메뉴 건너뛰기




Volumn 47, Issue 3-4, 2005, Pages 102-111

Antimicrobial activity of lactoferrin: Mechanisms and possible clinical applications;Actividad antimicrobiana de la lactoferrina: Mecanismos y aplicaciones clínicas potenciales

Author keywords

Antibacterial; Antiviral; Clinical applications; Host defense; Lactoferricin; Lactoferrin

Indexed keywords

GLYCOPROTEIN; IRON BINDING PROTEIN; LACTOFERRIN; METAL;

EID: 33646587652     PISSN: 01874640     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (44)

References (119)
  • 1
    • 0037515474 scopus 로고    scopus 로고
    • Cessation of feline calicivirus shedding coincident with resolution of chronic gingivostomatitis in a cat
    • Addie D.D., A. Radford, P.S. Yam, & D.J. Taylor. 2003. Cessation of feline calicivirus shedding coincident with resolution of chronic gingivostomatitis in a cat. J. Small Anim. Pract. 44:172-176.
    • (2003) J. Small Anim. Pract. , vol.44 , pp. 172-176
    • Addie, D.D.1    Radford, A.2    Yam, P.S.3    Taylor, D.J.4
  • 2
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution
    • Anderson, B.F., H.M. Baker, G.E. Norris, D.W. Rice, & E.N. Baker. 1989. Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution. J. Mol. Biol. 209:711-734.
    • (1989) J. Mol. Biol. , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 4
    • 0028618679 scopus 로고
    • Lactoferrin and the inflammatory response
    • Baynes, R.D., & W.R. Bezwoda. 1994. Lactoferrin and the inflammatory response. Adv. Exp. Med. Biol. 357:133-141.
    • (1994) Adv. Exp. Med. Biol. , vol.357 , pp. 133-141
    • Baynes, R.D.1    Bezwoda, W.R.2
  • 5
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy, W., M. Takase, H. Wakabayashi, K. Kawase, & Tomita, M. 1992a. Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J. Appl. Bacteriol. 73:472-479.
    • (1992) J. Appl. Bacteriol. , vol.73 , pp. 472-479
    • Bellamy, W.1    Takase, M.2    Wakabayashi, H.3    Kawase, K.4    Tomita, M.5
  • 7
    • 0027232811 scopus 로고
    • Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy, W., H. Wakabayashi, M. Takase, K. Kawase, S. Shimamura, & M. Tomita. 1993. Killing of Candida albicans by lactoferricin B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med. Microbiol. Immunol. 182:97-105.
    • (1993) Med. Microbiol. Immunol. , vol.182 , pp. 97-105
    • Bellamy, W.1    Wakabayashi, H.2    Takase, M.3    Kawase, K.4    Shimamura, S.5    Tomita, M.6
  • 8
    • 0015594111 scopus 로고
    • Lactoferrin: An iron binding protein in synovial fluid
    • Bennett, R.M., A.C. Eddie-Quartey, & P.J. Holt. 1973. Lactoferrin: an iron binding protein in synovial fluid. Arthritis Rheum. 16:186-190.
    • (1973) Arthritis Rheum. , vol.16 , pp. 186-190
    • Bennett, R.M.1    Eddie-Quartey, A.C.2    Holt, P.J.3
  • 9
    • 0034633834 scopus 로고    scopus 로고
    • Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice
    • Bernard, K.A., W.B. Klimstra, & R.E. Johnston. 2000. Mutations in the E2 glycoprotein of Venezuelan equine encephalitis virus confer heparan sulfate interaction, low morbidity, and rapid clearance from blood of mice. Virology 276:93-103.
    • (2000) Virology , vol.276 , pp. 93-103
    • Bernard, K.A.1    Klimstra, W.B.2    Johnston, R.E.3
  • 10
    • 0024347869 scopus 로고
    • Lactoferrin from human breast milk and from neutrophil granulocytes. Comparative studies of isolation, quantization, characterization and iron binding properties
    • Bezwoda, W.R., & N. Mansoor. 1989. Lactoferrin from human breast milk and from neutrophil granulocytes. Comparative studies of isolation, quantization, characterization and iron binding properties. Biomed. Chromatogr. 3:121-126.
    • (1989) Biomed. Chromatogr. , vol.3 , pp. 121-126
    • Bezwoda, W.R.1    Mansoor, N.2
  • 11
    • 0032932552 scopus 로고    scopus 로고
    • Influence of lactoferrin feeding and injection against systemic staphylococcal infections in mice
    • Bhimani, R.S., Y. Vendrov, & P. Furmanski. 1999. Influence of lactoferrin feeding and injection against systemic staphylococcal infections in mice. J. Appl. Microbiol. 86:135-144.
    • (1999) J. Appl. Microbiol. , vol.86 , pp. 135-144
    • Bhimani, R.S.1    Vendrov, Y.2    Furmanski, P.3
  • 12
    • 0035159830 scopus 로고    scopus 로고
    • Cell surface heparan sulfate is a receptor for human herpesvirus 8 and interacts with envelope glycoprotein K8.1
    • Birkmann, A., K. Mahr, A. Ensser, S. Yaguboglu, F. Titgemeyer, B. Fleckenstein, & F. Neipel. 2001. Cell surface heparan sulfate is a receptor for human herpesvirus 8 and interacts with envelope glycoprotein K8.1. J. Virol. 75:11583-11593.
    • (2001) J. Virol. , vol.75 , pp. 11583-11593
    • Birkmann, A.1    Mahr, K.2    Ensser, A.3    Yaguboglu, S.4    Titgemeyer, F.5    Fleckenstein, B.6    Neipel, F.7
  • 13
    • 0021888750 scopus 로고
    • Antimicrobial effects of human milk: Inhibitory activity on enteric pathogens
    • Boesman-Finkelstein, M., & R.A. Finkelstein. 1985. Antimicrobial effects of human milk: inhibitory activity on enteric pathogens. FEMS Microbiol. Lett. 27:167-174.
