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Volumn 198, Issue 1, 2016, Pages 32-46

Diversity of cyclic di-GMP-binding proteins and mechanisms

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ARGININE; ASPARTIC ACID; BINDING PROTEIN; CYCLIC DI GMP BINDING PROTEIN; CYCLIC GMP; CYCLIC GMP DERIVATIVE; DIMER; EAL PROTEIN; GLUTAMIC ACID; GUANINE; HYDROLASE; MEMBRANE PROTEIN; MONOMER; PHENYLALANINE; PILZ PROTEIN; RECEPTOR PROTEIN; TETRAMER; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR VPST; TYROSINE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; BIS(3',5')-CYCLIC DIGUANYLIC ACID; PROTEIN BINDING;

EID: 84953924413     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.00333-15     Document Type: Review
Times cited : (215)

References (94)
  • 1
    • 84874914744 scopus 로고    scopus 로고
    • Cyclic di-GMP: the first 25 years of a universal bacterial second messenger
    • Römling U, Galperin MY, Gomelsky M. 2013. Cyclic di-GMP: the first 25 years of a universal bacterial second messenger. Microbiol Mol Biol Rev 77:1-52. http://dx.doi.org/10.1128/MicrobiolMolBiolRev.00043-12.
    • (2013) Microbiol Mol Biol Rev , vol.77 , pp. 1-52
    • Römling, U.1    Galperin, M.Y.2    Gomelsky, M.3
  • 2
    • 84870208079 scopus 로고    scopus 로고
    • Second messenger regulation of biofilm formation: breakthroughs in understanding c-di-GMP effector systems
    • Boyd CD, O'Toole GA. 2012. Second messenger regulation of biofilm formation: breakthroughs in understanding c-di-GMP effector systems. Annu Rev Cell Dev Biol 28:439-462. http://dx.doi.org/10.1146/annurev-cellbio-101011-155705.
    • (2012) Annu Rev Cell Dev Biol , vol.28 , pp. 439-462
    • Boyd, C.D.1    O'Toole, G.A.2
  • 3
    • 84879835990 scopus 로고    scopus 로고
    • Cyclic di-GMP signalling and the regulation of bacterial virulence
    • Ryan RP. 2013. Cyclic di-GMP signalling and the regulation of bacterial virulence. Microbiology 159:1286-1297. http://dx.doi.org/10.1099/mic.0.068189-0.
    • (2013) Microbiology , vol.159 , pp. 1286-1297
    • Ryan, R.P.1
  • 4
    • 70349274104 scopus 로고    scopus 로고
    • Structural and mechanistic determinants of c-di-GMP signalling
    • Schirmer T, Jenal U. 2009. Structural and mechanistic determinants of c-di-GMP signalling. Nat Rev Microbiol 7:724-735. http://dx.doi.org/10.1038/nrmicro2203.
    • (2009) Nat Rev Microbiol , vol.7 , pp. 724-735
    • Schirmer, T.1    Jenal, U.2
  • 5
    • 84862527194 scopus 로고    scopus 로고
    • Sensing the messenger: the diverse ways that bacteria signal through c-di-GMP
    • Krasteva PV, Giglio KM, Sondermann H. 2012. Sensing the messenger: the diverse ways that bacteria signal through c-di-GMP. Protein Sci 21:929-948. http://dx.doi.org/10.1002/pro.2093.
    • (2012) Protein Sci , vol.21 , pp. 929-948
    • Krasteva, P.V.1    Giglio, K.M.2    Sondermann, H.3
  • 8
    • 0026093011 scopus 로고
    • Cellulose biosynthesis and function in bacteria
    • Ross P, Mayer R, Benziman M. 1991. Cellulose biosynthesis and function in bacteria. Microbiol Rev 55:35-58.
    • (1991) Microbiol Rev , vol.55 , pp. 35-58
    • Ross, P.1    Mayer, R.2    Benziman, M.3
  • 9
    • 0030734277 scopus 로고    scopus 로고
    • c-di-GMP-binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum
    • Weinhouse H, Sapir S, Amikam D, Shilo Y, Volman G, Ohana P, Benziman M. 1997. c-di-GMP-binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum. FEBS Lett 416:207-211. http://dx.doi.org/10.1016/S0014-5793(97)01202-7.
    • (1997) FEBS Lett , vol.416 , pp. 207-211
    • Weinhouse, H.1    Sapir, S.2    Amikam, D.3    Shilo, Y.4    Volman, G.5    Ohana, P.6    Benziman, M.7
  • 10
    • 0033222409 scopus 로고    scopus 로고
    • A specialized version of the HD hydrolase domain implicated in signal transduction
    • Galperin MY, Natale DA, Aravind L, Koonin EV. 1999. A specialized version of the HD hydrolase domain implicated in signal transduction. J Mol Microbiol Biotechnol 1:303-305. http://dx.doi.org/10.1159/issn.1464-1801.
    • (1999) J Mol Microbiol Biotechnol , vol.1 , pp. 303-305
    • Galperin, M.Y.1    Natale, D.A.2    Aravind, L.3    Koonin, E.V.4
  • 11
    • 0035845587 scopus 로고    scopus 로고
    • Novel domains of the prokaryotic two-component signal transduction systems
    • Galperin MY, Nikolskaya AN, Koonin EV. 2001. Novel domains of the prokaryotic two-component signal transduction systems. FEMS Microbiol Lett 203:11-21. http://dx.doi.org/10.1111/j.1574-6968.2001.tb10814.x.
    • (2001) FEMS Microbiol Lett , vol.203 , pp. 11-21
    • Galperin, M.Y.1    Nikolskaya, A.N.2    Koonin, E.V.3
  • 14
    • 34548303826 scopus 로고    scopus 로고
    • A cyclic-di-GMP receptor required for bacterial exopolysaccharide production
    • Lee VT, Matewish JM, Kessler JL, Hyodo M, Hayakawa Y, Lory S. 2007. A cyclic-di-GMP receptor required for bacterial exopolysaccharide production. Mol Microbiol 65:1474-1484. http://dx.doi.org/10.1111/j.1365-2958.2007.05879.x.
