Faraday Trans. , vol.84 , pp. 3821-3849
    • Forbes, J.1    Bowers, J.2    Shan, X.3    Moran, L.4    Oldfield, E.5    Moscarello, M.A.6
  • 12
    • 0028970552 scopus 로고
    • 1H nuclear magnetic resonance of a transmembrane peptide
    • 1H nuclear magnetic resonance of a transmembrane peptide, Biophys. J. 69, 1917-1932 (1995).
    • (1995) Biophys. J. , vol.69 , pp. 1917-1932
    • Davis, J.H.1    Auger, M.2    Hodges, R.S.3
  • 15
    • 0009632447 scopus 로고    scopus 로고
    • Rotational side bands in two-dimensional proton high-resolution MAS NMR spectra
    • A. Pampel and F. Volke, Rotational side bands in two-dimensional proton high-resolution MAS NMR spectra, J. Magn. Reson. Anal., 3, 222 (1997).
    • (1997) J. Magn. Reson. Anal. , vol.3 , pp. 222
    • Pampel, A.1    Volke, F.2
  • 16
    • 0030588816 scopus 로고    scopus 로고
    • Proton MAS NMR of a protein in a frozen aqueous-solution
    • F. Volke, A. Pampel, M. Haensler, and G. Ullmann, Proton MAS NMR of a protein in a frozen aqueous-solution, Chem. Phys. Lett. 262, 374-378 (1996).
    • (1996) Chem. Phys. Lett. , vol.262 , pp. 374-378
    • Volke, F.1    Pampel, A.2    Haensler, M.3    Ullmann, G.4
  • 17
    • 0028859424 scopus 로고
    • 1H nuclear-magnetic-resonance study of the conformation of gramicidin a in lipid bilayers
    • 1H nuclear-magnetic-resonance study of the conformation of gramicidin a in lipid bilayers, Biophys. J. 69, 1933-1938 (1995).
    • (1995) Biophys. J. , vol.69 , pp. 1933-1938
    • Bouchard, M.1    Davis, J.H.2    Auger, M.3
  • 18
    • 36549091040 scopus 로고
    • Theory and simulations of homonuclear spin pair systems in rotating solids
    • M. H. Levitt, D. P. Raleigh, F. Creuzet, and R. G. Griffin, Theory and simulations of homonuclear spin pair systems in rotating solids, J. Chem. Phys. 92, 6347-6364 (1990).
    • (1990) J. Chem. Phys. , vol.92 , pp. 6347-6364
    • Levitt, M.H.1    Raleigh, D.P.2    Creuzet, F.3    Griffin, R.G.4
  • 19
    • 4244132605 scopus 로고
    • Measurements of S-S dipole couplings in MAS NMR (DRAMA)
    • R. Tycko and G. Dabbagh, Measurements of S-S dipole couplings in MAS NMR (DRAMA), Chem. Phys. Lett. 173, 461 (1990).
    • (1990) Chem. Phys. Lett. , vol.173 , pp. 461
    • Tycko, R.1    Dabbagh, G.2
  • 20
    • 85011817347 scopus 로고
    • Detection of weak heteronuclear couplings by REDOR
    • T. Gullion and J. Schaefer, Detection of weak heteronuclear couplings by REDOR, Adv. Magn. Reson. 13, 57 (1989).
    • (1989) Adv. Magn. Reson. , vol.13 , pp. 57
    • Gullion, T.1    Schaefer, J.2
  • 21
    • 36449004247 scopus 로고
    • Internuclear distance measurements in solid-state nuclear-magnetic-resonance - Dipolar recoupling via rotor synchronized spin locking
    • B. Q. Sun, P. R. Costa, D. Kocisko, P. T. Lansbury, and R. G. Griffin, Internuclear distance measurements in solid-state nuclear-magnetic-resonance - dipolar recoupling via rotor synchronized spin locking, J. Chem. Phys. 102, 702-707 (1995).
    • (1995) J. Chem. Phys. , vol.102 , pp. 702-707
    • Sun, B.Q.1    Costa, P.R.2    Kocisko, D.3    Lansbury, P.T.4    Griffin, R.G.5
  • 22
    • 0003193780 scopus 로고
    • Efficient dipolar recoupling in the NMR of rotating solids - A sevenfold symmetrical radiofrequency pulse sequence
    • Y. K. Lee, N. D. Kurur, M. Helmle, O. G. Johannessen, N. C. Niexlsen, and M. H. Levitt, Efficient dipolar recoupling in the NMR of rotating solids - A sevenfold symmetrical radiofrequency pulse sequence, Chem. Phys. Lett. 242, 304-309 (1995).