    • (1985) FEMS Microbiol. Lett. , vol.27 , pp. 167-174
    • Boesman-Finkelstein, M.1    Finkelstein, R.A.2
  • 15
    • 14944363351 scopus 로고    scopus 로고
    • Antibiotic molecules: Intracellular
    • Nature Publishing Group
    • Borregaard, N. 2001. Antibiotic molecules: intracellular. Encyclopedia of Life Sciences. Nature Publishing Group. www.els.net.
    • (2001) Encyclopedia of Life Sciences
    • Borregaard, N.1
  • 16
    • 0023616190 scopus 로고
    • The immunogenecity and antigenicity of lipid A are influenced by its physicochemical state and environment
    • Brade, L., K. Brandebburg, H.M. Kuhn, S. Kutsomoto, I. Macher, E.T. Rietschel, & H. Brade. 1987. The immunogenecity and antigenicity of lipid A are influenced by its physicochemical state and environment. Infect. Immun. 55:2636-2644.
    • (1987) Infect. Immun. , vol.55 , pp. 2636-2644
    • Brade, L.1    Brandebburg, K.2    Kuhn, H.M.3    Kutsomoto, S.4    Macher, I.5    Rietschel, E.T.6    Brade, H.7
  • 17
    • 0018899060 scopus 로고
    • Lactoferrin in human milk: Its role in iron absorption and protection against enteric infection in the newborn infant
    • Brock, J.H. 1980. Lactoferrin in human milk: its role in iron absorption and protection against enteric infection in the newborn infant. Arch. Dis. Child. 55:417-421.
    • (1980) Arch. Dis. Child. , vol.55 , pp. 417-421
    • Brock, J.H.1
  • 18
    • 0029160707 scopus 로고
    • Lactoferrin: A multifunctional immunoregulatory protein?
    • Brock, J. 1995. Lactoferrin: a multifunctional immunoregulatory protein?. Immunol. Today, 16:417-419.
    • (1995) Immunol. Today , vol.16 , pp. 417-419
    • Brock, J.1
  • 19
    • 0019640696 scopus 로고
    • The significance of iron in infection
    • Bullen, J.J. 1981. The significance of iron in infection. Rev. Infect. Dis. 3:1127-1138.
    • (1981) Rev. Infect. Dis. , vol.3 , pp. 1127-1138
    • Bullen, J.J.1
  • 21
    • 0031849754 scopus 로고    scopus 로고
    • Binding of Sindbis virus to cell surface heparan sulfate
    • Byrnes, A.P., & D.E. Griffin. 1998. Binding of Sindbis virus to cell surface heparan sulfate. J. Virol. 72:7349-7356.
    • (1998) J. Virol. , vol.72 , pp. 7349-7356
    • Byrnes, A.P.1    Griffin, D.E.2
  • 22
  • 23
    • 0025883731 scopus 로고
    • Septic shock: Treatment
    • Cohen, J., & M.P. Glauser. 1991. Septic shock: treatment. Lancet 338:736-739.
    • (1991) Lancet , vol.338 , pp. 736-739
    • Cohen, J.1    Glauser, M.P.2
  • 24
    • 0026463507 scopus 로고
    • Interaction of lactoferrin and lipopolysaccharide (LPS): Effects on the antioxidant property of lactoferrin and the ability of LPS to prime human neutrophils for enhanced superoxide formation
    • Cohen, M.S., J. Mao, G.T. Rasmussen, J.S. Serody, & B.E. Britigan. 1992. Interaction of lactoferrin and lipopolysaccharide (LPS): effects on the antioxidant property of lactoferrin and the ability of LPS to prime human neutrophils for enhanced superoxide formation. J. Infect. Dis. 166:1375-1378.
    • (1992) J. Infect. Dis. , vol.166 , pp. 1375-1378
    • Cohen, M.S.1    Mao, J.2    Rasmussen, G.T.3    Serody, J.S.4    Britigan, B.E.5
  • 25
    • 0027315907 scopus 로고
    • Initiation of human cytomegalovirus infection requires initial interaction with cell surface heparan sulfate
    • Compton, T., D.M. Nowlin, & N.R. Cooper. 1993. Initiation of human cytomegalovirus infection requires initial interaction with cell surface heparan sulfate. Virology 193:834-841.
    • (1993) Virology , vol.193 , pp. 834-841
    • Compton, T.1    Nowlin, D.M.2    Cooper, N.R.3
  • 26
    • 0024404842 scopus 로고
    • Genetics and molecular biology of siderophore mediated iron transport in bacteria
    • Crosa, J.H. 1989. Genetics and molecular biology of siderophore mediated iron transport in bacteria. Microbiol. Rev. 53:517-530.
    • (1989) Microbiol. Rev. , vol.53 , pp. 517-530
    • Crosa, J.H.1
  • 28
    • 0032078096 scopus 로고    scopus 로고
    • Bovine lactoferrin induces both mucosal and systemic immune response in mice
    • Debbabi, H., M. Dubarry, M. Rautureau, & D. Tome. 1998. Bovine lactoferrin induces both mucosal and systemic immune response in mice. J. Dairy Res. 65:283-293.
    • (1998) J. Dairy Res. , vol.65 , pp. 283-293
    • Debbabi, H.1    Dubarry, M.2    Rautureau, M.3    Tome, D.4
  • 30
    • 0036191258 scopus 로고    scopus 로고
    • Effect of lactoferrin on. Helicobacter felis induced gastritis
    • Dial, E.J., & L.M. Lichtenberger, 2002. Effect of lactoferrin on. Helicobacter felis induced gastritis. Biochem. Cell. Biol. 80:113-117.
    • (2002) Biochem. Cell. Biol. , vol.80 , pp. 113-117
    • Dial, E.J.1    Lichtenberger, L.M.2
  • 32
    • 0031883875 scopus 로고    scopus 로고
    • Lactoferrin inhibits the endotoxin interaction with CD14 by competition with the lipopolysaccharide-binding protein
    • Elass-Rochard, E., D. Legrand, V. Salmon, A. Roseanu, M. Trif, P.S. Tobias, J. Mazurier, & G. Spik. 1998. Lactoferrin inhibits the endotoxin interaction with CD14 by competition with the lipopolysaccharide-binding protein. Infect. Immun. 66:486-491.
