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Volumn 7, Issue 25, 2008, Pages 4856-4867

Antimicrobial activity of lysozyme with special relevance to milk

Author keywords

Antimicrobial activity; Lysozyme; Mechanism of action; Milk; Resistance

Indexed keywords

LIPOPOLYSACCHARIDE; LYSOZYME; PEPTIDOGLYCAN;

EID: 58649122671     PISSN: None     EISSN: 16845315     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (112)

References (120)
  • 2
    • 0033807437 scopus 로고    scopus 로고
    • Immune components in porcine mammary secretions
    • Wagstrom AE, Yoon KJ, Zimmerman JJ (2000). Immune components in porcine mammary secretions. Viral Immunol. 13: 383-397.
    • (2000) Viral Immunol , vol.13 , pp. 383-397
    • Wagstrom, A.E.1    Yoon, K.J.2    Zimmerman, J.J.3
  • 3
    • 51349127691 scopus 로고    scopus 로고
    • Structure, cell wall elasticity and polysaccharide properties of living yeast cells, as probed by AFM
    • 9pp) doi:10.1088/0957-4484/ 19/38/384005 Open access
    • Alsteens D, Dupres V, McEvoy K, Wildling L, Gruber HJ, Dufrene YF (2008). Structure, cell wall elasticity and polysaccharide properties of living yeast cells, as probed by AFM. Nanotechnology. 19: 384005 (9pp) doi:10.1088/0957-4484/ 19/38/384005 (Open access).
    • (2008) Nanotechnology , vol.19 , pp. 384005
    • Alsteens, D.1    Dupres, V.2    McEvoy, K.3    Wildling, L.4    Gruber, H.J.5    Dufrene, Y.F.6
  • 4
    • 0015501830 scopus 로고
    • Occurrence of IV-Nonsubstituted Glucosamine Residues in Peptidoglycan of Lysozyme-resistant Cell Walls from Bacillus cereus
    • Araki T, Nakatani T, Nakayama K, Ito E (1972). Occurrence of IV-Nonsubstituted Glucosamine Residues in Peptidoglycan of Lysozyme-resistant Cell Walls from Bacillus cereus. J. Biol. Chem. 247: 6312-6322.
    • (1972) J. Biol. Chem , vol.247 , pp. 6312-6322
    • Araki, T.1    Nakatani, T.2    Nakayama, K.3    Ito, E.4
  • 5
    • 1642439861 scopus 로고    scopus 로고
    • The lysozyme of the starfish Asterias rubens. A paradygmatic type I lysozyme
    • Bachali S, Bailly X, Jolles J, Jolles P, Deutsch JS (2004). The lysozyme of the starfish Asterias rubens. A paradygmatic type I lysozyme. Eur.J. Biochem. 271: 237-242.
    • (2004) Eur.J. Biochem , vol.271 , pp. 237-242
    • Bachali, S.1    Bailly, X.2    Jolles, J.3    Jolles, P.4    Deutsch, J.S.5
  • 6
    • 0001755293 scopus 로고
    • Inhibition of pathogenic bacteria by camel's milk: Relation to whey lysozyme and stage of lactation
    • Barbour EK, Nabbut NH, Frerisch WM, Al-Nakhli HM (1984). Inhibition of pathogenic bacteria by camel's milk: relation to whey lysozyme and stage of lactation. J. Food Prot. 47: 838-840.
    • (1984) J. Food Prot , vol.47 , pp. 838-840
    • Barbour, E.K.1    Nabbut, N.H.2    Frerisch, W.M.3    Al-Nakhli, H.M.4
  • 8
    • 13444282403 scopus 로고    scopus 로고
    • Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus
    • Bera A, Herbert S, Jakob A, Vollmer W, Gotz F (2005). Why are pathogenic staphylococci so lysozyme resistant? The peptidoglycan O-acetyltransferase OatA is the major determinant for lysozyme resistance of Staphylococcus aureus. Mol. Microbiol. 55: 778-787.
    • (2005) Mol. Microbiol , vol.55 , pp. 778-787
    • Bera, A.1    Herbert, S.2    Jakob, A.3    Vollmer, W.4    Gotz, F.5
  • 9
    • 33746615159 scopus 로고    scopus 로고
    • The presence of peptidoglycan O-acetyltransferase in various staphylococcal species correlates with Lysozyme resistance and pathogenicity
    • Bera A, Biswas R, Herbert S, Gotz F (2006). The presence of peptidoglycan O-acetyltransferase in various staphylococcal species correlates with Lysozyme resistance and pathogenicity. Inf. immunol. 74: 4598-4604
    • (2006) Inf. immunol , vol.74 , pp. 4598-4604
    • Bera, A.1    Biswas, R.2    Herbert, S.3    Gotz, F.4
  • 10
    • 28844456836 scopus 로고
    • Les protéines du lait à activité enzymatique et hormonale.
    • Blanc B (1982). Les protéines du lait à activité enzymatique et hormonale. Le Lait 62: 350-395.
    • (1982) Le Lait , vol.62 , pp. 350-395
    • Blanc, B.1
  • 11
    • 14544282377 scopus 로고    scopus 로고
    • Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria?
    • Brogden KA (2005). Antimicrobial peptides: Pore formers or metabolic inhibitors in bacteria? Nat. Rev. Microbiol. 3: 238-250.
    • (2005) Nat. Rev. Microbiol , vol.3 , pp. 238-250
    • Brogden, K.A.1
  • 12
    • 42949124018 scopus 로고    scopus 로고
    • Callewaert L, Aertsen A, Deckers D, Vanoirbeek KGA, Vanderkelen L, Vanderkelen L, Masschalck B, Nakimbugwe D, Robben J, Van Herreweghe JM, Michiels CW (2008). A new family of lysozyme inhibitors contributing to lysozyme tolerance in gram-negative bacteria. PLos Pathog 4(3): e1000019.doi:10.1371/ journal.ppat.1000019 (open access)
    • Callewaert L, Aertsen A, Deckers D, Vanoirbeek KGA, Vanderkelen L, Vanderkelen L, Masschalck B, Nakimbugwe D, Robben J, Van Herreweghe JM, Michiels CW (2008). A new family of lysozyme inhibitors contributing to lysozyme tolerance in gram-negative bacteria. PLos Pathog 4(3): e1000019.doi:10.1371/ journal.ppat.1000019 (open access)
  • 14
    • 0002824304 scopus 로고
    • Lysozyme, lipase, and ribonuclease in milk of various species
    • Chandan RC, Parry RM, Shahani KM (1968). Lysozyme, lipase, and ribonuclease in milk of various species. J. Dairy Sci. 51: 606-607.
