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Volumn 28, Issue 3, 2010, Pages 419-427

Transgenic zebrafish eggs containing bactericidal peptide is a novel food supplement enhancing resistance to pathogenic infection of fish

Author keywords

Bactericide; Embryos; Feeding; Lactoferrincin; Transgenic; Zebrafish

Indexed keywords

AEROMONAS HYDROPHILA; BOVINAE; DANIO RERIO; EDWARDSIELLA TARDA; ESCHERICHIA COLI;

EID: 76749155815     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2009.11.019     Document Type: Article
Times cited : (17)

References (50)
  • 1
    • 0001395327 scopus 로고
    • The isolation of a red protein from milk
    • Groves M.L. The isolation of a red protein from milk. J Am Chem Soc 82 (1960) 3345-3350
    • (1960) J Am Chem Soc , vol.82 , pp. 3345-3350
    • Groves, M.L.1
  • 2
    • 0032893748 scopus 로고    scopus 로고
    • Lactoferrin: a multifunctional glycoprotein involved in the modulation of the inflammatory process
    • Baveye S., Elass E., Mazurier J., Spik G., and Legrand D. Lactoferrin: a multifunctional glycoprotein involved in the modulation of the inflammatory process. Clin Chem Lab Med 37 (1999) 281-286
    • (1999) Clin Chem Lab Med , vol.37 , pp. 281-286
    • Baveye, S.1    Elass, E.2    Mazurier, J.3    Spik, G.4    Legrand, D.5
  • 3
    • 0035749335 scopus 로고    scopus 로고
    • Antimicrobial actions of lactoferrin
    • Chierici R. Antimicrobial actions of lactoferrin. Adv Nutr Res 10 (2001) 247-269
    • (2001) Adv Nutr Res , vol.10 , pp. 247-269
    • Chierici, R.1
  • 4
    • 58149125767 scopus 로고    scopus 로고
    • A structural framework for understanding the multifunctional character of lactoferrin
    • Baker E.N., and Baker H.M. A structural framework for understanding the multifunctional character of lactoferrin. Biochimie 91 (2009) 3-10
    • (2009) Biochimie , vol.91 , pp. 3-10
    • Baker, E.N.1    Baker, H.M.2
  • 7
    • 0027465990 scopus 로고
    • Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment
    • Yamauchi K., Tomita M., Giehl T.J., and Ellison R.T. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect Immun 61 (1993) 719-728
    • (1993) Infect Immun , vol.61 , pp. 719-728
    • Yamauchi, K.1    Tomita, M.2    Giehl, T.J.3    Ellison, R.T.4
  • 8
    • 0026475489 scopus 로고
    • Antibacterial spectrum of lactoferricin-B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy W., Takase M., Wakabayashi H., Kawase K., and Tomita M. Antibacterial spectrum of lactoferricin-B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin. J Appl Bacteriol 73 (1992) 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
  • 9
    • 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., Wakabayashi H., Takase M., Kawase K., Shimamura S., and Tomita M. Killing of Candida albicans by lactoferricin-B, a potent antimicrobial peptide derived from the N-terminal region of bovine lactoferrin. Med Microbiol Immunol 182 (1993) 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
  • 10
    • 84903421873 scopus 로고    scopus 로고
    • Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin
    • Hwang P.M., Zhou N., Shan X., Arrowsmith C.H., and Vogel H.J. Three-dimensional solution structure of lactoferricin B, an antimicrobial peptide derived from bovine lactoferrin. Biochemistry 37 (1998) 4288-4298
    • (1998) Biochemistry , vol.37 , pp. 4288-4298
    • Hwang, P.M.1    Zhou, N.2    Shan, X.3    Arrowsmith, C.H.4    Vogel, H.J.5
  • 11