    • (1998) Infect. Immun. , vol.66 , pp. 486-491
    • Elass-Rochard, E.1    Legrand, D.2    Salmon, V.3    Roseanu, A.4    Trif, M.5    Tobias, P.S.6    Mazurier, J.7    Spik, G.8
  • 33
    • 0026095436 scopus 로고
    • Killing of Gram-negative bacteria by lactoferrin and lysozyme
    • Ellison R.T. III, & T.J. Giehl. 1991. Killing of Gram-negative bacteria by lactoferrin and lysozyme. J. Clin. Invest. 88:1080-1091.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1080-1091
    • Ellison III, R.T.1    Giehl, T.J.2
  • 34
    • 0017156263 scopus 로고
    • Enterovirus type 70 virion and intracellular proteins
    • Esposito, J.J., & J.F. Obljeski. 1976. Enterovirus type 70 virion and intracellular proteins. J. Virol. 18:1160-1162.
    • (1976) J. Virol. , vol.18 , pp. 1160-1162
    • Esposito, J.J.1    Obljeski, J.F.2
  • 35
    • 0036056151 scopus 로고    scopus 로고
    • Cellular glycosaminoglycans and low density lipoprotein receptor are involved in hepatitis C virus adsorption. Cellular glycosaminoglycans and low-density lipoprotein receptor are involved in hepatitis C virus adsorption
    • Germi, R., J.M. Crance, D. Garin, J. Guimet, H. Lortat-Jacob, R.W. Ruigrok, J.P. Zarski, & E. Drouet. 2002. Cellular glycosaminoglycans and low density lipoprotein receptor are involved in hepatitis C virus adsorption. Cellular glycosaminoglycans and low-density lipoprotein receptor are involved in hepatitis C virus adsorption. Virology. 292:162-168.
    • (2002) Virology , vol.292 , pp. 162-168
    • Germi, R.1    Crance, J.M.2    Garin, D.3    Guimet, J.4    Lortat-Jacob, H.5    Ruigrok, R.W.6    Zarski, J.P.7    Drouet, E.8
  • 36
  • 37
    • 0030946764 scopus 로고    scopus 로고
    • Effect of human milk prostaglandins and lactoferrin on respiratory syncytial virus and rotavirus
    • Grover, M., O. Giouzeppos, R. D. Schnagl, & J.T. May. 1997. Effect of human milk prostaglandins and lactoferrin on respiratory syncytial virus and rotavirus. Acta Paediatr. 86:315-316.
    • (1997) Acta Paediatr. , vol.86 , pp. 315-316
    • Grover, M.1    Giouzeppos, O.2    Schnagl, R.D.3    May, J.T.4
  • 38
    • 0029080953 scopus 로고
    • Antiviral effects of plasma and milk proteins: Lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro
    • Harmsen, M.C., P.J. Swart, M.P. Debethune, R. Pauwels, E. Declercq, T.H. The, & D.K.F. Meijer. 1995. Antiviral effects of plasma and milk proteins: lactoferrin shows potent activity against both human immunodeficiency virus and human cytomegalovirus replication in vitro. J. Infect. Dis. 172:380-388.
    • (1995) J. Infect. Dis. , vol.172 , pp. 380-388
    • Harmsen, M.C.1    Swart, P.J.2    Debethune, M.P.3    Pauwels, R.4    Declercq, E.5    The, T.H.6    Meijer, D.K.F.7
  • 39
    • 0028114753 scopus 로고
    • Inhibition with lactoferrin of in vitro infection with human herpes virus
    • Hasegawa, K., W. Motsuchi, S. Tanaka, & S. Dosako. 1994. Inhibition with lactoferrin of in vitro infection with human herpes virus. Jpn. J. Med. Sci. Biol. 47:73-85.
    • (1994) Jpn. J. Med. Sci. Biol. , vol.47 , pp. 73-85
    • Hasegawa, K.1    Motsuchi, W.2    Tanaka, S.3    Dosako, S.4
  • 40
    • 0034984146 scopus 로고    scopus 로고
    • An amino acid substitution in the coding region of the E2 glycoprotein adapts Ross River virus to utilize heparan sulfate as an attachment moiety
    • Heil, M.L., A. Albee, J.H. Strauss, & R.J. Kuhn. 2001. An amino acid substitution in the coding region of the E2 glycoprotein adapts Ross River virus to utilize heparan sulfate as an attachment moiety. J. Virol. 75:6303-6309.
    • (2001) J. Virol. , vol.75 , pp. 6303-6309
    • Heil, M.L.1    Albee, A.2    Strauss, J.H.3    Kuhn, R.J.4
  • 41
    • 0025957064 scopus 로고
    • Lysozyme, lactoferrin, and secretory immunoglobulin A content in breast milk: Influence of duration of lactation, nutrition status, prolactin status, and parity of mother
    • Hennart, P.F., D.J. Brasseur, J.B. Delogne, M. Desnoeck, M. Dramaix, & C.E. Robyn. 1991. Lysozyme, lactoferrin, and secretory immunoglobulin A content in breast milk: influence of duration of lactation, nutrition status, prolactin status, and parity of mother. Am. J. Clin. Nutr. 53:32-39.
    • (1991) Am. J. Clin. Nutr. , vol.53 , pp. 32-39
    • Hennart, P.F.1    Brasseur, D.J.2    Delogne, J.B.3    Desnoeck, M.4    Dramaix, M.5    Robyn, C.E.6
  • 42
    • 0033765641 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans initiate dengue virus infection of hepatocytes
    • Hilgard, P., & R. Stockert. 2000. Heparan sulfate proteoglycans initiate dengue virus infection of hepatocytes. Hepatology. 32:1069-1077.
    • (2000) Hepatology , vol.32 , pp. 1069-1077
    • Hilgard, P.1    Stockert, R.2
  • 44
    • 2342646131 scopus 로고    scopus 로고
    • A randomized controlled trial of consensus interferon with or without lactoferrin for chronic hepatitis C patients with genotype Ib and high viral load
    • Hirashima, N., E. Orito, & K. Ohba. 2004. A randomized controlled trial of consensus interferon with or without lactoferrin for chronic hepatitis C patients with genotype Ib and high viral load. Hepatol. Res. 29:9-12.
