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Volumn 708, Issue , 2010, Pages 44-65

Bivalve immunity

Author keywords

[No Author keywords available]

Indexed keywords

ACUTE PHASE PROTEIN; BETA 1,3 GLUCAN BINDING PROTEIN; CARBOHYDRATE BINDING PROTEIN; CATALASE; COMPLEMENT; CYTOKINE; GALECTIN; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; JANUS KINASE; LECTIN; LIPOPOLYSACCHARIDE BINDING PROTEIN; LYSOZYME; MITOGEN ACTIVATED PROTEIN KINASE; PEPTIDOGLYCAN RECOGNITION PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; SCAVENGER RECEPTOR; STAT PROTEIN; SUPEROXIDE DISMUTASE; TOLL LIKE RECEPTOR; UNCLASSIFIED DRUG;

EID: 79960714644     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-8059-5_3     Document Type: Article
Times cited : (205)

References (125)
  • 3
    • 37549048659 scopus 로고    scopus 로고
    • Increasing genomic information in bivalves through new EST collections in four species: Development of new genetic markers for environmental studies and genome evolution
    • Tanguy A, Bierne N, Saavedra C et al. Increasing genomic information in bivalves through new EST collections in four species: Development of new genetic markers for environmental studies and genome evolution. Gene 2008; 408:27-36.
    • (2008) Gene , vol.408 , pp. 27-36
    • Tanguy, A.1    Bierne, N.2    Saavedra, C.3
  • 5
    • 1642545529 scopus 로고    scopus 로고
    • Invertebrate immune systems - Not homogeneous, not simple, not well understood
    • DOI 10.1111/j.0105-2896.2004.0117.x
    • Loker ES, Adema CM, Zhang SM et al. Invertebrate immune systems-not homogeneous, not simple, not well understood. Immunol Rev 2004; 198:10-24. (Pubitemid 38406932)
    • (2004) Immunological Reviews , vol.198 , pp. 10-24
    • Loker, E.S.1    Adema, C.M.2    Zhang, S.-M.3    Kepler, T.B.4
  • 6
    • 0043074444 scopus 로고    scopus 로고
    • Bivalve immunity: Comparisons between the marine mussel (Mytilus edulis), the edible cockle (Cerastoderma edule) and the razor-shell (Ensis siliqua)
    • DOI 10.1016/S1050-4648(02)00161-4
    • Wootton EC, Dyrynda EA, Ratcliffe NA. Bivalve immunity: Comparisons between the marine mussel (Mytilus edulis), the edible cockle (Cerastoderma edule) and the razor-shell (Ensis siliqua). Fish Shellfish Immunol 2003; 15:195-210. (Pubitemid 36990182)
    • (2003) Fish and Shellfish Immunology , vol.15 , Issue.3 , pp. 195-210
    • Wootton, E.C.1    Dyrynda, E.A.2    Ratcliffe, N.A.3
  • 7
    • 0037097751 scopus 로고    scopus 로고
    • Bacteria-hemocyte interactions and phagocytosis in marine bivalves
    • DOI 10.1002/jemt.10100
    • Canesi L, Gallo G, Gavioli M et al. Bacteria-hemocyte interactions and phagocytosis in marine bivalves. Microsc Res Tech 2002; 57:469-476. (Pubitemid 34701147)
    • (2002) Microscopy Research and Technique , vol.57 , Issue.6 , pp. 469-476
    • Canesi, L.1    Gallo, G.2    Gavioli, M.3    Pruzzo, C.4
  • 8
    • 44449151024 scopus 로고    scopus 로고
    • Review: Cellular defense mechanisms in bivalve molluscs
    • DOI 10.3147/jsfp.43.1
    • Takahashi KG, Muroga K. Cellular Defense Mechanisms in Bivalve Molluscs. Fish Pathology 2008; 43:1-17. (Pubitemid 351762362)
    • (2008) Fish Pathology , vol.43 , Issue.1 , pp. 1-17
    • Takahashi, K.G.1    Muroga, K.2
  • 9
    • 33645492223 scopus 로고
