메뉴 건너뛰기




Volumn 58, Issue 4, 2014, Pages 2221-2228

In Vitro activities of dermaseptins K4S4and K 4K20S4 against Escherichia coli, Staphylococcus aureus, and Pseudomonas aeruginosa planktonic growth and biofilm formation

Author keywords

[No Author keywords available]

Indexed keywords

DERMASEPTIN; DERMASEPTIN K4 K20 S4; DERMASEPTIN K4 S4; UNCLASSIFIED DRUG;

EID: 84896975604     PISSN: 00664804     EISSN: 10986596     Source Type: Journal    
DOI: 10.1128/AAC.02142-13     Document Type: Article
Times cited : (23)

References (45)
  • 1
    • 0036228505 scopus 로고    scopus 로고
    • Biofilms: Survival mechanisms of clinically relevant microorganisms
    • DOI 10.1128/CMR.15.2.167-193.2002
    • Donlan RM, Costerton JW. 2002. Biofilms: survival mechanisms of clinically relevant microorganisms. Clin. Microbiol. Rev. 15:167-193. http://dx.doi.org/10.1128/CMR.15.2.167-193.2002. (Pubitemid 34303762)
    • (2002) Clinical Microbiology Reviews , vol.15 , Issue.2 , pp. 167-193
    • Donlan, R.M.1    Costerton, J.W.2
  • 3
    • 45549109081 scopus 로고    scopus 로고
    • Mucosal biofilms: Challenges and future directions
    • Dongari-Bagtzoglou A. 2008. Mucosal biofilms: challenges and future directions. Expert Rev. Anti Infect. Ther. 6:141-144. http://dx.doi.org/10.1586/ 14787210.6.2.141.
    • (2008) Expert Rev. Anti Infect. Ther. , vol.6 , pp. 141-144
    • Dongari-Bagtzoglou, A.1
  • 4
    • 77954645350 scopus 로고    scopus 로고
    • Prevention and control of biofilm-based medical device-related infections
    • Francolini I, Donelli G. 2010. Prevention and control of biofilm-based medical device-related infections. FEMS Immunol. Med. Microbiol. 59:227-238. http://dx.doi.org/10.1111/j.1574-695X.2010.00665.x.
    • (2010) FEMS Immunol. Med. Microbiol. , vol.59 , pp. 227-238
    • Francolini, I.1    Donelli, G.2
  • 7
    • 80053194288 scopus 로고    scopus 로고
    • Dermaseptin 01 as antimicrobial peptide with rich biotechnological potential: Study of peptide interaction with membranes containing Leishmania amazonensis lipid-rich extract and membrane models
    • Salay LC, Nobre TM, Colhone MC, Zaniquelli ME, Ciancaglini P, Stabeli RG, Leite JR, Zucolotto V. 2011. Dermaseptin 01 as antimicrobial peptide with rich biotechnological potential: study of peptide interaction with membranes containing Leishmania amazonensis lipid-rich extract and membrane models. J. Pept. Sci. 17:700-707. http://dx.doi.org/10.1002/psc.1392.
    • (2011) J. Pept. Sci. , vol.17 , pp. 700-707
    • Salay, L.C.1    Nobre, T.M.2    Colhone, M.C.3    Zaniquelli, M.E.4    Ciancaglini, P.5    Stabeli, R.G.6    Leite, J.R.7    Zucolotto, V.8
  • 8
    • 84896933714 scopus 로고    scopus 로고
    • Development of a novel biosensor using cationic antimicrobial peptide and nickel phthalocyanine ultrathin films for electrochemical detection of dopamine
    • Zampa MF, de S Araújo IM, dos Santos JR, Jr, Zucolotto V, de SA Leite JR, Eiras C. 2012. Development of a novel biosensor using cationic antimicrobial peptide and nickel phthalocyanine ultrathin films for electrochemical detection of dopamine. Int. J. Anal. Chem. 2012:850969. http://dx.doi.org/10.1155/2012/850969.