    • (2004) Hepatol. Res. , vol.29 , pp. 9-12
    • Hirashima, N.1    Orito, E.2    Ohba, K.3
  • 46
    • 0033028757 scopus 로고    scopus 로고
    • Inhibitory effects of bovine lactoferrin on colon carcinoma 26 lung metastasis in mice
    • Iigo, M., T. Kuhara, Y. Ushida, K. Sekine, M.A. Moore, & H. Tsuda. 1999. Inhibitory effects of bovine lactoferrin on colon carcinoma 26 lung metastasis in mice. Clin. Exp. Metastasis. 17:35-40.
    • (1999) Clin. Exp. Metastasis , vol.17 , pp. 35-40
    • Iigo, M.1    Kuhara, T.2    Ushida, Y.3    Sekine, K.4    Moore, M.A.5    Tsuda, H.6
  • 49
    • 0001618922 scopus 로고
    • Isolation of an iron containing red protein from human milk
    • Johansen, B.G. 1960. Isolation of an iron containing red protein from human milk. Acta Chem. Scand. 14:510-512.
    • (1960) Acta Chem. Scand. , vol.14 , pp. 510-512
    • Johansen, B.G.1
  • 50
    • 0031259205 scopus 로고    scopus 로고
    • Polymorphic sequence of Korean native goat lactoferrin exhibiting greater antibacterial activity
    • Lee, T.H., K. Shimazaki, S.L. Yu, M.S. Nam, S.J. Kim, K.K. Lee, & D.Y. Yu. 1997. Polymorphic sequence of Korean native goat lactoferrin exhibiting greater antibacterial activity. Anim. Genet. 28:367-369.
    • (1997) Anim. Genet. , vol.28 , pp. 367-369
    • Lee, T.H.1    Shimazaki, K.2    Yu, S.L.3    Nam, M.S.4    Kim, S.J.5    Lee, K.K.6    Yu, D.Y.7
  • 52
    • 0015168183 scopus 로고
    • Inhibition of growth of Candida albicans by iron-unsaturated lactoferrin: Relation to host-defense mechanisms in chronic mucocutaneous candidiasis
    • Kirkpatrick, C.H., I. Green, R.R. Rich, & A.L. Schade. 1971. Inhibition of growth of Candida albicans by iron-unsaturated lactoferrin: relation to host-defense mechanisms in chronic mucocutaneous candidiasis. J. Infect. Dis. 124:539-544.
    • (1971) J. Infect. Dis. , vol.124 , pp. 539-544
    • Kirkpatrick, C.H.1    Green, I.2    Rich, R.R.3    Schade, A.L.4
  • 53
    • 0032775770 scopus 로고    scopus 로고
    • Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor
    • Klimstra, W.B., H.W. Heidner, & R.E. Johnston. 1999. Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor. J. Virol. 73:6299-6306.
    • (1999) J. Virol. , vol.73 , pp. 6299-6306
    • Klimstra, W.B.1    Heidner, H.W.2    Johnston, R.E.3
  • 54
    • 0032707616 scopus 로고    scopus 로고
    • Synergistic fungistatic effects of lactoferrin in combination with antifungal drugs against clinical Candida isolates
    • Kuipers, M.E., H.G. de Vries, M.C. Eikelboom, D.K.F. Meijer, & P.J. Swart. 1999. Synergistic fungistatic effects of lactoferrin in combination with antifungal drugs against clinical Candida isolates. Antimicr. Agents Chemother. 43:2635-2641.
    • (1999) Antimicr. Agents Chemother. , vol.43 , pp. 2635-2641
    • Kuipers, M.E.1    De Vries, H.G.2    Eikelboom, M.C.3    Meijer, D.K.F.4    Swart, P.J.5
  • 55
    • 0034434232 scopus 로고    scopus 로고
    • Orally administered lactoferrina exerts an antimetastatic effect and enhances production of IL-18 in the intestinal epthielium
    • Kuhara, T., M. Iigo, T. Ito, Y. Ushida, K. Sekine, N. Terada, H. Okamura, & H. Tsuda. 2001. Orally administered lactoferrina exerts an antimetastatic effect and enhances production of IL-18 in the intestinal epthielium. Nutr. Cancer. 38:192-199.
    • (2001) Nutr. Cancer. , vol.38 , pp. 192-199
    • Kuhara, T.1    Iigo, M.2    Ito, T.3    Ushida, Y.4    Sekine, K.5    Terada, N.6    Okamura, H.7    Tsuda, H.8
  • 56
    • 0029126185 scopus 로고
    • Lactoferrin: A general review
    • Levay, P.F., & M. Viljoen. 1995. Lactoferrin: a general review. Acta Haematol. 80:252-267.
    • (1995) Acta Haematol. , vol.80 , pp. 252-267
    • Levay, P.F.1    Viljoen, M.2
  • 57
    • 0031866123 scopus 로고    scopus 로고
    • Identification and molecular analysis of LbpBa, which encodes the two-component meningococcal lactoferrin receptor
    • Lewis, L.A., K. Rohde, M. Gipson, B. Behrens, E. Gray, S.I. Toth, B.A. Roe, & D.W. Dyer. 1998. Identification and molecular analysis of LbpBa, which encodes the two-component meningococcal lactoferrin receptor. Infect. Immun. 66:3017-3023.
    • (1998) Infect. Immun. , vol.66 , pp. 3017-3023
    • Lewis, L.A.1    Rohde, K.2    Gipson, M.3    Behrens, B.4    Gray, E.5    Toth, S.I.6    Roe, B.A.7    Dyer, D.W.8
  • 58
    • 0029130333 scopus 로고
    • Lactoferrin: Molecular structure and biological function
    • Lönnerdal, B., & S. Iyer. 1995. Lactoferrin: molecular structure and biological function. Annu. Rev. Nutr. 15:93-110.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 93-110
    • Lönnerdal, B.1    Iyer, S.2
  • 59
    • 0038101672 scopus 로고    scopus 로고
    • Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain
    • Majerle, A., J. Kidric, & R. Jerala. 2003. Enhancement of antibacterial and lipopolysaccharide binding activities of a human lactoferrin peptide fragment by the addition of acyl chain. J. Antimicrob. Chemother. 51:1159-1165.