    • London: Acdemic Press; Ratcliffe NA, Rowley AF, eds. Invertebrate blood cell.
    • Cheng TC, ed. Bivalves. London: Acdemic Press; 1981. Ratcliffe NA, Rowley AF, eds. Invertebrate blood cell.
    • (1981) Bivalves
    • Cheng, T.C.1
  • 10
    • 0028881763 scopus 로고
    • Morphofunctional study of the haemocytes of the bivalve mollusc Mytilus galloprovincialis with emphasis on the endolysosomal compartment
    • Cajaraville MP, Pal SG. Morphofunctional study of the haemocytes of the bivalve mollusc Mytilus galloprovincialis with emphasis on the endolysosomal compartment. Cell Struct Funct 1995; 20:355-367.
    • (1995) Cell Struct Funct , vol.20 , pp. 355-367
    • Cajaraville, M.P.1    Pal, S.G.2
  • 11
    • 0030638367 scopus 로고    scopus 로고
    • Morphological characterization of the hemocytes of the clam, Ruditapes decussatus (Mollusca: Bivalvia)
    • Lopez C, Carballal MJ, Azevedo C et al. Morphological characterization of the hemocytes of the clam, Ruditapes decussatus (Mollusca: Bivalvia). J Invertebr Pathol 1997; 69:51-57. (Pubitemid 127346218)
    • (1997) Journal of Invertebrate Pathology , vol.69 , Issue.1 , pp. 51-57
    • Lopez, C.1    Carballal, M.J.2    Azevedo, C.3    Villalba, A.4
  • 12
    • 67650591010 scopus 로고    scopus 로고
    • Flow cytometry studies on the populations and immune parameters of the hemocytes of the Suminoe oyster, Crassostrea ariakensis
    • Donaghy L, Kim BK, Hong HKK et al. Flow cytometry studies on the populations and immune parameters of the hemocytes of the Suminoe oyster, Crassostrea ariakensis. Fish Shellfish Immunol 2009; 27:296-301.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 296-301
    • Donaghy, L.1    Kim, B.K.2    Hong, H.K.K.3
  • 13
    • 34047268684 scopus 로고    scopus 로고
    • The host defense of Drosophila melanogaster
    • DOI 10.1146/annurev.immunol.25.022106.141615
    • Lemaitre B, Hoffmann J. The host defense of Drosophila melanogaster. Annu Rev Immunol 2007; 25:697-743. (Pubitemid 46697922)
    • (2007) Annual Review of Immunology , vol.25 , pp. 697-743
    • Lemaitre, B.1    Hoffmann, J.2
  • 14
    • 0027489733 scopus 로고
    • Analysis of the attraction of haemocytes from Mytilus edulis by molecules of bacterial origin
    • DOI 10.1016/0145-305X(93)90029-P
    • Schneeweiss H, Renwrantz L. Analysis of the attraction of haemocytes from Mytilus edulis by molecules of bacterial origin. Dev Comp Immunol 1993; 17:377-387. (Pubitemid 23294063)
    • (1993) Developmental and Comparative Immunology , vol.17 , Issue.5 , pp. 377-387
    • Schneeweiss, H.1    Renwrantz, L.2
  • 15
    • 0038709401 scopus 로고    scopus 로고
    • Changes in circulating and tissue-infiltrating hemocyte parameters of European flat oysters, Ostrea edulis, naturally infected with Bonamia ostreae
    • DOI 10.1016/S0022-2011(03)00015-6
    • Cochennec-Laureau N, Auffret M, Renault T et al. Changes in circulating and tissue-infiltrating hemocyte parameters of European flat oysters, Ostrea edulis, naturally infected with Bonamia ostreae. J Invertebr Pathol 2003; 83:23-30. (Pubitemid 36531034)
    • (2003) Journal of Invertebrate Pathology , vol.83 , Issue.1 , pp. 23-30
    • Cochennec-Laureau, N.1    Auffret, M.2    Renault, T.3    Langlade, A.4
  • 16
    • 38949170128 scopus 로고    scopus 로고
    • Immune responses of mussel hemocyte subpopulations are differentially regulated by enzymes of the PI 3-K, PKC, and ERK kinase families
