메뉴 건너뛰기




Volumn 289, Issue 24, 2014, Pages 16954-16965

Structural basis for multiple sugar recognition of jacalin-related human ZG16p lectin

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; MAMMALS; POLYSACCHARIDES; PROTEINS;

EID: 84902440215     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.539114     Document Type: Article
Times cited : (32)

References (53)
  • 1
    • 0028587882 scopus 로고
    • cDNA cloning and characterization of a novel 16-kDa protein located in zymogen granules of rat pancreas and goblet cells of the gut
    • Cronshagen, U., Voland, P., and Kern, H. F. (1994) cDNA cloning and characterization of a novel 16-kDa protein located in zymogen granules of rat pancreas and goblet cells of the gut. Eur. J. Cell Biol. 65, 366-377
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 366-377
    • Cronshagen, U.1    Voland, P.2    Kern, H.F.3
  • 2
    • 0032587136 scopus 로고    scopus 로고
    • The secretary lectin ZG16p mediates sorting of enzyme proteins to the zymogen granule membrane in pancreatic acinar cells
    • Kleene, R., Dartsch, H., and Kern, H. F. (1999) The secretory lectin ZG16p mediates sorting of enzyme proteins to the zymogen granule membrane in pancreatic acinar cells. Eur. J. Cell Biol. 78, 79-90 (Pubitemid 29112469)
    • (1999) European Journal of Cell Biology , vol.78 , Issue.2 , pp. 79-90
    • Kleene, R.1    Dartsch, H.2    Kern, H.-F.3
  • 5
    • 0021961927 scopus 로고
    • Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR42J cells
    • DOI 10.1083/jcb.100.4.1200
    • Logsdon, C. D., Moessner, J., Williams, J. A., and Goldfine, I. D. (1985) Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR42J cells. J. Cell Biol. 100, 1200-1208 (Pubitemid 15093473)
    • (1985) Journal of Cell Biology , vol.100 , Issue.4 , pp. 1200-1208
    • Logsdon, C.D.1    Moessner, J.2    Williams, J.A.3    Goldfine, I.D.4
  • 6
    • 0023778584 scopus 로고
    • Coupled induction of exocrine proteins and intracellular compartments involved in the secretory pathway in AR4-2J cells by glucocorticoids
    • Swarovsky, B., Steinhilber, W., Scheele, G. A., and Kern, H. F. (1988) Coupled induction of exocrine proteins and intracellular compartments involved in the secretory pathway in AR4-2J cells by glucocorticoids. Eur. J. Cell Biol. 47, 101-111
    • (1988) Eur. J. Cell Biol. , vol.47 , pp. 101-111
    • Swarovsky, B.1    Steinhilber, W.2    Scheele, G.A.3    Kern, H.F.4
  • 7
    • 2942673023 scopus 로고    scopus 로고
    • Differential expression of the trypsin inhibitor SPINK3 mRNA and the mouse ortholog of secretory granule protein ZG-16p mRNA in the mouse pancreas after repetitive injury
    • Neuschwander-Tetri, B. A., Fimmel, C. J., Kladney, R. D., Wells, L. D., and Talkad, V. (2004) Differential expression of the trypsin inhibitor SPINK3 mRNA and the mouse ortholog of secretory granule protein ZG-16p mRNA in the mouse pancreas after repetitive injury. Pancreas 28, e104-111
    • (2004) Pancreas , vol.28
    • Neuschwander-Tetri, B.A.1    Fimmel, C.J.2    Kladney, R.D.3    Wells, L.D.4    Talkad, V.5
  • 8
    • 0035957985 scopus 로고    scopus 로고
    • Regulated apical secretion of zymogens in rat pancreas. Involvement of the glycosyl-phosphatidylinositol-anchored glycoprotein GP-2, the lectin ZG16p, and cholesterol-glycosphingolipid-enriched microdomains
    • Schmidt, K., Schrader, M., Kern, H. F., and Kleene, R. (2001) Regulated apical secretion of zymogens in rat pancreas. Involvement of the glycosyl-phosphatidylinositol-anchored glycoprotein GP-2, the lectin ZG16p, and cholesterol-glycosphingolipid-enriched microdomains. J. Biol. Chem. 276, 14315-14323
    • (2001) J. Biol. Chem. , vol.276 , pp. 14315-14323
    • Schmidt, K.1    Schrader, M.2    Kern, H.F.3    Kleene, R.4