    • (2003) J. Antimicrob. Chemother. , vol.51 , pp. 1159-1165
    • Majerle, A.1    Kidric, J.2    Jerala, R.3
  • 61
    • 0025156953 scopus 로고
    • Bactericidal/permeability increasing protein has endotoxin-neutralizing activity
    • Marra, M.N., C.G. Wilde, J.E. Griffith, J.L. Snable, & R.W. Scott. 1990. Bactericidal/permeability increasing protein has endotoxin-neutralizing activity. J. Immunol. 144:662-666.
    • (1990) J. Immunol. , vol.144 , pp. 662-666
    • Marra, M.N.1    Wilde, C.G.2    Griffith, J.E.3    Snable, J.L.4    Scott, R.W.5
  • 62
    • 0000000238 scopus 로고
    • Studies on lactoferrin, the iron binding protein of secretions
    • Masson, P.L., & J.F. Heremans. 1966. Studies on lactoferrin, the iron binding protein of secretions. Prot. Biol. Fluids. 14:115-124.
    • (1966) Prot. Biol. Fluids. , vol.14 , pp. 115-124
    • Masson, P.L.1    Heremans, J.F.2
  • 64
    • 0026036144 scopus 로고
    • Lactoferrin-lipopolysaccharide interactions. Effect on lactoferrin binding to monocyte/macrophage-differentiated HL-60 cells
    • Miyazawa, K., C. Mantel, L. Lu, D.C. Morrison, & H.E. Broxmeyer. 1991. Lactoferrin-lipopolysaccharide interactions. Effect on lactoferrin binding to monocyte/macrophage-differentiated HL-60 cells. J. Immunol. 146:723-729.
    • (1991) J. Immunol. , vol.146 , pp. 723-729
    • Miyazawa, K.1    Mantel, C.2    Lu, L.3    Morrison, D.C.4    Broxmeyer, H.E.5
  • 65
    • 0031626510 scopus 로고    scopus 로고
    • Antibiotic-mediated release of endotoxin and the pathogenesis of Gram-negative sepsis
    • Morrison, D.C. 1998. Antibiotic-mediated release of endotoxin and the pathogenesis of Gram-negative sepsis. Prog. Clin Biol. Res. 397:199-207.
    • (1998) Prog. Clin. Biol. Res. , vol.397 , pp. 199-207
    • Morrison, D.C.1
  • 67
    • 0032777103 scopus 로고    scopus 로고
    • Oral administration of lactoferrin enhances the production of IFN-γ and IL-10 in spleen cells cultured with concanavalin A or lipopolysaccharide
    • Nakajima, M., H. Iwamoto, T. Shirasawa, H. Miyauchi, Z. Takatsu, & N. Yamazaki. 1999. Oral administration of lactoferrin enhances the production of IFN-γ and IL-10 in spleen cells cultured with concanavalin A or lipopolysaccharide. Biomed. Res. 20:27-33.
    • (1999) Biomed. Res. , vol.20 , pp. 27-33
    • Nakajima, M.1    Iwamoto, H.2    Shirasawa, T.3    Miyauchi, H.4    Takatsu, Z.5    Yamazaki, N.6
  • 68
    • 0021975789 scopus 로고
    • The biological role of lactoferrin
    • Nemet, K., & I. Simonovits. 1985. The biological role of lactoferrin. Haematologia, 18:3-12.
    • (1985) Haematologia , vol.18 , pp. 3-12
    • Nemet, K.1    Simonovits, I.2
  • 70
    • 0031434232 scopus 로고    scopus 로고
    • Review paper: Growth factors and antimicrobial factors of bovine colostrums
    • Pakkanen, R., & J. Alto. 1997. Review paper: Growth factors and antimicrobial factors of bovine colostrums. Int. Dairy J. 7:285-297.
    • (1997) Int. Dairy J. , vol.7 , pp. 285-297
    • Pakkanen, R.1    Alto, J.2
  • 72
    • 0023134120 scopus 로고
    • Decreased binding of antibiotics to lipopolysaccharide from polymyxin-resistant strains of Escherichia coli and Salmonella typhimurium
    • Paterson, A.A., S.W. Fesik, & E.J. McGroarty. 1987. Decreased binding of antibiotics to lipopolysaccharide from polymyxin-resistant strains of Escherichia coli and Salmonella typhimurium. Antimicrob. Agents Chemother. 31:230-237.
    • (1987) Antimicrob. Agents Chemother. , vol.31 , pp. 230-237
    • Paterson, A.A.1    Fesik, S.W.2    McGroarty, E.J.3
  • 74
    • 0031762646 scopus 로고    scopus 로고
    • Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection
    • Puddu, P., P. Borghi, S. Gessani, P. Valenti, F. Belardelli, & L. Seganti. 1998. Antiviral effect of bovine lactoferrin saturated with metal ions on early steps of human immunodeficiency virus type 1 infection. Int. J. Biochem. Cell B. 30:1055-1063.
    • (1998) Int. J. Biochem. Cell B. , vol.30 , pp. 1055-1063
    • Puddu, P.1    Borghi, P.2    Gessani, S.3    Valenti, P.4    Belardelli, F.5    Seganti, L.6
  • 75
    • 0345035518 scopus 로고    scopus 로고
    • The secondary multidrug transporter LmrP contains multiple drug interaction sites
    • Putman, M., L.A. Koole, H.W. van Veen, & W.N. Konings. 1999. The secondary multidrug transporter LmrP contains multiple drug interaction sites. Biochemistry 38:13900-13905.