    • (2012) Int. J. Anal. Chem. , vol.2012 , pp. 850969
    • Zampa, M.F.1    Araújo, D.S.I.M.2    Dos Santos Jr., J.R.3    Zucolotto, V.4    De Sa Leite, J.R.5    Eiras, C.6
  • 9
    • 84859882976 scopus 로고    scopus 로고
    • Determining the mechanism of membrane permeabilizing peptides: Identification of potent, equilibrium pore-formers
    • Krauson AJ, He J, Wimley WC. 2012. Determining the mechanism of membrane permeabilizing peptides: identification of potent, equilibrium pore-formers. Biochim. Biophys. Acta 1818:1625-1632. http://dx.doi.org/10.1016/j.bbamem.2012. 02.009.
    • (2012) Biochim. Biophys. Acta , vol.1818 , pp. 1625-1632
    • Krauson, A.J.1    He, J.2    Wimley, W.C.3
  • 10
    • 67649262194 scopus 로고    scopus 로고
    • The dermaseptin superfamily: A gene-based combinatorial library of antimicrobial peptides
    • Nicolas P, El Amri C. 2009. The dermaseptin superfamily: a gene-based combinatorial library of antimicrobial peptides. Biochim. Biophys. Acta 1788:1537-1550. http://dx.doi.org/10.1016/j.bbamem.2008.09.006.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1537-1550
    • Nicolas, P.1    El Amri, C.2
  • 11
    • 67649268280 scopus 로고    scopus 로고
    • Amphibian antimicrobial peptides and protozoa: Lessons from parasites
    • Rivas L, Luque-Ortega JR, Andreu D. 2009. Amphibian antimicrobial peptides and protozoa: lessons from parasites. Biochim. Biophys. Acta 1788:1570-1581. http://dx.doi.org/10.1016/j.bbamem.2008.11.002.
    • (2009) Biochim. Biophys. Acta , vol.1788 , pp. 1570-1581
    • Rivas, L.1    Luque-Ortega, J.R.2    Andreu, D.3
  • 12
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • Zasloff M. 2002. Antimicrobial peptides of multicellular organisms. Nature 415:389-395. http://dx.doi.org/10.1038/415389a. (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 13
    • 0025787585 scopus 로고
    • Isolation, amino acid sequence and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin
    • Mor A, Nguyen VH, Delfour A, Migliore-Samour D, Nicolas P. 1991. Isolation, amino acid sequence and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin. Biochemistry 30:8824-8830. http://dx.doi.org/10.1021/bi00100a014.
    • (1991) Biochemistry , vol.30 , pp. 8824-8830
    • Mor, A.1    Nguyen, V.H.2    Delfour, A.3    Migliore-Samour, D.4    Nicolas, P.5
  • 14
    • 0007643173 scopus 로고
    • Natural and synthetic dermaseptins: In vitro large spectrum antimicrobial peptides
    • Mor A, Rouffaud MA, Montagne JJ, Nguyen VH, Nicolas P. 1993. Natural and synthetic dermaseptins: in vitro large spectrum antimicrobial peptides. J. Mycol. Med. 3:137-143.
    • (1993) J. Mycol. Med. , vol.3 , pp. 137-143
    • Mor, A.1    Rouffaud, M.A.2    Montagne, J.J.3    Nguyen, V.H.4    Nicolas, P.5
  • 15
    • 30744459874 scopus 로고    scopus 로고
    • Dermaseptin S9, an alpha-helical antimicrobial peptide with a hydrophobic core and cationic termini
    • DOI 10.1021/bi051711i
    • Lequin O, Ladram A, Chabbert L, Bruston F, Convert O, Vanhoye D, Chassaing G, Nicolas P, Amiche M. 2006. Dermaseptin S9, an alphahelical antimicrobial peptide with a hydrophobic core and cationic termini. Biochemistry 45:468-480. http://dx.doi.org/10.1021/bi051711i. (Pubitemid 43100413)
    • (2006) Biochemistry , vol.45 , Issue.2 , pp. 468-480
    • Lequin, O.1    Ladram, A.2    Chabbert, L.3    Bruston, F.4    Convert, O.5    Vanhoye, D.6    Chassaing, G.7    Nicolas, P.8    Amiche, M.9
  • 16
    • 84875204910 scopus 로고    scopus 로고
    • 4: A potential candidate for development of a new microbicide contraceptive agent: An in vitro study
    • 4: a potential candidate for development of a new microbicide contraceptive agent: an in vitro study. Eur. J. Contracept. Reprod. Health Care 18:79-87. http://dx.doi.org/10.3109/13625187.2013.769950.
