메뉴 건너뛰기




Volumn 31, Issue 6, 2011, Pages 925-937

Genomic characterization, phylogeny and gene regulation of g-type lysozyme in sole (Solea senegalensis)

Author keywords

Dexamethasone; G type lysozyme; PAMPs; Retinoic acid; Thyroid hormones

Indexed keywords

BACTERIA (MICROORGANISMS); PERCOMORPHA; SOLEA SENEGALENSIS;

EID: 81255176990     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2011.08.010     Document Type: Article
Times cited : (33)

References (86)
  • 1
    • 77951759131 scopus 로고    scopus 로고
    • Lysozymes in the animal kingdom
    • Callewaert L., Michiels C.W. Lysozymes in the animal kingdom. J Biosci 2010, 35:127-160.
    • (2010) J Biosci , vol.35 , pp. 127-160
    • Callewaert, L.1    Michiels, C.W.2
  • 2
    • 0020629394 scopus 로고
    • Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?
    • Grütter M.G., Weaver L.H., Matthews B.W. Goose lysozyme structure: an evolutionary link between hen and bacteriophage lysozymes?. Nature 1983, 303:828-831.
    • (1983) Nature , vol.303 , pp. 828-831
    • Grütter, M.G.1    Weaver, L.H.2    Matthews, B.W.3
  • 3
    • 0021713792 scopus 로고
    • Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution
    • Weaver L.H., Grutter M.G., Remington S.J., Gray T.M., Isaacs N.W., Matthews B.W. Comparison of goose-type, chicken-type, and phage-type lysozymes illustrates the changes that occur in both amino acid sequence and three-dimensional structure during evolution. J Mol Evol 1984, 21:97-111.
    • (1984) J Mol Evol , vol.21 , pp. 97-111
    • Weaver, L.H.1    Grutter, M.G.2    Remington, S.J.3    Gray, T.M.4    Isaacs, N.W.5    Matthews, B.W.6
  • 4
    • 0021315289 scopus 로고
    • Comparative study on the secondary structure of lysozymes from different sources
    • Gavilanes J.G., Menendez-Arias L., Rodriguez R. Comparative study on the secondary structure of lysozymes from different sources. Comp Biochem Physiol B 1984, 77:83-88.
    • (1984) Comp Biochem Physiol B , vol.77 , pp. 83-88
    • Gavilanes, J.G.1    Menendez-Arias, L.2    Rodriguez, R.3
  • 5
    • 0035973859 scopus 로고    scopus 로고
    • Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein
    • Hikima J., Minagawa S., Hirono I., Aoki T. Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein. Biochim Biophys Acta 2001, 1520:35-44.
    • (2001) Biochim Biophys Acta , vol.1520 , pp. 35-44
    • Hikima, J.1    Minagawa, S.2    Hirono, I.3    Aoki, T.4
  • 6
    • 0035019128 scopus 로고    scopus 로고
    • Expression of Japanese flounder c-type lysozyme cDNA in insect cells
    • Minagawa S., Hikima J., Hirono I., Aoki T., Mori H. Expression of Japanese flounder c-type lysozyme cDNA in insect cells. Dev Comp Immunol 2001, 25:439-445.
    • (2001) Dev Comp Immunol , vol.25 , pp. 439-445
    • Minagawa, S.1    Hikima, J.2    Hirono, I.3    Aoki, T.4    Mori, H.5
  • 7
    • 0028134275 scopus 로고
    • In vitro evidence for the antibacterial role of lysozyme in salmonid eggs
    • Yousif A.N., Albright L.J., Evelyn T.P.T. In vitro evidence for the antibacterial role of lysozyme in salmonid eggs. Dis Aquat Organ 1994, 19:15-19.
    • (1994) Dis Aquat Organ , vol.19 , pp. 15-19
    • Yousif, A.N.1    Albright, L.J.2    Evelyn, T.P.T.3
  • 8
    • 35248885592 scopus 로고    scopus 로고
    • Molecular characterization of goose-type lysozyme homologue of large yellow croaker and its involvement in immune response induced by trivalent bacterial vaccine as an acute-phase protein
    • Zheng W., Tian C., Chen X. Molecular characterization of goose-type lysozyme homologue of large yellow croaker and its involvement in immune response induced by trivalent bacterial vaccine as an acute-phase protein. Immunol Lett 2007, 113:107-116.
    • (2007) Immunol Lett , vol.113 , pp. 107-116
    • Zheng, W.1    Tian, C.2    Chen, X.3
  • 9
    • 59349113566 scopus 로고    scopus 로고
    • Molecular characterisation of a goose-type lysozyme gene in Atlantic cod (Gadus morhua L.)
    • Larsen A.N., Solstad T., Svineng G., Seppola M., Jorgensen T.O. Molecular characterisation of a goose-type lysozyme gene in Atlantic cod (Gadus morhua L.). Fish Shellfish Immunol 2009, 26:122-132.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 122-132
    • Larsen, A.N.1    Solstad, T.2    Svineng, G.3    Seppola, M.4    Jorgensen, T.O.5
  • 10
    • 77953416821 scopus 로고    scopus 로고
    • Identification and expression analysis of the g-type and c-type lysozymes in grass carp Ctenopharyngodon idellus
    • Ye X., Zhang L., Tian Y., Tan A., Bai J., Li S. Identification and expression analysis of the g-type and c-type lysozymes in grass carp Ctenopharyngodon idellus. Dev Comp Immunol 2010, 34:501-509.