    • (2007) Mol Microbiol , vol.65 , pp. 1474-1484
    • Lee, V.T.1    Matewish, J.M.2    Kessler, J.L.3    Hyodo, M.4    Hayakawa, Y.5    Lory, S.6
  • 15
    • 62549150834 scopus 로고    scopus 로고
    • LapD is a bis-(3',5')-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1
    • Newell PD, Monds RD, O'Toole GA. 2009. LapD is a bis-(3',5')-cyclic dimeric GMP-binding protein that regulates surface attachment by Pseudomonas fluorescens Pf0-1. Proc Natl Acad Sci U S A 106:3461-3466. http://dx.doi.org/10.1073/pnas.0808933106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3461-3466
    • Newell, P.D.1    Monds, R.D.2    O'Toole, G.A.3
  • 16
    • 0028810683 scopus 로고
    • The novel cyclic dinucleotide 3'-5' cyclic diguanylic acid binds to p21ras and enhances DNA synthesis but not cell replication in the Molt 4 cell line
    • Amikam D, Steinberger O, Shkolnik T, Ben-Ishai Z. 1995. The novel cyclic dinucleotide 3'-5' cyclic diguanylic acid binds to p21ras and enhances DNA synthesis but not cell replication in the Molt 4 cell line. Biochem J 311:921-927. http://dx.doi.org/10.1016/S0014-5793(99)00036-8.
    • (1995) Biochem J , vol.311 , pp. 921-927
    • Amikam, D.1    Steinberger, O.2    Shkolnik, T.3    Ben-Ishai, Z.4
  • 17
    • 0033044554 scopus 로고    scopus 로고
    • Elevated expression of the CD4 receptor and cell cycle arrest are induced in Jurkat cells by treatment with the novel cyclic dinucleotide 3',5'-cyclic diguanylic acid
    • Steinberger O, Lapidot Z, Ben-Ishai Z, Amikam D. 1999. Elevated expression of the CD4 receptor and cell cycle arrest are induced in Jurkat cells by treatment with the novel cyclic dinucleotide 3',5'-cyclic diguanylic acid. FEBS Lett 444:125-129. http://dx.doi.org/10.1016/S0014-5793(99)00036-8.
    • (1999) FEBS Lett , vol.444 , pp. 125-129
    • Steinberger, O.1    Lapidot, Z.2    Ben-Ishai, Z.3    Amikam, D.4
  • 18
    • 30344469912 scopus 로고    scopus 로고
    • PilZ domain is part of the bacterial c-di-GMP binding protein
    • Amikam D, Galperin MY. 2006. PilZ domain is part of the bacterial c-di-GMP binding protein. Bioinformatics 22:3-6. http://dx.doi.org/10.1093/bioinformatics/bti739.
    • (2006) Bioinformatics , vol.22 , pp. 3-6
    • Amikam, D.1    Galperin, M.Y.2
  • 19
    • 33750044865 scopus 로고    scopus 로고
    • The PilZ domain is a receptor for the second messenger c-di-GMP. The PilZ domain protein YcgR controls motility in enterobacteria
    • Ryjenkov DA, Simm R, Römling U, Gomelsky M. 2006. The PilZ domain is a receptor for the second messenger c-di-GMP. The PilZ domain protein YcgR controls motility in enterobacteria. J Biol Chem 281:30310-30314. http://dx.doi.org/10.1074/jbc.C600179200.
    • (2006) J Biol Chem , vol.281 , pp. 30310-30314
    • Ryjenkov, D.A.1    Simm, R.2    Römling, U.3    Gomelsky, M.4
  • 21
    • 34247213819 scopus 로고    scopus 로고
    • DgrA is a member of a new family of cyclic diguanosine monophosphate receptors and controls flagellar motor function in Caulobacter crescentus
    • Christen M, Christen B, Allan MG, Folcher M, Jeno P, Grzesiek S, Jenal U. 2007. DgrA is a member of a new family of cyclic diguanosine monophosphate receptors and controls flagellar motor function in Caulobacter crescentus. Proc Natl Acad Sci U S A 104:4112-4117. http://dx.doi.org/10.1073/pnas.0607738104.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 4112-4117
    • Christen, M.1    Christen, B.2    Allan, M.G.3    Folcher, M.4    Jeno, P.5    Grzesiek, S.6    Jenal, U.7
  • 22
    • 34250358327 scopus 로고    scopus 로고
    • PilZ domain proteins bind cyclic diguanylate and regulate diverse processes in Vibrio cholerae
    • Pratt JT, Tamayo R, Tischler AD, Camilli A. 2007. PilZ domain proteins bind cyclic diguanylate and regulate diverse processes in Vibrio cholerae. J Biol Chem 282:12860-12870. http://dx.doi.org/10.1074/jbc.M611593200.
    • (2007) J Biol Chem , vol.282 , pp. 12860-12870
    • Pratt, J.T.1    Tamayo, R.2    Tischler, A.D.3    Camilli, A.4
  • 23
    • 33846006935 scopus 로고    scopus 로고
    • NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein
    • Ramelot TA, Yee A, Cort JR, Semesi A, Arrowsmith CH, Kennedy MA. 2007. NMR structure and binding studies confirm that PA4608 from Pseudomonas aeruginosa is a PilZ domain and a c-di-GMP binding protein. Proteins 66:266-271. http://dx.doi.org/10.1002/prot.21199.
    • (2007) Proteins , vol.66 , pp. 266-271
    • Ramelot, T.A.1    Yee, A.2    Cort, J.R.3    Semesi, A.4    Arrowsmith, C.H.5    Kennedy, M.A.6
  • 24
    • 23944523895 scopus 로고    scopus 로고
    • A census of membrane-bound and intracellular signal transduction proteins in bacteria: bacterial IQ, extroverts and introverts
    • Galperin MY. 2005. A census of membrane-bound and intracellular signal transduction proteins in bacteria: bacterial IQ, extroverts and introverts. BMC Microbiol 5:35. http://dx.doi.org/10.1186/1471-2180-5-35.