    • (2013) Eur. J. Contracept. Reprod. Health Care , vol.18 , pp. 79-87
    • Zaïri, A.1    Tangy, F.2    Hani, K.3
  • 17
    • 33846397753 scopus 로고    scopus 로고
    • In Vitro Discriminative Antipseudomonal Properties Resulting from Acyl Substitution of N-Terminal Sequence of Dermaseptin S4 Derivatives
    • DOI 10.1016/j.chembiol.2006.11.009, PII S1074552106004261
    • Marynka K, Rotem S, Portnaya I, Cogan U, Mor A. 2007. In vitro discriminative antipseudomonal properties resulting from acyl substitution of N-terminal sequence of dermaseptin S4 derivatives. Chem. Biol. 14:75-85. http://dx.doi.org/10.1016/j.chembiol.2006.11.009. (Pubitemid 46127846)
    • (2007) Chemistry and Biology , vol.14 , Issue.1 , pp. 75-85
    • Marynka, K.1    Rotem, S.2    Portnaya, I.3    Cogan, U.4    Mor, A.5
  • 18
    • 33847300973 scopus 로고    scopus 로고
    • Susceptibility of Neisseria gonorrhoeae to antimicrobial peptides from amphibian skin, dermaseptin, and derivatives
    • DOI 10.1016/j.diagmicrobio.2006.11.006, PII S0732889306004354
    • Zairi A, Tangy F, Ducos-Galand M, Alonso JM, Hani K. 2007. Susceptibility of Neisseria gonorrhoeae to antimicrobial peptides from amphibian skin, dermaseptin, and derivatives. Diagn. Microbiol. Infect. Dis. 57:319-324. http://dx.doi.org/10.1016/j.diagmicrobio.2006.11.006. (Pubitemid 46330659)
    • (2007) Diagnostic Microbiology and Infectious Disease , vol.57 , Issue.3 , pp. 319-324
    • Zairi, A.1    Tangy, F.2    Ducos-Galand, M.3    Alonso, J.-M.4    Hani, K.5
  • 19
    • 33845246336 scopus 로고    scopus 로고
    • Acyl-substituted dermaseptin S4 derivatives with improved bactericidal properties, including on oral microflora
    • DOI 10.1128/AAC.00750-06
    • Porat Y, Marynka K, Tam A, Steinberg D, Mor A. 2006. Acyl-substituted dermaseptin S4 derivatives with improved bactericidal properties, including on oral microflora. Antimicrob. Agents Chemother. 50:4153-4160. http://dx.doi.org/10.1128/AAC.00750-06. (Pubitemid 44865160)
    • (2006) Antimicrobial Agents and Chemotherapy , vol.50 , Issue.12 , pp. 4153-4160
    • Porat, Y.1    Marynka, K.2    Tam, A.3    Steinberg, D.4    Mor, A.5
  • 21
    • 0037025297 scopus 로고    scopus 로고
    • Direct interaction of dermaseptin S4 aminoheptanoyl derivative with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity in culture
    • DOI 10.1074/jbc.M202089200
    • Efron L, Dagan A, Gaidukov L, Ginsburg H, Mor A. 2002. Direct interaction of dermaseptin S4 aminoheptanoyl derivative with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity in culture. J. Biol. Chem. 277:24067-24072. http://dx.doi.org/10.1074/jbc.M202089200. (Pubitemid 34951919)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24067-24072
    • Efron, L.1    Dagan, A.2    Gaidukov, L.3    Ginsburg, H.4    Mor, A.5
  • 22
    • 80053194288 scopus 로고    scopus 로고
    • Dermaseptin S1 as antimicrobial peptide with rich biotechnological potential: Study of peptide interaction with membranes containing Leishmania amazonensis lipid-rich extract and membrane models
    • Salay LC, Nobre TM, Colhone MC, Zaniquelli ME, Ciancaglini P, Stabeli RG, Leite JR, Zucolotto V. 2011. Dermaseptin S1 as antimicrobial peptide with rich biotechnological potential: study of peptide interaction with membranes containing Leishmania amazonensis lipid-rich extract and membrane models. J. Pept. Sci. 17:700-707. http://dx.doi.org/10.1002/psc.1392.