    • 0032701261 scopus 로고    scopus 로고
    • Initial binding sites of antimicrobial peptides in Staphylococcus aureus and Escherichia coli
    • Vorland L.H., Ulvatne H., Rekdal O., and Svendsen J.S. Initial binding sites of antimicrobial peptides in Staphylococcus aureus and Escherichia coli. Scand J Infect Dis 31 (1999) 467-473
    • (1999) Scand J Infect Dis , vol.31 , pp. 467-473
    • Vorland, L.H.1    Ulvatne, H.2    Rekdal, O.3    Svendsen, J.S.4
  • 12
  • 13
    • 18044401665 scopus 로고    scopus 로고
    • Reduction of the infectivity of Toxoplasma gondii and Eimeria stiedae sporozoites by treatment with bovine lactoferricin
    • Omata Y., Satake M., Maeda R., Saito A., Shimazaki K., Yamauchi K., et al. Reduction of the infectivity of Toxoplasma gondii and Eimeria stiedae sporozoites by treatment with bovine lactoferricin. J Vet Med Sci 63 (2001) 187-190
    • (2001) J Vet Med Sci , vol.63 , pp. 187-190
    • Omata, Y.1    Satake, M.2    Maeda, R.3    Saito, A.4    Shimazaki, K.5    Yamauchi, K.6
  • 14
    • 0028828203 scopus 로고
    • Giardicidal activity of lactoferrin and N-terminal peptides
    • Turchany J.M., Aley S.B., and Gillin F.D. Giardicidal activity of lactoferrin and N-terminal peptides. Infect Immun 63 (1995) 4550-4552
    • (1995) Infect Immun , vol.63 , pp. 4550-4552
    • Turchany, J.M.1    Aley, S.B.2    Gillin, F.D.3
  • 15
    • 0029584910 scopus 로고
    • Toxoplasma gondii: parasiticidal effects of bovine lactoferricin against parasites
    • Tanaka T., Omata Y., Saito A., Shimazaki K., Yamauchi K., Takase M., et al. Toxoplasma gondii: parasiticidal effects of bovine lactoferricin against parasites. Exp Parasitol 81 (1995) 614-617
    • (1995) Exp Parasitol , vol.81 , pp. 614-617
    • Tanaka, T.1    Omata, Y.2    Saito, A.3    Shimazaki, K.4    Yamauchi, K.5    Takase, M.6
  • 16
    • 0028309575 scopus 로고
    • Antifungal properties of lactoferricin-B, a peptide derived from the N-terminal region of bovine lactoferrin
    • Bellamy W., Yamauchi K., Wakabayashi H., Takase M., Takakura N., Shimamura S., et al. Antifungal properties of lactoferricin-B, a peptide derived from the N-terminal region of bovine lactoferrin. Lett Appl Microbiol 18 (1994) 230-233
    • (1994) Lett Appl Microbiol , vol.18 , pp. 230-233
    • Bellamy, W.1    Yamauchi, K.2    Wakabayashi, H.3    Takase, M.4    Takakura, N.5    Shimamura, S.6
  • 17
    • 33750795816 scopus 로고    scopus 로고
    • Activity and mode of action against fungal phytopathogens of bovine lactoferricin-derived peptides
    • Munoz A., and Marcos J.F. Activity and mode of action against fungal phytopathogens of bovine lactoferricin-derived peptides. J Appl Microbiol 101 (2006) 1199-1207
    • (2006) J Appl Microbiol , vol.101 , pp. 1199-1207
    • Munoz, A.1    Marcos, J.F.2
  • 18
  • 19
    • 0344304749 scopus 로고    scopus 로고
    • Anti-HSV activity of lactoferricin analogues is only partly related to their affinity for heparan sulfate
    • Jenssen H., Andersen J.H., Uhlin-Hansen L., Gutteberg T.J., and Rekdal O. Anti-HSV activity of lactoferricin analogues is only partly related to their affinity for heparan sulfate. Antivir Res 61 (2004) 101-109
    • (2004) Antivir Res , vol.61 , pp. 101-109
    • Jenssen, H.1    Andersen, J.H.2    Uhlin-Hansen, L.3    Gutteberg, T.J.4    Rekdal, O.5
  • 20
    • 29344463703 scopus 로고    scopus 로고
    • Anti herpes simplex virus activity of lactoferrin/lactoferricin - an example of antiviral activity of antimicrobial protein/peptide