    • (1999) Biochemistry , vol.38 , pp. 13900-13905
    • Putman, M.1    Koole, L.A.2    Van Veen, H.W.3    Konings, W.N.4
  • 76
    • 0034488923 scopus 로고    scopus 로고
    • Antibacterial and binding characteristics of bovine, ovine and caprine lactoferrins: A comparative study
    • Recio, I., & S. Visser. 2000. Antibacterial and binding characteristics of bovine, ovine and caprine lactoferrins: A comparative study Int. Dairy J. 10:597-605.
    • (2000) Int. Dairy J. , vol.10 , pp. 597-605
    • Recio, I.1    Visser, S.2
  • 77
    • 0022580536 scopus 로고
    • Bacteriostasis of E. coli by bovine lactoferrin, transferrin and immunoglobulins (IgG1, IgG2, IgM) acting alone or in combination
    • Reinard, P. 1986. Bacteriostasis of E. coli by bovine lactoferrin, transferrin and immunoglobulins (IgG1, IgG2, IgM) acting alone or in combination. Vet. Microbiol. 11:103-115.
    • (1986) Vet. Microbiol. , vol.11 , pp. 103-115
    • Reinard, P.1
  • 78
    • 0020528432 scopus 로고
    • The biological significance of lactoferrin
    • Reiter, B. 1983. The biological significance of lactoferrin. Int. J. Tissue React. 5:87-96.
    • (1983) Int. J. Tissue React. , vol.5 , pp. 87-96
    • Reiter, B.1
  • 79
    • 0001295809 scopus 로고
    • The biological significance of the non-immunoglobulin protective proteins in milk
    • Reiter, B. 1985. The biological significance of the non-immunoglobulin protective proteins in milk. Dev. Daily Chem. 3:281-336.
    • (1985) Dev. Daily Chem. , vol.3 , pp. 281-336
    • Reiter, B.1
  • 80
    • 0028085132 scopus 로고
    • Bacterial endotoxin: Molecular relationships of structure to activity and function
    • Rietschel, E.T., T. Kirikae, F.U. Schade, U. Mamat, G. Schmidt, & H. Loppnow. 1994. Bacterial endotoxin: molecular relationships of structure to activity and function. FASEB J. 8:217-25.
    • (1994) FASEB J. , vol.8 , pp. 217-225
    • Rietschel, E.T.1    Kirikae, T.2    Schade, F.U.3    Mamat, U.4    Schmidt, G.5    Loppnow, H.6
  • 81
    • 0026537260 scopus 로고
    • Supplementation of an adapted formula with bovine lactoferrin: 1. Effect on the infant fecal flora
    • Roberts, A.K., R. Chierici, G. Sawatzki, M.J. Hill, S. Volpato, & V. Vigi. 1992. Supplementation of an adapted formula with bovine lactoferrin: 1. Effect on the infant fecal flora. Acta Paediatr. 81:119-124.
    • (1992) Acta Paediatr. , vol.81 , pp. 119-124
    • Roberts, A.K.1    Chierici, R.2    Sawatzki, G.3    Hill, M.J.4    Volpato, S.5    Vigi, V.6
  • 82
    • 0017872616 scopus 로고
    • Bacteriostatic effect of human milk on E. coli: The role of IgA
    • Rogers, H.J., & C. Synge. 1978. Bacteriostatic effect of human milk on E. coli: The role of IgA. Immunology. 34:19-28.
    • (1978) Immunology , vol.34 , pp. 19-28
    • Rogers, H.J.1    Synge, C.2
  • 83
    • 0023854864 scopus 로고
    • Polycation binding to isolates lipopolysaccharide from antibiotic-hypersusceptible mutants strains of Escherichia coli
    • Roque, W.J., S.W. Fesik, A. Haug, & E.J. McGroarty. 1987. Polycation binding to isolates lipopolysaccharide from antibiotic-hypersusceptible mutants strains of Escherichia coli. Antimicrob Agents Chemother. 32:308-313.
    • (1987) Antimicrob Agents Chemother , vol.32 , pp. 308-313
    • Roque, W.J.1    Fesik, S.W.2    Haug, A.3    McGroarty, E.J.4
  • 84
    • 0018611704 scopus 로고
    • Secretory IgA does not enhance the bacteriostatic effect of iron-binding or vitamin B12-binding protein in human colostrum
    • Samson, R.R., C. Mirtle, & D.B.L. McClelland. 1979. Secretory IgA does not enhance the bacteriostatic effect of iron-binding or vitamin B12-binding protein in human colostrum. Immunology. 38: 367-373.
    • (1979) Immunology , vol.38 , pp. 367-373
    • Samson, R.R.1    Mirtle, C.2    McClelland, D.B.L.3
  • 85
    • 0029962565 scopus 로고    scopus 로고
    • Oral administration of bovine lactoferrin for treatment of intractable stomatitis in feline immunodeficiency virus (FIV)-positive and FIV-negative cats
    • Sato, R., O. Inanami, Y. Tanaka, M. Takase, & Y. Naito. 1996. Oral administration of bovine lactoferrin for treatment of intractable stomatitis in feline immunodeficiency virus (FIV)-positive and FIV-negative cats. Am J. Vet. Res. 57:1443-1446.
    • (1996) Am. J. Vet. Res. , vol.57 , pp. 1443-1446
    • Sato, R.1    Inanami, O.2    Tanaka, Y.3    Takase, M.4    Naito, Y.5
  • 87
    • 0031469568 scopus 로고    scopus 로고
    • Inhibition of initiation and early stage development of aberrant crypt foci and enhanced natural killer activity in male rats administered bovine lactoferrin concomitantly with azoxymethane
    • Sekine, K., Y. Ushida, T. Kuhara, M. Iigo, H. Baba-Toriyama, & M.A. Moore. 1997. Inhibition of initiation and early stage development of aberrant crypt foci and enhanced natural killer activity in male rats administered bovine lactoferrin concomitantly with azoxymethane. Cancer Lett. 121:211-216.
