메뉴 건너뛰기




Volumn 190, Issue 17, 2008, Pages 5944-5952

Salmonella enterica serovar Typhimurium BipA exhibits two distinct ribosome binding modes

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; PROTEIN BIP A; UNCLASSIFIED DRUG;

EID: 50249130207     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.00763-08     Document Type: Article
Times cited : (41)

References (52)
  • 1
    • 36348955613 scopus 로고    scopus 로고
    • A developmentally regulated GTP binding tyrosine phosphorylated protein A-like cDNA in cucumber (Cucumis sativus L.)
    • Barak, M., and T. Trebitsh. 2007. A developmentally regulated GTP binding tyrosine phosphorylated protein A-like cDNA in cucumber (Cucumis sativus L.). Plant Mol. Biol. 65:829-837.
    • (2007) Plant Mol. Biol , vol.65 , pp. 829-837
    • Barak, M.1    Trebitsh, T.2
  • 2
    • 0009002119 scopus 로고    scopus 로고
    • Formate protects stationary-phase Escherichia coli and Salmonella cells from killing by a cationic antimicrobial peptide
    • Barker, H. C., N. Kinsella, A. Jaspe, T. Friedrich, and C. D. O'Connor. 2000. Formate protects stationary-phase Escherichia coli and Salmonella cells from killing by a cationic antimicrobial peptide. Mol. Microbiol. 35:1518-1529.
    • (2000) Mol. Microbiol , vol.35 , pp. 1518-1529
    • Barker, H.C.1    Kinsella, N.2    Jaspe, A.3    Friedrich, T.4    O'Connor, C.D.5
  • 3
    • 0036844248 scopus 로고    scopus 로고
    • Genomewide transcriptional analysis of the cold shock response in Bacillus subtilis
    • Beckering, C. L., L. Steil, M. H. W. Weber, U. Volker, and M. A. Marahiel. 2002. Genomewide transcriptional analysis of the cold shock response in Bacillus subtilis. J. Bacteriol. 184:6395-6402.
    • (2002) J. Bacteriol , vol.184 , pp. 6395-6402
    • Beckering, C.L.1    Steil, L.2    Weber, M.H.W.3    Volker, U.4    Marahiel, M.A.5
  • 4
    • 33751075737 scopus 로고    scopus 로고
    • A cooperative and critical role for both G domains in the GTPase activity and cellular function of ribosome-associated Escherichia coli EngA
    • Bharat, A., M. Jiang, S. M. Sullivan, J. R. Maddock, and E. D. Brown. 2006. A cooperative and critical role for both G domains in the GTPase activity and cellular function of ribosome-associated Escherichia coli EngA. J. Bacteriol. 188:7992-7996.
    • (2006) J. Bacteriol , vol.188 , pp. 7992-7996
    • Bharat, A.1    Jiang, M.2    Sullivan, S.M.3    Maddock, J.R.4    Brown, E.D.5
  • 5
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature 349:1117-1127.
    • (1991) Nature , vol.349 , pp. 1117-1127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 6
  • 8
    • 32044468906 scopus 로고    scopus 로고
    • Conserved P-loop GTPases of unknown function in bacteria: An emerging vital ensemble in bacterial physiology
    • Brown, E. D. 2005. Conserved P-loop GTPases of unknown function in bacteria: an emerging vital ensemble in bacterial physiology. Biochem. Cell Biol. 83:738-746.
    • (2005) Biochem. Cell Biol , vol.83 , pp. 738-746
    • Brown, E.D.1
  • 9
    • 0036849768 scopus 로고    scopus 로고
    • Structural and biochemical analysis of the Obg GTP binding protein
    • Buglino, J., V. Shen, P. Hakimian, and C. D. Lima. 2002. Structural and biochemical analysis of the Obg GTP binding protein. Structure 10:1581-1592.
