메뉴 건너뛰기




Volumn 33, Issue 4, 2012, Pages 801-812

Molecular characterization and immunological response analysis of a novel transferrin-like, pacifastin heavy chain protein in giant freshwater prawn, Macrobrachium rosenbergii (De Man, 1879)

Author keywords

Aeromonas hydrophila; Expression analysis; Giant freshwater prawn; Pacifastin heavy chain; Glucan

Indexed keywords

AEROMONAS HYDROPHILA; ANIMALIA; BACTERIA (MICROORGANISMS); CRUSTACEA; DECAPODA (CRUSTACEA); MACROBRACHIUM ROSENBERGII;

EID: 84866759630     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2012.07.007     Document Type: Article
Times cited : (20)

References (52)
  • 1
    • 84889341782 scopus 로고    scopus 로고
    • History and global status of freshwater prawn farming
    • A John Wiley&Sons, Ltd, Publication, M.B. New, W.C. Valenti, J.H. Tidwell, L.R. D'Abramo, M.N. Kutty (Eds.)
    • New M.B. History and global status of freshwater prawn farming. Freshwater prawns biology and farming 2010, 1-9. A John Wiley&Sons, Ltd, Publication. M.B. New, W.C. Valenti, J.H. Tidwell, L.R. D'Abramo, M.N. Kutty (Eds.).
    • (2010) Freshwater prawns biology and farming , pp. 1-9
    • New, M.B.1
  • 2
    • 78650781699 scopus 로고    scopus 로고
    • Viral diseases of the giant freshwater prawn Macrobrachium rosenbergii: a review
    • Bonami J.R., Sri Widada J. Viral diseases of the giant freshwater prawn Macrobrachium rosenbergii: a review. J Invertebr Pathol 2011, 106(1):131-142.
    • (2011) J Invertebr Pathol , vol.106 , Issue.1 , pp. 131-142
    • Bonami, J.R.1    Sri Widada, J.2
  • 3
    • 0034521257 scopus 로고    scopus 로고
    • Responses of giant freshwater prawn (Macrobrachium rosenbergii) to challenge by two strains of Aeromonas spp.
    • Sung H.H., Hwang S.F., Tasi F.M. Responses of giant freshwater prawn (Macrobrachium rosenbergii) to challenge by two strains of Aeromonas spp. J Invertebr Pathol 2000, 76(4):278-284.
    • (2000) J Invertebr Pathol , vol.76 , Issue.4 , pp. 278-284
    • Sung, H.H.1    Hwang, S.F.2    Tasi, F.M.3
  • 4
    • 0035829315 scopus 로고    scopus 로고
    • The susceptibility of the giant freshwater prawn Macrobrachium rosenbergii to Lactococcus garvieae and its resistance under copper sulfate stress
    • Chen W., Wang C.H. The susceptibility of the giant freshwater prawn Macrobrachium rosenbergii to Lactococcus garvieae and its resistance under copper sulfate stress. Dis Aquat Org 2001, 47(2):137-144.
    • (2001) Dis Aquat Org , vol.47 , Issue.2 , pp. 137-144
    • Chen, W.1    Wang, C.H.2
  • 5
    • 0036007843 scopus 로고    scopus 로고
    • The virulence of Enterococcus to freshwater prawn Macrobrachium rosenbergii and its immune resistance under ammonia stress
    • Cheng W., Chen J.C. The virulence of Enterococcus to freshwater prawn Macrobrachium rosenbergii and its immune resistance under ammonia stress. Fish Shellfish Immunol 2002, 12(2):97-109.
    • (2002) Fish Shellfish Immunol , vol.12 , Issue.2 , pp. 97-109
    • Cheng, W.1    Chen, J.C.2
  • 6
    • 0042267419 scopus 로고    scopus 로고
    • Metschnikowia bicuspidata and Enterococcus faecium co-infection in the giant freshwater prawn Macrobrachium rosenbergii
    • Chen S.C., Chen T.H., Wang P.C., Chen Y.C., Huang J.P., Lin Y.D., et al. Metschnikowia bicuspidata and Enterococcus faecium co-infection in the giant freshwater prawn Macrobrachium rosenbergii. Dis Aquat Organ 2003, 55(2):161-167.