    • (1997) Cancer Lett. , vol.121 , pp. 211-216
    • Sekine, K.1    Ushida, Y.2    Kuhara, T.3    Iigo, M.4    Baba-Toriyama, H.5    Moore, M.A.6
  • 88
    • 0034883314 scopus 로고    scopus 로고
    • Herpesviruses and heparan sulfate: An intimate relationship in aid of viral entry
    • Shukla, D., & P.G. Spear. 2001. Herpesviruses and heparan sulfate: an intimate relationship in aid of viral entry J. Clin. Invest. 108:503-510.
    • (2001) J. Clin. Invest. , vol.108 , pp. 503-510
    • Shukla, D.1    Spear, P.G.2
  • 90
    • 0019135235 scopus 로고
    • Differences in inhibition of the growth of commensal and enteropathogenic strains of E. coli by lactoferrin and sIgA isolated from human milk
    • Stephens, S., J.M. Dolby, J. Montreuil, & G. Spik. 1980. Differences in inhibition of the growth of commensal and enteropathogenic strains of E. coli by lactoferrin and sIgA isolated from human milk. Immunology. 41:597-603.
    • (1980) Immunology , vol.41 , pp. 597-603
    • Stephens, S.1    Dolby, J.M.2    Montreuil, J.3    Spik, G.4
  • 91
    • 0024340980 scopus 로고
    • Polymyxin B prevents lipopolysaccharide-induced release of tumor necrosis factor-alpha from alveolar macrophages
    • Stokes, D.C., J.L. Shenep, M. Fishman, W.K. Hildner, G.K. Bysani, & K. Rufus. 1989. Polymyxin B prevents lipopolysaccharide-induced release of tumor necrosis factor-alpha from alveolar macrophages. J. Infect. Dis. 160:52-57.
    • (1989) J. Infect. Dis. , vol.160 , pp. 52-57
    • Stokes, D.C.1    Shenep, J.L.2    Fishman, M.3    Hildner, W.K.4    Bysani, G.K.5    Rufus, K.6
  • 92
    • 0031906147 scopus 로고    scopus 로고
    • Membrane-associated heparan sulfate
    • Summerford, C., & R.J. Samulski. 1998. Membrane-associated heparan sulfate. J. Virol. 72:1438-1445.
    • (1998) J. Virol. , vol.72 , pp. 1438-1445
    • Summerford, C.1    Samulski, R.J.2
  • 93
    • 0030661831 scopus 로고    scopus 로고
    • Antirotaviral activity of milk proteins: Lactoferrin prevents rotavirus infection in the enterocyte-like cell line HT-29
    • Superti, F., M. G. Ammendolia, P. Valenti, & L. Seganti. 1997. Antirotaviral activity of milk proteins: lactoferrin prevents rotavirus infection in the enterocyte-like cell line HT-29. Med. Microbiol. Immunol. 186:83-91.
    • (1997) Med. Microbiol. Immunol. , vol.186 , pp. 83-91
    • Superti, F.1    Ammendolia, M.G.2    Valenti, P.3    Seganti, L.4
  • 96
    • 0029892820 scopus 로고    scopus 로고
    • Antiviral effects of milk proteins: Acylation results in polyanionic compounds with portent activity against human immunodeficiency virus types 1 and 2 in vitro
    • Swart, P.J., M.E. Kuipers, C. Smit, R. Pauwels, M.P. DeBethune, E. DeCleroq, D.K. Meijer, & J.G. Huisman, J.G. 1996. Antiviral effects of milk proteins: acylation results in polyanionic compounds with portent activity against human immunodeficiency virus types 1 and 2 in vitro. Aids Res. Human Retroviruses 12:769-775.
    • (1996) Aids Res. Human Retroviruses , vol.12 , pp. 769-775
    • Swart, P.J.1    Kuipers, M.E.2    Smit, C.3    Pauwels, R.4    DeBethune, M.P.5    DeCleroq, E.6    Meijer, D.K.7    Huisman, J.G.8
  • 97
    • 0032962172 scopus 로고    scopus 로고
    • Lactoferrin inhibits hepatitis C virus viremia in patients with chronic hepatitis C: A pilot study
    • Tanaka, K., M. Ikeda, A. Nozaki, N. Kato, H. Tsuda, S. Saito, & H. Sekihara. 1999. Lactoferrin inhibits hepatitis C virus viremia in patients with chronic hepatitis C: a pilot study. Jpn. J. Cancer Res. 90:367-371.
    • (1999) Jpn. J. Cancer Res. , vol.90 , pp. 367-371
    • Tanaka, K.1    Ikeda, M.2    Nozaki, A.3    Kato, N.4    Tsuda, H.5    Saito, S.6    Sekihara, H.7
  • 100
    • 0036714306 scopus 로고    scopus 로고
    • Orally ingested human lactoferrin is digested and secreted in the upper gastrointestinal tract in vivo in women with ileostomies
    • Troost, F.J., W.H.M. Saris, & R-J.M. Brummer. 2002. Orally ingested human lactoferrin is digested and secreted in the upper gastrointestinal tract in vivo in women with ileostomies. J. Nutr. 78:2597-2600.
    • (2002) J. Nutr. , vol.78 , pp. 2597-2600
    • Troost, F.J.1    Saris, W.H.M.2    Brummer, R.-J.M.3
  • 102
    • 0036438885 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 glycoprotein C is necessary for efficient infection of chondroitin sulfate-expressing gro2C cells
    • Trybala, E., A. Roth, M. Johansson, J.A. Liljeqvist, E. Rekabdar, O. Larm, & T. Bergstrom. 2002. Herpes simplex virus type 1 glycoprotein C is necessary for efficient infection of chondroitin sulfate-expressing gro2C cells. Virology. 302:413-419.
    • (2002) Virology , vol.302 , pp. 413-419
    • Trybala, E.1    Roth, A.2    Johansson, M.3    Liljeqvist, J.A.4    Rekabdar, E.5    Larm, O.6    Bergstrom, T.7
  • 104
    • 0030664951 scopus 로고    scopus 로고
    • N-terminal stretch arg2, arg3, arg4 and arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA
    • Van Berkel, P.H., M.E. Geerts, H.A. van Veen, M. Mericskay, H.A. de Boer, & J.H. Nuijens. 1997. N-terminal stretch arg2, arg3, arg4 and arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA. Biochem. J. 328:145-151.