    • (2002) Structure , vol.10 , pp. 1581-1592
    • Buglino, J.1    Shen, V.2    Hakimian, P.3    Lima, C.D.4
  • 10
    • 0038352105 scopus 로고    scopus 로고
    • Function of the universally conserved bacterial GTPases
    • Caldon, C. E., and P. E. March. 2003. Function of the universally conserved bacterial GTPases. Curr. Opin. Microbiol. 6:135-139.
    • (2003) Curr. Opin. Microbiol , vol.6 , pp. 135-139
    • Caldon, C.E.1    March, P.E.2
  • 11
    • 0003174053 scopus 로고    scopus 로고
    • The stringent response
    • F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger ed, 2nd ed. ASM Press, Washington, DC
    • Cashel, M., D. M. Gentry, V. J. Hernandez, and D. Vinella. 1996. The stringent response, p. 1458-1496. In F. C. Neidhardt, R. Curtiss III, J. L. Ingraham, E. C. C. Lin, K. B. Low, B. Magasanik, W. S. Reznikoff, M. Riley, M. Schaechter, and H. E. Umbarger (ed.), Escherichia coli and Salmonella: cellular and molecular biology, 2nd ed. ASM Press, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and molecular biology , pp. 1458-1496
    • Cashel, M.1    Gentry, D.M.2    Hernandez, V.J.3    Vinella, D.4
  • 12
    • 33748414041 scopus 로고    scopus 로고
    • Non-ribosomal factors in ribosome subunit assembly are emerging targets for new antibacterial drugs
    • Comartin, D. J., and E. D. Brown. 2006. Non-ribosomal factors in ribosome subunit assembly are emerging targets for new antibacterial drugs. Curr. Opin. Pharmacol. 6:453-458.
    • (2006) Curr. Opin. Pharmacol , vol.6 , pp. 453-458
    • Comartin, D.J.1    Brown, E.D.2
  • 13
    • 1342346614 scopus 로고    scopus 로고
    • Studies of the interaction of Escherichia coli YjeQ with the ribosome in vitro
    • Daigle, D. M., and E. D. Brown. 2004. Studies of the interaction of Escherichia coli YjeQ with the ribosome in vitro. J. Bacteriol. 186:1381-1387.
    • (2004) J. Bacteriol , vol.186 , pp. 1381-1387
    • Daigle, D.M.1    Brown, E.D.2
  • 14
    • 0037125960 scopus 로고    scopus 로고
    • YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics
    • Daigle, D. M., L. Rossi, A. M. Berghuis, L. Aravind, E. V. Koonin, and E. D. Brown. 2002. YjeQ, an essential, conserved, uncharacterized protein from Escherichia coli, is an unusual GTPase with circularly permuted G-motifs and marked burst kinetics. Biochemistry 41:11109-11117.
    • (2002) Biochemistry , vol.41 , pp. 11109-11117
    • Daigle, D.M.1    Rossi, L.2    Berghuis, A.M.3    Aravind, L.4    Koonin, E.V.5    Brown, E.D.6
  • 15
    • 50249126831 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 16
    • 0031919615 scopus 로고    scopus 로고
    • BipA: A tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells
    • Farris, M., A. Grant, T. B. Richardson, and C. D. O'Connor. 1998. BipA: a tyrosine-phosphorylated GTPase that mediates interactions between enteropathogenic Escherichia coli (EPEC) and epithelial cells. Mol. Microbiol. 28:265-279.
    • (1998) Mol. Microbiol , vol.28 , pp. 265-279
    • Farris, M.1    Grant, A.2    Richardson, T.B.3    O'Connor, C.D.4
  • 18
    • 0017413237 scopus 로고
    • Anomalous synthesis of ppGpp in growing cells
    • Gallant, J., L. Palmer, and C. C. Pao. 1977. Anomalous synthesis of ppGpp in growing cells. Cell 11:181-185.