    • (2003) Dis Aquat Organ , vol.55 , Issue.2 , pp. 161-167
    • Chen, S.C.1    Chen, T.H.2    Wang, P.C.3    Chen, Y.C.4    Huang, J.P.5    Lin, Y.D.6
  • 7
    • 34248230248 scopus 로고    scopus 로고
    • In vivo humoral and cellular reactions, and fate of injected bacteria Aeromonas hydrophila in freshwater prawn Macrobrachium rosenbergii
    • Sahoo P.K., Pillai B.R., Mohanty J., Kumari J., Mohanty S., Mishra B.K. In vivo humoral and cellular reactions, and fate of injected bacteria Aeromonas hydrophila in freshwater prawn Macrobrachium rosenbergii. Fish Shellfish Immunol 2007, 23(2):327-340.
    • (2007) Fish Shellfish Immunol , vol.23 , Issue.2 , pp. 327-340
    • Sahoo, P.K.1    Pillai, B.R.2    Mohanty, J.3    Kumari, J.4    Mohanty, S.5    Mishra, B.K.6
  • 8
    • 77955778916 scopus 로고    scopus 로고
    • Quorum quenching bacteria protect Macrobrachium rosenbergii larvae from Vibrio harveyi infection
    • Nhan D.T., Cam D.T., Wille M., Defoirdt T., Bossier P., Sorgeloos P. Quorum quenching bacteria protect Macrobrachium rosenbergii larvae from Vibrio harveyi infection. J Appl Microbiol 2010, 109(3):1007-1016.
    • (2010) J Appl Microbiol , vol.109 , Issue.3 , pp. 1007-1016
    • Nhan, D.T.1    Cam, D.T.2    Wille, M.3    Defoirdt, T.4    Bossier, P.5    Sorgeloos, P.6
  • 9
    • 38849143950 scopus 로고    scopus 로고
    • Invertebrate immune systems specific, quasi-specific, or non-specific?
    • Rowley A.F., Powell A. Invertebrate immune systems specific, quasi-specific, or non-specific?. J Immunol 2010, 179:7209-7214.
    • (2010) J Immunol , vol.179 , pp. 7209-7214
    • Rowley, A.F.1    Powell, A.2
  • 10
    • 33646363763 scopus 로고    scopus 로고
    • Iron-withholding strategy in innate immunity
    • Ong S.T., Ho J.Z.S., Ho B., Ding J.L. Iron-withholding strategy in innate immunity. J Immunol 2006, 211:295-314.
    • (2006) J Immunol , vol.211 , pp. 295-314
    • Ong, S.T.1    Ho, J.Z.S.2    Ho, B.3    Ding, J.L.4
  • 11
    • 84857355874 scopus 로고    scopus 로고
    • Molecular evolution of the transferrin family and associated receptors
    • Lambert L.A. Molecular evolution of the transferrin family and associated receptors. Biochim Biophys Acta 2012, 1820(3):244-255.
    • (2012) Biochim Biophys Acta , vol.1820 , Issue.3 , pp. 244-255
    • Lambert, L.A.1
  • 12
    • 0005449523 scopus 로고
    • Mutagenicity of oxygen free radicals
    • Moody C.S., Hassan H.M. Mutagenicity of oxygen free radicals. Proc Natl Acad Sci U S A 1982, 79(9):2855-2859.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , Issue.9 , pp. 2855-2859
    • Moody, C.S.1    Hassan, H.M.2
  • 13
    • 0021964203 scopus 로고
    • Prooxidant states and tumor promotion
    • Cerutti P.A. Prooxidant states and tumor promotion. Science 1985, 227(4685):375-381.
    • (1985) Science , vol.227 , Issue.4685 , pp. 375-381
    • Cerutti, P.A.1
  • 15
    • 0028216288 scopus 로고
    • Molecular cloning of bullfrog saxiphilin: a unique relative of the transferrin family that binds saxitoxin
    • Morabito M.A., Moczydlowski E. Molecular cloning of bullfrog saxiphilin: a unique relative of the transferrin family that binds saxitoxin. Proc Natl Acad Sci U S A 1994, 91:2478-2482.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 2478-2482
    • Morabito, M.A.1    Moczydlowski, E.2
  • 16
    • 0034686047 scopus 로고    scopus 로고
    • Saxiphilin, a saxitoxin-binding protein with two thyroglobulin type 1 domains, is an inhibitor of papain-like cysteine proteinases
    • Lenarcic B., Krishnan G., Borukhovich R., Ruck B., Turk V., Moczydlowski E. Saxiphilin, a saxitoxin-binding protein with two thyroglobulin type 1 domains, is an inhibitor of papain-like cysteine proteinases. J Biol Chem 2000, 275:15572-15577.