    • (1997) Biochem. J. , vol.328 , pp. 145-151
    • Van Berkel, P.H.1    Geerts, M.E.2    Van Veen, H.A.3    Mericskay, M.4    De Boer, H.A.5    Nuijens, J.H.6
  • 106
    • 0034490329 scopus 로고    scopus 로고
    • In vivo antimicrobial and antiviral activity of components in bovine milk and colostrum involved in non-specific defense
    • Van Hooijdonk, A., K.D. Kussendrager, & J. Steijns. M. 2000. In vivo antimicrobial and antiviral activity of components in bovine milk and colostrum involved in non-specific defense. Br. J. Nutr. 84:127-134.
    • (2000) Br. J. Nutr. , vol.84 , pp. 127-134
    • Van Hooijdonk, A.1    Kussendrager, K.D.2    Steijns, M.J.3
  • 109
    • 0032737846 scopus 로고    scopus 로고
    • Lactoferrin: A multifunctional glycoprotein
    • Vorland, L.H. 1999. Lactoferrin: a multifunctional glycoprotein. Apmis 107:971-981.
    • (1999) Apmis , vol.107 , pp. 971-981
    • Vorland, L.H.1
  • 110
    • 33646581517 scopus 로고    scopus 로고
    • Antiviral activity of human lactoferrin: Inhibition of alphavirus interaction with heparan sulfate
    • B.L. Waarts (Eds). Groningen University. The Netherlands
    • Waarts, B.L., O. Aneke, J.M. Smit, K. Kimata, R. Bittman, D. Meijer, & J. Wilschut. 2004. Antiviral activity of human lactoferrin: Inhibition of alphavirus interaction with heparan sulfate. pp 108-120 In B.L. Waarts (Eds). Cell entry mechanisms of alphavirus editor. Groningen University. The Netherlands.
    • (2004) Cell Entry Mechanisms of Alphavirus Editor , pp. 108-120
    • Waarts, B.L.1    Aneke, O.2    Smit, J.M.3    Kimata, K.4    Bittman, R.5    Meijer, D.6    Wilschut, J.7
  • 111
    • 0030457861 scopus 로고    scopus 로고
    • Cooperative anti-Candida effects of lactoferrin or its peptides in combination with azole antifungal agents
    • Wakabayashi, H., S. Abe, T. Okutomi, S. Tansho, K. Kawase, & H. Yamaguchi. 1996. Cooperative anti-Candida effects of lactoferrin or its peptides in combination with azole antifungal agents. Microbiol. Immunol. 40:821-825.
    • (1996) Microbiol. Immunol. , vol.40 , pp. 821-825
    • Wakabayashi, H.1    Abe, S.2    Okutomi, T.3    Tansho, S.4    Kawase, K.5    Yamaguchi, H.6
  • 113
    • 0033767482 scopus 로고    scopus 로고
    • Activation of intestinal mucosal immunity in tumor-bearing mice by lactoferrin
    • Wang, W.P., M. Iigo, J. Sato, K. Kazuhiro, I. Adachi, & H. Tsuda, H. 2000. Activation of intestinal mucosal immunity in tumor-bearing mice by lactoferrin. Jpn. J. Cancer Res. 91:1022-1027.
    • (2000) Jpn. J. Cancer Res. , vol.91 , pp. 1022-1027
    • Wang, W.P.1    Iigo, M.2    Sato, J.3    Kazuhiro, K.4    Adachi, I.5    Tsuda, H.6
  • 115
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi, K., M. Tomita, T.J. Giehl, & R.T. Ellison III. 1993. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect. Immun. 61:719-728.
    • (1993) Infect. Immun. , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison III, R.T.4
  • 116
    • 0030740063 scopus 로고    scopus 로고
    • Hepatitis C virus envelope proteins bind lactoferrin
    • Yi, M.Y., S. Kaneko, D.Y. Yu, & S. Murakami. 1997. Hepatitis C virus envelope proteins bind lactoferrin. J. Virol. 71:5997-6002.
    • (1997) J. Virol. , vol.71 , pp. 5997-6002
    • Yi, M.Y.1    Kaneko, S.2    Yu, D.Y.3    Murakami, S.4
  • 117
    • 0034303264 scopus 로고    scopus 로고
    • Separation of lactoferrin-a and lactoferrin-b from bovine colostrum
    • Yoshida, S., Z. Wei, Y. Shinmura, & N. Fukunaga. 2000. Separation of lactoferrin-a and lactoferrin-b from bovine colostrum. J. Dairy Sci. 83:2211-2215.
    • (2000) J. Dairy Sci. , vol.83 , pp. 2211-2215
    • Yoshida, S.1    Wei, Z.2    Shinmura, Y.3    Fukunaga, N.4
  • 118
    • 0031982046 scopus 로고    scopus 로고
    • Antibacterial system generated by lactoferrin in mice in vivo is primarily a killing system
    • Zagulski, T., P. Lipinski, A. Zagulska, & Z. Jarzabek. 1998. Antibacterial system generated by lactoferrin in mice in vivo is primarily a killing system. Int J. Exp. Pathol. 79:117-123.
    • (1998) Int J. Exp. Pathol. , vol.79 , pp. 117-123
    • Zagulski, T.1    Lipinski, P.2    Zagulska, A.3    Jarzabek, Z.4
  • 119
    • 0031697592 scopus 로고    scopus 로고
    • Immunoregulatory effects of a nutritional preparation containing bovine lactoferrin taken orally by healthy individuals
    • Zimecki, M., A. Wlaszczyk, P. Cheneau, A-S. Brunel, J. Mazurier, & G. Spik. 1998. Immunoregulatory effects of a nutritional preparation containing bovine lactoferrin taken orally by healthy individuals. Arch. Immun. Ther. Exp. 46:231-40.
    • (1998) Arch. Immun. Ther. Exp. , vol.46 , pp. 231-240
    • Zimecki, M.1    Wlaszczyk, A.2    Cheneau, P.3    Brunel, A.-S.4    Mazurier, J.5    Spik, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.