    • (1977) Cell , vol.11 , pp. 181-185
    • Gallant, J.1    Palmer, L.2    Pao, C.C.3
  • 19
    • 0029069592 scopus 로고
    • Cellular localization of the Escherichia coli SpoT protein
    • Gentry, D. R., and M. Cashel. 1995. Cellular localization of the Escherichia coli SpoT protein. J. Bacteriol. 177:3890-3893.
    • (1995) J. Bacteriol , vol.177 , pp. 3890-3893
    • Gentry, D.R.1    Cashel, M.2
  • 20
    • 0038011029 scopus 로고    scopus 로고
    • Co-ordination of pathogenicity island expression by the BipA GTPase in enteropathogenic Escherichia coli (EPEC)
    • Grant, A. J., M. Farris, P. Alefounder, P. H. Williams, M. J. Woodward, and C. D. O'Connor. 2003. Co-ordination of pathogenicity island expression by the BipA GTPase in enteropathogenic Escherichia coli (EPEC). Mol. Microbiol. 48:507-521.
    • (2003) Mol. Microbiol , vol.48 , pp. 507-521
    • Grant, A.J.1    Farris, M.2    Alefounder, P.3    Williams, P.H.4    Woodward, M.J.5    O'Connor, C.D.6
  • 21
    • 0035660388 scopus 로고    scopus 로고
    • An in vitro transposon system for highly regulated gene expression: Construction of Escherichia coli strains with arabinose-dependent growth at low temperatures
    • Grant, A. J., R. Haigh, P. Williams, and C. D. O'Connor. 2001. An in vitro transposon system for highly regulated gene expression: construction of Escherichia coli strains with arabinose-dependent growth at low temperatures. Gene 280:145-151.
    • (2001) Gene , vol.280 , pp. 145-151
    • Grant, A.J.1    Haigh, R.2    Williams, P.3    O'Connor, C.D.4
  • 22
    • 0021396255 scopus 로고
    • Accumulation of relA gene-independent ppGpp in Bacillus subtilis vegetative cells upon temperature shift-down
    • Ikehara, K., H. Okada, K. Maeda, A. Ogura, and K. Sugae. 1984. Accumulation of relA gene-independent ppGpp in Bacillus subtilis vegetative cells upon temperature shift-down. J. Biochem. 95:895-897.
    • (1984) J. Biochem , vol.95 , pp. 895-897
    • Ikehara, K.1    Okada, H.2    Maeda, K.3    Ogura, A.4    Sugae, K.5
  • 23
    • 33646824923 scopus 로고    scopus 로고
    • ppGpp: Stringent response and survival
    • Jain, V., M. Kumar, and D. Chatterji. 2006. ppGpp: stringent response and survival. J. Microbiol. 44:1-10.
    • (2006) J. Microbiol , vol.44 , pp. 1-10
    • Jain, V.1    Kumar, M.2    Chatterji, D.3
  • 24
    • 34548513288 scopus 로고    scopus 로고
    • G-protein control of the ribosome-associated stress response protein SpoT
    • Jiang, M., S. M. Sullivan, P. K. Wout, and J. R. Maddock. 2007. G-protein control of the ribosome-associated stress response protein SpoT. J. Bacteriol. 189:6140-6147.
    • (2007) J. Bacteriol , vol.189 , pp. 6140-6147
    • Jiang, M.1    Sullivan, S.M.2    Wout, P.K.3    Maddock, J.R.4
  • 25
    • 0026680453 scopus 로고
    • Function of a relaxed-like state following temperature downshifts in Escherichia coli
    • Jones, P. G., M. Cashel, G. Glaser, and F. C. Neidhardt. 1992. Function of a relaxed-like state following temperature downshifts in Escherichia coli. J. Bacteriol. 174:3903-3914.