    • (2011) J. Pept. Sci. , vol.17 , pp. 700-707
    • Salay, L.C.1    Nobre, T.M.2    Colhone, M.C.3    Zaniquelli, M.E.4    Ciancaglini, P.5    Stabeli, R.G.6    Leite, J.R.7    Zucolotto, V.8
  • 23
    • 79952819338 scopus 로고    scopus 로고
    • Leishmanicidal activity of synthetic antimicrobial peptides in an infection model with human dendritic cells
    • Pérez-Cordero JJ, Lozano JM, Cortés J, Delgado G. 2011. Leishmanicidal activity of synthetic antimicrobial peptides in an infection model with human dendritic cells. Peptides 32:683-690. http://dx.doi.org/10. 1016/j.peptides.2011.01.011.
    • (2011) Peptides , vol.32 , pp. 683-690
    • Pérez-Cordero, J.J.1    Lozano, J.M.2    Cortés, J.3    Delgado, G.4
  • 24
    • 34447320461 scopus 로고    scopus 로고
    • An amphibian-derived, cationic, alpha-helical antimicrobial peptide kills yeast by caspase-independent but AIF-dependent programmed cell death
    • DOI 10.1111/j.1365-2958.2007.05801.x
    • Morton CO, Dos Santos SC, Coote P. 2007. An amphibian-derived, cationic, alpha-helical antimicrobial peptide kills yeast by caspase-independent but AIF-dependent programmed cell death. Mol. Microbiol. 65:494-507. http://dx.doi.org/10.1111/j.1365-2958.2007.05801.x. (Pubitemid 47052730)
    • (2007) Molecular Microbiology , vol.65 , Issue.2 , pp. 494-507
    • Morton, C.O.1    Dos, S.S.C.2    Coote, P.3
  • 25
    • 84871037094 scopus 로고    scopus 로고
    • In vitro antiviral activity of dermaseptin S4 and derivatives from amphibian skin against herpes simplex virus type 2
    • Bergaoui I, Zairi A, Tangy F, Aouni M, Selmi B, Hani K. 2013. In vitro antiviral activity of dermaseptin S4 and derivatives from amphibian skin against herpes simplex virus type 2. J. Med. Virol. 85:272-281. http://dx.doi.org/10. 1002/jmv.23450.
    • (2013) J. Med. Virol. , vol.85 , pp. 272-281
    • Bergaoui, I.1    Zairi, A.2    Tangy, F.3    Aouni, M.4    Selmi, B.5    Hani, K.6
  • 26
    • 15244349233 scopus 로고    scopus 로고
    • The antimicrobial peptide Dermaseptin S4 inhibits HIV-1 infectivity in vitro
    • DOI 10.1016/j.virol.2005.02.002
    • Lorin C, Saidi H, Belaid A, Zairi A, Baleux F, Hocini H, Bélec L, Hani K, Tangy F. 2005. The antimicrobial peptide dermaseptin S4 inhibits HIV-1 infectivity in vitro. Virology 334:264-275. http://dx.doi.org/10.1016/j.virol. 2005.02.002. (Pubitemid 40386960)
    • (2005) Virology , vol.334 , Issue.2 , pp. 264-275
    • Lorin, C.1    Saidi, H.2    Belaid, A.3    Zairi, A.4    Baleux, F.5    Hocini, H.6    Belec, L.7    Hani, K.8    Tangy, F.9
  • 27
    • 0036137074 scopus 로고    scopus 로고
    • In vitro antiviral activity of dermaseptins against herpes simplex virus type 1
    • DOI 10.1002/jmv.2134
    • Belaid A, Aouni M, Khelifa R, Trabelsi A, Jemmali M, Hani K. 2002. In vitro antiviral activity of dermaseptins against herpes simplex virus type 1. J. Med. Virol. 66:229-234. http://dx.doi.org/10.1002/jmv.2134. (Pubitemid 34020073)
    • (2002) Journal of Medical Virology , vol.66 , Issue.2 , pp. 229-234
    • Belaid, A.1    Aouni, M.2    Khelifa, R.3    Trabelsi, A.4    Jemmali, M.5    Hani, K.6
  • 28
    • 79960444560 scopus 로고    scopus 로고
    • Dermaseptins as models for the elucidation of membrane-acting helical amphipathic antimicrobial peptides
    • Amiche M, Galanth C. 2011. Dermaseptins as models for the elucidation of membrane-acting helical amphipathic antimicrobial peptides. Curr. Pharm. Biotechnol. 12: 1184-1193. http://dx.doi.org/10.2174/138920111796117319.