    • (1995) Chem. Phys. Lett. , vol.242 , pp. 304-309
    • Lee, Y.K.1    Kurur, N.D.2    Helmle, M.3    Johannessen, O.G.4    Niexlsen, N.C.5    Levitt, M.H.6
  • 23
    • 0000539530 scopus 로고
    • NMR in rotating solids
    • M. M. Maricq and J. S. Waugh, NMR in rotating solids, J. Chem. Phys. 70, 3300-3316 (1979).
    • (1979) J. Chem. Phys. , vol.70 , pp. 3300-3316
    • Maricq, M.M.1    Waugh, J.S.2
  • 24
    • 33750405141 scopus 로고
    • Sideband intensities in NMR spectra
    • J. Herzfeld and A. E. Berger, Sideband intensities in NMR spectra, J. Chem. Phys. 73, 6021 (1980).
    • (1980) J. Chem. Phys. , vol.73 , pp. 6021
    • Herzfeld, J.1    Berger, A.E.2
  • 29
    • 0027370072 scopus 로고
    • Secondary structure of M13 coat protein in phospholipids studied by circular-dichroism, RAMAN, and Fourier-transform IR
    • J. C. Sanders, P. I. Haris, D. Chapman, C. Otto, and M. A. Hemminga, Secondary structure of M13 coat protein in phospholipids studied by circular-dichroism, RAMAN, and Fourier-transform IR, Biochemistry 32, 12446-12454 (1993).
    • (1993) Biochemistry , vol.32 , pp. 12446-12454
    • Sanders, J.C.1    Haris, P.I.2    Chapman, D.3    Otto, C.4    Hemminga, M.A.5
  • 31
    • 85030073026 scopus 로고    scopus 로고
    • personal communication
    • M. H. Levitt, personal communication.
    • Levitt, M.H.1
  • 32
    • 0026768029 scopus 로고
    • Melittin-induced changes in lipid multilayers - A solid state NMR study
    • R. Smith, F. Separovic, F. C. Bennet, and B. A. Cornell, Melittin-induced changes in lipid multilayers - A solid state NMR study, Biophys. J. 63, 469-474 (1992).
    • (1992) Biophys. J. , vol.63 , pp. 469-474
    • Smith, R.1    Separovic, F.2    Bennet, F.C.3    Cornell, B.A.4
  • 34
    • 0018827839 scopus 로고
    • The description of membrane lipid conformation, order and dynamics by deuterium NMR
    • J. Davis, The description of membrane lipid conformation, order and dynamics by deuterium NMR, BBA 597, 477-491 (1980).
    • (1980) BBA , vol.597 , pp. 477-491
    • Davis, J.1
  • 35
    • 0017752553 scopus 로고
    • Deuterium magnetic resonance: Theory and application to lipid membranes
    • J. Seelig, Deuterium magnetic resonance: Theory and application to lipid membranes, Q. Rev. Biophys. 10, 345-418 (1977).
    • (1977) Q. Rev. Biophys. , vol.10 , pp. 345-418
    • Seelig, J.1
  • 36
    • 0003922654 scopus 로고
    • High resolution in solids: Selective averaging
    • Academic Press, New York
    • U. Haeberlen, High resolution in solids: Selective averaging, in "Advances in Magnetic Resonance," Supplement 1, Academic Press, New York (1976).
    • (1976) Advances in Magnetic Resonance , Issue.1 SUPPL.
    • Haeberlen, U.1
  • 38
    • 0345696658 scopus 로고
    • S. Harding and A. J. Rowe, Eds., Royal Chem. Soc., London
    • A. Watts, "Dynamic Properties of Biomolecular Assemblies" (S. Harding and A. J. Rowe, Eds.), pp. 320-347, Royal Chem. Soc., London (1988).