    • (1968) J. Dairy Sci , vol.51 , pp. 606-607
    • Chandan, R.C.1    Parry, R.M.2    Shahani, K.M.3
  • 16
    • 0342656403 scopus 로고    scopus 로고
    • Egg white lysozyme purification by ultrafiltration and affinity chromatography
    • Chiang BH, Su CK, Tsai GJ, Tsao GT (2006). Egg white lysozyme purification by ultrafiltration and affinity chromatography. J. Food Sci. 58: 303-306.
    • (2006) J. Food Sci , vol.58 , pp. 303-306
    • Chiang, B.H.1    Su, C.K.2    Tsai, G.J.3    Tsao, G.T.4
  • 17
    • 0034199281 scopus 로고    scopus 로고
    • Bioactive Milk Peptides: A Prospectus
    • Clare DA, Swaisgood HE (2000). Bioactive Milk Peptides: A Prospectus. J. Dairy Sci. 83: 1187-1195.
    • (2000) J. Dairy Sci , vol.83 , pp. 1187-1195
    • Clare, D.A.1    Swaisgood, H.E.2
  • 18
    • 0026605558 scopus 로고
    • O-acetylated peptidoglycan: Its occurrence, pathobiological significance, and biosynthesis
    • Clarke AJ, Dupont C (1991). O-acetylated peptidoglycan: its occurrence, pathobiological significance, and biosynthesis. Can. J. Microbiol. 38: 85-91.
    • (1991) Can. J. Microbiol , vol.38 , pp. 85-91
    • Clarke, A.J.1    Dupont, C.2
  • 19
    • 1842431398 scopus 로고    scopus 로고
    • Resistance screening essay of wine lactic acid bacteria on lysozyme: Efficacy of lysozyme in unclarified grape musts
    • Delfini C, Cersosimo M, Del Prete V, Strano M, Gaetano G, Pagliara A, Ambrò S (2004) Resistance screening essay of wine lactic acid bacteria on lysozyme: efficacy of lysozyme in unclarified grape musts. J. Agric. Food Chem. 52: 1861-1866.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 1861-1866
    • Delfini, C.1    Cersosimo, M.2    Del Prete, V.3    Strano, M.4    Gaetano, G.5    Pagliara, A.6    Ambrò, S.7
  • 20
    • 0024218969 scopus 로고
    • Purification of camel milk lysozyme and its lytic effect on Escherichia coli and Micrococcus lysodeikticus
    • Duhaiman AS (1988). Purification of camel milk lysozyme and its lytic effect on Escherichia coli and Micrococcus lysodeikticus. Comp. Biochem. Phys. 91B: 793-796.
    • (1988) Comp. Biochem. Phys , vol.91 B , pp. 793-796
    • Duhaiman, A.S.1
  • 22
    • 0033990823 scopus 로고    scopus 로고
    • Effect of heat treatment on camel milk proteins with respect to antimicrobial factors: A comparison with cows' and buffalo milk proteins
    • El Agamy EI (2000). Effect of heat treatment on camel milk proteins with respect to antimicrobial factors: a comparison with cows' and buffalo milk proteins. Food Chem. 68: 227-232.
    • (2000) Food Chem , vol.68 , pp. 227-232
    • El Agamy, E.I.1
  • 23
    • 0030455418 scopus 로고    scopus 로고
    • Purification and characterization of lactoferrin, lactoperoxidase, lysozyme and immunoglobulins from camel's milk
    • El Agamy EI, Ruppanner R, Ismail A, Champagne CP, Assaf R (1996). Purification and characterization of lactoferrin, lactoperoxidase, lysozyme and immunoglobulins from camel's milk. Int. Dairy J. 6:129-145.
    • (1996) Int. Dairy J , vol.6 , pp. 129-145
    • El Agamy, E.I.1    Ruppanner, R.2    Ismail, A.3    Champagne, C.P.4    Assaf, R.5
  • 25
    • 34247466023 scopus 로고    scopus 로고
    • Characterization of whey proteins of camel (Camelus dromedarius) milk and colostrums
    • El Hatmi H, Giradet JM, Gaillard JL, Yahyaoui MH, Attia H (2007). Characterization of whey proteins of camel (Camelus dromedarius) milk and colostrums. Small Rum. Res. 70: 267-271.
    • (2007) Small Rum. Res , vol.70 , pp. 267-271
    • El Hatmi, H.1    Giradet, J.M.2    Gaillard, J.L.3    Yahyaoui, M.H.4    Attia, H.5
  • 26
    • 0026095436 scopus 로고
    • Killing of gram-negative bacteria by lactoferrin and lysozyme
    • Ellison RT, Giehl TJ (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, R.T.1    Giehl, T.J.2
  • 27
    • 0032717048 scopus 로고    scopus 로고
    • Review Diversity of antimicrobial peptides and their mechanisms of action
    • Epand RM, Vogel HJ (1999). Review Diversity of antimicrobial peptides and their mechanisms of action. Bioch. Biophs. Acta. 1462: 11-28.
    • (1999) Bioch. Biophs. Acta , vol.1462 , pp. 11-28
    • Epand, R.M.1    Vogel, H.J.2
  • 28
    • 33847352163 scopus 로고    scopus 로고
    • Streptococcal DRS (distantly related to SIC) and SIC inhibit antimicrobial peptides, components of mucosal innate immunity: A comparison of their activities
    • Fernie-King BA, Seilly DJ, Binks MJ, Sriprakash KS, Lachmann PJ (2007). Streptococcal DRS (distantly related to SIC) and SIC inhibit antimicrobial peptides, components of mucosal innate immunity: a comparison of their activities. Microbes Infect. 9: 300-307.