    • (2010) Dev Comp Immunol , vol.34 , pp. 501-509
    • Ye, X.1    Zhang, L.2    Tian, Y.3    Tan, A.4    Bai, J.5    Li, S.6
  • 11
    • 0043074437 scopus 로고    scopus 로고
    • Molecular cloning of G type lysozyme cDNA in common carp (Cyprinus carpio L.)
    • Savan R., Aman A., Sakai M. Molecular cloning of G type lysozyme cDNA in common carp (Cyprinus carpio L.). Fish Shellfish Immunol 2003, 15:263-268.
    • (2003) Fish Shellfish Immunol , vol.15 , pp. 263-268
    • Savan, R.1    Aman, A.2    Sakai, M.3
  • 12
    • 32344443468 scopus 로고    scopus 로고
    • Gene structure of goose-type lysozyme in the mandarin fish Siniperca chuatsi with analysis on the lytic activity of its recombinant in Escherichia coli
    • Sun B.J., Wang G.L., Xie H.X., Gao Q., Nie P. Gene structure of goose-type lysozyme in the mandarin fish Siniperca chuatsi with analysis on the lytic activity of its recombinant in Escherichia coli. Aquaculture 2006, 252:106-113.
    • (2006) Aquaculture , vol.252 , pp. 106-113
    • Sun, B.J.1    Wang, G.L.2    Xie, H.X.3    Gao, Q.4    Nie, P.5
  • 13
    • 0042267811 scopus 로고    scopus 로고
    • Molecular cloning, expression of orange-spotted grouper goose-type lysozyme cDNA, and lytic activity of its recombinant protein
    • Yin Z.X., He J.G., Deng W.X., Chan S.M. Molecular cloning, expression of orange-spotted grouper goose-type lysozyme cDNA, and lytic activity of its recombinant protein. Dis Aquat Organ 2003, 55:117-123.
    • (2003) Dis Aquat Organ , vol.55 , pp. 117-123
    • Yin, Z.X.1    He, J.G.2    Deng, W.X.3    Chan, S.M.4
  • 15
    • 77950299346 scopus 로고    scopus 로고
    • Immune responses and expression profiles of some immune-related genes in Indian major carp, Labeo rohita to Edwardsiella tarda infection
    • Mohanty B.R., Sahoo P.K. Immune responses and expression profiles of some immune-related genes in Indian major carp, Labeo rohita to Edwardsiella tarda infection. Fish Shellfish Immunol 2010, 28:613-621.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 613-621
    • Mohanty, B.R.1    Sahoo, P.K.2
  • 16
    • 67349180239 scopus 로고    scopus 로고
    • Profiling gene expression in the spleen of Atlantic cod, Gadus morhua upon vaccination with Vibrio anguillarum antigen
    • Caipang C.M., Brinchmann M.F., Kiron V. Profiling gene expression in the spleen of Atlantic cod, Gadus morhua upon vaccination with Vibrio anguillarum antigen. Comp Biochem Physiol B Biochem Mol Biol 2009, 153:261-267.
    • (2009) Comp Biochem Physiol B Biochem Mol Biol , vol.153 , pp. 261-267
    • Caipang, C.M.1    Brinchmann, M.F.2    Kiron, V.3
  • 18
    • 79551631178 scopus 로고    scopus 로고
    • The g-type lysozyme of Scophthalmus maximus has a broad substrate spectrum and is involved in the immune response against bacterial infection
    • Zhao L., Sun J.S., Sun L. The g-type lysozyme of Scophthalmus maximus has a broad substrate spectrum and is involved in the immune response against bacterial infection. Fish Shellfish Immunol 2011, 30:630-637.
    • (2011) Fish Shellfish Immunol , vol.30 , pp. 630-637
    • Zhao, L.1    Sun, J.S.2    Sun, L.3
  • 19
    • 79551634460 scopus 로고    scopus 로고
    • Characterization and expression analysis of a goose-type lysozyme from the rock bream Oplegnathus fasciatus, and antimicrobial activity of its recombinant protein
    • Whang I., Lee Y., Lee S., Oh M.J., Jung S.J., Choi C.Y., et al. Characterization and expression analysis of a goose-type lysozyme from the rock bream Oplegnathus fasciatus, and antimicrobial activity of its recombinant protein. Fish Shellfish Immunol 2011, 30:532-542.
    • (2011) Fish Shellfish Immunol , vol.30 , pp. 532-542
    • Whang, I.1    Lee, Y.2    Lee, S.3    Oh, M.J.4    Jung, S.J.5    Choi, C.Y.6
  • 20
    • 0034731566 scopus 로고    scopus 로고
    • Modulation of the fish immune system by hormones
    • Harris J., Bird D.J. Modulation of the fish immune system by hormones. Vet Immunol Immunopathol 2000, 77:163-176.