    • (2011) Curr. Pharm. Biotechnol. , vol.12 , pp. 1184-1193
    • Amiche, M.1    Galanth, C.2
  • 29
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • Wimley WC. 2010. Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem. Biol. 5:905-917. http://dx.doi.org/10.1021/cb1001558.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 30
    • 0036174437 scopus 로고    scopus 로고
    • Antibacterial properties of dermaseptin S4 derivatives with in vivo activity
    • DOI 10.1128/AAC.46.3.689-694.2002
    • Navon-Venezia SN, Feder R, Gaidukov L, Carmeli Y, Mor A. 2002. Antimicrobial properties of dermaseptin S4 derivatives with in vivo activity. Antimicrob. Agents Chemother. 46:689-694. http://dx.doi.org/10.1128/AAC.46.3. 689-694.2002. (Pubitemid 34157652)
    • (2002) Antimicrobial Agents and Chemotherapy , vol.46 , Issue.3 , pp. 689-694
    • Navon-Venezia, S.1    Feder, R.2    Gaidukov, L.3    Carmeli, Y.4    Mor, A.5
  • 31
    • 0037053317 scopus 로고    scopus 로고
    • Structural requirements for potent versus selective cytotoxicity for antimicrobial dermaseptin S4 derivatives
    • DOI 10.1074/jbc.M111071200
    • Kustanovich I, Shallev DE, Mikhlin M, Gaidukov L, Mor A. 2002. Structural requirements for potent versus selective cytotoxicity for antimicrobial dermaseptin S4 derivates. J. Biol. Chem. 277:16941-16951. http://dx.doi.org/10. 1074/jbc.M111071200. (Pubitemid 34967722)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16941-16951
    • Kustanovich, I.1    Shalev, D.E.2    Mikhlin, M.3    Gaidukov, L.4    Mor, A.5
  • 32
    • 0037025297 scopus 로고    scopus 로고
    • Direct interaction of dermaseptin S4 aminoheptanoyl derivative with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity in culture
    • DOI 10.1074/jbc.M202089200
    • Efron L, Dagan A, Gaidukov L, Ginsburg H, Mor A. 2002. Direct interaction of dermaseptin S4 aminoheptanoyl derivate with intraerythrocytic malaria parasite leading to increased specific antiparasitic activity in culture. J. Biol. Chem. 277:24067-24072. http://dx.doi.org/10.1074/jbc.M202089200. (Pubitemid 34951919)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.27 , pp. 24067-24072
    • Efron, L.1    Dagan, A.2    Gaidukov, L.3    Ginsburg, H.4    Mor, A.5
  • 34
    • 0041959338 scopus 로고    scopus 로고
    • SAS Institute. release 6.12. SAS Institute, Cary, NC
    • SAS Institute. 2000. SAS/STAT, user's guide, release 6.12. SAS Institute, Cary, NC.