    • Jenssen H. Anti herpes simplex virus activity of lactoferrin/lactoferricin - an example of antiviral activity of antimicrobial protein/peptide. Cell Mol Life Sci 62 (2005) 3002-3013
    • (2005) Cell Mol Life Sci , vol.62 , pp. 3002-3013
    • Jenssen, H.1
  • 21
    • 31444434715 scopus 로고    scopus 로고
    • Bovine lactoferrin peptidic fragments involved in inhibition of Echovirus 6 in vitro infection
    • Pietrantoni A., Ammendolia M.G., Tinari A., Siciliano R., Valenti P., and Superti F. Bovine lactoferrin peptidic fragments involved in inhibition of Echovirus 6 in vitro infection. Antivir Res 69 (2006) 98-106
    • (2006) Antivir Res , vol.69 , pp. 98-106
    • Pietrantoni, A.1    Ammendolia, M.G.2    Tinari, A.3    Siciliano, R.4    Valenti, P.5    Superti, F.6
  • 23
    • 2942536480 scopus 로고    scopus 로고
    • Application of inducible and targeted gene strategies to produce transgenic fish: a review
    • Rocha A., Ruiz S., Estepa A., and Joll J.M. Application of inducible and targeted gene strategies to produce transgenic fish: a review. Mar Biotechnol 6 (2004) 118-127
    • (2004) Mar Biotechnol , vol.6 , pp. 118-127
    • Rocha, A.1    Ruiz, S.2    Estepa, A.3    Joll, J.M.4
  • 24
    • 16844386104 scopus 로고    scopus 로고
    • Fish as bioreactors: transgene expression of human coagulation factor VII in fish embryos
    • Hwang G.L., Muller F., Rahman M.A., Williams D.W., Murdock P.J., Pasi K.J., et al. Fish as bioreactors: transgene expression of human coagulation factor VII in fish embryos. Mar Biotechnol 6 (2004) 485-492
    • (2004) Mar Biotechnol , vol.6 , pp. 485-492
    • Hwang, G.L.1    Muller, F.2    Rahman, M.A.3    Williams, D.W.4    Murdock, P.J.5    Pasi, K.J.6
  • 25
    • 18244399124 scopus 로고    scopus 로고
    • Fish eggs as bioreactors: the production of bioactive luteinizing hormone in transgenic trout embryos
    • Morita T., Yoshizaki G., Kobayashi M., Watabe S., and Takeuchi T. Fish eggs as bioreactors: the production of bioactive luteinizing hormone in transgenic trout embryos. Transgenic Res 13 (2004) 551-557
    • (2004) Transgenic Res , vol.13 , pp. 551-557
    • Morita, T.1    Yoshizaki, G.2    Kobayashi, M.3    Watabe, S.4    Takeuchi, T.5
  • 26
    • 62749154915 scopus 로고    scopus 로고
    • Immune response and inhibition of bacterial growth by electrotransfer of plasmid DNA containing the antimicrobial peptide, epinecidin-1, into zebrafish muscle
    • Lin S.B., Fan T.W., Wu J.L., Hui C.F., and Chen J.Y. Immune response and inhibition of bacterial growth by electrotransfer of plasmid DNA containing the antimicrobial peptide, epinecidin-1, into zebrafish muscle. Fish Shellfish Immunol 26 (2009) 451-458
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 451-458
    • Lin, S.B.1    Fan, T.W.2    Wu, J.L.3    Hui, C.F.4    Chen, J.Y.5
  • 27
    • 33751004432 scopus 로고    scopus 로고
    • Myogenic regulatory factors Myf5 and Myod function distinctly during craniofacial myogenesis of zebrafish
    • Lin C.Y., Yung R.F., Lee H.C., Chen W.T., Chen Y.H., and Tsai H.J. Myogenic regulatory factors Myf5 and Myod function distinctly during craniofacial myogenesis of zebrafish. Dev Biol 299 (2006) 594-608
    • (2006) Dev Biol , vol.299 , pp. 594-608
    • Lin, C.Y.1    Yung, R.F.2    Lee, H.C.3    Chen, W.T.4    Chen, Y.H.5    Tsai, H.J.6
  • 28
    • 0035082481 scopus 로고    scopus 로고