    • (2007) Microbes Infect , vol.9 , pp. 300-307
    • Fernie-King, B.A.1    Seilly, D.J.2    Binks, M.J.3    Sriprakash, K.S.4    Lachmann, P.J.5
  • 29
    • 0036716438 scopus 로고    scopus 로고
    • Streptococcal inhibitor of complement inhibits two additional components of the mucosal innate immune system: Secretory leukocyte proteinase inhibitor and lysozyme
    • Fernie-King BA, Seilly DJ, Davies A, Lachmann PJ (2002). Streptococcal inhibitor of complement inhibits two additional components of the mucosal innate immune system: secretory leukocyte proteinase inhibitor and lysozyme. Infect. Immunol. 70: 4908-4916.
    • (2002) Infect. Immunol , vol.70 , pp. 4908-4916
    • Fernie-King, B.A.1    Seilly, D.J.2    Davies, A.3    Lachmann, P.J.4
  • 30
    • 0000646464 scopus 로고
    • On a remarkable bacteriolytic element found in tissues and secretions
    • Fleming A (1922). On a remarkable bacteriolytic element found in tissues and secretions. Proc. Roy. Soc. Ser. B. 93: 306-17.
    • (1922) Proc. Roy. Soc. Ser. B , vol.93 , pp. 306-317
    • Fleming, A.1
  • 31
    • 34447291808 scopus 로고    scopus 로고
    • Binding of Lysozyme to Phospholipid Bilayers: Evidence for Protein Aggregation upon Membrane Association
    • Gorbenko GP, Ioffe VM, Kinnunen, Paavo KJ (2007). Binding of Lysozyme to Phospholipid Bilayers: Evidence for Protein Aggregation upon Membrane Association. Biophys. J. 93: 140-153.
    • (2007) Biophys. J , vol.93 , pp. 140-153
    • Gorbenko, G.P.1    Ioffe, V.M.2    Kinnunen, P.K.J.3
  • 32
    • 0003051996 scopus 로고
    • Yeast hyphal dimorphism
    • Edited by N.A.R. Gow & G.M. Gadd. London: Chapman & Hall. pp
    • Gow NAR (1994). Yeast hyphal dimorphism. In The Growing fungus, Edited by N.A.R. Gow & G.M. Gadd. London: Chapman & Hall. pp. 403-422.
    • (1994) The Growing fungus , pp. 403-422
    • Gow, N.A.R.1
  • 33
    • 0028132924 scopus 로고
    • Sequences of two highly divergent canine type c lysozymes: Implications for the evolutionary origins of the lysozyme/alpha-lactalbumin superfamily
    • Grobler JA, Rao KR, Pervaiz S, Brew K (1994). Sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme/alpha-lactalbumin superfamily. Arch. Biochem. Biophys. 313: 360-366.
    • (1994) Arch. Biochem. Biophys , vol.313 , pp. 360-366
    • Grobler, J.A.1    Rao, K.R.2    Pervaiz, S.3    Brew, K.4
  • 34
    • 0022375625 scopus 로고
    • Comparison of biosynthesis and subcellular distribution of lysozyme and lysosomal enzymes in U937 monocytes
    • Gupta DK, Theisen N, von Figura K, Hasilik A (1985). Comparison of biosynthesis and subcellular distribution of lysozyme and lysosomal enzymes in U937 monocytes. Biochem. Biophys. Acta 847: 217-222.
    • (1985) Biochem. Biophys. Acta , vol.847 , pp. 217-222
    • Gupta, D.K.1    Theisen, N.2    von Figura, K.3    Hasilik, A.4
  • 37
    • 0015579786 scopus 로고
    • Occurrence of glucosamine residues with free amino groups in cell wall peptidoglycan from bacilli as a factor responsible for resistance to lysozyme
    • Hayashi H, Araki Y, Ito E (1973). Occurrence of glucosamine residues with free amino groups in cell wall peptidoglycan from bacilli as a factor responsible for resistance to lysozyme. J. Bact. 113: 592-598.
    • (1973) J. Bact , vol.113 , pp. 592-598
    • Hayashi, H.1    Araki, Y.2    Ito, E.3
  • 38
    • 0026552361 scopus 로고
    • Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence
    • Heinz DW, Baase WA, Matthews BW (1992). Folding and function of a T4 lysozyme containing 10 consecutive alanines illustrate the redundancy of information in an amino acid sequence. Proc. Nat. Acad. (USA). 89: 3751-3755.
    • (1992) Proc. Nat. Acad. (USA) , vol.89 , pp. 3751-3755
    • Heinz, D.W.1    Baase, W.A.2    Matthews, B.W.3
  • 39
    • 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 PF, Brasseur DJ, Delogne-Desnoeck JB, Dramaix MM, Robyn CE (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. 53:32-9.
    • (1991) Am. J. Clin, Nutr , vol.53 , pp. 32-39
    • Hennart, P.F.1    Brasseur, D.J.2    Delogne-Desnoeck, J.B.3    Dramaix, M.M.4    Robyn, C.E.5
  • 41
    • 0001406217 scopus 로고
    • Length of hydrocarbon chain and antimicrobial action to gram-negative bacteria of fatty acylated lysozyme
    • Ibrahim HR, Kobayashi K, Kato A (1993). Length of hydrocarbon chain and antimicrobial action to gram-negative bacteria of fatty acylated lysozyme. J. Agric. Food Chem. 41: 1164-1168.
    • (1993) J. Agric. Food Chem , vol.41 , pp. 1164-1168
    • Ibrahim, H.R.1    Kobayashi, K.2    Kato, A.3
  • 42
    • 0001256923 scopus 로고    scopus 로고
    • Partially unfolded lysozyme at neutral pH agglutinates and kills gram-negative and gram-positive bacteria through membrane damage mechanism
    • Ibrahim H, Higashiguchi S, Koketsu M, Juneja F, Kim M, Yamamoto T, Sugimoto Y, Aoki T (1996). Partially unfolded lysozyme at neutral pH agglutinates and kills gram-negative and gram-positive bacteria through membrane damage mechanism. J. Agric. Food. Chem. 44: 3799-3806.