  • 9
    • 0036499901 scopus 로고    scopus 로고
    • Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains
    • DOI 10.1042/0264-6021:3620433
    • Kalus, I., Hodel, A., Koch, A., Kleene, R., Edwardson, J. M., and Schrader, M. (2002) Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains. Biochem. J. 362, 433-442 (Pubitemid 34214486)
    • (2002) Biochemical Journal , vol.362 , Issue.2 , pp. 433-442
    • Kalus, I.1    Hodel, A.2    Koch, A.3    Kleene, R.4    Edwardson, J.M.5    Schrader, M.6
  • 10
    • 34548164149 scopus 로고    scopus 로고
    • Proteomic analysis of pancreatic zymogen granules: Identification of new granule proteins
    • DOI 10.1021/pr0607029
    • Rindler, M. J., Xu, C. F., Gumper, I., Smith, N. N., and Neubert, T. A. (2007) Proteomic analysis of pancreatic zymogen granules: identification of new granule proteins. J. Proteome Res. 6, 2978-2992 (Pubitemid 47310183)
    • (2007) Journal of Proteome Research , vol.6 , Issue.8 , pp. 2978-2992
    • Rindler, M.J.1    Xu, C.-F.2    Gumper, I.3    Smith, N.N.4    Neubert, T.A.5
  • 13
    • 0020826111 scopus 로고
    • Purification of human milk bile saltactivated lipase
    • Wang, C. S., and Johnson, K. (1983) Purification of human milk bile saltactivated lipase. Anal. Biochem. 133, 457-461
    • (1983) Anal. Biochem. , vol.133 , pp. 457-461
    • Wang, C.S.1    Johnson, K.2
  • 15
    • 0033934448 scopus 로고    scopus 로고
    • A submembranous matrix of proteoglycans on zymogen granule membranes is involved in granule formation in rat pancreatic acinar cells
    • Schmidt, K., Dartsch, H., Linder, D., Kern, H. F., and Kleene, R. (2000) A submembranous matrix of proteoglycans on zymogen granule membranes is involved in granule formation in rat pancreatic acinar cells. J. Cell Sci. 113, 2233-2242 (Pubitemid 30426837)
    • (2000) Journal of Cell Science , vol.113 , Issue.12 , pp. 2233-2242
    • Schmidt, K.1    Dartsch, H.2    Linder, D.3    Kern, H.-F.4    Kleene, R.5
  • 17
    • 79951968931 scopus 로고    scopus 로고
    • Influence of glycosidic linkage on the nature of carbohydrate binding in β-prism I-fold lectins: An x-ray and molecular dynamics investigation on banana lectin-carbohydrate complexes
    • Sharma, A., and Vijayan, M. (2011) Influence of glycosidic linkage on the nature of carbohydrate binding in β-prism I-fold lectins: an x-ray and molecular dynamics investigation on banana lectin-carbohydrate complexes. Glycobiology 21, 23-33
    • (2011) Glycobiology , vol.21 , pp. 23-33
    • Sharma, A.1    Vijayan, M.2
  • 18
    • 0033573149 scopus 로고    scopus 로고
    • Helianthus tuberosus lectin reveals a widespread scaffold for mannose- binding lectins
    • DOI 10.1016/S0969-2126(00)88338-0
    • Bourne, Y., Zamboni, V., Barre, A., Peumans, W. J., Van Damme, E. J., and Rougé, P. (1999) Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins. Structure 7, 1473-1482 (Pubitemid 30007233)
    • (1999) Structure , vol.7 , Issue.12 , pp. 1473-1482
    • Bourne, Y.1    Zamboni, V.2    Barre, A.3    Peumans, W.J.4    Van Damme, E.J.M.5    Rouge, P.6
  • 19
    • 0036295206 scopus 로고    scopus 로고
    • Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-α-D-mannose: Implications to the generation of carbohydrate specificity
    • DOI 10.1006/jmbi.2001.5432
    • Pratap, J. V., Jeyaprakash, A. A., Rani, P. G., Sekar, K., Surolia, A., and Vijayan, M. (2002) Crystal structures of artocarpin, a Moraceae lectin with mannose specificity, and its complex with methyl-α-D -mannose: implications to the generation of carbohydrate specificity. J. Mol. Biol. 317, 237-247 (Pubitemid 34722191)
    • (2002) Journal of Molecular Biology , vol.317 , Issue.2 , pp. 237-247