    • (2000) J Biol Chem , vol.275 , pp. 15572-15577
    • Lenarcic, B.1    Krishnan, G.2    Borukhovich, R.3    Ruck, B.4    Turk, V.5    Moczydlowski, E.6
  • 17
    • 0033865870 scopus 로고    scopus 로고
    • Molecular cloning and expression of an otolith matrix protein cDNA from the rainbow trout, Oncorhynchus mykiss
    • Murayama E., Okuno A., Ohira T., Takagi Y., Nagasawa H. Molecular cloning and expression of an otolith matrix protein cDNA from the rainbow trout, Oncorhynchus mykiss. Comp Biochem Physiol B Biochem Mol Biol 2000, 126(4):511-520.
    • (2000) Comp Biochem Physiol B Biochem Mol Biol , vol.126 , Issue.4 , pp. 511-520
    • Murayama, E.1    Okuno, A.2    Ohira, T.3    Takagi, Y.4    Nagasawa, H.5
  • 19
    • 0025695557 scopus 로고
    • Isolation and molecular cloning of transferrin from the tobacco hornworm, Manduca sexta; sequence similarity to the vertebrate transferrins
    • Bartfeld N.S., Law J.H. Isolation and molecular cloning of transferrin from the tobacco hornworm, Manduca sexta; sequence similarity to the vertebrate transferrins. J Biol Chem 1990, 265:21684-21691.
    • (1990) J Biol Chem , vol.265 , pp. 21684-21691
    • Bartfeld, N.S.1    Law, J.H.2
  • 20
    • 0028902673 scopus 로고
    • Molecular characterization of an insect transferrin and its selective incorporation into eggs during oogenesis
    • Kurama T., Kurata S., Natori S. Molecular characterization of an insect transferrin and its selective incorporation into eggs during oogenesis. Eur J Biochem 1995, 228:229-235.
    • (1995) Eur J Biochem , vol.228 , pp. 229-235
    • Kurama, T.1    Kurata, S.2    Natori, S.3
  • 21
    • 0030817280 scopus 로고    scopus 로고
    • Mosquito transferrin, an acute-phase protein that is up-regulated upon infection
    • Yoshiga T., Hernandez V.P., Fallon A.M., Law J.H. Mosquito transferrin, an acute-phase protein that is up-regulated upon infection. Proc Natl Acad Sci U S A 1997, 94:12337-12342.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12337-12342
    • Yoshiga, T.1    Hernandez, V.P.2    Fallon, A.M.3    Law, J.H.4
  • 22
    • 0033388612 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a cDNA encoding a transferrin homologue from Bombyx mori
    • Yun E.Y., Kang S.W., Hwang J.S., Goo T.W., Kim S.H., Jin B.R., et al. Molecular cloning and characterization of a cDNA encoding a transferrin homologue from Bombyx mori. J Biol Chem 1999, 380:1455-1459.
    • (1999) J Biol Chem , vol.380 , pp. 1455-1459
    • Yun, E.Y.1    Kang, S.W.2    Hwang, J.S.3    Goo, T.W.4    Kim, S.H.5    Jin, B.R.6
  • 23
    • 0034185884 scopus 로고    scopus 로고
    • A juvenile hormone-repressible transferrin-like protein from the bean bug, Riptortus clavatus: cDNA sequence analysis and protein identification during diapause and vitellogenesis
    • Hirai M., Watanabe D., Chinzei Y. A juvenile hormone-repressible transferrin-like protein from the bean bug, Riptortus clavatus: cDNA sequence analysis and protein identification during diapause and vitellogenesis. Arch Insect Biochem Physiol 2000, 44:17-26.
    • (2000) Arch Insect Biochem Physiol , vol.44 , pp. 17-26
    • Hirai, M.1    Watanabe, D.2    Chinzei, Y.3
  • 24
    • 0027453014 scopus 로고    scopus 로고
    • Transferrin in a cockroach: molecular cloning, characterization, and suppression by juvenile hormone
    • Jamroz R.C., Gasdaska J.R., Bradfield J.Y., Law J.H. Transferrin in a cockroach: molecular cloning, characterization, and suppression by juvenile hormone. Proc Natl Acad Sci U S A 2003, 90:1320-1324.