    • (1996) J. Agric. Food. Chem , vol.44 , pp. 3799-3806
    • Ibrahim, H.1    Higashiguchi, S.2    Koketsu, M.3    Juneja, F.4    Kim, M.5    Yamamoto, T.6    Sugimoto, Y.7    Aoki, T.8
  • 43
    • 15444373235 scopus 로고    scopus 로고
    • Evolution of cow nonstomach lysozyme genes
    • Irwin DM (2004). Evolution of cow nonstomach lysozyme genes. Genome 47: 1082-1090.
    • (2004) Genome , vol.47 , pp. 1082-1090
    • Irwin, D.M.1
  • 44
    • 0020345076 scopus 로고
    • Localization of a lipopeptidophosphoglycan extracted by phenol water from trophozoites of the HK-9 strain of Entamoeba histolytica
    • Isibasi A, Santa Cruz M, Soto Montano X, Ramirez A, Kumate J (1982). Localization of a lipopeptidophosphoglycan extracted by phenol water from trophozoites of the HK-9 strain of Entamoeba histolytica. Arch. Invest. Med. 13: 57-62.
    • (1982) Arch. Invest. Med , vol.13 , pp. 57-62
    • Isibasi, A.1    Santa Cruz, M.2    Soto Montano, X.3    Ramirez, A.4    Kumate, J.5
  • 45
    • 0016517114 scopus 로고
    • Heat stability and reactivation of mare milk lysozyme
    • Jauregui-Adell J (1974). Heat stability and reactivation of mare milk lysozyme. J. Dairy Sci. 58: 835-838.
    • (1974) J. Dairy Sci , vol.58 , pp. 835-838
    • Jauregui-Adell, J.1
  • 46
    • 0016517114 scopus 로고
    • Heat stability and reactivation of mare mi1k lysozyme
    • Jauregui-Adell J (1975). Heat stability and reactivation of mare mi1k lysozyme. J. Dairy Sci. 58: 835-838.
    • (1975) J. Dairy Sci , vol.58 , pp. 835-838
    • Jauregui-Adell, J.1
  • 49
    • 0010539913 scopus 로고
    • Lysozyme from human milk
    • Jolles P, Jolles J (1961). Lysozyme from human milk. Nature. 192:1187-1188.
    • (1961) Nature , vol.192 , pp. 1187-1188
    • Jolles, P.1    Jolles, J.2
  • 50
    • 0038814294 scopus 로고    scopus 로고
    • 5-Flanking regions of camel milk genes are highly similar to homologue regions of other species and can be divided into two distinct groups
    • Kappeler SR, Farah Z, Puhan Z (2003). 5-Flanking regions of camel milk genes are highly similar to homologue regions of other species and can be divided into two distinct groups. J. Dairy Sci. 86: 498-508.
    • (2003) J. Dairy Sci , vol.86 , pp. 498-508
    • Kappeler, S.R.1    Farah, Z.2    Puhan, Z.3
  • 51
    • 0028041334 scopus 로고
    • Sensitization of Heat Treated Listeria monocytogenes to Added Lysozyme in Milk
    • Kihm DJ, Leyer GJ, An GH, Johnson EA (1994). Sensitization of Heat Treated Listeria monocytogenes to Added Lysozyme in Milk. Appl. Environ. Microbiol. 60: 3854-386.
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 3854-4386
    • Kihm, D.J.1    Leyer, G.J.2    An, G.H.3    Johnson, E.A.4
  • 53
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R, Billeter M, Wüthrich K (1996). MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics. 14: 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 54
    • 0348062818 scopus 로고    scopus 로고
    • The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models
    • Kopp J, Schwede T (2004). The SWISS-MODEL Repository of annotated three-dimensional protein structure homology models. Nucleic Acids Res. 32: D230-D234.
    • (2004) Nucleic Acids Res , vol.32
    • Kopp, J.1    Schwede, T.2
  • 55
    • 0033529853 scopus 로고    scopus 로고
    • Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site
    • Kuroki R, Weaver LH, Matthews BW (1999). Structural basis of the conversion of T4 lysozyme into a transglycosidase by reengineering the active site. Proc. Natl. Acad. Sci. (USA). 96: 8949-8954.
    • (1999) Proc. Natl. Acad. Sci. (USA) , vol.96 , pp. 8949-8954
    • Kuroki, R.1    Weaver, L.H.2    Matthews, B.W.3
  • 57
    • 0033013458 scopus 로고    scopus 로고
    • Lee-Huang S, Huang PL, Sun Y, Kung Hf, Blithe DL, Chen HC (1999). Lysozyme and RNases as anti-HIV components in beta-core preparations of human chorionic gonadotropin. Proceed. Natl. Acad. Sci. (U S A). 96: 2678-2681.
    • Lee-Huang S, Huang PL, Sun Y, Kung Hf, Blithe DL, Chen HC (1999). Lysozyme and RNases as anti-HIV components in beta-core preparations of human chorionic gonadotropin. Proceed. Natl. Acad. Sci. (U S A). 96: 2678-2681.
  • 58
    • 0035124612 scopus 로고    scopus 로고
    • Chondroitin sulfate is involved in lysosomal transport of lysozyme in U937 cells
    • Lemansky P, Hasilik A (2001). Chondroitin sulfate is involved in lysosomal transport of lysozyme in U937 cells. J. Cell Sci. 114: 345-352.
    • (2001) J. Cell Sci , vol.114 , pp. 345-352
    • Lemansky, P.1    Hasilik, A.2
  • 60
    • 4644220718 scopus 로고    scopus 로고
    • Human milk proteins: Key components for the biological activity of human milk
    • Lonnerdal B (2004). Human milk proteins: key components for the biological activity of human milk. Adv. Exp. Med. Biol. 554: 11-25.
