메뉴 건너뛰기




Volumn 402, Issue 2, 2012, Pages 721-729

Ultra-thin layer MALDI mass spectrometry of membrane proteins in nanodiscs

Author keywords

Cytochrome P450 3A4; Cytochrome p450 reductase; MALDI TOF mass spectrometry; Membrane proteins; Nanodisc; Rhodopsin

Indexed keywords

CYTOCHROME P450 REDUCTASE; CYTOCHROME P450-3A4; MALDI-TOF MASS SPECTROMETRY; MEMBRANE PROTEINS; NANODISCS; RHODOPSIN;

EID: 84856228232     PISSN: 16182642     EISSN: 16182650     Source Type: Journal    
DOI: 10.1007/s00216-011-5512-3     Document Type: Article
Times cited : (26)

References (36)
  • 1
    • 0043007514 scopus 로고    scopus 로고
    • Self-Assembly of Discoidal Phospholipid Bilayer Nanoparticles with Membrane Scaffold Proteins
    • DOI 10.1021/nl025623k
    • TH Bayburt YV Grinkova SG Sligar 2002 Self-assembly of discoidal phospholipid bilayer nanoparticles with membrane scaffold proteins Nano Lett 2 8 853 856 10.1021/nl025623k 1:CAS:528:DC%2BD38XltlCnur4%3D (Pubitemid 135706448)
    • (2002) Nano Letters , vol.2 , Issue.8 , pp. 853-856
    • Bayburt, T.H.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 2
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into nanodiscs
    • 10.1016/j.febslet.2009.10.024 1:CAS:528:DC%2BC3cXkvFKqurw%3D
    • TH Bayburt SG Sligar 2010 Membrane protein assembly into nanodiscs FEBS Lett 584 9 1721 1727 10.1016/j.febslet.2009.10.024 1:CAS:528: DC%2BC3cXkvFKqurw%3D
    • (2010) FEBS Lett , vol.584 , Issue.9 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 3
    • 1642382983 scopus 로고    scopus 로고
    • Directed Self-Assembly of Monodisperse Phospholipid Bilayer Nanodiscs with Controlled Size
    • DOI 10.1021/ja0393574
    • IG Denisov YV Grinkova AA Lazarides SG Sligar 2004 Directed self-assembly of monodisperse phospholipid bilayer nanodiscs with controlled size J Am Chem Soc 126 11 3477 3487 10.1021/ja0393574 1:CAS:528:DC%2BD2cXhs1ylsr4%3D (Pubitemid 38366738)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.11 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 4
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • DOI 10.1021/bi602371n
    • A Nath WM Atkins SG Sligar 2007 Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins Biochemistry 46 8 2059 2069 10.1021/bi602371n 1:CAS:528:DC%2BD2sXhtVOmt74%3D (Pubitemid 46355317)
    • (2007) Biochemistry , vol.46 , Issue.8 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 5
    • 36849083490 scopus 로고    scopus 로고
    • Magic-angle spinning solid-state NMR spectroscopy of nanodisc-embedded human CYP3A4
    • DOI 10.1021/bi701411g
    • AZ Kijac Y Li SG Sligar CM Rienstra 2007 Magic-angle spinning solid-state NMR spectroscopy of nanodisc-embedded human CYP3A4 Biochemistry 46 48 13696 13703 10.1021/bi701411g 1:CAS:528:DC%2BD2sXht1KitrnJ (Pubitemid 350223897)
    • (2007) Biochemistry , vol.46 , Issue.48 , pp. 13696-13703
    • Kijac, A.Z.1    Li, Y.2    Sligar, S.G.3    Rienstra, C.M.4
  • 6
    • 77649244670 scopus 로고    scopus 로고
    • Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles
    • 10.1073/pnas.1000100107 1:CAS:528:DC%2BC3cXjtFymuro%3D
    • H Katayama J Wang F Tama L Chollet EP Gogol RJ Collier MT Fisher 2010 Three-dimensional structure of the anthrax toxin pore inserted into lipid nanodiscs and lipid vesicles Proc Natl Acad Sci 107 8 3453 3457 10.1073/pnas.1000100107 1:CAS:528:DC%2BC3cXjtFymuro%3D
    • (2010) Proc Natl Acad Sci , vol.107 , Issue.8 , pp. 3453-3457
    • Katayama, H.1    Wang, J.2    Tama, F.3    Chollet, L.4    Gogol, E.P.5    Collier, R.J.6    Fisher, M.T.7
  • 7
    • 75749154495 scopus 로고    scopus 로고
    • Recreation of the terminal events in physiological integrin activation
    • 10.1083/jcb.200908045 1:CAS:528:DC%2BC3cXntFKgsA%3D%3D
    • F Ye G Hu D Taylor B Ratnikov AA Bobkov MA McLean SG Sligar KA Taylor MH Ginsberg 2010 Recreation of the terminal events in physiological integrin activation J Cell Biol 188 1 157 173 10.1083/jcb.200908045 1:CAS:528: DC%2BC3cXntFKgsA%3D%3D
    • (2010) J Cell Biol , vol.188 , Issue.1 , pp. 157-173
    • Ye, F.1    Hu, G.2    Taylor, D.3    Ratnikov, B.4    Bobkov, A.A.5    McLean, M.A.6    Sligar, S.G.7    Taylor, K.A.8    Ginsberg, M.H.9
  • 9
    • 66149100484 scopus 로고    scopus 로고
    • Screening of type i and II drug binding to human cytochrome P450-3A4 in nanodiscs by localized surface plasmon resonance spectroscopy
    • 10.1021/ac802612z 1:CAS:528:DC%2BD1MXksVSlsbc%3D
    • A Das J Zhao GC Schatz SG Sligar DRP Van 2009 Screening of type I and II drug binding to human cytochrome P450-3A4 in nanodiscs by localized surface plasmon resonance spectroscopy Anal Chem 81 3754 3759 10.1021/ac802612z 1:CAS:528:DC%2BD1MXksVSlsbc%3D
    • (2009) Anal Chem , vol.81 , pp. 3754-3759
    • Das, A.1    Zhao, J.2    Schatz, G.C.3    Sligar, S.G.4    Van, D.R.P.5
  • 10
    • 50049101521 scopus 로고    scopus 로고
    • Nanodiscs for immobilization of lipid bilayers and membrane receptors: Kinetic analysis of cholera toxin binding to a glycolipid receptor
    • 10.1021/ac8000644 1:CAS:528:DC%2BD1cXotlOntb4%3D
    • J Borch F Torta SG Sligar P Roepstorff 2008 Nanodiscs for immobilization of lipid bilayers and membrane receptors: kinetic analysis of cholera toxin binding to a glycolipid receptor Anal Chem 80 6245 6252 10.1021/ac8000644 1:CAS:528:DC%2BD1cXotlOntb4%3D
    • (2008) Anal Chem , vol.80 , pp. 6245-6252
    • Borch, J.1    Torta, F.2    Sligar, S.G.3    Roepstorff, P.4
  • 11
    • 34250365394 scopus 로고    scopus 로고
    • The local phospholipid environment modulates the activation of blood clotting
    • DOI 10.1074/jbc.M607973200
    • AW Shaw VS Pureza SG Sligar JH Morrissey 2007 The local phospholipid environment modulates the activation of blood clotting J Biol Chem 282 6556 6563 10.1074/jbc.M607973200 1:CAS:528:DC%2BD2sXitVCisbc%3D (Pubitemid 47100852)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.9 , pp. 6556-6563
    • Shaw, A.W.1    Pureza, V.S.2    Sligar, S.G.3    Morrissey, J.H.4
  • 12
    • 77954193701 scopus 로고    scopus 로고
    • Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry
    • 10.1021/ac100962c 1:CAS:528:DC%2BC3cXmvVSksrs%3D