    • (2003) Proc Natl Acad Sci U S A , vol.90 , pp. 1320-1324
    • Jamroz, R.C.1    Gasdaska, J.R.2    Bradfield, J.Y.3    Law, J.H.4
  • 25
    • 0037321923 scopus 로고    scopus 로고
    • Isolation and characterization of a termite transferrin gene up-regulated on infection
    • Thompson G.J., Crozier Y.C., Crozier R.H. Isolation and characterization of a termite transferrin gene up-regulated on infection. J Insect Mol Biol 2003, 12:1-7.
    • (2003) J Insect Mol Biol , vol.12 , pp. 1-7
    • Thompson, G.J.1    Crozier, Y.C.2    Crozier, R.H.3
  • 26
    • 0036570143 scopus 로고    scopus 로고
    • The major yolk protein in sea urchins is a transferrin-like, iron binding protein
    • Brooks J.M., Wessel G.M. The major yolk protein in sea urchins is a transferrin-like, iron binding protein. J Dev Biol 2002, 245:1-12.
    • (2002) J Dev Biol , vol.245 , pp. 1-12
    • Brooks, J.M.1    Wessel, G.M.2
  • 27
    • 1242318691 scopus 로고    scopus 로고
    • A transferrin-like protein that does not bind iron is induced by iron deficiency in the alga Dunaliella salina
    • Schwarz M., Sal-Man N., Zamir A., Pick U. A transferrin-like protein that does not bind iron is induced by iron deficiency in the alga Dunaliella salina. Biochim Biophys Acta 2003, 1649:190-200.
    • (2003) Biochim Biophys Acta , vol.1649 , pp. 190-200
    • Schwarz, M.1    Sal-Man, N.2    Zamir, A.3    Pick, U.4
  • 28
    • 0031019989 scopus 로고    scopus 로고
    • A structurally novel transferrin-like protein accumulates in the plasma membrane of the unicellular green alga Dunaliella salina grown in high salinities
    • Fisher M., Gokhman I., Pick U., Zamir A. A structurally novel transferrin-like protein accumulates in the plasma membrane of the unicellular green alga Dunaliella salina grown in high salinities. J Biol Chem 1997, 272:1565-1570.
    • (1997) J Biol Chem , vol.272 , pp. 1565-1570
    • Fisher, M.1    Gokhman, I.2    Pick, U.3    Zamir, A.4
  • 29
    • 0032504198 scopus 로고    scopus 로고
    • Iron uptake by the halotolerant alga Dunaliella is mediated by a plasma membrane transferrin
    • Fisher M., Zamir A., Pick U. Iron uptake by the halotolerant alga Dunaliella is mediated by a plasma membrane transferrin. J Biol Chem 1998, 273:17553-17558.
    • (1998) J Biol Chem , vol.273 , pp. 17553-17558
    • Fisher, M.1    Zamir, A.2    Pick, U.3
  • 30
    • 34247884339 scopus 로고    scopus 로고
    • A multicopper ferroxidase involved in iron binding to transferrins in Dunaliella salina plasma membranes
    • Paz Y., Katz U., Pick A. A multicopper ferroxidase involved in iron binding to transferrins in Dunaliella salina plasma membranes. J Biol Chem 2007, 282:8658-8666.
    • (2007) J Biol Chem , vol.282 , pp. 8658-8666
    • Paz, Y.1    Katz, U.2    Pick, A.3
  • 31
    • 0030917010 scopus 로고    scopus 로고
    • Pacifastin, a novel 155-kDa heterodimeric proteinase inhibitor containing a unique transferrin chain
    • Liang Z., Sottrup-Jensen L., Aspan A., Hall M., Söderhäll K. Pacifastin, a novel 155-kDa heterodimeric proteinase inhibitor containing a unique transferrin chain. Proc Natl Acad Sci U S A 1997, 94:6682-6687.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6682-6687
    • Liang, Z.1    Sottrup-Jensen, L.2    Aspan, A.3    Hall, M.4    Söderhäll, K.5
  • 33
    • 0027968068 scopus 로고
    • "Clustal W": improving the sensitivity of progressive multiple sequence alignment and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. "Clustal W": improving the sensitivity of progressive multiple sequence alignment and weight matrix choice. Nucleic Acids Res 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 34
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2[-Delta Delta C(T)] method
    • Livak K.J., Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2[-Delta Delta C(T)] method. Methods 2001, 25:402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 35
    • 0020629655 scopus 로고
    • The primary of human serum transferrin. The structure of seven cyanogens bromide fragments and the assembly of the complete structure
    • MacGillivray R.T.A., Mendez E., Shewale J., Sinha S.K., Lineback-Zins J., Brew K. The primary of human serum transferrin. The structure of seven cyanogens bromide fragments and the assembly of the complete structure. J Biol Chem 1983, 258:3543-3553.