    • (2004) Adv. Exp. Med. Biol , vol.554 , pp. 11-25
    • Lonnerdal, B.1
  • 61
    • 17444385593 scopus 로고    scopus 로고
    • The mechanism of PNIPAAm-assisted refolding of lysozyme denatured by urea
    • Lua D, Liua Z, Zhanga M, Liua Z, Zhoub H (2005). The mechanism of PNIPAAm-assisted refolding of lysozyme denatured by urea. Biochem. Eng. J. 24: 55-64.
    • (2005) Biochem. Eng. J , vol.24 , pp. 55-64
    • Lua, D.1    Liua, Z.2    Zhanga, M.3    Liua, Z.4    Zhoub, H.5
  • 62
    • 0000709385 scopus 로고
    • Lysozyme, chitinase and exo-N-acetyl L□̃ D-Glucosaminidase (NAGase) in lymphomyeloid tissue of marine fishes
    • Lundblad G, Fänge R, Slettengren K, Lind J (1979). Lysozyme, chitinase and exo-N-acetyl L□̃ D-Glucosaminidase (NAGase) in lymphomyeloid tissue of marine fishes. Marine Biol. 53: 311-315.
    • (1979) Marine Biol , vol.53 , pp. 311-315
    • Lundblad, G.1    Fänge, R.2    Slettengren, K.3    Lind, J.4
  • 63
    • 0035703976 scopus 로고    scopus 로고
    • Changes in lactoferrin and lysozyme levels in human milk during the first twelve weeks of lactation
    • Montagne P, Cuilliere ML, Mole C, Bene MC, Faure G (2001). Changes in lactoferrin and lysozyme levels in human milk during the first twelve weeks of lactation. Adv. Exp. Med. Biol. 501: 241-247.
    • (2001) Adv. Exp. Med. Biol , vol.501 , pp. 241-247
    • Montagne, P.1    Cuilliere, M.L.2    Mole, C.3    Bene, M.C.4    Faure, G.5
  • 64
    • 0034930632 scopus 로고    scopus 로고
    • Relationship between mammary gland infections and some milk immune parameters in Sardinian breed ewes
    • Maroni P, Cuccuri C (2001). Relationship between mammary gland infections and some milk immune parameters in Sardinian breed ewes. Small Rum. Res. 41: 1-7.
    • (2001) Small Rum. Res , vol.41 , pp. 1-7
    • Maroni, P.1    Cuccuri, C.2
  • 65
    • 0018855980 scopus 로고
    • Sequential metabolic expressions of the lethal process in human serum-treated Escherichia coli: Role of lysozyme
    • Martinez RJ, Carroll SF (1980). Sequential metabolic expressions of the lethal process in human serum-treated Escherichia coli: Role of lysozyme. INFECTION AND IMMUNITY, 28: 735-745.
    • (1980) INFECTION AND IMMUNITY , vol.28 , pp. 735-745
    • Martinez, R.J.1    Carroll, S.F.2
  • 66
    • 0036909240 scopus 로고    scopus 로고
    • Lytic and nonlytic mechanism of inactivation of gram-positive bacteria by lysozyme under atmospheric and high hydrostatic pressure
    • Masschalck B, Deckers, D, Michiels CW (2002). Lytic and nonlytic mechanism of inactivation of gram-positive bacteria by lysozyme under atmospheric and high hydrostatic pressure. J. Food Prot. 65: 1916-23.
    • (2002) J. Food Prot , vol.65 , pp. 1916-1923
    • Masschalck, B.1    Deckers, D.2    Michiels, C.W.3
  • 67
    • 0141450720 scopus 로고    scopus 로고
    • Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria
    • Masschalck B, Michiels CW (2003). Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria. Crit. Rev. Microbiol. 29: 191-214.
    • (2003) Crit. Rev. Microbiol , vol.29 , pp. 191-214
    • Masschalck, B.1    Michiels, C.W.2
  • 68
    • 0141450720 scopus 로고    scopus 로고
    • Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria
    • Masschalck B, Michiels CW (2003). Antimicrobial properties of lysozyme in relation to foodborne vegetative bacteria. Crit. Rev. Microbiol. 29: 191-214.
    • (2003) Crit. Rev. Microbiol , vol.29 , pp. 191-214
    • Masschalck, B.1    Michiels, C.W.2
  • 69
    • 0035158386 scopus 로고    scopus 로고
    • Inactivation of gram-negative bacteria by lysozyme, denatured lysozyme, and lysozyme-derived peptides under high hydrostatic pressure
    • Masschalck B, Van Houdt R, Van Haver EGR, Michiels CW (2001). Inactivation of gram-negative bacteria by lysozyme, denatured lysozyme, and lysozyme-derived peptides under high hydrostatic pressure. Appl. Environ. Microbiol. 67(1): 339-344.
    • (2001) Appl. Environ. Microbiol , vol.67 , Issue.1 , pp. 339-344
    • Masschalck, B.1    Van Houdt, R.2    Van Haver, E.G.R.3    Michiels, C.W.4
  • 72
    • 0035947615 scopus 로고    scopus 로고
    • Escherichia coli ykfE ORFan. (2001). Gene encodes a potent inhibitor of C-type lysozyme
    • Monchois V, Abergel C, Sturgis J, Jeudy S, Claverie JM (2001). Escherichia coli ykfE ORFan. (2001). Gene encodes a potent inhibitor of C-type lysozyme. J. Biol. Chem. 276: 18437-18441.
    • (2001) J. Biol. Chem , vol.276 , pp. 18437-18441
    • Monchois, V.1    Abergel, C.2    Sturgis, J.3    Jeudy, S.4    Claverie, J.M.5
  • 73
    • 0031875136 scopus 로고    scopus 로고
    • Microparticle-enhanced nephelometric immune assay of lysozyme in milk and other human body fluids
    • Montagne P, Cuillière ML, Mole C, Béńe MC, Faure G (1998). Microparticle-enhanced nephelometric immune assay of lysozyme in milk and other human body fluids. Clin. Chem. 44: 1610-1615.
    • (1998) Clin. Chem , vol.44 , pp. 1610-1615
    • Montagne, P.1    Cuillière, M.L.2    Mole, C.3    Béńe, M.C.4    Faure, G.5
  • 74
    • 34250351484 scopus 로고    scopus 로고
    • Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins
    • Narita SI, Tokuda H (2007). Amino acids at positions 3 and 4 determine the membrane specificity of Pseudomonas aeruginosa lipoproteins. J. Biol. Chem. 282(18): 13372-13378.