    • (1988) Dynamic Properties of Biomolecular Assemblies , pp. 320-347
    • Watts, A.1
  • 39
    • 0026590504 scopus 로고
    • Deuteron nuclear magnetic resonance study for the dynamic organization of phospholipid/cholesterol bilayer membranes: Molecular properties and viscoelastic behavior
    • K. Weisz, G. Gröbner, C. Mayer, J. Stohrer, and G. Kothe, Deuteron nuclear magnetic resonance study for the dynamic organization of phospholipid/cholesterol bilayer membranes: Molecular properties and viscoelastic behavior, Biochemistry 31, 1100-1112 (1992).
    • (1992) Biochemistry , vol.31 , pp. 1100-1112
    • Weisz, K.1    Gröbner, G.2    Mayer, C.3    Stohrer, J.4    Kothe, G.5
  • 40
    • 0001569362 scopus 로고
    • Collective lipid motions in bilayer-membranes studied by transverse deuteron spin relaxation
    • J. Stohrer, G. Grob̈ner, D. Reimer, K. Weisz, C. Mayer, and G. Kothe, Collective lipid motions in bilayer-membranes studied by transverse deuteron spin relaxation, J. Chem. Phys. 95, 672-678 (1991).
    • (1991) J. Chem. Phys. , vol.95 , pp. 672-678
    • Stohrer, J.1    Grob̈ner, G.2    Reimer, D.3    Weisz, K.4    Mayer, C.5    Kothe, G.6
  • 41
    • 0002075860 scopus 로고
    • Observations of surface undulations on the mesoscopic length scale by NMR
    • L. Pellti, Ed., Plenum Press, New York
    • M. Bloom and E. Evans, Observations of surface undulations on the mesoscopic length scale by NMR, in "Biologically Inspired Physics" (L. Pellti, Ed.), Plenum Press, New York (1991).
    • (1991) Biologically Inspired Physics
    • Bloom, M.1    Evans, E.2
  • 42
    • 36049055838 scopus 로고
    • Coherent averaging effects in magnetic resonance
    • U. Haeberlen and J. S. Waugh, Coherent averaging effects in magnetic resonance, Phys. Rev. 175, 453-467 (1968).
    • (1968) Phys. Rev. , vol.175 , pp. 453-467
    • Haeberlen, U.1    Waugh, J.S.2
  • 43
    • 0028210494 scopus 로고
    • The structure of an integral membrane peptide: A deuterium NMR relaxation study of gramicidin
    • R. S. Prosser, S. I. Daleman, and J. H. Davis, The structure of an integral membrane peptide: A deuterium NMR relaxation study of gramicidin. Biophys. J. 66, 1415-1428 (1994).
    • (1994) Biophys. J. , vol.66 , pp. 1415-1428
    • Prosser, R.S.1    Daleman, S.I.2    Davis, J.H.3
  • 44
    • 0028330797 scopus 로고
    • Dynamics of an integral membrane peptide: A deuterium NMR relaxation study of gramicidin
    • R. S. Prosser and J. H. Davis, Dynamics of an integral membrane peptide: A deuterium NMR relaxation study of gramicidin, Biophys. J. 66, 1429-1440 (1994).
    • (1994) Biophys. J. , vol.66 , pp. 1429-1440
    • Prosser, R.S.1    Davis, J.H.2
  • 45
    • 0346938543 scopus 로고    scopus 로고
    • 13C NMR heteronuclear dipolar-correlation spectroscopy of solids with frequency-switched Lee-Goldburg homonuclear decoupling
    • 13C NMR heteronuclear dipolar-correlation spectroscopy of solids with frequency-switched Lee-Goldburg homonuclear decoupling, J. Magn. Reson. 124, 516-519 (1997).
    • (1997) J. Magn. Reson. , vol.124 , pp. 516-519
    • Van Rossum, B.J.1    Forster, H.2    De Groot, H.J.3
  • 46
    • 0031230149 scopus 로고    scopus 로고
    • Shimming a high-resolution MAS probe
    • A. Sodickson and D. G. Cory, Shimming a high-resolution MAS probe, J. Magn. Reson. 128, 87-91 (1997).
    • (1997) J. Magn. Reson. , vol.128 , pp. 87-91
    • Sodickson, A.1    Cory, D.G.2
  • 48
    • 0026610833 scopus 로고
    • 15N NMR resonances in detergent-solubized M13 coat protein: A model for the coat protein dimer
    • 15N NMR resonances in detergent-solubized M13 coat protein: A model for the coat protein dimer, Biochemistry 31, 5284-5297 (1992).