    • (1983) J Biol Chem , vol.258 , pp. 3543-3553
    • MacGillivray, R.T.A.1    Mendez, E.2    Shewale, J.3    Sinha, S.K.4    Lineback-Zins, J.5    Brew, K.6
  • 37
    • 0035138073 scopus 로고    scopus 로고
    • Isolation, characterization and cDNA cloning of a one-lobed transferrin from the ascidian Halocynthia roretzi
    • Abe Y., Nagata R., Hasunuma Y., Yokosawa H. Isolation, characterization and cDNA cloning of a one-lobed transferrin from the ascidian Halocynthia roretzi. Comp Biochem Physiol B Biochem Mol Biol 2001, 128(1):73-79.
    • (2001) Comp Biochem Physiol B Biochem Mol Biol , vol.128 , Issue.1 , pp. 73-79
    • Abe, Y.1    Nagata, R.2    Hasunuma, Y.3    Yokosawa, H.4
  • 39
    • 0025806527 scopus 로고
    • The distribution of cerebral expression of the transferrin gene is species specific
    • Tu G.-F., Acen M.G., Aldred A.R., Southwell B.R., Schreiber G. The distribution of cerebral expression of the transferrin gene is species specific. J Biol Chem 1991, 266:148-153.
    • (1991) J Biol Chem , vol.266 , pp. 148-153
    • Tu, G.-F.1    Acen, M.G.2    Aldred, A.R.3    Southwell, B.R.4    Schreiber, G.5
  • 40
    • 0027639930 scopus 로고
    • Cloning and characterization of Atlantic salmon (Salmo salar) serum transferrin cDNA
    • Kvingedal A.M., Rorvik K.A., Alestrom P. Cloning and characterization of Atlantic salmon (Salmo salar) serum transferrin cDNA. Mol Mar Biol Biotechnol 1993, 2:233-238.
    • (1993) Mol Mar Biol Biotechnol , vol.2 , pp. 233-238
    • Kvingedal, A.M.1    Rorvik, K.A.2    Alestrom, P.3
  • 41
    • 0029881250 scopus 로고    scopus 로고
    • Nucleotide sequence of transferrin cDNAs and tissue-specific expression of the transferrin gene in Atlantic cod (Gadus morhua)
    • Denovan-Wright E.M., Bruce Ramsey N., McCormick C.J., Lazier C.B., Wright J.M. Nucleotide sequence of transferrin cDNAs and tissue-specific expression of the transferrin gene in Atlantic cod (Gadus morhua). Comp Biochem Physiol 1996, 113(B):269-273.
    • (1996) Comp Biochem Physiol , vol.113 , Issue.B , pp. 269-273
    • Denovan-Wright, E.M.1    Bruce Ramsey, N.2    McCormick, C.J.3    Lazier, C.B.4    Wright, J.M.5
  • 42
    • 35649020193 scopus 로고    scopus 로고
    • Polymorphism of transferrin of carp seminal plasma: relationship to blood transferrin and sperm motility characteristics
    • Wojtczak M., Dietrich G.J., Imazaraw I., Jurecka P., Slowinska M., Ciereszko A. Polymorphism of transferrin of carp seminal plasma: relationship to blood transferrin and sperm motility characteristics. Comp Biochem Physiol 2007, 148(B):426-431.
    • (2007) Comp Biochem Physiol , vol.148 , Issue.B , pp. 426-431
    • Wojtczak, M.1    Dietrich, G.J.2    Imazaraw, I.3    Jurecka, P.4    Slowinska, M.5    Ciereszko, A.6
  • 43
    • 73249124822 scopus 로고    scopus 로고
    • Structure and expression of transferrin gene of channel catfish, Ictalurus puntatus
    • Liu H., Takano T., Abernathy J., Wang S., Sha Z., Jiang Y., et al. Structure and expression of transferrin gene of channel catfish, Ictalurus puntatus. Fish Shellfish Immunol 2010, 28:159-166.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 159-166
    • Liu, H.1    Takano, T.2    Abernathy, J.3    Wang, S.4    Sha, Z.5    Jiang, Y.6
  • 44
    • 1942429543 scopus 로고    scopus 로고
    • Transcriptional profiling reveals multifunctional roles for transferrin in the honey bee, Apis mellifera
    • Kucharski R., Maleszka R. Transcriptional profiling reveals multifunctional roles for transferrin in the honey bee, Apis mellifera. J Insect Sci 2003, 3:27.