    • (2005) BMC Microbiol , vol.5 , pp. 35
    • Galperin, M.Y.1
  • 25
    • 63449138218 scopus 로고    scopus 로고
    • The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection
    • Lai TH, Kumagai Y, Hyodo M, Hayakawa Y, Rikihisa Y. 2009. The Anaplasma phagocytophilum PleC histidine kinase and PleD diguanylate cyclase two-component system and role of cyclic Di-GMP in host cell infection. J Bacteriol 191:693-700. http://dx.doi.org/10.1128/JB.01218-08.
    • (2009) J Bacteriol , vol.191 , pp. 693-700
    • Lai, T.H.1    Kumagai, Y.2    Hyodo, M.3    Hayakawa, Y.4    Rikihisa, Y.5
  • 26
    • 66149087307 scopus 로고    scopus 로고
    • XC1028 from Xanthomonas campestris adopts a PilZ domain-like structure without a c-di-GMP switch
    • Li TN, Chin KH, Liu JH, Wang AH, Chou SH. 2009. XC1028 from Xanthomonas campestris adopts a PilZ domain-like structure without a c-di-GMP switch. Proteins 75:282-288. http://dx.doi.org/10.1002/prot.22330.
    • (2009) Proteins , vol.75 , pp. 282-288
    • Li, T.N.1    Chin, K.H.2    Liu, J.H.3    Wang, A.H.4    Chou, S.H.5
  • 27
    • 84866702967 scopus 로고    scopus 로고
    • Structural polymorphism of c-di-GMP bound to an EAL domain and in complex with a type II PilZ-domain protein
    • Chin KH, Kuo WT, Yu YJ, Liao YT, Yang MT, Chou SH. 2012. Structural polymorphism of c-di-GMP bound to an EAL domain and in complex with a type II PilZ-domain protein. Acta Crystallogr D Biol Crystallogr 68:1380-1392. http://dx.doi.org/10.1107/S0907444912030594.
    • (2012) Acta Crystallogr D Biol Crystallogr , vol.68 , pp. 1380-1392
    • Chin, K.H.1    Kuo, W.T.2    Yu, Y.J.3    Liao, Y.T.4    Yang, M.T.5    Chou, S.H.6
  • 28
    • 84878261687 scopus 로고    scopus 로고
    • Structure of the PilZ-FimXEAL-c-di-GMP complex responsible for the regulation of bacterial type IV pilus biogenesis
    • Guzzo CR, Dunger G, Salinas RK, Farah CS. 2013. Structure of the PilZ-FimXEAL-c-di-GMP complex responsible for the regulation of bacterial type IV pilus biogenesis. J Mol Biol 425:2174-2197. http://dx.doi.org/10.1016/j.jmb.2013.03.021.
    • (2013) J Mol Biol , vol.425 , pp. 2174-2197
    • Guzzo, C.R.1    Dunger, G.2    Salinas, R.K.3    Farah, C.S.4
  • 29
    • 79960053518 scopus 로고    scopus 로고
    • A novel tetrameric PilZ domain structure from xanthomonads
    • Li TN, Chin KH, Fung KM, Yang MT, Wang AH, Chou SH. 2011. A novel tetrameric PilZ domain structure from xanthomonads. PLoS One 6:e22036. http://dx.doi.org/10.1371/journal.pone.0022036.
    • (2011) PLoS One , vol.6
    • Li, T.N.1    Chin, K.H.2    Fung, K.M.3    Yang, M.T.4    Wang, A.H.5    Chou, S.H.6
  • 30
    • 77955630859 scopus 로고    scopus 로고
    • An allosteric self-splicing ribozyme triggered by a bacterial second messenger
    • Lee ER, Baker JL, Weinberg Z, Sudarsan N, Breaker RR. 2010. An allosteric self-splicing ribozyme triggered by a bacterial second messenger. Science 329:845-848. http://dx.doi.org/10.1126/science.1190713.
    • (2010) Science , vol.329 , pp. 845-848
    • Lee, E.R.1    Baker, J.L.2    Weinberg, Z.3    Sudarsan, N.4    Breaker, R.R.5
  • 31
    • 47749152941 scopus 로고    scopus 로고
    • Riboswitches in eubacteria sense the second messenger cyclic di-GMP
    • Sudarsan N, Lee ER, Weinberg Z, Moy RH, Kim JN, Link KH, Breaker RR. 2008. Riboswitches in eubacteria sense the second messenger cyclic di-GMP. Science 321:411-413. http://dx.doi.org/10.1126/science.1159519.
    • (2008) Science , vol.321 , pp. 411-413
    • Sudarsan, N.1    Lee, E.R.2    Weinberg, Z.3    Moy, R.H.4    Kim, J.N.5    Link, K.H.6    Breaker, R.R.7
  • 32
    • 0035010211 scopus 로고    scopus 로고
    • Geometric nomenclature and classification of RNA base pairs
    • Leontis NB, Westhof E. 2001. Geometric nomenclature and classification of RNA base pairs. RNA 7:499-512. http://dx.doi.org/10.1017/S1355838201002515.
    • (2001) RNA , vol.7 , pp. 499-512
    • Leontis, N.B.1    Westhof, E.2
  • 33
    • 84907308411 scopus 로고    scopus 로고
    • Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development
    • Tschowri N, Schumacher MA, Schlimpert S, Chinnam NB, Findlay KC, Brennan RG, Buttner MJ. 2014. Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development. Cell 158:1136-1147. http://dx.doi.org/10.1016/j.cell.2014.07.022.