    • Pratap, J.V.1    Jeyaprakash, A.A.2    Rani, P.G.3    Sekar, K.4    Surolia, A.5    Vijayan, M.6
  • 20
    • 22544453589 scopus 로고    scopus 로고
    • Structural analysis of the jacalin-related lectin MornigaM from the black mulberry (Morus nigra) in complex with mannose
    • DOI 10.1111/j.1742-4658.2005.04801.x
    • Rabijns, A., Barre, A., Van Damme, E. J., Peumans, W. J., De Ranter, C. J., and Rougé, P. (2005) Structural analysis of the jacalin-related lectin Morniga M from the black mulberry (Morus nigra) in complex with mannose. FEBS J. 272, 3725-3732 (Pubitemid 41021183)
    • (2005) FEBS Journal , vol.272 , Issue.14 , pp. 3725-3732
    • Rabijns, A.1    Barre, A.2    Van Damme, E.J.M.3    Peumans, W.J.4    De Ranter, C.J.5    Rouge, P.6
  • 21
    • 26444524471 scopus 로고    scopus 로고
    • The first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain
    • DOI 10.1016/j.jmb.2005.08.055, PII S0022283605010090
    • Gallego del Sol, F., Nagano, C., Cavada, B. S., and Calvete, J. J. (2005) The first crystal structure of a Mimosoideae lectin reveals a novel quaternary arrangement of a widespread domain. J. Mol. Biol. 353, 574-583 (Pubitemid 41417738)
    • (2005) Journal of Molecular Biology , vol.353 , Issue.3 , pp. 574-583
    • Gallego, D.S.F.1    Nagano, C.2    Cavada, B.S.3    Calvete, J.J.4
  • 22
    • 33745808885 scopus 로고    scopus 로고
    • Domain-Swapped Structure of the Potent Antiviral Protein Griffithsin and Its Mode of Carbohydrate Binding
    • DOI 10.1016/j.str.2006.05.017, PII S0969212606002565
    • Ziółkowska, N. E., O'Keefe, B. R., Mori, T., Zhu, C., Giomarelli, B., Vojdani, F., Palmer, K. E., McMahon, J. B., and Wlodawer, A. (2006) Domainswapped structure of the potent antiviral protein griffithsin and its mode of carbohydrate binding. Structure 14, 1127-1135 (Pubitemid 44056021)
    • (2006) Structure , vol.14 , Issue.7 , pp. 1127-1135
    • Ziolkowska, N.E.1    O'Keefe, B.R.2    Mori, T.3    Zhu, C.4    Giomarelli, B.5    Vojdani, F.6    Palmer, K.E.7    McMahon, J.B.8    Wlodawer, A.9
  • 23
    • 27244432997 scopus 로고    scopus 로고
    • Crystal structure of banana lectin reveals a novel second sugar binding site
    • DOI 10.1093/glycob/cwi088
    • Meagher, J. L., Winter, H. C., Ezell, P., Goldstein, I. J., and Stuckey, J. A. (2005) Crystal structure of banana lectin reveals a novel second sugar binding site. Glycobiology 15, 1033-1042 (Pubitemid 41511498)
    • (2005) Glycobiology , vol.15 , Issue.10 , pp. 1033-1042
    • Meagher, J.L.1    Winter, H.C.2    Ezell, P.3    Goldstein, I.J.4    Stuckey, J.A.5
  • 24
    • 0032523417 scopus 로고    scopus 로고
    • Characterization of heparin oligosaccharide mixtures as ammonium salts using electrospray mass spectrometry
    • Chai, W., Luo, J., Lim, C. K., and Lawson, A. M. (1998) Characterization of heparin oligosaccharide mixtures as ammonium salts using electrospray mass spectrometry. Anal. Chem. 70, 2060-2066
    • (1998) Anal. Chem. , vol.70 , pp. 2060-2066
    • Chai, W.1    Luo, J.2    Lim, C.K.3    Lawson, A.M.4
  • 25
    • 0035167226 scopus 로고    scopus 로고
    • Inhibition of adhesion of Plasmodium falciparum-infected erythrocytes by structurally defined hyaluronic acid dodecasaccharides
    • DOI 10.1128/IAI.69.1.420-425.2001
    • Chai, W., Beeson, J. G., Kogelberg, H., Brown, G. V., and Lawson, A. M. (2001) Inhibition of adhesion of Plasmodium falciparum-infected erythrocytes by structurally defined hyaluronic acid dodecasaccharides. Infect. Immun. 69, 420-425 (Pubitemid 32038341)
    • (2001) Infection and Immunity , vol.69 , Issue.1 , pp. 420-425
    • Chai, W.1    Beeson, J.G.2    Kogelberg, H.3    Brown, G.V.4    Lawson, A.M.5
  • 26
    • 0026729007 scopus 로고