    • Enhanced expression and stable transmission of transgenes flanked by inverted terminal repeats from adeno-associated virus in zebrafish
    • Hsiao C.D., Hsieh F.J., and Tsai H.J. Enhanced expression and stable transmission of transgenes flanked by inverted terminal repeats from adeno-associated virus in zebrafish. Dev Dyn 220 (2001) 323-336
    • (2001) Dev Dyn , vol.220 , pp. 323-336
    • Hsiao, C.D.1    Hsieh, F.J.2    Tsai, H.J.3
  • 29
    • 34648843845 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 alpha and 3 beta have distinct functions during cardiogenesis of zebrafish embryo
    • Lee H.C., Tsai J.N., Liao P.Y., Tsai W.Y., Lin K.Y., Chuang C.C., et al. Glycogen synthase kinase 3 alpha and 3 beta have distinct functions during cardiogenesis of zebrafish embryo. BMC Dev Biol 7 (2007) 93-104
    • (2007) BMC Dev Biol , vol.7 , pp. 93-104
    • Lee, H.C.1    Tsai, J.N.2    Liao, P.Y.3    Tsai, W.Y.4    Lin, K.Y.5    Chuang, C.C.6
  • 30
    • 0031842009 scopus 로고    scopus 로고
    • Biodegradation of poly (ethylene adipate) microcapsules in physiological media
    • Atkins T.W. Biodegradation of poly (ethylene adipate) microcapsules in physiological media. Biomaterials 19 (1998) 61-67
    • (1998) Biomaterials , vol.19 , pp. 61-67
    • Atkins, T.W.1
  • 31
    • 60649118336 scopus 로고    scopus 로고
    • Transgenic microalgae as a non-antibiotic bactericide producer to defend against bacterial pathogen infection in the fish digestive tract
    • Li S.S., and Tsai H.J. Transgenic microalgae as a non-antibiotic bactericide producer to defend against bacterial pathogen infection in the fish digestive tract. Fish Shellfish Immunol 26 (2009) 316-325
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 316-325
    • Li, S.S.1    Tsai, H.J.2
  • 32
    • 0345148813 scopus 로고    scopus 로고
    • Origin and development of the zebrafish endoderm
    • Warga R.M., and Nusslein-Volhard C. Origin and development of the zebrafish endoderm. Development 126 (1999) 827-838
    • (1999) Development , vol.126 , pp. 827-838
    • Warga, R.M.1    Nusslein-Volhard, C.2
  • 33
    • 14744268846 scopus 로고    scopus 로고
    • Pathogenesis and inflammatory response to Edwardsiella tarda infection in the zebrafish
    • Pressley M.E., Phelan P.E., Witten P.E., Mellon M.T., and Kim C.H. Pathogenesis and inflammatory response to Edwardsiella tarda infection in the zebrafish. Dev Comp Immunol 29 (2005) 501-513
    • (2005) Dev Comp Immunol , vol.29 , pp. 501-513
    • Pressley, M.E.1    Phelan, P.E.2    Witten, P.E.3    Mellon, M.T.4    Kim, C.H.5
  • 34
    • 33747718706 scopus 로고    scopus 로고
    • Expression of the cationic antimicrobial peptide lactoferricin fused with the anionic peptide in Escherichia coli
    • Kim H.K., Chun D.S., Kim J.S., Yun C.H., Lee J.H., Hong S.K., et al. Expression of the cationic antimicrobial peptide lactoferricin fused with the anionic peptide in Escherichia coli. Appl Microbiol Biotechnol 72 (2006) 330-338
    • (2006) Appl Microbiol Biotechnol , vol.72 , pp. 330-338
    • Kim, H.K.1    Chun, D.S.2    Kim, J.S.3    Yun, C.H.4    Lee, J.H.5    Hong, S.K.6
  • 35
    • 33646118231 scopus 로고    scopus 로고
    • Fusion expression of bovine lactoferricin in Escherichia coli
    • Feng X., Wang J., Shan A., Teng D., Yang Y., Yao Y., et al. Fusion expression of bovine lactoferricin in Escherichia coli. Protein Expr Purif 47 (2006) 110-117
    • (2006) Protein Expr Purif , vol.47 , pp. 110-117