    • (2014) Cell , vol.158 , pp. 1136-1147
    • Tschowri, N.1    Schumacher, M.A.2    Schlimpert, S.3    Chinnam, N.B.4    Findlay, K.C.5    Brennan, R.G.6    Buttner, M.J.7
  • 35
    • 84863611012 scopus 로고    scopus 로고
    • Structure of the cytoplasmic region of PelD, a degenerate diguanylate cyclase receptor that regulates exopolysaccharide production in Pseudomonas aeruginosa
    • Whitney JC, Colvin KM, Marmont LS, Robinson H, Parsek MR, Howell PL. 2012. Structure of the cytoplasmic region of PelD, a degenerate diguanylate cyclase receptor that regulates exopolysaccharide production in Pseudomonas aeruginosa. J Biol Chem 287:23582-23593. http://dx.doi.org/10.1074/jbc.M112.375378.
    • (2012) J Biol Chem , vol.287 , pp. 23582-23593
    • Whitney, J.C.1    Colvin, K.M.2    Marmont, L.S.3    Robinson, H.4    Parsek, M.R.5    Howell, P.L.6
  • 36
    • 34547659282 scopus 로고    scopus 로고
    • Structure of BeF3-modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition
    • Wassmann P, Chan C, Paul R, Beck A, Heerklotz H, Jenal U, Schirmer T. 2007. Structure of BeF3-modified response regulator PleD: implications for diguanylate cyclase activation, catalysis, and feedback inhibition. Structure 15:915-927. http://dx.doi.org/10.1016/j.str.2007.06.016.
    • (2007) Structure , vol.15 , pp. 915-927
    • Wassmann, P.1    Chan, C.2    Paul, R.3    Beck, A.4    Heerklotz, H.5    Jenal, U.6    Schirmer, T.7
  • 37
    • 70349783823 scopus 로고    scopus 로고
    • Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR
    • De N, Navarro MV, Raghavan RV, Sondermann H. 2009. Determinants for the activation and autoinhibition of the diguanylate cyclase response regulator WspR. J Mol Biol 393:619-633. http://dx.doi.org/10.1016/j.jmb.2009.08.030.
    • (2009) J Mol Biol , vol.393 , pp. 619-633
    • De, N.1    Navarro, M.V.2    Raghavan, R.V.3    Sondermann, H.4
  • 38
  • 39
    • 84904859048 scopus 로고    scopus 로고
    • GIL, a new c-di-GMP-binding protein domain involved in regulation of cellulose synthesis in enterobacteria
    • Fang X, Ahmad I, Blanka A, Schottkowski M, Cimdins A, Galperin MY, Römling U, Gomelsky M. 2014. GIL, a new c-di-GMP-binding protein domain involved in regulation of cellulose synthesis in enterobacteria. Mol Microbiol 93:439-452. http://dx.doi.org/10.1111/mmi.12672.
    • (2014) Mol Microbiol , vol.93 , pp. 439-452
    • Fang, X.1    Ahmad, I.2    Blanka, A.3    Schottkowski, M.4    Cimdins, A.5    Galperin, M.Y.6    Römling, U.7    Gomelsky, M.8
  • 40
    • 84940462046 scopus 로고    scopus 로고
    • Bacterial cellulose biosynthesis: diversity of operons, subunits, products and functions
    • Römling U, Galperin MY. 2015. Bacterial cellulose biosynthesis: diversity of operons, subunits, products and functions. Trends Microbiol 23:545-557. http://dx.doi.org/10.1016/j.tim.2015.05.005.
    • (2015) Trends Microbiol , vol.23 , pp. 545-557
    • Römling, U.1    Galperin, M.Y.2
  • 42
    • 67649746308 scopus 로고    scopus 로고
    • Crystal structures of YkuI and its complex with second messenger cyclic di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains
    • Minasov G, Padavattan S, Shuvalova L, Brunzelle JS, Miller DJ, Basle A, Massa C, Collart FR, Schirmer T, Anderson WF. 2009. Crystal structures of YkuI and its complex with second messenger cyclic di-GMP suggest catalytic mechanism of phosphodiester bond cleavage by EAL domains. J Biol Chem 284:13174-13184. http://dx.doi.org/10.1074/jbc.M808221200.
    • (2009) J Biol Chem , vol.284 , pp. 13174-13184
    • Minasov, G.1    Padavattan, S.2    Shuvalova, L.3    Brunzelle, J.S.4    Miller, D.J.5    Basle, A.6    Massa, C.7    Collart, F.R.8    Schirmer, T.9    Anderson, W.F.10
  • 44
    • 68149172669 scopus 로고    scopus 로고
    • Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX
    • Navarro MV, De N, Bae N, Wang Q, Sondermann H. 2009. Structural analysis of the GGDEF-EAL domain-containing c-di-GMP receptor FimX. Structure 17:1104-1116. http://dx.doi.org/10.1016/j.str.2009.06.010.
    • (2009) Structure , vol.17 , pp. 1104-1116
    • Navarro, M.V.1    De, N.2    Bae, N.3    Wang, Q.4    Sondermann, H.5
  • 46
    • 0000445736 scopus 로고    scopus 로고
    • The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer
    • Passner JM, Steitz TA. 1997. The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer. Proc Natl Acad Sci U S A 94:2843-2847.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2843-2847
    • Passner, J.M.1    Steitz, T.A.2
  • 47
    • 84902080356 scopus 로고    scopus 로고
    • Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP
    • Morgan JL, McNamara JT, Zimmer J. 2014. Mechanism of activation of bacterial cellulose synthase by cyclic di-GMP. Nat Struct Mol Biol 21:489-496. http://dx.doi.org/10.1038/nsmb.2803.
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 489-496
    • Morgan, J.L.1    McNamara, J.T.2    Zimmer, J.3
  • 49
    • 77950859347 scopus 로고    scopus 로고
    • Structure of PP4397 reveals the molecular basis for different c-di-GMP binding modes by PilZ domain proteins
    • Ko J, Ryu KS, Kim H, Shin JS, Lee JO, Cheong C, Choi BS. 2010. Structure of PP4397 reveals the molecular basis for different c-di-GMP binding modes by PilZ domain proteins. J Mol Biol 398:97-110. http://dx.doi.org/10.1016/j.jmb.2010.03.007.