    • (2000) Vet Immunol Immunopathol , vol.77 , pp. 163-176
    • Harris, J.1    Bird, D.J.2
  • 21
    • 79955164576 scopus 로고    scopus 로고
    • Neuroendocrine-Immune interactions in teleost fish
    • Academic Press, London, N.J. Bernier, G. Kraak, A.P. Farrel, C.J. Brauner (Eds.)
    • Verburg-Van Kemenade B.M.L., Stolte E.H., Metz M.R.C. Neuroendocrine-Immune interactions in teleost fish. Fish neuroendocrinology 2009, Academic Press, London. N.J. Bernier, G. Kraak, A.P. Farrel, C.J. Brauner (Eds.).
    • (2009) Fish neuroendocrinology
    • Verburg-Van Kemenade, B.M.L.1    Stolte, E.H.2    Metz, M.R.C.3
  • 23
    • 0030885073 scopus 로고    scopus 로고
    • The immediate effects of stress on hormones and plasma lysozyme in rainbow trout
    • Demers N.E., Bayne C.J. The immediate effects of stress on hormones and plasma lysozyme in rainbow trout. Dev Comp Immunol 1997, 21:363-373.
    • (1997) Dev Comp Immunol , vol.21 , pp. 363-373
    • Demers, N.E.1    Bayne, C.J.2
  • 24
    • 76049086110 scopus 로고    scopus 로고
    • Supra-physiological levels of cortisol suppress lysozyme but not the antibody response in Atlantic salmon, Salmo salar L., following vaccine injection
    • Skinner L.A., LaPatra S.E., Adams A., Thompson K.D., Balfry S.K., McKinley R.S., et al. Supra-physiological levels of cortisol suppress lysozyme but not the antibody response in Atlantic salmon, Salmo salar L., following vaccine injection. Aquaculture 2010, 300:223-230.
    • (2010) Aquaculture , vol.300 , pp. 223-230
    • Skinner, L.A.1    LaPatra, S.E.2    Adams, A.3    Thompson, K.D.4    Balfry, S.K.5    McKinley, R.S.6
  • 25
    • 84986431512 scopus 로고
    • Lysozyme activity in rainbow trout, Oncorhynchus mykiss (Walbaum), stressed by handling, transport and water pollution
    • Möck A., Peters G. Lysozyme activity in rainbow trout, Oncorhynchus mykiss (Walbaum), stressed by handling, transport and water pollution. J Fish Biol 1990, 37:873-885.
    • (1990) J Fish Biol , vol.37 , pp. 873-885
    • Möck, A.1    Peters, G.2
  • 26
    • 0030783640 scopus 로고    scopus 로고
    • Non-specific immune responses in the red porgy, Pagrus pagrus after crowding stress
    • Rotllant J., Pavildis M., Kentouri M., Abad M.E., Tort L. Non-specific immune responses in the red porgy, Pagrus pagrus after crowding stress. Aquaculture 1997, 156:279-290.
    • (1997) Aquaculture , vol.156 , pp. 279-290
    • Rotllant, J.1    Pavildis, M.2    Kentouri, M.3    Abad, M.E.4    Tort, L.5
  • 27
    • 20344375192 scopus 로고    scopus 로고
    • Effects of thyroid hormone on the development of immune system in zebrafish
    • Lam S.H., Sin Y.M., Gong Z., Lam T.J. Effects of thyroid hormone on the development of immune system in zebrafish. Gen Comp Endocrinol 2005, 142:325-335.
    • (2005) Gen Comp Endocrinol , vol.142 , pp. 325-335
    • Lam, S.H.1    Sin, Y.M.2    Gong, Z.3    Lam, T.J.4
  • 28
    • 0025336820 scopus 로고
    • Modular structure of a chicken lysozyme silencer: involvement of an unusual thyroid hormone receptor binding site
    • Baniahmad A., Steiner C., Kohne A.C., Renkawitz R. Modular structure of a chicken lysozyme silencer: involvement of an unusual thyroid hormone receptor binding site. Cell 1990, 61:505-514.
    • (1990) Cell , vol.61 , pp. 505-514
    • Baniahmad, A.1    Steiner, C.2    Kohne, A.C.3    Renkawitz, R.4
  • 29
    • 0033856697 scopus 로고    scopus 로고
    • Modulation of thyroid hormone receptor silencing function by co-repressors and a synergizing transcription factor
    • Lutz M., Baniahmad A., Renkawitz R. Modulation of thyroid hormone receptor silencing function by co-repressors and a synergizing transcription factor. Biochem Soc Trans 2000, 28:386-389.
    • (2000) Biochem Soc Trans , vol.28 , pp. 386-389
    • Lutz, M.1    Baniahmad, A.2    Renkawitz, R.3
  • 30
    • 50249179101 scopus 로고    scopus 로고
    • Vitamin effects on the immune system: vitamins A and D take centre stage
    • Mora J.R., Iwata M., von Andrian U.H. Vitamin effects on the immune system: vitamins A and D take centre stage. Nat Rev Immunol 2008, 8:685-698.
    • (2008) Nat Rev Immunol , vol.8 , pp. 685-698
    • Mora, J.R.1    Iwata, M.2    von Andrian, U.H.3
  • 31
    • 0016284984 scopus 로고
    • Lysozyme activity in plasma and leucocytes in malnourished children
    • Mohanram M., Reddy V., Mishra S. Lysozyme activity in plasma and leucocytes in malnourished children. Br J Nutr 1974, 32:313-316.