    • Synthesis and conformational and NMR studies of α-D-mannopyranosyl and α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl linked to L-serine and L-threonine
    • Helander, A., Kenne, L., Oscarson, S., Peters, T., and Brisson, J. R. (1992) Synthesis and conformational and NMR studies of α-D-mannopyranosyl and α-D-mannopyranosyl-(1→2)-α-D-mannopyranosyl linked to L-serine and L-threonine. Carbohydr. Res. 230, 299-318
    • (1992) Carbohydr. Res. , vol.230 , pp. 299-318
    • Helander, A.1    Kenne, L.2    Oscarson, S.3    Peters, T.4    Brisson, J.R.5
  • 28
    • 79960319417 scopus 로고    scopus 로고
    • Synthesis of Tn/T antigen MUC1 glycopeptide BSA conjugates and their evaluation as vaccines
    • Cai, H., Huang, Z. H., Shi, L., Zou, P., Zhao, Y. F., Kunz, H., and Li, Y. M. (2011) Synthesis of Tn/T antigen MUC1 glycopeptide BSA conjugates and their evaluation as vaccines. Eur. J. Org. Chem. 2011, 3685-3689
    • (2011) Eur. J. Org. Chem. , vol.2011 , pp. 3685-3689
    • Cai, H.1    Huang, Z.H.2    Shi, L.3    Zou, P.4    Zhao, Y.F.5    Kunz, H.6    Li, Y.M.7
  • 30
    • 52949123215 scopus 로고    scopus 로고
    • pCold-GST vector: A novel cold-shock vector containing GST tag for soluble protein production
    • Hayashi, K., and Kojima, C. (2008) pCold-GST vector: a novel cold-shock vector containing GST tag for soluble protein production. Protein Expr. Purif. 62, 120-127
    • (2008) Protein Expr. Purif. , vol.62 , pp. 120-127
    • Hayashi, K.1    Kojima, C.2
  • 31
    • 0036788485 scopus 로고    scopus 로고
    • Oligosaccharide microarrays for high-throughput detection and specificity assignments of carbohydrate-protein interactions
    • Fukui, S., Feizi, T., Galustian, C., Lawson, A. M., and Chai, W. (2002) Oligosaccharide microarrays for high-throughput detection and specificity assignments of carbohydrate-protein interactions. Nat. Biotechnol. 20, 1011-1017
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1011-1017
    • Fukui, S.1    Feizi, T.2    Galustian, C.3    Lawson, A.M.4    Chai, W.5
  • 33
    • 82355193805 scopus 로고    scopus 로고
    • Neoglycolipid-based oligosaccharide microarray system: Preparation of NGLs and their noncovalent immobilization on nitrocellulose-coated glass slides for microarray analyses
    • Liu, Y., Childs, R. A., Palma, A. S., Campanero-Rhodes, M. A., Stoll, M. S., Chai, W., and Feizi, T. (2012) Neoglycolipid-based oligosaccharide microarray system: preparation of NGLs and their noncovalent immobilization on nitrocellulose-coated glass slides for microarray analyses. Methods Mol. Biol. 808, 117-136
    • (2012) Methods Mol. Biol. , vol.808 , pp. 117-136
    • Liu, Y.1    Childs, R.A.2    Palma, A.S.3    Campanero-Rhodes, M.A.4    Stoll, M.S.5    Chai, W.6    Feizi, T.7
  • 34
    • 82355168081 scopus 로고    scopus 로고
    • Software tools for storing, processing and displaying carbohydrate microarray data
    • (Kettner, C., ed)
    • Stoll, M. S., and Feizi, T. (2009) Software tools for storing, processing and displaying carbohydrate microarray data in Proceeding of the Beilstein Symposium on Glyco-Bioinformatics (Kettner, C., ed) pp. 123-140
    • (2009) Proceeding of the Beilstein Symposium on Glyco-Bioinformatics , pp. 123-140
    • Stoll, M.S.1    Feizi, T.2
  • 36
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 37
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An Automated Program for Molecular Replacement
    • Vagin, A., and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025 (Pubitemid 127485985)
    • (1997) Journal of Applied Crystallography , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 41
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 42
    • 0023756891 scopus 로고
    • Protective role of glutathione and glutathione transferases in mutagenesis and carcinogenesis