    • CM Hebling CR Morgan DW Stafford JW Jorgenson KD Rand JR Engen 2010 Conformational analysis of membrane proteins in phospholipid bilayer nanodiscs by hydrogen exchange mass spectrometry Anal Chem 82 13 5415 5419 10.1021/ac100962c 1:CAS:528:DC%2BC3cXmvVSksrs%3D
    • (2010) Anal Chem , vol.82 , Issue.13 , pp. 5415-5419
    • Hebling, C.M.1    Morgan, C.R.2    Stafford, D.W.3    Jorgenson, J.W.4    Rand, K.D.5    Engen, J.R.6
  • 13
    • 84855195456 scopus 로고    scopus 로고
    • Nanodisc-based co-immunoprecipitation for mass spectrometric identification of membrane-interacting proteins
    • 10.1074/mcp.O110.006775
    • J Borch P Roepstorff J Moller-Jensen 2011 Nanodisc-based co-immunoprecipitation for mass spectrometric identification of membrane-interacting proteins Mol Cell Proteomics 10 7 O110.006775 10.1074/mcp.O110.006775
    • (2011) Mol Cell Proteomics , vol.10 , Issue.7 , pp. 110006775
    • Borch, J.1    Roepstorff, P.2    Moller-Jensen, J.3
  • 14
    • 36748999908 scopus 로고    scopus 로고
    • Functional assays of membrane-bound proteins with SAMDI-TOF mass spectrometry
    • DOI 10.1002/anie.200702694
    • VL Marin TH Bayburt SG Sligar M Mrksich 2007 Functional assays of membrane-bound proteins with SAMDI-TOF mass spectrometry Angew Chem-Int Edit 46 46 8796 8798 10.1002/anie.200702694 1:CAS:528:DC%2BD2sXhsVWqsbbI (Pubitemid 350207929)
    • (2007) Angewandte Chemie - International Edition , vol.46 , Issue.46 , pp. 8796-8798
    • Marin, V.L.1    Bayburt, T.H.2    Sligar, S.G.3    Mrksich, M.4
  • 16
    • 0344838440 scopus 로고    scopus 로고
    • Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry
    • DOI 10.1093/emboj/cdg145
    • AB Weinglass JP Whitelegge Y Hu GE Verner KF Faull HR Kaback 2003 Elucidation of substrate binding interactions in a membrane transport protein by mass spectrometry EMBO J 22 7 1467 1477 10.1093/emboj/cdg145 1:CAS:528:DC%2BD3sXisFeqsbs%3D (Pubitemid 36417396)
    • (2003) EMBO Journal , vol.22 , Issue.7 , pp. 1467-1477
    • Weinglass, A.B.1    Whitelegge, J.P.2    Hu, Y.3    Verner, G.E.4    Faull, K.F.5    Kaback, H.R.6
  • 17
    • 55649102275 scopus 로고    scopus 로고
    • Mass spectrometry of full-length integral membrane proteins to define functionally relevant structural features
    • 10.1016/j.ymeth.2008.10.021 1:CAS:528:DC%2BD1cXhtlyhsbvI
    • G Gabant M Cadene 2008 Mass spectrometry of full-length integral membrane proteins to define functionally relevant structural features Methods 46 2 54 61 10.1016/j.ymeth.2008.10.021 1:CAS:528:DC%2BD1cXhtlyhsbvI
    • (2008) Methods , vol.46 , Issue.2 , pp. 54-61
    • Gabant, G.1    Cadene, M.2
  • 18
    • 33947415352 scopus 로고    scopus 로고
    • Analysis of an intact G-protein coupled receptor by MALDI-TOF mass spectrometry: Molecular heterogeneity of the tachykinin NK-1 receptor
    • DOI 10.1021/ac062415u
    • ID Alves E Sachon G Bolbach L Millstine S Lavielle S Sagan 2007 Analysis of an intact G-protein coupled receptor by MALDI-TOF mass spectrometry: molecular heterogeneity of the tachykinin NK-1 receptor Anal Chem 79 6 2189 2198 10.1021/ac062415u 1:CAS:528:DC%2BD2sXhsFOltbc%3D (Pubitemid 46448997)