    • (2010) J Mol Biol , vol.398 , pp. 97-110
    • Ko, J.1    Ryu, K.S.2    Kim, H.3    Shin, J.S.4    Lee, J.O.5    Cheong, C.6    Choi, B.S.7
  • 50
    • 84862996389 scopus 로고    scopus 로고
    • Cyclic di-GMP sensing via the innate immune signaling protein STING
    • Yin Q, Tian Y, Kabaleeswaran V, Jiang X, Tu D, Eck MJ, Chen ZJ, Wu H. 2012. Cyclic di-GMP sensing via the innate immune signaling protein STING. Mol Cell 46:735-745. http://dx.doi.org/10.1016/j.molcel.2012.05.029.
    • (2012) Mol Cell , vol.46 , pp. 735-745
    • Yin, Q.1    Tian, Y.2    Kabaleeswaran, V.3    Jiang, X.4    Tu, D.5    Eck, M.J.6    Chen, Z.J.7    Wu, H.8
  • 51
    • 84863726252 scopus 로고    scopus 로고
    • Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system
    • Shu C, Yi G, Watts T, Kao CC, Li P. 2012. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Nat Struct Mol Biol 19:722-724. http://dx.doi.org/10.1038/nsmb.2331.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 722-724
    • Shu, C.1    Yi, G.2    Watts, T.3    Kao, C.C.4    Li, P.5
  • 54
    • 84863722786 scopus 로고    scopus 로고
    • The structural basis for the sensing and binding of cyclic di-GMP by STING
    • Huang YH, Liu XY, Du XX, Jiang ZF, Su XD. 2012. The structural basis for the sensing and binding of cyclic di-GMP by STING. Nat Struct Mol Biol 19:728-730. http://dx.doi.org/10.1038/nsmb.2333.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 728-730
    • Huang, Y.H.1    Liu, X.Y.2    Du, X.X.3    Jiang, Z.F.4    Su, X.D.5
  • 55
    • 84871046431 scopus 로고    scopus 로고
    • Cation-π interaction: its role and relevance in chemistry, biology, and material science
    • Mahadevi AS, Sastry GN. 2013. Cation-π interaction: its role and relevance in chemistry, biology, and material science. Chem Rev 113:2100-2138. http://dx.doi.org/10.1021/cr300222d.
    • (2013) Chem Rev , vol.113 , pp. 2100-2138
    • Mahadevi, A.S.1    Sastry, G.N.2
  • 56
    • 0033578302 scopus 로고    scopus 로고
    • Cation-π interactions in structural biology
    • Gallivan JP, Dougherty DA. 1999. Cation-π interactions in structural biology. Proc Natl Acad Sci U S A 96:9459-9464. http://dx.doi.org/10.1073/pnas.96.17.9459.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 9459-9464
    • Gallivan, J.P.1    Dougherty, D.A.2
  • 57
    • 76749083886 scopus 로고    scopus 로고
    • Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP
    • Krasteva PV, Fong JC, Shikuma NJ, Beyhan S, Navarro MV, Yildiz FH, Sondermann H. 2010. Vibrio cholerae VpsT regulates matrix production and motility by directly sensing cyclic di-GMP. Science 327:866-868. http://dx.doi.org/10.1126/science.1181185.
    • (2010) Science , vol.327 , pp. 866-868
    • Krasteva, P.V.1    Fong, J.C.2    Shikuma, N.J.3    Beyhan, S.4    Navarro, M.V.5    Yildiz, F.H.6    Sondermann, H.7
  • 58
    • 82455163827 scopus 로고    scopus 로고
    • The structure and inhibition of a GGDEF diguanylate cyclase complexed with (c-di-GMP)2 at the active site
    • Yang CY, Chin KH, Chuah ML, Liang ZX, Wang AH, Chou SH. 2011. The structure and inhibition of a GGDEF diguanylate cyclase complexed with (c-di-GMP)2 at the active site. Acta Crystallogr D Biol Crystallogr 67:997-1008. http://dx.doi.org/10.1107/S090744491104039X.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 997-1008
    • Yang, C.Y.1    Chin, K.H.2    Chuah, M.L.3    Liang, Z.X.4    Wang, A.H.5    Chou, S.H.6
  • 59
    • 84873569415 scopus 로고    scopus 로고
    • Allosteric activation of exopolysaccharide synthesis through cyclic di-GMP-stimulated protein-protein interaction
    • Steiner S, Lori C, Boehm A, Jenal U. 2013. Allosteric activation of exopolysaccharide synthesis through cyclic di-GMP-stimulated protein-protein interaction. EMBO J 32:354-368. http://dx.doi.org/10.1038/emboj.2012.315.
    • (2013) EMBO J , vol.32 , pp. 354-368
    • Steiner, S.1    Lori, C.2    Boehm, A.3    Jenal, U.4
  • 60
    • 79954598477 scopus 로고    scopus 로고
    • Solution structure of the PilZ domain protein PA4608 complex with cyclic di-GMP identifies charge clustering as molecular readout
    • Habazettl J, Allan MG, Jenal U, Grzesiek S. 2011. Solution structure of the PilZ domain protein PA4608 complex with cyclic di-GMP identifies charge clustering as molecular readout. J Biol Chem 286:14304-14314. http://dx.doi.org/10.1074/jbc.M110.209007.
    • (2011) J Biol Chem , vol.286 , pp. 14304-14314
    • Habazettl, J.1    Allan, M.G.2    Jenal, U.3    Grzesiek, S.4
  • 61
    • 77949325119 scopus 로고    scopus 로고
    • The cAMP receptor-like protein CLP is a novel c-di-GMP receptor linking cell-cell signaling to virulence gene expression in Xanthomonas campestris
    • Chin KH, Lee YC, Tu ZL, Chen CH, Tseng YH, Yang JM, Ryan RP, McCarthy Y, Dow JM, Wang AH, Chou SH. 2010. The cAMP receptor-like protein CLP is a novel c-di-GMP receptor linking cell-cell signaling to virulence gene expression in Xanthomonas campestris. J Mol Biol 396:646-662. http://dx.doi.org/10.1016/j.jmb.2009.11.076.