    • (2003) J Insect Sci , vol.3 , pp. 27
    • Kucharski, R.1    Maleszka, R.2
  • 45
    • 81455132793 scopus 로고    scopus 로고
    • Biochemical and ultrastructural changes in the hepatopancreas of Bellamya aeruginosa (Gastropoda) fed with toxic Cyanobacteria
    • Zhu J., Lu K., Zhang C., Liang J., Hu Z. Biochemical and ultrastructural changes in the hepatopancreas of Bellamya aeruginosa (Gastropoda) fed with toxic Cyanobacteria. ScientificWorldJournal 2011, 11:2091-2105.
    • (2011) ScientificWorldJournal , vol.11 , pp. 2091-2105
    • Zhu, J.1    Lu, K.2    Zhang, C.3    Liang, J.4    Hu, Z.5
  • 46
    • 56949101447 scopus 로고    scopus 로고
    • Molecular characterization of iron binding proteins, transferrin and ferritin heavy chain subunit, from the bumblebee Bombus ignites
    • Wang D., Kim B.Y., Lee K.S., Yoon H.J., Cui Z., Lu W., et al. Molecular characterization of iron binding proteins, transferrin and ferritin heavy chain subunit, from the bumblebee Bombus ignites. J Comp Biochem Physiol B 2009, 152:20-27.
    • (2009) J Comp Biochem Physiol B , vol.152 , pp. 20-27
    • Wang, D.1    Kim, B.Y.2    Lee, K.S.3    Yoon, H.J.4    Cui, Z.5    Lu, W.6
  • 47
    • 0033106306 scopus 로고    scopus 로고
    • Drosophila melanogaster transferrin. Cloning, deduced protein sequence, expression during the life cycle, gene localization and up-regulation on bacterial infection
    • Yoshiga T., Georgieva T., Dunkov B.C., Harizanova N., Ralchev K., Law J.H. Drosophila melanogaster transferrin. Cloning, deduced protein sequence, expression during the life cycle, gene localization and up-regulation on bacterial infection. Eur J Biochem 1997, 60:414-420.
    • (1997) Eur J Biochem , vol.60 , pp. 414-420
    • Yoshiga, T.1    Georgieva, T.2    Dunkov, B.C.3    Harizanova, N.4    Ralchev, K.5    Law, J.H.6
  • 48
    • 24944515848 scopus 로고    scopus 로고
    • Solenopsis invicta transferrin: cDNA cloning, gene architecture, and up-regulation in response to Beauveria bassiana infection
    • Valles S.M., Pereira R.M. Solenopsis invicta transferrin: cDNA cloning, gene architecture, and up-regulation in response to Beauveria bassiana infection. Gene 2005, 358:60-66.
    • (2005) Gene , vol.358 , pp. 60-66
    • Valles, S.M.1    Pereira, R.M.2
  • 49
    • 33748312147 scopus 로고    scopus 로고
    • Transferrin inhibits stress-induced apoptosis in a beetle
    • Lee K.S., Kim B.Y., Kim H.J., Seo S.J., Yoon H.J., Choi Y.S., et al. Transferrin inhibits stress-induced apoptosis in a beetle. J Biol Med 2006, 41:1151-1161.
    • (2006) J Biol Med , vol.41 , pp. 1151-1161
    • Lee, K.S.1    Kim, B.Y.2    Kim, H.J.3    Seo, S.J.4    Yoon, H.J.5    Choi, Y.S.6
  • 50
    • 43049163230 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a transferrin cDNA from the white-spotted flower chafer, Protaetia brevitarsis
    • Kim B.Y., Lee K.S., Choo Y.M., Kim I., Hwang J.S., Sohn H.D., et al. Molecular cloning and characterization of a transferrin cDNA from the white-spotted flower chafer, Protaetia brevitarsis. DNA Seq 2008, 19:146-150.
    • (2008) DNA Seq , vol.19 , pp. 146-150
    • Kim, B.Y.1    Lee, K.S.2    Choo, Y.M.3    Kim, I.4    Hwang, J.S.5    Sohn, H.D.6
  • 52
    • 0031050034 scopus 로고    scopus 로고
    • Innate immunity: impact on the adaptive immune response
    • Medzhitov R., Janeway C.A. Innate immunity: impact on the adaptive immune response. Curr Opin Immunol 1997, 9:4-9.
    • (1997) Curr Opin Immunol , vol.9 , pp. 4-9
    • Medzhitov, R.1    Janeway, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.