    • (1974) Br J Nutr , vol.32 , pp. 313-316
    • Mohanram, M.1    Reddy, V.2    Mishra, S.3
  • 32
    • 0028833730 scopus 로고
    • The effect of dietary vitamin A and astaxanthin on the immunocompetence of rainbow trout
    • Thompson I., Choubert G., Houlihan D.F., Secombes C.J. The effect of dietary vitamin A and astaxanthin on the immunocompetence of rainbow trout. Aquaculture 1995, 133:91-102.
    • (1995) Aquaculture , vol.133 , pp. 91-102
    • Thompson, I.1    Choubert, G.2    Houlihan, D.F.3    Secombes, C.J.4
  • 33
    • 0036784940 scopus 로고    scopus 로고
    • Changes in some innate defence parameters of seabream (Sparus aurata L.) induced by retinol acetate
    • Cuesta A., Ortuño J., Rodriguez A., Esteban M.A., Meseguer J. Changes in some innate defence parameters of seabream (Sparus aurata L.) induced by retinol acetate. Fish Shellfish Immunol 2002, 13:279-291.
    • (2002) Fish Shellfish Immunol , vol.13 , pp. 279-291
    • Cuesta, A.1    Ortuño, J.2    Rodriguez, A.3    Esteban, M.A.4    Meseguer, J.5
  • 34
    • 33846680021 scopus 로고    scopus 로고
    • Effects of vitamin A on growth, serum anti-bacterial activity and transaminase activities in the juvenile Japanese flounder, Paralichthys olivaceus
    • Hernandez-Hernandez L.H., Teshima S.-I., Koshio S., Ishikawa M., Tanaka Y., Alam M.S. Effects of vitamin A on growth, serum anti-bacterial activity and transaminase activities in the juvenile Japanese flounder, Paralichthys olivaceus. Aquaculture 2007, 262:444-450.
    • (2007) Aquaculture , vol.262 , pp. 444-450
    • Hernandez-Hernandez, L.H.1    Teshima, S.-I.2    Koshio, S.3    Ishikawa, M.4    Tanaka, Y.5    Alam, M.S.6
  • 35
    • 43149120646 scopus 로고    scopus 로고
    • Molecular characterization, gene expression and transcriptional regulation of cytosolic HSP90 genes in the flatfish Senegalese sole (Solea senegalensis Kaup)
    • Manchado M., Salas-Leiton E., Infante C., Ponce M., Asensio E., Crespo A., et al. Molecular characterization, gene expression and transcriptional regulation of cytosolic HSP90 genes in the flatfish Senegalese sole (Solea senegalensis Kaup). Gene 2008, 416:77-84.
    • (2008) Gene , vol.416 , pp. 77-84
    • Manchado, M.1    Salas-Leiton, E.2    Infante, C.3    Ponce, M.4    Asensio, E.5    Crespo, A.6
  • 36
    • 58149263041 scopus 로고    scopus 로고
    • Molecular characterization, gene expression and transcriptional regulation of thyroid hormone receptors in Senegalese sole
    • Manchado M., Infante C., Rebordinos L., Cañavate J.P. Molecular characterization, gene expression and transcriptional regulation of thyroid hormone receptors in Senegalese sole. Gen Comp Endocrinol 2009, 160:139-147.
    • (2009) Gen Comp Endocrinol , vol.160 , pp. 139-147
    • Manchado, M.1    Infante, C.2    Rebordinos, L.3    Cañavate, J.P.4
  • 37
    • 37649015333 scopus 로고    scopus 로고
    • Thyroid hormones down-regulate thyrotropin β subunit and thyroglobulin during metamorphosis in the flatfish Senegalese sole (Solea senegalensis Kaup)
    • Manchado M., Infante C., Asensio E., Planas J.V., Cañavate J.P. Thyroid hormones down-regulate thyrotropin β subunit and thyroglobulin during metamorphosis in the flatfish Senegalese sole (Solea senegalensis Kaup). Gen Comp Endocrinol 2008, 155:447-455.
    • (2008) Gen Comp Endocrinol , vol.155 , pp. 447-455
    • Manchado, M.1    Infante, C.2    Asensio, E.3    Planas, J.V.4    Cañavate, J.P.5
  • 38
    • 58149299281 scopus 로고    scopus 로고
    • Genomic resources for a commercial flatfish, the Senegalese sole (Solea senegalensis): EST sequencing, oligo microarray design, and development of the Soleamold bioinformatic platform
    • Cerda J., Mercade J., Lozano J.J., Manchado M., Tingaud-Sequeira A., Astola A., et al. Genomic resources for a commercial flatfish, the Senegalese sole (Solea senegalensis): EST sequencing, oligo microarray design, and development of the Soleamold bioinformatic platform. BMC Genomics 2008, 9:508.