    • (1992) Biochemistry , vol.31 , pp. 5284-5297
    • Henry, G.D.1    Sykes, B.D.2
  • 50
    • 0030787637 scopus 로고    scopus 로고
    • Conventional and saturation-transfer EPR of spin-labeled mutant bacteriophage M13 coat protein in phospholipid bilayers
    • W. F. Wolkers, R. B. Spruijt, A. Kaan, R. N. H. Konings, and M. A. Hemminga, Conventional and saturation-transfer EPR of spin-labeled mutant bacteriophage M13 coat protein in phospholipid bilayers, BBA - Biomembr. 1327, 5-16 (1997).
    • (1997) BBA - Biomembr. , vol.1327 , pp. 5-16
    • Wolkers, W.F.1    Spruijt, R.B.2    Kaan, A.3    Konings, R.N.H.4    Hemminga, M.A.5
  • 51
    • 0019884742 scopus 로고
    • 13C nuclear magnetic resonance of the aromatic residues of fd coat protein
    • 13C nuclear magnetic resonance of the aromatic residues of fd coat protein, Biochemistry 20, 290-297 (1981).
    • (1981) Biochemistry , vol.20 , pp. 290-297
    • Cross, T.A.1    Opella, S.J.2
  • 52
    • 0027438626 scopus 로고
    • fd coat protein-structure in membrane environments
    • P. A. McDonnell, L. Shon, Y. Kim, and S. J. Opella, fd coat protein-structure in membrane environments, J. Mol. Biol. 233, 447-463 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 447-463
    • McDonnell, P.A.1    Shon, L.2    Kim, Y.3    Opella, S.J.4
  • 53
    • 0031577283 scopus 로고    scopus 로고
    • fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix
    • F. C. L. Almeida and S. J. Opella, fd coat protein structure in membrane environments: Structural dynamics of the loop between the hydrophobic trans-membrane helix and the amphipathic in-plane helix, J. Mol. Biol. 270, 481-495 (1997).
    • (1997) J. Mol. Biol. , vol.270 , pp. 481-495
    • Almeida, F.C.L.1    Opella, S.J.2
  • 55
    • 38249027483 scopus 로고
    • Dynamic properties of M13 coat protein in mixed bilayers. a deuterium NMR study of exchangeable sites
    • K. P. Datema, B. J. H. van Boxtel, and M. A. Hemminga, Dynamic properties of M13 coat protein in mixed bilayers. A deuterium NMR study of exchangeable sites, J. Magn. Reson. 77, 372-376 (1988).
    • (1988) J. Magn. Reson. , vol.77 , pp. 372-376
    • Datema, K.P.1    Van Boxtel, B.J.H.2    Hemminga, M.A.3
  • 56
    • 0022543092 scopus 로고
    • 13C NMR-spectroscopy of alanine methyl-groups in detergent-solubilized M13 coat protein
    • 13C NMR-spectroscopy of alanine methyl-groups in detergent-solubilized M13 coat protein, Biochemistry 25, 590-598 (1986).
    • (1986) Biochemistry , vol.25 , pp. 590-598
    • Henry, G.D.1    Weiner, J.H.2    Sykes, B.D.3
  • 57
    • 0344858674 scopus 로고
    • Phenylalanyl and tyrosyl side-chain mobility in the M13 coat protein reconstituted in phospholipid-vesicles
    • H. D. Dettman, J. H. Weiner, and B. D. Sykes, Phenylalanyl and tyrosyl side-chain mobility in the M13 coat protein reconstituted in phospholipid-vesicles, Biochemistry 23, 705-712 (1984).
    • (1984) Biochemistry , vol.23 , pp. 705-712
    • Dettman, H.D.1    Weiner, J.H.2    Sykes, B.D.3
  • 58
    • 0017138422 scopus 로고
    • Nature of the thermal pretransition of synthetic phospholipids: Dimyristoyl- And dipalmitoyl-lecithin
    • M. J. Janiak, D. M. Small, and G. G. Shipley, Nature of the thermal pretransition of synthetic phospholipids: Dimyristoyl- and dipalmitoyl-lecithin, Biochemistry 15, 4575-4577 (1976).
    • (1976) Biochemistry , vol.15 , pp. 4575-4577
    • Janiak, M.J.1    Small, D.M.2    Shipley, G.G.3
  • 59
    • 0018140708 scopus 로고
    • Control of structure and fluidity of phosphatidylglycerol bilayers by pH-titration
    • A. Watts, K. Harlos, W. Maschke, and D. Marsh, Control of structure and fluidity of phosphatidylglycerol bilayers by pH-titration, Biochim. Biophys. Acta 510, 63-74 (1978).