    • (2007) J. Biol. Chem , vol.282 , Issue.18 , pp. 13372-13378
    • Narita, S.I.1    Tokuda, H.2
  • 75
    • 38349056428 scopus 로고    scopus 로고
    • Characterization of chitosan and chitosan-glucan complex extracted from the cell wall of fungus Gongronella butleri USDB 0201 by enzymatic method
    • Nwe N, Stevens WF, Tokura S, Tamura H (2008). Characterization of chitosan and chitosan-glucan complex extracted from the cell wall of fungus Gongronella butleri USDB 0201 by enzymatic method. Enzyme Microbial Technol. 42: 242-251.
    • (2008) Enzyme Microbial Technol , vol.42 , pp. 242-251
    • Nwe, N.1    Stevens, W.F.2    Tokura, S.3    Tamura, H.4
  • 76
    • 1642475071 scopus 로고    scopus 로고
    • Staphylococcus aureus capsular polysaccharides
    • O'Riordan K, Lee JC (2004). Staphylococcus aureus capsular polysaccharides. Clin. Microbiol. Rev. 17: 218-234.
    • (2004) Clin. Microbiol. Rev , vol.17 , pp. 218-234
    • O'Riordan, K.1    Lee, J.C.2
  • 77
    • 0020108288 scopus 로고
    • Calf rennet lysozyme
    • Pahud JJ, Widmer F (1982). Calf rennet lysozyme. Biochem. J. 201: 661-664.
    • (1982) Biochem. J , vol.201 , pp. 661-664
    • Pahud, J.J.1    Widmer, F.2
  • 79
    • 0014481750 scopus 로고    scopus 로고
    • (l960). Isolation and characterization of human milk lysozyme
    • Parry RM, Chandan RC Shahani KM (l960). Isolation and characterization of human milk lysozyme. Arch Biochem Bioph. 103: 59-65.
    • Arch Biochem Bioph , vol.103 , pp. 59-65
    • Parry, R.M.1    Chandan, R.C.2    Shahani, K.M.3
  • 80
    • 0026560481 scopus 로고
    • Bactericidal activities of lysozyme and aprotinin against gram-negative and gram positive bacteria related to their basic character
    • Pellegrini A, Thomas U, von Fellenberg R, Wild P (1992). Bactericidal activities of lysozyme and aprotinin against gram-negative and gram positive bacteria related to their basic character. J. Appl. Bacteriol. 72: 180-7.
    • (1992) J. Appl. Bacteriol , vol.72 , pp. 180-187
    • Pellegrini, A.1    Thomas, U.2    von Fellenberg, R.3    Wild, P.4
  • 82
    • 0035799705 scopus 로고    scopus 로고
    • Isolation and characterization of four bactericidal domains in the bovine β- lactoglobulin
    • Pellegrini A, Dettling C, Thomas U, Hunziker P (2001). Isolation and characterization of four bactericidal domains in the bovine β- lactoglobulin. Biochem. Bioph. Acta. 1526: 131-140.
    • (2001) Biochem. Bioph. Acta , vol.1526 , pp. 131-140
    • Pellegrini, A.1    Dettling, C.2    Thomas, U.3    Hunziker, P.4
  • 83
    • 0000916620 scopus 로고
    • The hen egg-white lysozyme molecule
    • Phillips DC (1967). The hen egg-white lysozyme molecule. Proc. Nat. Acad. Sci. U.S.A. 57: 484-495.
    • (1967) Proc. Nat. Acad. Sci. U.S.A , vol.57 , pp. 484-495
    • Phillips, D.C.1
  • 84
    • 24944449486 scopus 로고    scopus 로고
    • Comparison of blood and milk non-specific immune parameters in heifers after calving in relation to udder health
    • Piccinini R, Binda E, Belotti M, Casirani G, Zecconi A (2005). Comparison of blood and milk non-specific immune parameters in heifers after calving in relation to udder health. Vet. Res. 36: 747-757.
    • (2005) Vet. Res , vol.36 , pp. 747-757
    • Piccinini, R.1    Binda, E.2    Belotti, M.3    Casirani, G.4    Zecconi, A.5
  • 85
    • 84986435947 scopus 로고
    • Assay of lysozyme by its lytic action on Leuconostoc oenos: A suitable substrate at acidic pH
    • Pitotti A, Zironi R, Dal Bo A, Boschelle O (1991). Assay of lysozyme by its lytic action on Leuconostoc oenos: a suitable substrate at acidic pH. J. Food Biochem. 15: 393-403.
    • (1991) J. Food Biochem , vol.15 , pp. 393-403
    • Pitotti, A.1    Zironi, R.2    Dal Bo, A.3    Boschelle, O.4
  • 86
    • 0016288414 scopus 로고
    • Widespread Distribution of Lysozyme in Egg White of Birds
    • Prager EM, Wilson AC (1974). Widespread Distribution of Lysozyme in Egg White of Birds, J. Biol. Chem. 249: 7295-7297.
    • (1974) J. Biol. Chem , vol.249 , pp. 7295-7297
    • Prager, E.M.1    Wilson, A.C.2
  • 87
    • 0242404305 scopus 로고    scopus 로고
    • Biochemical characterization of buffalo (Bubalus bubalis) milk lysozyme
    • Priyadarshini S, Kansal VK (2003). Biochemical characterization of buffalo (Bubalus bubalis) milk lysozyme. Journal of Dairy Research. 70: 467-472.
    • (2003) Journal of Dairy Research , vol.70 , pp. 467-472
    • Priyadarshini, S.1    Kansal, V.K.2
  • 88
    • 0023728756 scopus 로고
    • The chemistry of lysozyme and its use as a food preservative and a pharmaceutical
    • Proctor VA, Cunningham FE (1988). The chemistry of lysozyme and its use as a food preservative and a pharmaceutical. Crit. Rev. Food Sci. Nutr. 26: 359-395.