    • (2008) BMC Genomics , vol.9 , pp. 508
    • Cerda, J.1    Mercade, J.2    Lozano, J.J.3    Manchado, M.4    Tingaud-Sequeira, A.5    Astola, A.6
  • 40
    • 0000122573 scopus 로고
    • PHYLIP - Phylogeny inference package (Version 3.2)
    • Felsenstein J. PHYLIP - Phylogeny inference package (Version 3.2). Cladistics 1989, 5:164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 41
    • 0036270185 scopus 로고    scopus 로고
    • Codon-substitution models for detecting molecular adaptation at individual sites along specific lineages
    • Yang Z., Nielsen R. Codon-substitution models for detecting molecular adaptation at individual sites along specific lineages. Mol Biol Evol 2002, 19:908-917.
    • (2002) Mol Biol Evol , vol.19 , pp. 908-917
    • Yang, Z.1    Nielsen, R.2
  • 42
    • 0031897964 scopus 로고    scopus 로고
    • Likelihood ratio tests for detecting positive selection and application to primate lysozyme evolution
    • Yang Z. Likelihood ratio tests for detecting positive selection and application to primate lysozyme evolution. Mol Biol Evol 1998, 15:568-573.
    • (1998) Mol Biol Evol , vol.15 , pp. 568-573
    • Yang, Z.1
  • 43
    • 16344378246 scopus 로고    scopus 로고
    • Bayes empirical bayes inference of amino acid sites under positive selection
    • Yang Z., Wong W.S., Nielsen R. Bayes empirical bayes inference of amino acid sites under positive selection. Mol Biol Evol 2005, 22:1107-1118.
    • (2005) Mol Biol Evol , vol.22 , pp. 1107-1118
    • Yang, Z.1    Wong, W.S.2    Nielsen, R.3
  • 45
    • 67650960649 scopus 로고    scopus 로고
    • Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism
    • Helland R., Larsen R.L., Finstad S., Kyomuhendo P., Larsen A.N. Crystal structures of g-type lysozyme from Atlantic cod shed new light on substrate binding and the catalytic mechanism. Cell Mol Life Sci 2009, 66:2585-2598.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2585-2598
    • Helland, R.1    Larsen, R.L.2    Finstad, S.3    Kyomuhendo, P.4    Larsen, A.N.5
  • 46
    • 0030980842 scopus 로고    scopus 로고
    • Human BAC library: construction and rapid screening
    • Asakawa S., Abe I., Kudoh Y., Kishi N., Wang Y., Kubota R., et al. Human BAC library: construction and rapid screening. Gene 1997, 191:69-79.
    • (1997) Gene , vol.191 , pp. 69-79
    • Asakawa, S.1    Abe, I.2    Kudoh, Y.3    Kishi, N.4    Wang, Y.5    Kubota, R.6
  • 47
    • 41449097016 scopus 로고    scopus 로고
    • Selection of housekeeping genes for gene expression studies in larvae from flatfish using real-time PCR
    • Infante C., Matsuoka M.P., Asensio E., Cañavate J.P., Reith M., Manchado M. Selection of housekeeping genes for gene expression studies in larvae from flatfish using real-time PCR. BMC Mol Biol 2008, 9:28.
    • (2008) BMC Mol Biol , vol.9 , pp. 28
    • Infante, C.1    Matsuoka, M.P.2    Asensio, E.3    Cañavate, J.P.4    Reith, M.5    Manchado, M.6
  • 48
    • 34548132383 scopus 로고    scopus 로고
    • Differential gene expression and dependence on thyroid hormones of two glyceraldehyde-3-phosphate dehydrogenases in the flatfish Senegalese sole (Solea senegalensis Kaup)
    • Manchado M., Infante C., Asensio E., Cañavate J.P. Differential gene expression and dependence on thyroid hormones of two glyceraldehyde-3-phosphate dehydrogenases in the flatfish Senegalese sole (Solea senegalensis Kaup). Gene 2007, 400:1-8.
    • (2007) Gene , vol.400 , pp. 1-8
    • Manchado, M.1    Infante, C.2    Asensio, E.3    Cañavate, J.P.4
  • 50
    • 33749620059 scopus 로고    scopus 로고
    • Cytogenetic characterization of the sole Solea senegalensis (Teleostei: Pleuronectiformes: Soleidae): Ag-NOR, (GATA)n, (TTAGGG)n and ribosomal genes by one-color and two-color FISH
    • Cross I., Merlo A., Manchado M., Infante C., Cañavate J.P., Rebordinos L. Cytogenetic characterization of the sole Solea senegalensis (Teleostei: Pleuronectiformes: Soleidae): Ag-NOR, (GATA)n, (TTAGGG)n and ribosomal genes by one-color and two-color FISH. Genetica 2006, 128:253-259.
    • (2006) Genetica , vol.128 , pp. 253-259
    • Cross, I.1    Merlo, A.2    Manchado, M.3    Infante, C.4    Cañavate, J.P.5    Rebordinos, L.6
  • 51
    • 0037309920 scopus 로고    scopus 로고
    • Molecular evolution of vertebrate goose-type lysozyme genes
    • Irwin D.M., Gong Z. Molecular evolution of vertebrate goose-type lysozyme genes. J Mol Evol 2003, 56:234-242.
    • (2003) J Mol Evol , vol.56 , pp. 234-242
    • Irwin, D.M.1    Gong, Z.2
  • 52
    • 38549125019 scopus 로고    scopus 로고
    • A cold-active salmon goose-type lysozyme with high heat tolerance
    • Kyomuhendo P., Myrnes B., Nilsen I.W. A cold-active salmon goose-type lysozyme with high heat tolerance. Cell Mol Life Sci 2007, 64:2841-2847.