    • (2000) SAS/STAT, User's Guide
  • 35
    • 77952743439 scopus 로고    scopus 로고
    • Antimicrobial and antibiofilm activity of cathelicidins and short, synthetic peptides against Francisella
    • Amer LS, Bishop BM, van Hoek ML. 2010. Antimicrobial and antibiofilm activity of cathelicidins and short, synthetic peptides against Francisella. Biochem. Biophys. Res. Commun. 396:246-251. http://dx.doi.org/10.1016/j.bbrc. 2010.04.073.
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 246-251
    • Amer, L.S.1    Bishop, B.M.2    Van Hoek, M.L.3
  • 37
    • 33749170651 scopus 로고    scopus 로고
    • Effect of MUC7 peptides on the growth of bacteria and on Streptococcus mutans biofilm
    • DOI 10.1093/jac/dkl120
    • Wei GX, Campagna AN, Bobek LA. 2006. Effect of MUC7 peptides on the growth of bacteria and on Streptococcus mutans biofilm. J. Antimicrob. Chemother. 57:1100-1109. http://dx.doi.org/10.1093/jac/dkl120. (Pubitemid 44644411)
    • (2006) Journal of Antimicrobial Chemotherapy , vol.57 , Issue.6 , pp. 1100-1109
    • Wei, G.-X.1    Campagna, A.N.2    Bobek, L.A.3
  • 40
    • 84873435611 scopus 로고    scopus 로고
    • Gene expression analysis by ESTs sequencing of the Brazilian frog Phyllomedusa nordestina skin glands
    • Neiva M, Vargas DC, Conceição K, Rádis-Baptista G, Assakura MT, Jared C, Hayashi MA. 2013. Gene expression analysis by ESTs sequencing of the Brazilian frog Phyllomedusa nordestina skin glands. Toxicon 61:139-150. http://dx.doi.org/10.1016/j.toxicon.2012.10.016.
    • (2013) Toxicon , vol.61 , pp. 139-150
    • Neiva, M.1    Vargas, D.C.2    Conceição, K.3    Rádis-Baptista, G.4    Assakura, M.T.5    Jared, C.6    Hayashi, M.A.7
  • 41
    • 84866558088 scopus 로고    scopus 로고
    • Antimicrobial peptide pleurocidin synergizes with antibiotics through hydroxyl radical formation and membrane damage, and exerts antibiofilm activity
    • Choi H, Lee DG. 2012. Antimicrobial peptide pleurocidin synergizes with antibiotics through hydroxyl radical formation and membrane damage, and exerts antibiofilm activity. Biochim. Biophys. Acta 1820:1831-1838. http://dx.doi.org/10.1016/j.bbagen.2012.08.012.
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 1831-1838
    • Choi, H.1    Lee, D.G.2
  • 43
    • 77953610597 scopus 로고    scopus 로고
    • Phylloseptin-1 (PSN-1) from Phyllomedusa sauvagei skin secretion: A novel broad-spectrum antimicrobial peptide with antibiofilm activity
    • Zhang R, Zhou M, Wang L, McGrath S, Chen T, Chen X, Shaw C. 2010. Phylloseptin-1 (PSN-1) from Phyllomedusa sauvagei skin secretion: a novel broad-spectrum antimicrobial peptide with antibiofilm activity. Mol. Immunol. 47:2030-2037. http://dx.doi.org/10.1016/j.molimm.2010.04.010.
    • (2010) Mol. Immunol. , vol.47 , pp. 2030-2037
    • Zhang, R.1    Zhou, M.2    Wang, L.3    McGrath, S.4    Chen, T.5    Chen, X.6    Shaw, C.7
  • 44
    • 0035014383 scopus 로고    scopus 로고
    • Mechanisms of biofilm resistance to antimicrobial agents
    • Mah TF, O'Toole GA. 2001. Mechanisms of biofilm resistance to antimicrobial agents. Trends Microbiol. 9:34-39. http://dx.doi.org/10.1016/ S0966-842X(00)01913-2.
    • (2001) Trends Microbiol. , vol.9 , pp. 34-39
    • Mah, T.F.1    O'Toole, G.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.