    • (2010) J Mol Biol , vol.396 , pp. 646-662
    • Chin, K.H.1    Lee, Y.C.2    Tu, Z.L.3    Chen, C.H.4    Tseng, Y.H.5    Yang, J.M.6    Ryan, R.P.7    McCarthy, Y.8    Dow, J.M.9    Wang, A.H.10    Chou, S.H.11
  • 63
  • 65
    • 61449219844 scopus 로고    scopus 로고
    • The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light response of Escherichia coli
    • Tschowri N, Busse S, Hengge R. 2009. The BLUF-EAL protein YcgF acts as a direct anti-repressor in a blue-light response of Escherichia coli. Genes Dev 23:522-534. http://dx.doi.org/10.1101/gad.499409.
    • (2009) Genes Dev , vol.23 , pp. 522-534
    • Tschowri, N.1    Busse, S.2    Hengge, R.3
  • 66
    • 84870597147 scopus 로고    scopus 로고
    • Structural insight of a concentrationdependent mechanism by which YdiV inhibits Escherichia coli flagellum biogenesis and motility
    • Li B, Li N, Wang F, Guo L, Huang Y, Liu X, Wei T, Zhu D, Liu C, Pan H, Xu S, Wang HW, Gu L. 2012. Structural insight of a concentrationdependent mechanism by which YdiV inhibits Escherichia coli flagellum biogenesis and motility. Nucleic Acids Res 40:11073-11085. http://dx.doi.org/10.1093/nar/gks869.
    • (2012) Nucleic Acids Res , vol.40 , pp. 11073-11085
    • Li, B.1    Li, N.2    Wang, F.3    Guo, L.4    Huang, Y.5    Liu, X.6    Wei, T.7    Zhu, D.8    Liu, C.9    Pan, H.10    Xu, S.11    Wang, H.W.12    Gu, L.13
  • 67
    • 33748705968 scopus 로고    scopus 로고
    • Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E
    • Suzuki K, Babitzke P, Kushner SR, Romeo T. 2006. Identification of a novel regulatory protein (CsrD) that targets the global regulatory RNAs CsrB and CsrC for degradation by RNase E. Genes Dev 20:2605-2617. http://dx.doi.org/10.1101/gad.1461606.
    • (2006) Genes Dev , vol.20 , pp. 2605-2617
    • Suzuki, K.1    Babitzke, P.2    Kushner, S.R.3    Romeo, T.4
  • 68
    • 33749180794 scopus 로고    scopus 로고
    • The HD-GYP domain of RpfG mediates a direct linkage between the Rpf quorum-sensing pathway and a subset of diguanylate cyclase proteins in the phytopathogen Xanthomonas axonopodis pv citri
    • Andrade MO, Alegria MC, Guzzo CR, Docena C, Rosa MC, Ramos CH, Farah CS. 2006. The HD-GYP domain of RpfG mediates a direct linkage between the Rpf quorum-sensing pathway and a subset of diguanylate cyclase proteins in the phytopathogen Xanthomonas axonopodis pv citri. Mol Microbiol 62:537-551. http://dx.doi.org/10.1111/j.1365-2958.2006.05386.x.
    • (2006) Mol Microbiol , vol.62 , pp. 537-551
    • Andrade, M.O.1    Alegria, M.C.2    Guzzo, C.R.3    Docena, C.4    Rosa, M.C.5    Ramos, C.H.6    Farah, C.S.7
  • 69
    • 84868101467 scopus 로고    scopus 로고
    • Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris
    • Ryan RP, McCarthy Y, Kiely PA, O'Connor R, Farah CS, Armitage JP, Dow JM. 2012. Dynamic complex formation between HD-GYP, GGDEF and PilZ domain proteins regulates motility in Xanthomonas campestris. Mol Microbiol 86:557-567. http://dx.doi.org/10.1111/mmi.12000.
    • (2012) Mol Microbiol , vol.86 , pp. 557-567
    • Ryan, R.P.1    McCarthy, Y.2    Kiely, P.A.3    O'Connor, R.4    Farah, C.S.5    Armitage, J.P.6    Dow, J.M.7
  • 70
    • 80053932725 scopus 로고    scopus 로고
    • The CRP/FNR family protein Bcam1349 is a c-di-GMP effector that regulates biofilm formation in the respiratory pathogen Burkholderia cenocepacia
    • Fazli M, O'Connell A, Nilsson M, Niehaus K, Dow JM, Givskov M, Ryan RP, Tolker-Nielsen T. 2011. The CRP/FNR family protein Bcam1349 is a c-di-GMP effector that regulates biofilm formation in the respiratory pathogen Burkholderia cenocepacia. Mol Microbiol 82:327-341. http://dx.doi.org/10.1111/j.1365-2958.2011.07814.x.
    • (2011) Mol Microbiol , vol.82 , pp. 327-341
    • Fazli, M.1    O'Connell, A.2    Nilsson, M.3    Niehaus, K.4    Dow, J.M.5    Givskov, M.6    Ryan, R.P.7    Tolker-Nielsen, T.8
  • 71
    • 84899629752 scopus 로고    scopus 로고
    • BrlR from Pseudomonas aeruginosa is a c-di-GMP-responsive transcription factor
    • Chambers JR, Liao J, Schurr MJ, Sauer K. 2014. BrlR from Pseudomonas aeruginosa is a c-di-GMP-responsive transcription factor. Mol Microbiol 92:471-487. http://dx.doi.org/10.1111/mmi.12562.