    • (2007) Cell Mol Life Sci , vol.64 , pp. 2841-2847
    • Kyomuhendo, P.1    Myrnes, B.2    Nilsen, I.W.3
  • 53
    • 41949104607 scopus 로고    scopus 로고
    • Vaccination of larvae of the bony fish gilthead seabream reveals a lack of correlation between lymphocyte development and adaptive immunocompetence
    • Mulero I., Sepulcre M.P., Fuentes I., Garcia-Alcazar A., Meseguer J., Garcia-Ayala A., et al. Vaccination of larvae of the bony fish gilthead seabream reveals a lack of correlation between lymphocyte development and adaptive immunocompetence. Mol Immunol 2008, 45:2981-2989.
    • (2008) Mol Immunol , vol.45 , pp. 2981-2989
    • Mulero, I.1    Sepulcre, M.P.2    Fuentes, I.3    Garcia-Alcazar, A.4    Meseguer, J.5    Garcia-Ayala, A.6
  • 55
    • 0035104119 scopus 로고    scopus 로고
    • LPS induction of gene expression in human monocytes
    • Guha M., Mackman N. LPS induction of gene expression in human monocytes. Cell Signal 2001, 13:85-94.
    • (2001) Cell Signal , vol.13 , pp. 85-94
    • Guha, M.1    Mackman, N.2
  • 56
    • 0030872393 scopus 로고    scopus 로고
    • Multiple control elements mediate activation of the murine and human interleukin 12 p40 promoters: evidence of functional synergy between C/EBP and Rel proteins
    • Plevy S.E., Gemberling J.H., Hsu S., Dorner A.J., Smale S.T. Multiple control elements mediate activation of the murine and human interleukin 12 p40 promoters: evidence of functional synergy between C/EBP and Rel proteins. Mol Cell Biol 1997, 17:4572-4588.
    • (1997) Mol Cell Biol , vol.17 , pp. 4572-4588
    • Plevy, S.E.1    Gemberling, J.H.2    Hsu, S.3    Dorner, A.J.4    Smale, S.T.5
  • 57
    • 0027379055 scopus 로고
    • Distinct mechanisms for regulation of the interleukin-8 gene involve synergism and cooperativity between C/EBP and NF-κB
    • Stein B., Baldwin A.S. Distinct mechanisms for regulation of the interleukin-8 gene involve synergism and cooperativity between C/EBP and NF-κB. Mol Cell Biol 1993, 13:7191-7198.
    • (1993) Mol Cell Biol , vol.13 , pp. 7191-7198
    • Stein, B.1    Baldwin, A.S.2
  • 58
    • 0038316508 scopus 로고    scopus 로고
    • Developmentally regulated recruitment of transcription factors and chromatin modification activities to chicken lysozyme cis-regulatory elements in vivo
    • Lefevre P., Melnik S., Wilson N., Riggs A.D., Bonifer C. Developmentally regulated recruitment of transcription factors and chromatin modification activities to chicken lysozyme cis-regulatory elements in vivo. Mol Cell Biol 2003, 23:4386-4400.
    • (2003) Mol Cell Biol , vol.23 , pp. 4386-4400
    • Lefevre, P.1    Melnik, S.2    Wilson, N.3    Riggs, A.D.4    Bonifer, C.5
  • 59
    • 2842610984 scopus 로고
    • Two interferon-induced nuclear factors bind a single promoter element in interferon-stimulated genes
    • Kessler D.S., Levy D.E., Darnell J.E. Two interferon-induced nuclear factors bind a single promoter element in interferon-stimulated genes. Proc Natl Acad Sci U S A 1988, 85:8521-8525.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 8521-8525
    • Kessler, D.S.1    Levy, D.E.2    Darnell, J.E.3
  • 61
    • 11244336489 scopus 로고    scopus 로고
    • Synergistic activation of interleukin-12 p35 gene transcription by interferon regulatory factor-1 and interferon consensus sequence-binding protein
    • Liu J., Guan X., Tamura T., Ozato K., Ma X. Synergistic activation of interleukin-12 p35 gene transcription by interferon regulatory factor-1 and interferon consensus sequence-binding protein. J Biol Chem 2004, 279:55609-55617.
    • (2004) J Biol Chem , vol.279 , pp. 55609-55617
    • Liu, J.1    Guan, X.2    Tamura, T.3    Ozato, K.4    Ma, X.5
  • 62
    • 34548697554 scopus 로고    scopus 로고
    • Zebrafish peptidoglycan recognition proteins are bactericidal amidases essential for defense against bacterial infections
    • Li X., Wang S., Qi J., Echtenkamp S.F., Chatterjee R., Wang M., et al. Zebrafish peptidoglycan recognition proteins are bactericidal amidases essential for defense against bacterial infections. Immunity 2007, 27:518-529.
    • (2007) Immunity , vol.27 , pp. 518-529
    • Li, X.1    Wang, S.2    Qi, J.3    Echtenkamp, S.F.4    Chatterjee, R.5    Wang, M.6
  • 63
    • 54049156405 scopus 로고    scopus 로고
    • The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel
    • Dong X.P., Cheng X., Mills E., Delling M., Wang F., Kurz T., et al. The type IV mucolipidosis-associated protein TRPML1 is an endolysosomal iron release channel. Nature 2008, 455:992-996.