    • Feng, X.1    Wang, J.2    Shan, A.3    Teng, D.4    Yang, Y.5    Yao, Y.6
  • 36
    • 34547237719 scopus 로고    scopus 로고
    • Heterologous expression of bovine lactoferricin in Pichia methanolica
    • Wang H.K., Zhao X.H., and Lu F.P. Heterologous expression of bovine lactoferricin in Pichia methanolica. Biochemistry (Mosc) 72 (2007) 640-643
    • (2007) Biochemistry (Mosc) , vol.72 , pp. 640-643
    • Wang, H.K.1    Zhao, X.H.2    Lu, F.P.3
  • 37
    • 29444441202 scopus 로고    scopus 로고
    • Staphylococcus aureus small colony variants are resistant to the antimicrobial peptide lactoferricin B
    • Samuelsen O., Haukland H.H., Kahl B.C., von Eiff C., Proctor R.A., Ulvatne H., et al. Staphylococcus aureus small colony variants are resistant to the antimicrobial peptide lactoferricin B. J Antimicrob Chemother 56 (2005) 1126-1129
    • (2005) J Antimicrob Chemother , vol.56 , pp. 1126-1129
    • Samuelsen, O.1    Haukland, H.H.2    Kahl, B.C.3    von Eiff, C.4    Proctor, R.A.5    Ulvatne, H.6
  • 38
    • 51249096960 scopus 로고    scopus 로고
    • Zebrafish as a model for infectious disease and immune function
    • Sullivan C., and Kim C.H. Zebrafish as a model for infectious disease and immune function. Fish Shellfish Immunol 25 (2008) 341-350
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 341-350
    • Sullivan, C.1    Kim, C.H.2
  • 39
    • 0032170832 scopus 로고    scopus 로고
    • Expression of a novel piscine growth hormone gene results in growth enhancement in transgenic tilapia (Oreochromis niloticus)
    • Rahman M.A., Mak R., Ayad H., Smith A., and Maclean N. Expression of a novel piscine growth hormone gene results in growth enhancement in transgenic tilapia (Oreochromis niloticus). Transgenic Res 7 (1998) 357-369
    • (1998) Transgenic Res , vol.7 , pp. 357-369
    • Rahman, M.A.1    Mak, R.2    Ayad, H.3    Smith, A.4    Maclean, N.5
  • 40
    • 0342545457 scopus 로고    scopus 로고
    • Growth efficiency in transgenic tilapia (Oreochromis sp.) carrying a single copy of an homologous cDNA growth hormone
    • Martinez R., Juncal J., Zaldivar C., Arenal A., Guillen I., Morera V., et al. Growth efficiency in transgenic tilapia (Oreochromis sp.) carrying a single copy of an homologous cDNA growth hormone. Biochem Biophys Res Commun 267 (2000) 466-472
    • (2000) Biochem Biophys Res Commun , vol.267 , pp. 466-472
    • Martinez, R.1    Juncal, J.2    Zaldivar, C.3    Arenal, A.4    Guillen, I.5    Morera, V.6
  • 41
    • 0034257213 scopus 로고    scopus 로고
    • Growth rate, body composition and feed digestibility/conversion of growth-enhanced transgenic Atlantic salmon (Salmo salar)
    • Cook J.T., McNiven M.A., Richardson G.F., and Sutterlin A.M. Growth rate, body composition and feed digestibility/conversion of growth-enhanced transgenic Atlantic salmon (Salmo salar). Aquaculture 188 (2000) 15-32
    • (2000) Aquaculture , vol.188 , pp. 15-32
    • Cook, J.T.1    McNiven, M.A.2    Richardson, G.F.3    Sutterlin, A.M.4
  • 42
    • 0034845831 scopus 로고    scopus 로고
    • Dramatically accelerated growth and extraordinary gigantism of transgenic mud loach Misgurnus mizolepis
    • Nam Y.K., Noh J.K., Cho Y.S., Cho H.J., Cho K.N., Kim C.G., et al. Dramatically accelerated growth and extraordinary gigantism of transgenic mud loach Misgurnus mizolepis. Transgenic Res 10 (2001) 353-362
    • (2001) Transgenic Res , vol.10 , pp. 353-362