    • (1988) Crit. Rev. Food Sci. Nutr , vol.26 , pp. 359-395
    • Proctor, V.A.1    Cunningham, F.E.2
  • 89
    • 0017115997 scopus 로고
    • Lysozyme synthesis by established human and murine histiocytic lymphoma cell lines
    • Ralph P, Moore MAS, Nilsson K (1976). Lysozyme synthesis by established human and murine histiocytic lymphoma cell lines. J. Exp. Med. 143: 1528-1533.
    • (1976) J. Exp. Med , vol.143 , pp. 1528-1533
    • Ralph, P.1    Moore, M.A.S.2    Nilsson, K.3
  • 90
    • 0032826523 scopus 로고    scopus 로고
    • The Antifungal Activity Of Butylated Hydroxyanizole And Lysozyme
    • Razavi-Rohani SM, Griffiths MW (1999). The Antifungal Activity Of Butylated Hydroxyanizole And Lysozyme. J. Food Safety. 19: 97-108.
    • (1999) J. Food Safety , vol.19 , pp. 97-108
    • Razavi-Rohani, S.M.1    Griffiths, M.W.2
  • 91
  • 92
    • 84965184660 scopus 로고
    • Lysis of gram-negative bacteria by lysozyme
    • Repaske R (1956). Lysis of gram-negative bacteria by lysozyme. Biochem. Biophys. Acta. 22: 189-191.
    • (1956) Biochem. Biophys. Acta , vol.22 , pp. 189-191
    • Repaske, R.1
  • 94
    • 58649124988 scopus 로고    scopus 로고
    • Salton MRJ (1957). The properties of lysozyme and its action on microorganisms. Bacteriol. Revs. 21: 82-100. Sarwar A, Enbergs H, Klug E (2001). Influences of parity, age and mineral and trace element mixture on lysozyme activity in mare's milk during early lactation period. Vet. Arhiv 71: 139-147.
    • Salton MRJ (1957). The properties of lysozyme and its action on microorganisms. Bacteriol. Revs. 21: 82-100. Sarwar A, Enbergs H, Klug E (2001). Influences of parity, age and mineral and trace element mixture on lysozyme activity in mare's milk during early lactation period. Vet. Arhiv 71: 139-147.
  • 95
    • 84987319366 scopus 로고
    • The relationship of lysozyme content of egg white to volume and stability of foams
    • Sauter EA, Montoure JE (1972). The relationship of lysozyme content of egg white to volume and stability of foams. J. Food Sci. 37: 6, 918.
    • (1972) J. Food Sci , vol.37 , Issue.6 , pp. 918
    • Sauter, E.A.1    Montoure, J.E.2
  • 96
    • 0019287608 scopus 로고    scopus 로고
    • Lysozyme in sow's milk and its importance to bacterial population of the gastrointestinal tract in suckling piglets
    • Schulze F, Muller G (1980). Lysozyme in sow's milk and its importance to bacterial population of the gastrointestinal tract in suckling piglets. Arch Exp. Veterinarmed. 34: 317-24.
    • (1980) Arch Exp. Veterinarmed , vol.34 , pp. 317-324
    • Schulze, F.1    Muller, G.2
  • 97
    • 29344466959 scopus 로고    scopus 로고
    • Milk biologically active components as nutraceuticals: Review
    • Severin S, Wenshui X (2005). Milk biologically active components as nutraceuticals: Review. Crit. Rev. Food Sci. Nutr. 45: 645-656.
    • (2005) Crit. Rev. Food Sci. Nutr , vol.45 , pp. 645-656
    • Severin, S.1    Wenshui, X.2
  • 99
    • 33750548441 scopus 로고    scopus 로고
    • Identification of lipopolysaccharide-binding proteins in porcine milk
    • Shahriar F, Gordon JR, Simko E (2006). Identification of lipopolysaccharide-binding proteins in porcine milk. Can. J. Vet. Res. 70: 243-250.
    • (2006) Can. J. Vet. Res , vol.70 , pp. 243-250
    • Shahriar, F.1    Gordon, J.R.2    Simko, E.3
  • 101
    • 0019287608 scopus 로고    scopus 로고
    • to bacterial population of the gastrointestinal tract in suckling piglets. Arch. Exp. Veterinarmed. 34: 317-24.
    • to bacterial population of the gastrointestinal tract in suckling piglets. Arch. Exp. Veterinarmed. 34: 317-24.
  • 102
    • 11944256494 scopus 로고
    • Catalytic mechanisms of enzymic glycosyl transfer
    • Sinnott ML (1990). Catalytic mechanisms of enzymic glycosyl transfer. Chem. Rev. 90: 1171-1202.
    • (1990) Chem. Rev , vol.90 , pp. 1171-1202
    • Sinnott, M.L.1
  • 103
    • 0011082141 scopus 로고
    • Composition and nutritional quality of mare's milk
    • Solaroli G, Pagliarini E, Peri C (1993). Composition and nutritional quality of mare's milk, Ital. J.Food Sci. 1: 3-10.
    • (1993) Ital. J.Food Sci , vol.1 , pp. 3-10
    • Solaroli, G.1    Pagliarini, E.2    Peri, C.3
  • 104
    • 0036840580 scopus 로고    scopus 로고
    • Cationic hydrophobic peptides with antimicrobial activity
    • Stark M, Liu LP, Deber CM (2002). Cationic hydrophobic peptides with antimicrobial activity. Antimicrobial Agents Chemother. 46: 3585-3590.
    • (2002) Antimicrobial Agents Chemother , vol.46 , pp. 3585-3590
    • Stark, M.1    Liu, L.P.2    Deber, C.M.3
  • 105
    • 3242743729 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda H, Matsuyama SI (2004). Sorting of lipoproteins to the outer membrane in E. coli. Biochem. Bioph. Acta 1693: 5-13.
    • (2004) Biochem. Bioph. Acta , vol.1693 , pp. 5-13
    • Tokuda, H.1    Matsuyama, S.I.2
  • 106
    • 0242607058 scopus 로고    scopus 로고
    • Relationships between conformational changes and antimicrobial activity of lysozyme upon reduction of its disulfide bonds
    • Touch V, Hayakawa S, Saitoh K (2004). Relationships between conformational changes and antimicrobial activity of lysozyme upon reduction of its disulfide bonds. Food Chem. 84: 421-428.