    • (2008) Nature , vol.455 , pp. 992-996
    • Dong, X.P.1    Cheng, X.2    Mills, E.3    Delling, M.4    Wang, F.5    Kurz, T.6
  • 64
    • 1842427830 scopus 로고    scopus 로고
    • The evolutionary dynamics of eukaryotic gene order
    • Hurst L.D., Pal C., Lercher M.J. The evolutionary dynamics of eukaryotic gene order. Nat Rev Genet 2004, 5:299-310.
    • (2004) Nat Rev Genet , vol.5 , pp. 299-310
    • Hurst, L.D.1    Pal, C.2    Lercher, M.J.3
  • 65
    • 1542377379 scopus 로고    scopus 로고
    • Mini-review: defense strategies and immunity-related genes
    • Trowsdale J., Parham P. Mini-review: defense strategies and immunity-related genes. Eur J Immunol 2004, 34:7-17.
    • (2004) Eur J Immunol , vol.34 , pp. 7-17
    • Trowsdale, J.1    Parham, P.2
  • 66
    • 49749120556 scopus 로고    scopus 로고
    • Interacting gene clusters and the evolution of the vertebrate immune system
    • Makino T., McLysaght A. Interacting gene clusters and the evolution of the vertebrate immune system. Mol Biol Evol 2008, 25:1855-1862.
    • (2008) Mol Biol Evol , vol.25 , pp. 1855-1862
    • Makino, T.1    McLysaght, A.2
  • 67
    • 34248594184 scopus 로고    scopus 로고
    • Characterization of the opossum immune genome provides insights into the evolution of the mammalian immune system
    • Belov K., Sanderson C.E., Deakin J.E., Wong E.S., Assange D., McColl K.A., et al. Characterization of the opossum immune genome provides insights into the evolution of the mammalian immune system. Genome Res 2007, 17:982-991.
    • (2007) Genome Res , vol.17 , pp. 982-991
    • Belov, K.1    Sanderson, C.E.2    Deakin, J.E.3    Wong, E.S.4    Assange, D.5    McColl, K.A.6
  • 69
    • 10844254878 scopus 로고    scopus 로고
    • Rapid evolution through gene duplication and subfunctionalization of the testes-specific alpha4 proteasome subunits in Drosophila
    • Torgerson D.G., Singh R.S. Rapid evolution through gene duplication and subfunctionalization of the testes-specific alpha4 proteasome subunits in Drosophila. Genetics 2004, 168:1421-1432.
    • (2004) Genetics , vol.168 , pp. 1421-1432
    • Torgerson, D.G.1    Singh, R.S.2
  • 70
    • 66349114360 scopus 로고    scopus 로고
    • Signatures of natural selection are not uniform across genes of innate immune system, but purifying selection is the dominant signature
    • Mukherjee S., Sarkar-Roy N., Wagener D.K., Majumder P.P. Signatures of natural selection are not uniform across genes of innate immune system, but purifying selection is the dominant signature. Proc Natl Acad Sci U S A 2009, 106:7073-7078.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7073-7078
    • Mukherjee, S.1    Sarkar-Roy, N.2    Wagener, D.K.3    Majumder, P.P.4
  • 72
    • 62949134534 scopus 로고    scopus 로고
    • Genomic characterization and gene expression analysis of four hepcidin genes in the redbanded seabream (Pagrus auriga)
    • Martin-Antonio B., Jimenez-Cantizano R.M., Salas-Leiton E., Infante C., Manchado M. Genomic characterization and gene expression analysis of four hepcidin genes in the redbanded seabream (Pagrus auriga). Fish Shellfish Immunol 2009, 26:483-491.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 483-491
    • Martin-Antonio, B.1    Jimenez-Cantizano, R.M.2    Salas-Leiton, E.3    Infante, C.4    Manchado, M.5
  • 73
    • 41149133447 scopus 로고    scopus 로고
    • Evidence for positive Darwinian selection on the hepcidin gene of Perciform and Pleuronectiform fishes
    • Padhi A., Verghese B. Evidence for positive Darwinian selection on the hepcidin gene of Perciform and Pleuronectiform fishes. Mol Divers 2007, 11:119-130.
    • (2007) Mol Divers , vol.11 , pp. 119-130
    • Padhi, A.1    Verghese, B.2
  • 74
    • 44649155133 scopus 로고    scopus 로고
    • Adaptive evolution of hepcidin genes in antarctic notothenioid fishes
    • Xu Q., Cheng C.H., Hu P., Ye H., Chen Z., Cao L., et al. Adaptive evolution of hepcidin genes in antarctic notothenioid fishes. Mol Biol Evol 2008, 25:1099-1112.