    • Nam, Y.K.1    Noh, J.K.2    Cho, Y.S.3    Cho, H.J.4    Cho, K.N.5    Kim, C.G.6
  • 43
    • 15044352320 scopus 로고    scopus 로고
    • Expression of endogenous and exogenous growth hormone (GH) messenger (m) RNA in a GH-transgenic tilapia (Oreochromis niloticus)
    • Caelers A., Maclean N., Hwang G.L., Eppler E., and Reinecke M. Expression of endogenous and exogenous growth hormone (GH) messenger (m) RNA in a GH-transgenic tilapia (Oreochromis niloticus). Transgenic Res 14 (2005) 95-104
    • (2005) Transgenic Res , vol.14 , pp. 95-104
    • Caelers, A.1    Maclean, N.2    Hwang, G.L.3    Eppler, E.4    Reinecke, M.5
  • 45
    • 0036069316 scopus 로고    scopus 로고
    • Enhanced bacterial disease resistance of transgenic channel catfish Ictalurus punctatus possessing cecropin genes
    • Dunham R.A., Warr G.W., Nichols A., Duncan P.L., Argue B., Middleton D., et al. Enhanced bacterial disease resistance of transgenic channel catfish Ictalurus punctatus possessing cecropin genes. Mar Biotechnol 4 (2002) 338-344
    • (2002) Mar Biotechnol , vol.4 , pp. 338-344
    • Dunham, R.A.1    Warr, G.W.2    Nichols, A.3    Duncan, P.L.4    Argue, B.5    Middleton, D.6
  • 46
    • 33745180199 scopus 로고    scopus 로고
    • Transgenic zebrafish expressing chicken lysozyme show resistance against bacterial diseases
    • Yazawa R., Hirono I., and Aoki T. Transgenic zebrafish expressing chicken lysozyme show resistance against bacterial diseases. Transgenic Res 15 (2006) 385-391
    • (2006) Transgenic Res , vol.15 , pp. 385-391
    • Yazawa, R.1    Hirono, I.2    Aoki, T.3
  • 47
    • 0029257418 scopus 로고
    • Expression of the antifreeze protein gene in transgenic goldfish (Carassius auratus) and its implication in cold adaptation
    • Wang R., Zhang P., Gong Z., and Hew C.L. Expression of the antifreeze protein gene in transgenic goldfish (Carassius auratus) and its implication in cold adaptation. Mol Mar Biol Biotechnol 4 (1995) 20-26
    • (1995) Mol Mar Biol Biotechnol , vol.4 , pp. 20-26
    • Wang, R.1    Zhang, P.2    Gong, Z.3    Hew, C.L.4
  • 48
    • 0033730915 scopus 로고    scopus 로고
    • Detection of mutations in transgenic fish carrying a bacteriophage lambda cll transgene target
    • Winn R.N., Norris M.B., Brayer K.J., Torres C., and Muller S.L. Detection of mutations in transgenic fish carrying a bacteriophage lambda cll transgene target. Proc Natl Acad Sci U S A 97 (2000) 12655-12660
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 12655-12660
    • Winn, R.N.1    Norris, M.B.2    Brayer, K.J.3    Torres, C.4    Muller, S.L.5
  • 49
    • 0012975676 scopus 로고    scopus 로고
    • Bacteriophage lambda and plasmid pUR288 transgenic fish models for detecting in vivo mutations
    • Winn R.N., Norris M., Muller S., Torres C., and Brayer K. Bacteriophage lambda and plasmid pUR288 transgenic fish models for detecting in vivo mutations. Mar Biotechnol 3 (2001) S185-S195
    • (2001) Mar Biotechnol , vol.3
    • Winn, R.N.1    Norris, M.2    Muller, S.3    Torres, C.4    Brayer, K.5
  • 50
    • 0036079373 scopus 로고    scopus 로고
    • Production of transgenic medaka with increased resistance to bacterial pathogens
    • Sarmasik A., Warr G., and Chen T.T. Production of transgenic medaka with increased resistance to bacterial pathogens. Mar Biotechnol 4 (2002) 310-322
    • (2002) Mar Biotechnol , vol.4 , pp. 310-322
    • Sarmasik, A.1    Warr, G.2    Chen, T.T.3


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