    • (1978) Biochim. Biophys. Acta , vol.510 , pp. 63-74
    • Watts, A.1    Harlos, K.2    Maschke, W.3    Marsh, D.4
  • 60
    • 0028909941 scopus 로고
    • New approach to study fast and slow motions in lipid bilayers - Application to dimyristoylphosphatidylcholine-cholesterol interactions
    • C. Le Guerneve and M. Auger, New approach to study fast and slow motions in lipid bilayers - Application to dimyristoylphosphatidylcholine-cholesterol interactions, Biophys. J. 68, 1952-1959 (1995).
    • (1995) Biophys. J. , vol.68 , pp. 1952-1959
    • Le Guerneve, C.1    Auger, M.2
  • 61
    • 0030300090 scopus 로고    scopus 로고
    • Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopy
    • B. Bechinger, L. M. Gierasch, M. Montal, M. Zasloff, and S. J. Opella, Orientations of helical peptides in membrane bilayers by solid state NMR spectroscopy, Solid State NMR 7, 185-191 (1996).
    • (1996) Solid State NMR , vol.7 , pp. 185-191
    • Bechinger, B.1    Gierasch, L.M.2    Montal, M.3    Zasloff, M.4    Opella, S.J.5
  • 62
    • 33845326963 scopus 로고
    • Two-dimensional sideband separation in magic-angle-spinning NMR
    • O. N. Antzutkin, S. C. Shekar, and M. H. Levitt, Two-dimensional sideband separation in magic-angle-spinning NMR, J. Magn. Reson. A 115, 7-19 (1995).
    • (1995) J. Magn. Reson. A , vol.115 , pp. 7-19
    • Antzutkin, O.N.1    Shekar, S.C.2    Levitt, M.H.3
  • 65
    • 84989039097 scopus 로고
    • Determination of chemical-shift tensor orientations in methylene groups by separated-local-field NMR
    • K. Schmidt-Rohr, M. Wilhelm, A. Johansson, and H. W. Spiess, Determination of chemical-shift tensor orientations in methylene groups by separated-local-field NMR, Magn. Reson. Chem. 31, 352-356 (1993).
    • (1993) Magn. Reson. Chem. , vol.31 , pp. 352-356
    • Schmidt-Rohr, K.1    Wilhelm, M.2    Johansson, A.3    Spiess, H.W.4
  • 66
    • 0031189051 scopus 로고    scopus 로고
    • Site-resolved determination of peptide torsion angle phi from the relative orientations of backbone N-H and C-H bonds by solid-state NMR
    • M. Hong, J. D. Gross, and R. G. Griffin, Site-resolved determination of peptide torsion angle phi from the relative orientations of backbone N-H and C-H bonds by solid-state NMR, J. Phys. Chem. B 101, 5869-5874 (1997).
    • (1997) J. Phys. Chem. B , vol.101 , pp. 5869-5874
    • Hong, M.1    Gross, J.D.2    Griffin, R.G.3
  • 68
    • 0028139553 scopus 로고
    • A method for dihedral angle measurement in solids - Rotational resonance NMR of a transition-state inhibitor of triose phosphate isomerase
    • Y. Tomita, E. J. O'Connor, and A. McDermott, A method for dihedral angle measurement in solids - Rotational resonance NMR of a transition-state inhibitor of triose phosphate isomerase, J. Am. Chem. Soc. 116, 8766-8771 (1994).
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 8766-8771
    • Tomita, Y.1    O'Connor, E.J.2    McDermott, A.3
  • 69
    • 0026795003 scopus 로고
    • Protein rotational diffusion and lipid protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines - Different chain lengths studied by conventional and saturation-transfer electron-spin-resonance
    • N. J. P. Ryba and D. Marsh, Protein rotational diffusion and lipid protein interactions in recombinants of bovine rhodopsin with saturated diacylphosphatidylcholines - Different chain lengths studied by conventional and saturation-transfer electron-spin-resonance, Biochemistry 31, 7511-7518 (1992).
    • (1992) Biochemistry , vol.31 , pp. 7511-7518
    • Ryba, N.J.P.1    Marsh, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.