    • (2007) Analytical Chemistry , vol.79 , Issue.6 , pp. 2189-2198
    • Alves, I.D.1    Sachon, E.2    Bolbach, G.3    Millstine, L.4    Lavielle, S.5    Sagan, S.6
  • 19
    • 0034987721 scopus 로고    scopus 로고
    • Mass spectrometry as a tool for protein crystallography
    • DOI 10.1146/annurev.biophys.30.1.67
    • SL Cohen BT Chait 2001 Mass spectrometry as a tool for protein crystallography Annu Rev Biophys Biomol Struct 30 1 67 85 10.1146/annurev. biophys.30.1.67 1:CAS:528:DC%2BD3MXkvVaqsb8%3D (Pubitemid 32566156)
    • (2001) Annual Review of Biophysics and Biomolecular Structure , vol.30 , pp. 67-85
    • Cohen, S.L.1    Chait, B.T.2
  • 20
    • 77956873612 scopus 로고    scopus 로고
    • Mass spectrometry guided in situ proteolysis to obtain crystals for X-ray structure determination
    • 10.1016/j.jasms.2010.06.015 1:CAS:528:DC%2BC3cXht1Wmt7fI
    • T Gheyi L Rodgers R Romero JM Sauder SK Burley 2010 Mass spectrometry guided in situ proteolysis to obtain crystals for X-ray structure determination J Am Soc Mass Spectrom 21 10 1795 1801 10.1016/j.jasms.2010.06.015 1:CAS:528:DC%2BC3cXht1Wmt7fI
    • (2010) J Am Soc Mass Spectrom , vol.21 , Issue.10 , pp. 1795-1801
    • Gheyi, T.1    Rodgers, L.2    Romero, R.3    Sauder, J.M.4    Burley, S.K.5
  • 21
    • 39049099831 scopus 로고    scopus 로고
    • Fragmentation of Multiply-Charged Intact Protein Ions Using MALDI TOF-TOF Mass Spectrometry
    • DOI 10.1016/j.jasms.2007.06.006, PII S1044030507004667
    • Z Liu K Schey 2008 Fragmentation of multiply-charged intact protein ions using MALDI TOF-TOF mass spectrometry J Am Soc Mass Spectrom 19 2 231 238 10.1016/j.jasms.2007.06.006 (Pubitemid 351249128)
    • (2008) Journal of the American Society for Mass Spectrometry , vol.19 , Issue.2 , pp. 231-238
    • Liu, Z.1    Schey, K.L.2
  • 22
    • 0025217244 scopus 로고
    • Primary sequence information from intact proteins by electrospray ionization tandem mass spectrometry
    • 10.1126/science.2326633 1:CAS:528:DyaK3cXitFegtL8%3D
    • JA Loo CG Edmonds RD Smith 1990 Primary sequence information from intact proteins by electrospray ionization tandem mass spectrometry Science 248 4952 201 204 10.1126/science.2326633 1:CAS:528:DyaK3cXitFegtL8%3D
    • (1990) Science , vol.248 , Issue.4952 , pp. 201-204
    • Loo, J.A.1    Edmonds, C.G.2    Smith, R.D.3
  • 23
    • 79551524680 scopus 로고    scopus 로고
    • High-performance liquid chromatography separation and intact mass analysis of detergent-solubilized integral membrane proteins
    • 10.1016/j.ab.2010.11.008 1:CAS:528:DC%2BC3MXhtlGktr4%3D
    • G Berridge R Chalk N D'Avanzo L Dong D Doyle J-I Kim X Xia N Burgess-Brown A deRiso EP Carpenter O Gileadi 2011 High-performance liquid chromatography separation and intact mass analysis of detergent-solubilized integral membrane proteins Anal Biochem 410 2 272 280 10.1016/j.ab.2010.11.008 1:CAS:528:DC%2BC3MXhtlGktr4%3D