    • Ketterer, B. (1988) Protective role of glutathione and glutathione transferases in mutagenesis and carcinogenesis. Mutat. Res. 202, 343-361
    • (1988) Mutat. Res. , vol.202 , pp. 343-361
    • Ketterer, B.1
  • 43
    • 0028931691 scopus 로고
    • Crystal structures of a schistosomal drug and vaccine target: Glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel
    • McTigue, M. A., Williams, D. R., and Tainer, J. A. (1995) Crystal structures of a schistosomal drug and vaccine target: glutathione S-transferase from Schistosoma japonica and its complex with the leading antischistosomal drug praziquantel. J. Mol. Biol. 246, 21-27
    • (1995) J. Mol. Biol. , vol.246 , pp. 21-27
    • McTigue, M.A.1    Williams, D.R.2    Tainer, J.A.3
  • 44
    • 0024021040 scopus 로고
    • Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
    • Casu, B., Petitou, M., Provasoli, M., and Sinaÿ, P. (1988) Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans. Trends Biochem. Sci. 13, 221-225
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 221-225
    • Casu, B.1    Petitou, M.2    Provasoli, M.3    Sinaÿ, P.4
  • 45
    • 67650159384 scopus 로고    scopus 로고
    • Protein O-mannosylation: Conserved from bacteria to humans
    • Lommel, M., and Strahl, S. (2009) Protein O-mannosylation: conserved from bacteria to humans. Glycobiology 19, 816-828
    • (2009) Glycobiology , vol.19 , pp. 816-828
    • Lommel, M.1    Strahl, S.2
  • 46
    • 27744542116 scopus 로고    scopus 로고
    • Protein O-mannosyltransferase A of Aspergillus awamori is involved in O-mannosylation of glucoamylase I
    • DOI 10.1099/mic.0.28088-0
    • Oka, T., Sameshima, Y., Koga, T., Kim, H., Goto, M., and Furukawa, K. (2005) Protein O-mannosyltransferase A of Aspergillus awamori is involved in O-mannosylation of glucoamylase I. Microbiology 151, 3657-3667 (Pubitemid 41632076)
    • (2005) Microbiology , vol.151 , Issue.11 , pp. 3657-3667
    • Oka, T.1    Sameshima, Y.2    Koga, T.3    Kim, H.4    Goto, M.5    Furukawa, K.6
  • 47
    • 23244440497 scopus 로고    scopus 로고
    • Microbiology: Export-mediated assembly of mycobacterial glycoproteins parallels eukaryotic pathways
    • DOI 10.1126/science.1114347
    • VanderVen, B. C., Harder, J. D., Crick, D. C., and Belisle, J. T. (2005) Export-mediated assembly of mycobacterial glycoproteins parallels eukaryotic pathways. Science 309, 941-943 (Pubitemid 41099932)
    • (2005) Science , vol.309 , Issue.5736 , pp. 941-943
    • VanderVen, B.C.1    Harder, J.D.2    Crick, D.C.3    Belisle, J.T.4
  • 48
    • 34347327263 scopus 로고    scopus 로고
    • Protein O-glycosylation in fungi: Diverse structures and multiple functions
    • Goto, M. (2007) Protein O-glycosylation in fungi: diverse structures and multiple functions. Biosci. Biotechnol. Biochem. 71, 1415-1427
    • (2007) Biosci. Biotechnol. Biochem. , vol.71 , pp. 1415-1427
    • Goto, M.1
  • 49
    • 39749162836 scopus 로고    scopus 로고
    • Protein-O-mannosyl-transferases in virulence and development
    • Lengeler, K. B., Tielker, D., and Ernst, J. F. (2008) Protein-O-mannosyl-transferases in virulence and development. Cell Mol. Life Sci. 65, 528-544
    • (2008) Cell Mol. Life Sci. , vol.65 , pp. 528-544
    • Lengeler, K.B.1    Tielker, D.2    Ernst, J.F.3
  • 52
    • 0041620359 scopus 로고    scopus 로고
    • MATRAS: A program for protein 3D structure comparison
    • Kawabata, T. (2003) MATRAS: A program for protein 3D structure comparison. Nucleic Acids Res. 31, 3367-3369
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3367-3369
    • Kawabata, T.1
  • 53
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G., and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22, 4673-4680 (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.