    • (1992) J. Bacteriol , vol.174 , pp. 3903-3914
    • Jones, P.G.1    Cashel, M.2    Glaser, G.3    Neidhardt, F.C.4
  • 26
    • 34548606694 scopus 로고    scopus 로고
    • Role of GTPases in ribosome assembly
    • Karbstein, K. 2007. Role of GTPases in ribosome assembly. Biopolymers 87:1-11.
    • (2007) Biopolymers , vol.87 , pp. 1-11
    • Karbstein, K.1
  • 27
    • 1642505776 scopus 로고    scopus 로고
    • The typA gene is required for stress adaptation as well as for symbiosis of Sinorhizobium meliloti 1021 with certain Medicago truncatula lines
    • Kiss, E., T. Huguet, V. Poinsot, and J. Batut. 2004. The typA gene is required for stress adaptation as well as for symbiosis of Sinorhizobium meliloti 1021 with certain Medicago truncatula lines. Mol. Plant-Microbe Interact. 17:235-244.
    • (2004) Mol. Plant-Microbe Interact , vol.17 , pp. 235-244
    • Kiss, E.1    Huguet, T.2    Poinsot, V.3    Batut, J.4
  • 28
    • 0018600707 scopus 로고
    • An improved assay for nanomole amounts of inorganic phosphate
    • Lanzetta, P. A., L. J. Alvaez, P. S. Reinach, and O. A. Candia. 1979. An improved assay for nanomole amounts of inorganic phosphate. Anal. Biochem. 100:95-97.
    • (1979) Anal. Biochem , vol.100 , pp. 95-97
    • Lanzetta, P.A.1    Alvaez, L.J.2    Reinach, P.S.3    Candia, O.A.4
  • 29
    • 0021034291 scopus 로고
    • Correlation between RNA synthesis and ppGpp content in Escherichia coli
    • Mackow, E. R., and F. N. Chang. 1983. Correlation between RNA synthesis and ppGpp content in Escherichia coli. Mol. Gen. Genet. 192:5-9.
    • (1983) Mol. Gen. Genet , vol.192 , pp. 5-9
    • Mackow, E.R.1    Chang, F.N.2
  • 30
    • 18044367581 scopus 로고    scopus 로고
    • ppGpp: A global regulator in Escherichia coli
    • Magnusson, L. U., A. Farewell, and T. Nystrom. 2005. ppGpp: a global regulator in Escherichia coli. Trends Microbiol. 13:238-242.
    • (2005) Trends Microbiol , vol.13 , pp. 238-242
    • Magnusson, L.U.1    Farewell, A.2    Nystrom, T.3
  • 31
    • 33846887420 scopus 로고    scopus 로고
    • Phylogenetic distribution of translational GTPases in bacteria
    • Margus, T., M. Remm, and T. Tenson. 2007. Phylogenetic distribution of translational GTPases in bacteria. BMC Genomics 10:8-15.
    • (2007) BMC Genomics , vol.10 , pp. 8-15
    • Margus, T.1    Remm, M.2    Tenson, T.3
  • 32
    • 0036837783 scopus 로고    scopus 로고
    • Tightly regulated gene expression system in Salmonella enterica serovar Typhimurium
    • McKinney, J., C. Guerrier-Takada, J. Gala, and S. Altman. 2002. Tightly regulated gene expression system in Salmonella enterica serovar Typhimurium. J. Bacteriol. 184:6056-6059.
    • (2002) J. Bacteriol , vol.184 , pp. 6056-6059
    • McKinney, J.1    Guerrier-Takada, C.2    Gala, J.3    Altman, S.4
  • 34
    • 0029943235 scopus 로고    scopus 로고
    • Control of spoT-dependent ppGpp synthesis and degradation in Escherichia coli
    • Murray, K. D., and H. Bremer. 1996. Control of spoT-dependent ppGpp synthesis and degradation in Escherichia coli. Biochemistry 259:41-57.