    • (2008) Mol Biol Evol , vol.25 , pp. 1099-1112
    • Xu, Q.1    Cheng, C.H.2    Hu, P.3    Ye, H.4    Chen, Z.5    Cao, L.6
  • 75
    • 77954552336 scopus 로고    scopus 로고
    • A new lysozyme from the eastern oyster, Crassostrea virginica, and a possible evolutionary pathway for i-type lysozymes in bivalves from host defense to digestion
    • Xue Q., Hellberg M.E., Schey K.L., Itoh N., Eytan R.I., Cooper R.K., et al. A new lysozyme from the eastern oyster, Crassostrea virginica, and a possible evolutionary pathway for i-type lysozymes in bivalves from host defense to digestion. BMC Evol Biol 2010, 10:213.
    • (2010) BMC Evol Biol , vol.10 , pp. 213
    • Xue, Q.1    Hellberg, M.E.2    Schey, K.L.3    Itoh, N.4    Eytan, R.I.5    Cooper, R.K.6
  • 76
    • 43549106617 scopus 로고    scopus 로고
    • Diversification and adaptive sequence evolution of Caenorhabditis lysozymes (Nematoda: Rhabditidae)
    • Schulenburg H., Boehnisch C. Diversification and adaptive sequence evolution of Caenorhabditis lysozymes (Nematoda: Rhabditidae). BMC Evol Biol 2008, 8:114.
    • (2008) BMC Evol Biol , vol.8 , pp. 114
    • Schulenburg, H.1    Boehnisch, C.2
  • 77
    • 5444236355 scopus 로고    scopus 로고
    • Positive selection on the human genome
    • Vallender E.J., Lahn B.T. Positive selection on the human genome. Hum Mol Genet 2004, 13(Spec No 2):R245-R254.
    • (2004) Hum Mol Genet , vol.13 , Issue.SPEC. NO. 2
    • Vallender, E.J.1    Lahn, B.T.2
  • 78
    • 0023666025 scopus 로고
    • Adaptive evolution in the stomach lysozymes of foregut fermenters
    • Stewart C.B., Schilling J.W., Wilson A.C. Adaptive evolution in the stomach lysozymes of foregut fermenters. Nature 1987, 330:401-404.
    • (1987) Nature , vol.330 , pp. 401-404
    • Stewart, C.B.1    Schilling, J.W.2    Wilson, A.C.3
  • 79
    • 0029686292 scopus 로고    scopus 로고
    • Molecular evolution of ruminant lysozymes
    • Irwin D.M. Molecular evolution of ruminant lysozymes. Exs 1996, 75:347-361.
    • (1996) Exs , vol.75 , pp. 347-361
    • Irwin, D.M.1
  • 80
    • 77949916732 scopus 로고    scopus 로고
    • Protection of blue shrimp (Litopenaeus stylirostris) against the White Spot Syndrome Virus (WSSV) when injected with shrimp lysozyme
    • Mai W.J., Wang W.N. Protection of blue shrimp (Litopenaeus stylirostris) against the White Spot Syndrome Virus (WSSV) when injected with shrimp lysozyme. Fish Shellfish Immunol 2010, 28:727-733.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 727-733
    • Mai, W.J.1    Wang, W.N.2
  • 81
    • 0001182675 scopus 로고
    • The effects of crowding stress on the non-specific immune response of the fancy carp (Cyprinus carpio)
    • Yin Z., Lam T.J., Sin Y.M. The effects of crowding stress on the non-specific immune response of the fancy carp (Cyprinus carpio). Fish Shellfish Immunol 1995, 5:519-529.
    • (1995) Fish Shellfish Immunol , vol.5 , pp. 519-529
    • Yin, Z.1    Lam, T.J.2    Sin, Y.M.3
  • 82
    • 0035902605 scopus 로고    scopus 로고
    • Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice
    • Nicolas G., Bennoun M., Devaux I., Beaumont C., Grandchamp B., Kahn A., et al. Lack of hepcidin gene expression and severe tissue iron overload in upstream stimulatory factor 2 (USF2) knockout mice. Proc Natl Acad Sci U S A 2001, 98:8780-8785.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 8780-8785
    • Nicolas, G.1    Bennoun, M.2    Devaux, I.3    Beaumont, C.4    Grandchamp, B.5    Kahn, A.6
  • 83
    • 0030856061 scopus 로고    scopus 로고
    • Prevention of stress in rainbow trout (Oncorhynchus mykiss) fed diets containing different doses of glucan
    • Jeney G., Galeotti M., Volpatti D., Jeney Z., Anderson D.P. Prevention of stress in rainbow trout (Oncorhynchus mykiss) fed diets containing different doses of glucan. Aquaculture 1997, 154:1-15.
    • (1997) Aquaculture , vol.154 , pp. 1-15
    • Jeney, G.1    Galeotti, M.2    Volpatti, D.3    Jeney, Z.4    Anderson, D.P.5
  • 84
    • 74649084922 scopus 로고    scopus 로고
    • Effects of stocking density and feed ration on growth and gene expression in the Senegalese sole (Solea senegalensis): potential effects on the immune response
    • Salas-Leiton E., Anguis V., Martin-Antonio B., Crespo D., Planas J.V., Infante C., et al. Effects of stocking density and feed ration on growth and gene expression in the Senegalese sole (Solea senegalensis): potential effects on the immune response. Fish Shellfish Immunol 2010, 28:296-302.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 296-302
    • Salas-Leiton, E.1    Anguis, V.2    Martin-Antonio, B.3    Crespo, D.4    Planas, J.V.5    Infante, C.6
  • 86


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.