    • (2004) Food Chem , vol.84 , pp. 421-428
    • Touch, V.1    Hayakawa, S.2    Saitoh, K.3
  • 107
    • 0026802197 scopus 로고
    • Agents that increase the permeability of the outer membrane
    • Vaara M (1992). Agents that increase the permeability of the outer membrane. Microbiol. Rev. 56: 395-411.
    • (1992) Microbiol. Rev , vol.56 , pp. 395-411
    • Vaara, M.1
  • 108
  • 110
    • 33751362127 scopus 로고    scopus 로고
    • Identifcation of an essential gene responsible for D-Asp incorporation in the Lactococcus lactis peptidoglycan crossbridge
    • Veiga P, Piquet S, Maisons A, Furlan S, Courtin P, Chapot-Chartier MP, Kulakauskas S (2006). Identifcation of an essential gene responsible for D-Asp incorporation in the Lactococcus lactis peptidoglycan crossbridge. Mol. Microbiol. 62: 1713-1724.
    • (2006) Mol. Microbiol , vol.62 , pp. 1713-1724
    • Veiga, P.1    Piquet, S.2    Maisons, A.3    Furlan, S.4    Courtin, P.5    Chapot-Chartier, M.P.6    Kulakauskas, S.7
  • 111
    • 33751362127 scopus 로고    scopus 로고
    • Identification of an essential gene responsible for d-Aspin corporation in the Lactococcus lactis peptidoglycan crossbridge
    • Veiga P, Piquet S, Maisons A, Furlan S, Courtin P, Chapot-Chartier MP, Kulakauskas S (2006) Identification of an essential gene responsible for d-Aspin corporation in the Lactococcus lactis peptidoglycan crossbridge. Mol. Microbiol 62: 1713-1724.
    • (2006) Mol. Microbiol , vol.62 , pp. 1713-1724
    • Veiga, P.1    Piquet, S.2    Maisons, A.3    Furlan, S.4    Courtin, P.5    Chapot-Chartier, M.P.6    Kulakauskas, S.7
  • 112
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg white lysozyme proceeds via a covalent intermediate
    • Vocadlo DJ, Davies GJ, Laine R, Withers SG (2001). Catalysis by hen egg white lysozyme proceeds via a covalent intermediate. Nature. 412: 835-3838.
    • (2001) Nature , vol.412 , pp. 835-3838
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3    Withers, S.G.4
  • 113
    • 0034617218 scopus 로고    scopus 로고
    • The pgdA gene encodes for a peptidoglycan N-Acetylglucosamine deacetylase in Streptococcus pneumonia
    • Vollmer W, Tomasz A (2000). The pgdA gene encodes for a peptidoglycan N-Acetylglucosamine deacetylase in Streptococcus pneumonia. J. Biol. Chem. 275: 20496-20501.
    • (2000) J. Biol. Chem , vol.275 , pp. 20496-20501
    • Vollmer, W.1    Tomasz, A.2
  • 114
    • 11844303551 scopus 로고    scopus 로고
    • First report of a novel plant lysozyme with both antifungal and antibacterial activities
    • Wang S, Ng TB, Chen T, Lin D, Wu J, Rao P, Ye X (2005). First report of a novel plant lysozyme with both antifungal and antibacterial activities. Biochem Biophy. Res. Commun. 327: 820-827.
    • (2005) Biochem Biophy. Res. Commun , vol.327 , pp. 820-827
    • Wang, S.1    Ng, T.B.2    Chen, T.3    Lin, D.4    Wu, J.5    Rao, P.6    Ye, X.7
  • 115
    • 33644871537 scopus 로고    scopus 로고
    • Therapeutic effectiveness of bacteriophages in the rescue of mice with extended spectrum beta-lactamase-producing Escherichia coli bacteremia
    • Wang J, Hu B, Xu M, Yan Q, Liu S, Zhu X, Sun Z, Tao D (2006) Therapeutic effectiveness of bacteriophages in the rescue of mice with extended spectrum beta-lactamase-producing Escherichia coli bacteremia. Int. J. Mol. Med. 17: 347-355.
    • (2006) Int. J. Mol. Med , vol.17 , pp. 347-355
    • Wang, J.1    Hu, B.2    Xu, M.3    Yan, Q.4    Liu, S.5    Zhu, X.6    Sun, Z.7    Tao, D.8
  • 117
    • 0013913479 scopus 로고
    • Lysis of Vibrio suvcinogenes by ethylenediaminetetraacetic acid or lysozyme
    • Wolin MJ (1966). Lysis of Vibrio suvcinogenes by ethylenediaminetetraacetic acid or lysozyme. J. Bacteriol. 91: 1781-1786.
    • (1966) J. Bacteriol , vol.91 , pp. 1781-1786
    • Wolin, M.J.1
  • 118
    • 0032878759 scopus 로고    scopus 로고
    • Inhibition of growth and secreted aspartyl proteinase production in Candida albicans by lysozyme
    • Wu T, Samaranayake LP, Leung WK, Sullivan PA (1999). Inhibition of growth and secreted aspartyl proteinase production in Candida albicans by lysozyme. J. Med. microbiol. 48: 721-730.
    • (1999) J. Med. microbiol , vol.48 , pp. 721-730
    • Wu, T.1    Samaranayake, L.P.2    Leung, W.K.3    Sullivan, P.A.4
  • 119
    • 0033151774 scopus 로고    scopus 로고
    • Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli
    • Wu MH, Maier E, Benz R., and Hancock, R.E.W. 1999. Mechanism of interaction of different classes of cationic antimicrobial peptides with planar bilayers and with the cytoplasmic membrane of Escherichia coli. Biochemistry-US. 38: 7235-7242.
    • (1999) Biochemistry-US , vol.38 , pp. 7235-7242
    • Wu, M.H.1    Maier, E.2    Benz, R.3    Hancock, R.E.W.4


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