    • (1996) Biochemistry , vol.259 , pp. 41-57
    • Murray, K.D.1    Bremer, H.2
  • 36
    • 0025310575 scopus 로고
    • Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: Implications for the mechanism of GTP hydrolysis
    • Pai, E. F., U. Krengel, G. A. Petsko, R. S. Goody, W. Kabsch, and A. Wittinghofer. 1990. Refined crystal structure of the triphosphate conformation of H-ras p21 at 1.35 A resolution: implications for the mechanism of GTP hydrolysis. EMBO J. 9:2351-2359.
    • (1990) EMBO J , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5    Wittinghofer, A.6
  • 37
    • 0034790216 scopus 로고    scopus 로고
    • BipA is required for growth of Escherichia coli K12 at low temperature
    • Pfennig, P. L., and A. M. Flower. 2001. BipA is required for growth of Escherichia coli K12 at low temperature. Mol. Genet. Genomics 266:313-317.
    • (2001) Mol. Genet. Genomics , vol.266 , pp. 313-317
    • Pfennig, P.L.1    Flower, A.M.2
  • 38
    • 0029095544 scopus 로고
    • Salmonella typhimurium responses to a bactericidal protein from human neutrophils
    • Qi, S. Y., Y. Li, A. Szyroki, I. G. Giles, A. Moir, and C. D. O'Connor. 1995. Salmonella typhimurium responses to a bactericidal protein from human neutrophils. Mol. Microbiol. 17:523-531.
    • (1995) Mol. Microbiol , vol.17 , pp. 523-531
    • Qi, S.Y.1    Li, Y.2    Szyroki, A.3    Giles, I.G.4    Moir, A.5    O'Connor, C.D.6
  • 39
    • 2442563845 scopus 로고
    • Localization of the stringent protein of Escherichia coli on the 50S ribosomal subunit
    • Ramagopal, S., and B. D. Davis. 1974. Localization of the stringent protein of Escherichia coli on the 50S ribosomal subunit. Proc. Natl. Acad. Sci. USA 71:820-824.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 820-824
    • Ramagopal, S.1    Davis, B.D.2
  • 40
    • 34248328786 scopus 로고    scopus 로고
    • Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae
    • Raskin, D. M., N. Judson, and J. J. Mekalanos. 2007. Regulation of the stringent response is the essential function of the conserved bacterial G protein CgtA in Vibrio cholerae. Proc. Natl. Acad. Sci. USA 104:4636-4641.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 4636-4641
    • Raskin, D.M.1    Judson, N.2    Mekalanos, J.J.3
  • 42
    • 0016801495 scopus 로고
    • Escherichia coli stringent factor binds to ribosomes at a site different from that of elongation factor Tu or G
    • Richter, D., P. Nowak, and U. Kleinert. 1975. Escherichia coli stringent factor binds to ribosomes at a site different from that of elongation factor Tu or G. Biochemistry 14:4414-4420.
    • (1975) Biochemistry , vol.14 , pp. 4414-4420
    • Richter, D.1    Nowak, P.2    Kleinert, U.3
  • 43
    • 1842848075 scopus 로고    scopus 로고
    • Domain arrangement of Der, a switch protein containing two GTPase domains
    • Robinson, V. L., J. Hwang, E. Fox, M. Inouye, and A. M. Stock. 2002. Domain arrangement of Der, a switch protein containing two GTPase domains. Structure 10:1649-1658.
    • (2002) Structure , vol.10 , pp. 1649-1658
    • Robinson, V.L.1    Hwang, J.2    Fox, E.3    Inouye, M.4    Stock, A.M.5
  • 44
    • 0034098679 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli K5 capsule gene cluster: Evidence for the roles of H-NS, BipA, and integration host factor in regulation of group 2 capsule gene clusters in pathogenic E. coli
    • Rowe, S., N. Hodson, G. Griffiths, and I. S. Roberts. 2000. Regulation of the Escherichia coli K5 capsule gene cluster: evidence for the roles of H-NS, BipA, and integration host factor in regulation of group 2 capsule gene clusters in pathogenic E. coli. J. Bacteriol. 182:2741-2745.