    • (2011) Anal Biochem , vol.410 , Issue.2 , pp. 272-280
    • Berridge, G.1    Chalk, R.2    D'Avanzo, N.3    Dong, L.4    Doyle, D.5    Kim, J.-I.6    Xia, X.7    Burgess-Brown, N.8    Deriso, A.9    Carpenter, E.P.10    Gileadi, O.11
  • 24
    • 0034669677 scopus 로고    scopus 로고
    • A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins
    • 10.1021/ac000811l 1:CAS:528:DC%2BD3cXnsVantrs%3D
    • M Cadene BT Chait 2000 A robust, detergent-friendly method for mass spectrometric analysis of integral membrane proteins Anal Chem 72 22 5655 5658 10.1021/ac000811l 1:CAS:528:DC%2BD3cXnsVantrs%3D
    • (2000) Anal Chem , vol.72 , Issue.22 , pp. 5655-5658
    • Cadene, M.1    Chait, B.T.2
  • 26
    • 4444297536 scopus 로고    scopus 로고
    • Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment
    • DOI 10.1016/j.abb.2004.07.003, PII S0003986104003819
    • BJ Baas IG Denisov SG Sligar 2004 Homotropic cooperativity of monomeric cytochrome P450 3A4 in a nanoscale native bilayer environment Arch Biochem Biophys 430 218 228 10.1016/j.abb.2004.07.003 1:CAS:528:DC%2BD2cXnsVyqsL4%3D (Pubitemid 39208969)
    • (2004) Archives of Biochemistry and Biophysics , vol.430 , Issue.2 , pp. 218-228
    • Baas, B.J.1    Denisov, I.G.2    Sligar, S.G.3
  • 27
    • 34147112191 scopus 로고    scopus 로고
    • Cooperativity in cytochrome P450 3A4: Linkages in substrate binding, spin state, uncoupling, and product formation
    • DOI 10.1074/jbc.M609589200
    • IG Denisov BJ Baas YV Grinkova SG Sligar 2007 Cooperativity in cytochrome P450 3A4: linkages in substrate binding, spin state, uncoupling, and product formation J Biol Chem 282 10 7066 7076 10.1074/jbc.M609589200 1:CAS:528:DC%2BD2sXitlSrs7g%3D (Pubitemid 47093646)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 7066-7076
    • Denisov, I.G.1    Baas, B.J.2    Grinkova, Y.V.3    Sligar, S.G.4
  • 28
    • 73149090794 scopus 로고    scopus 로고
    • Modulation of the cytochrome P450 reductase redox potential by the phospholipid bilayer
    • 10.1021/bi9011435 1:CAS:528:DC%2BD1MXhsFSrsbfK
    • A Das SG Sligar 2009 Modulation of the cytochrome P450 reductase redox potential by the phospholipid bilayer Biochemistry 48 51 12104 12112 10.1021/bi9011435 1:CAS:528:DC%2BD1MXhsFSrsbfK
    • (2009) Biochemistry , vol.48 , Issue.51 , pp. 12104-12112
    • Das, A.1    Sligar, S.G.2
  • 30
    • 77955056487 scopus 로고    scopus 로고
    • Functional reconstitution of monomeric CYP3A4 with multiple cytochrome P450 reductase molecules in nanodiscs
    • 10.1016/j.bbrc.2010.06.058 1:CAS:528:DC%2BC3cXptlalu70%3D
    • YV Grinkova IG Denisov SG Sligar 2010 Functional reconstitution of monomeric CYP3A4 with multiple cytochrome P450 reductase molecules in nanodiscs Biochem Biophys Res Commun 398 2 194 198 10.1016/j.bbrc.2010.06.058 1:CAS:528:DC%2BC3cXptlalu70%3D
    • (2010) Biochem Biophys Res Commun , vol.398 , Issue.2 , pp. 194-198
    • Grinkova, Y.V.1    Denisov, I.G.2    Sligar, S.G.3
  • 31
    • 78651390998 scopus 로고    scopus 로고
    • Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding
    • 10.1074/jbc.M110.151043 1:CAS:528:DC%2BC3MXjtFehtQ%3D%3D
    • TH Bayburt SA Vishnivetskiy MA McLean T Morizumi C-C Huang JJG Tesmer OP Ernst SG Sligar VV Gurevich 2011 Monomeric rhodopsin is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding J Biol Chem 286 2 1420 1428 10.1074/jbc.M110.151043 1:CAS:528:DC%2BC3MXjtFehtQ%3D%3D
    • (2011) J Biol Chem , vol.286 , Issue.2 , pp. 1420-1428
    • Bayburt, T.H.1    Vishnivetskiy, S.A.2    McLean, M.A.3    Morizumi, T.4    Huang, C.-C.5    Tesmer, J.J.G.6    Ernst, O.P.7    Sligar, S.G.8    Gurevich, V.V.9
  • 32
    • 78649450188 scopus 로고    scopus 로고
    • Cytochromes P450 in nanodiscs
    • 10.1016/j.bbapap.2010.05.017 1:CAS:528:DC%2BC3cXhsVygs7zO
    • IG Denisov SG Sligar 2011 Cytochromes P450 in nanodiscs Biochim Biophys Acta Proteins Proteomics 1814 1 223 229 10.1016/j.bbapap.2010.05.017 1:CAS:528:DC%2BC3cXhsVygs7zO
    • (2011) Biochim Biophys Acta Proteins Proteomics , vol.1814 , Issue.1 , pp. 223-229
    • Denisov, I.G.1    Sligar, S.G.2
  • 33
    • 33847305993 scopus 로고    scopus 로고
    • Investigation of the first shot phenomenon in MALDI mass spectrometry of protein complexes
    • DOI 10.1039/b615411e
    • A Wortmann T Pimenova S Alves R Zenobi 2007 Investigation of the first shot phenomenon in MALDI mass spectrometry of protein complexes Analyst 132 3 199 207 10.1039/b615411e 1:CAS:528:DC%2BD2sXitVOksrY%3D (Pubitemid 46328097)
    • (2007) Analyst , vol.132 , Issue.3 , pp. 199-207
    • Wortmann, A.1    Pimenova, T.2    Alves, S.3    Zenobi, R.4
  • 34
    • 0029979976 scopus 로고    scopus 로고
    • Influence of matrix solution conditions on the MALDI-MS analysis of peptides and proteins
    • DOI 10.1021/ac9507956
    • SL Cohen BT Chait 1996 Influence of matrix solution conditions on the MALDI-MS analysis of peptides and proteins Anal Chem 68 1 31 37 10.1021/ac9507956 1:CAS:528:DyaK2MXpslSrurk%3D (Pubitemid 26199301)
    • (1996) Analytical Chemistry , vol.68 , Issue.1 , pp. 31-37
    • Cohen, S.L.1    Chait, B.T.2
  • 35
    • 0027556729 scopus 로고
    • Epitaxial protein inclusion in sinapic acid crystals
    • 10.1088/0022-3727/26/3/015 1:CAS:528:DyaK3sXit12msLw%3D
    • RC Beavis JN Bridson 1993 Epitaxial protein inclusion in sinapic acid crystals J Phys D: Appl Phys 26 3 442 10.1088/0022-3727/26/3/015 1:CAS:528:DyaK3sXit12msLw%3D
    • (1993) J Phys D: Appl Phys , vol.26 , Issue.3 , pp. 442
    • Beavis, R.C.1    Bridson, J.N.2
  • 36
    • 0033950784 scopus 로고    scopus 로고
    • The integration of SPR biosensors with mass spectrometry: Possible applications for proteome analysis
    • DOI 10.1016/S0167-7799(99)01389-X, PII S016777999901389X
    • C Williams TA Addona 2000 The integration of SPR biosensors with mass spectrometry: possible applications for proteome analysis Trends Biotechnol 18 2 45 48 10.1016/S0167-7799(99)01389-X 1:CAS:528:DC%2BD3cXpsV2quw%3D%3D (Pubitemid 30084694)
    • (2000) Trends in Biotechnology , vol.18 , Issue.2 , pp. 45-48
    • Williams, C.1    Addona, T.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.