    • (2014) Mol Microbiol , vol.92 , pp. 471-487
    • Chambers, J.R.1    Liao, J.2    Schurr, M.J.3    Sauer, K.4
  • 72
    • 84887482378 scopus 로고    scopus 로고
    • Cyclic diguanosine monophosphate represses bacterial flagella synthesis by interacting with the Walker A motif of the enhancer-binding protein FleQ
    • Baraquet C, Harwood CS. 2013. Cyclic diguanosine monophosphate represses bacterial flagella synthesis by interacting with the Walker A motif of the enhancer-binding protein FleQ. Proc Natl Acad Sci U S A 110:18478-18483. http://dx.doi.org/10.1073/pnas.1318972110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 18478-18483
    • Baraquet, C.1    Harwood, C.S.2
  • 73
    • 84890114269 scopus 로고    scopus 로고
    • Cyclic di-GMP inhibits Vibrio cholerae motility by repressing induction of transcription and inducing extracellular polysaccharide production
    • Srivastava D, Hsieh ML, Khataokar A, Neiditch MB, Waters CM. 2013. Cyclic di-GMP inhibits Vibrio cholerae motility by repressing induction of transcription and inducing extracellular polysaccharide production. Mol Microbiol 90:1262-1276. http://dx.doi.org/10.1111/mmi.12432.
    • (2013) Mol Microbiol , vol.90 , pp. 1262-1276
    • Srivastava, D.1    Hsieh, M.L.2    Khataokar, A.3    Neiditch, M.B.4    Waters, C.M.5
  • 74
    • 84871200600 scopus 로고    scopus 로고
    • LtmA, a novel cyclic di-GMP-responsive activator, broadly regulates the expression of lipid transport and metabolism genes in Mycobacterium smegmatis
    • Li W, He ZG. 2012. LtmA, a novel cyclic di-GMP-responsive activator, broadly regulates the expression of lipid transport and metabolism genes in Mycobacterium smegmatis. Nucleic Acids Res 40:11292-11307. http://dx.doi.org/10.1093/nar/gks923.
    • (2012) Nucleic Acids Res , vol.40 , pp. 11292-11307
    • Li, W.1    He, Z.G.2
  • 75
    • 80655125443 scopus 로고    scopus 로고
    • Integration of cyclic di-GMP and quorum sensing in the control of vpsT and aphA in Vibrio cholerae
    • Srivastava D, Harris RC, Waters CM. 2011. Integration of cyclic di-GMP and quorum sensing in the control of vpsT and aphA in Vibrio cholerae. J Bacteriol 193:6331-6341. http://dx.doi.org/10.1128/JB.05167-11.
    • (2011) J Bacteriol , vol.193 , pp. 6331-6341
    • Srivastava, D.1    Harris, R.C.2    Waters, C.M.3
  • 77
    • 80053091424 scopus 로고    scopus 로고
    • Differential radial capillary action of ligand assay for high-throughput detection of protein-metabolite interactions
    • Roelofs KG, Wang J, Sintim HO, Lee VT. 2011. Differential radial capillary action of ligand assay for high-throughput detection of protein-metabolite interactions. Proc Natl Acad Sci U S A 108:15528-15533. http://dx.doi.org/10.1073/pnas.1018949108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 15528-15533
    • Roelofs, K.G.1    Wang, J.2    Sintim, H.O.3    Lee, V.T.4
  • 78
    • 84864078697 scopus 로고    scopus 로고
    • A novel capture compound for the identification and analysis of cyclic di-GMP binding proteins
    • Nesper J, Reinders A, Glatter T, Schmidt A, Jenal U. 2012. A novel capture compound for the identification and analysis of cyclic di-GMP binding proteins. J Proteomics 75:4874-4878. http://dx.doi.org/10.1016/j.jprot.2012.05.033.
    • (2012) J Proteomics , vol.75 , pp. 4874-4878
    • Nesper, J.1    Reinders, A.2    Glatter, T.3    Schmidt, A.4    Jenal, U.5
  • 80
    • 77953244382 scopus 로고    scopus 로고
    • Asymmetrical distribution of the second messenger c-di-GMP upon bacterial cell division
    • Christen M, Kulasekara HD, Christen B, Kulasekara BR, Hoffman LR, Miller SI. 2010. Asymmetrical distribution of the second messenger c-di-GMP upon bacterial cell division. Science 328:1295-1297. http://dx.doi.org/10.1126/science.1188658.
    • (2010) Science , vol.328 , pp. 1295-1297
    • Christen, M.1    Kulasekara, H.D.2    Christen, B.3    Kulasekara, B.R.4    Hoffman, L.R.5    Miller, S.I.6
  • 81
    • 84870985711 scopus 로고    scopus 로고
    • The response threshold of Salmonella PilZ domain proteins is determined by their binding affinities for c-di-GMP
    • Pultz IS, Christen M, Kulasekara HD, Kennard A, Kulasekara B, Miller SI. 2012. The response threshold of Salmonella PilZ domain proteins is determined by their binding affinities for c-di-GMP. Mol Microbiol 86:1424-1440. http://dx.doi.org/10.1111/mmi.12066.
    • (2012) Mol Microbiol , vol.86 , pp. 1424-1440
    • Pultz, I.S.1    Christen, M.2    Kulasekara, H.D.3    Kennard, A.4    Kulasekara, B.5    Miller, S.I.6
  • 82
    • 84875261797 scopus 로고    scopus 로고
    • The c-di-GMP recognition mechanism of the PilZ domain of bacterial cellulose synthase subunit A
    • Fujiwara T, Komoda K, Sakurai N, Tajima K, Tanaka I, Yao M. 2013. The c-di-GMP recognition mechanism of the PilZ domain of bacterial cellulose synthase subunit A. Biochem Biophys Res Commun 431:802-807. http://dx.doi.org/10.1016/j.bbrc.2012.12.103.
    • (2013) Biochem Biophys Res Commun , vol.431 , pp. 802-807
    • Fujiwara, T.1    Komoda, K.2    Sakurai, N.3    Tajima, K.4    Tanaka, I.5    Yao, M.6
  • 83
    • 34547682212 scopus 로고    scopus 로고
    • The second messenger bis-(3'-5')-cyclic-GMP and its PilZ domain-containing receptor Alg44 are required for alginate biosynthesis in Pseudomonas aeruginosa
    • Merighi M, Lee VT, Hyodo M, Hayakawa Y, Lory S. 2007. The second messenger bis-(3'-5')-cyclic-GMP and its PilZ domain-containing receptor Alg44 are required for alginate biosynthesis in Pseudomonas aeruginosa. Mol Microbiol 65:876-895. http://dx.doi.org/10.1111/j.1365-2958.2007.05817.x.