    • (2000) J. Bacteriol , vol.182 , pp. 2741-2745
    • Rowe, S.1    Hodson, N.2    Griffiths, G.3    Roberts, I.S.4
  • 45
    • 0035374345 scopus 로고    scopus 로고
    • 2+ is not catalytically required in the intrinsic and kirromycin-stimulated GTPase action of Thermus thermophilus EF-Tu
    • 2+ is not catalytically required in the intrinsic and kirromycin-stimulated GTPase action of Thermus thermophilus EF-Tu. Biochemistry 276:18728-18733.
    • (2001) Biochemistry , vol.276 , pp. 18728-18733
    • Rutthard, H.1    Banerjee, A.2    Makinen, M.W.3
  • 46
    • 0141452069 scopus 로고    scopus 로고
    • TypA is a virulence regulator and is present in many pathogenic bacteria
    • Scott, K., M. A. Diggle, and S. C. Clarke. 2003. TypA is a virulence regulator and is present in many pathogenic bacteria. Br. J. Biomed. Sci. 60:168-170.
    • (2003) Br. J. Biomed. Sci , vol.60 , pp. 168-170
    • Scott, K.1    Diggle, M.A.2    Clarke, S.C.3
  • 47
    • 0002477677 scopus 로고
    • Isolation and analysis of ribosomes from prokaryotes, eukaryotes and organelles
    • G. Spedding ed, IRL Press, New York, NY
    • Spedding, G. 1990. Isolation and analysis of ribosomes from prokaryotes, eukaryotes and organelles, p. 5-8. In G. Spedding (ed.), Ribosomes and protein synthesis: a practical approach. IRL Press, New York, NY.
    • (1990) Ribosomes and protein synthesis: A practical approach , pp. 5-8
    • Spedding, G.1
  • 48
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang, S. R. 1997. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66:639-678.
    • (1997) Annu. Rev. Biochem , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 49
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase promoter system for controlled exclusive expression of specific genes
    • Tabor, S., and C. C. Richardson. 1985. A bacteriophage T7 RNA polymerase promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. USA 82:1074-1078.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 50
    • 0017862007 scopus 로고
    • The temperature sensitive mutant 72c. II. Accumulation at high temperature of ppGpp and pppGpp in the presence of protein synthesis
    • Takata, R., and L. A. Isaksson. 1978. The temperature sensitive mutant 72c. II. Accumulation at high temperature of ppGpp and pppGpp in the presence of protein synthesis. Mol. Genet. Genomics 161:15-21.
    • (1978) Mol. Genet. Genomics , vol.161 , pp. 15-21
    • Takata, R.1    Isaksson, L.A.2
  • 51
    • 0015079354 scopus 로고
    • Biochemical basis for the antimetabolite action of L-serine hydroxamate
    • Tosa, T., and L. I. Pizer. 1971. Biochemical basis for the antimetabolite action of L-serine hydroxamate. J. Bacteriol. 106:972-982.
    • (1971) J. Bacteriol , vol.106 , pp. 972-982
    • Tosa, T.1    Pizer, L.I.2
  • 52
    • 3843074167 scopus 로고    scopus 로고
    • The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase
    • Wout, P., K. Pu, S. M. Sullivan, V. Reese, S. Zhou, B. Lin, and J. R. Maddock. 2004. The Escherichia coli GTPase CgtAE cofractionates with the 50S ribosomal subunit and interacts with SpoT, a ppGpp synthetase/hydrolase. J. Bacteriol. 186:5249-5257.
    • (2004) J. Bacteriol , vol.186 , pp. 5249-5257
    • Wout, P.1    Pu, K.2    Sullivan, S.M.3    Reese, V.4    Zhou, S.5    Lin, B.6    Maddock, J.R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.