    • (2007) Mol Microbiol , vol.65 , pp. 876-895
    • Merighi, M.1    Lee, V.T.2    Hyodo, M.3    Hayakawa, Y.4    Lory, S.5
  • 84
    • 84880068681 scopus 로고    scopus 로고
    • Integration of the second messenger c-di-GMP into the chemotactic signaling pathway
    • Russell MH, Bible AN, Fang X, Gooding J, Campagna S, Gomelsky M, Alexandre G. 2013. Integration of the second messenger c-di-GMP into the chemotactic signaling pathway. mBio 4:e00001-00013. http://dx.doi.org/10.1128/mBio.00001-13.
    • (2013) mBio , vol.4 , pp. e00001-00013
    • Russell, M.H.1    Bible, A.N.2    Fang, X.3    Gooding, J.4    Campagna, S.5    Gomelsky, M.6    Alexandre, G.7
  • 85
    • 84865741837 scopus 로고    scopus 로고
    • Structures of the PelD cyclic diguanylate effector involved in pellicle formation in Pseudomonas aeruginosa PAO1
    • Li Z, Chen JH, Hao Y, Nair SK. 2012. Structures of the PelD cyclic diguanylate effector involved in pellicle formation in Pseudomonas aeruginosa PAO1. J Biol Chem 287:30191-30204. http://dx.doi.org/10.1074/jbc.M112.378273.
    • (2012) J Biol Chem , vol.287 , pp. 30191-30204
    • Li, Z.1    Chen, J.H.2    Hao, Y.3    Nair, S.K.4
  • 86
    • 58149485506 scopus 로고    scopus 로고
    • Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression
    • Duerig A, Abel S, Folcher M, Nicollier M, Schwede T, Amiot N, Giese B, Jenal U. 2009. Second messenger-mediated spatiotemporal control of protein degradation regulates bacterial cell cycle progression. Genes Dev 23:93-104. http://dx.doi.org/10.1101/gad.502409.
    • (2009) Genes Dev , vol.23 , pp. 93-104
    • Duerig, A.1    Abel, S.2    Folcher, M.3    Nicollier, M.4    Schwede, T.5    Amiot, N.6    Giese, B.7    Jenal, U.8
  • 87
    • 84866316294 scopus 로고    scopus 로고
    • Type IV pilus assembly in Pseudomonas aeruginosa over a broad range of cyclic di-GMP concentrations
    • Jain R, Behrens AJ, Kaever V, Kazmierczak BI. 2012. Type IV pilus assembly in Pseudomonas aeruginosa over a broad range of cyclic di-GMP concentrations. J Bacteriol 194:4285-4294. http://dx.doi.org/10.1128/JB.00803-12.
    • (2012) J Bacteriol , vol.194 , pp. 4285-4294
    • Jain, R.1    Behrens, A.J.2    Kaever, V.3    Kazmierczak, B.I.4
  • 88
    • 78951471881 scopus 로고    scopus 로고
    • Binding of cyclic diguanylate in the non-catalytic EAL domain of FimX induces a long-range conformational change
    • Qi Y, Chuah ML, Dong X, Xie K, Luo Z, Tang K, Liang ZX. 2011. Binding of cyclic diguanylate in the non-catalytic EAL domain of FimX induces a long-range conformational change. J Biol Chem 286:2910-2917. http://dx.doi.org/10.1074/jbc.M110.196220.
    • (2011) J Biol Chem , vol.286 , pp. 2910-2917
    • Qi, Y.1    Chuah, M.L.2    Dong, X.3    Xie, K.4    Luo, Z.5    Tang, K.6    Liang, Z.X.7
  • 89
    • 84899843009 scopus 로고    scopus 로고
    • The degenerate EAL-GGDEF domain protein Filp functions as a cyclic di-GMP receptor and specifically interacts with the PilZ-domain protein PXO_02715 to regulate virulence in Xanthomonas oryzae pv. oryzae
    • Yang F, Tian F, Li X, Fan S, Chen H, Wu M, Yang CH, He C. 2014. The degenerate EAL-GGDEF domain protein Filp functions as a cyclic di-GMP receptor and specifically interacts with the PilZ-domain protein PXO_02715 to regulate virulence in Xanthomonas oryzae pv. oryzae. Mol Plant Microbe Interact 27:578-589. http://dx.doi.org/10.1094/MPMI-12-13-0371-R.
    • (2014) Mol Plant Microbe Interact , vol.27 , pp. 578-589
    • Yang, F.1    Tian, F.2    Li, X.3    Fan, S.4    Chen, H.5    Wu, M.6    Yang, C.H.7    He, C.8
  • 92
    • 79952078501 scopus 로고    scopus 로고
    • Engineering a novel c-di-GMP-binding protein for biofilm dispersal
    • Ma Q, Yang Z, Pu M, Peti W, Wood TK. 2011. Engineering a novel c-di-GMP-binding protein for biofilm dispersal. Environ Microbiol 13:631-642. http://dx.doi.org/10.1111/j.1462-2920.2010.02368.x.
    • (2011) Environ Microbiol , vol.13 , pp. 631-642
    • Ma, Q.1    Yang, Z.2    Pu, M.3    Peti, W.4    Wood, T.K.5
  • 93
    • 79952735655 scopus 로고    scopus 로고
    • Cyclic di-GMP activation of polynucleotide phosphorylase signal-dependent RNA processing
    • Tuckerman JR, Gonzalez G, Gilles-Gonzalez MA. 2011. Cyclic di-GMP activation of polynucleotide phosphorylase signal-dependent RNA processing. J Mol Biol 407:633-639. http://dx.doi.org/10.1016/j.jmb.2011.02.019.
    • (2011) J Mol Biol , vol.407 , pp. 633-639
    • Tuckerman, J.R.1    Gonzalez, G.2    Gilles-Gonzalez, M.A.3


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