    • DOI 10.1016/j.dci.2007.10.004, PII S0145305X0700136X
    • Garcia-Garcia E, Prado-Alvarez M, Novoa B et al. Immune responses of mussel hemocyte subpopulations are differentially regulated by enzymes of the PI 3-K, PKC and ERKK kinase families. Dev Comp Immunol 2008; 32:637-653. (Pubitemid 351210681)
    • (2008) Developmental and Comparative Immunology , vol.32 , Issue.6 , pp. 637-653
    • Garcia-Garcia, E.1    Prado-Alvarez, M.2    Novoa, B.3    Figueras, A.4    Rosales, C.5
  • 17
    • 0001632151 scopus 로고    scopus 로고
    • Enfield Science Publishers Inc; Fingerman M, Nagabhushanam R, eds. Recent advances in marine biotechnology No. 5
    • Chu FE, ed. Defense mechanisms of marine bivalves. Enfield Science Publishers Inc; 2000. Fingerman M, Nagabhushanam R, eds. Recent advances in marine biotechnology No. 5.
    • (2000) Defense Mechanisms of Marine Bivalves
    • Chu, F.E.1
  • 18
    • 34247345795 scopus 로고    scopus 로고
    • Oxidative burst in hard clam (Mercenaria mercenaria) haemocytes
    • DOI 10.1016/j.fsi.2006.10.006, PII S105046480600194X
    • Bugge DM, Hegaret H, Wikfors GH et al. Oxidative burst in hard clam (Mercenaria mercenaria) haemocytes. Fish Shellfish Immunol 2007; 23:188-196. (Pubitemid 46635176)
    • (2007) Fish and Shellfish Immunology , vol.23 , Issue.1 , pp. 188-196
    • Bugge, D.M.1    Hegaret, H.2    Wikfors, G.H.3    Allam, B.4
  • 19
    • 0029155874 scopus 로고
    • Role of lectins (C-reactive protein) in defense of marine bivalves against bacteria
    • Olafsen JA. Role of lectins (C-reactive protein) in defense of marine bivalves against bacteria. Adv Exp MedBiol 1995; 371A:343-348.
    • (1995) Adv Exp MedBiol , vol.371 A , pp. 343-348
    • Olafsen, J.A.1
  • 20
    • 66149141443 scopus 로고    scopus 로고
    • Infestation of the cupped oysters Crassostrea angulata, C. gigas and their first-generation hybrids by the copepod Myicola ostreae: Differences in susceptibility and host response
    • Batista FM, Boudry P, Dos Santos A et al. Infestation of the cupped oysters Crassostrea angulata, C. gigas and their first-generation hybrids by the copepod Myicola ostreae: Differences in susceptibility and host response. Parasitology 2009; 136:537-543.
    • (2009) Parasitology , vol.136 , pp. 537-543
    • Batista, F.M.1    Boudry, P.2    Dos Santos, A.3
  • 21
    • 0036802913 scopus 로고    scopus 로고
    • Histological analysis of trematodes in Dreissena polymorpha: Their location, pathogenicity, and distinguishing morphological characteristics
    • Laruelle F, Molloy DP, Roitman VA. Histological analysis of trematodes in Dreissena polymorpha: Their location, pathogenicity and distinguishing morphological characteristics. J Parasitol 2002; 88:856-863. (Pubitemid 35278728)
    • (2002) Journal of Parasitology , vol.88 , Issue.5 , pp. 856-863
    • Laruelle, F.1    Molloy, D.P.2    Roitman, V.A.3
  • 23
    • 0037066502 scopus 로고    scopus 로고
    • Decoding the patterns of self and nonself by the innate immune system
    • DOI 10.1126/science.1068883
    • Medzhitov R, Janeway CA, Jr. Decoding the patterns of self and nonself by the innate immune system. Science 2002; 296:298-300. (Pubitemid 34303673)
    • (2002) Science , vol.296 , Issue.5566 , pp. 298-300
    • Medzhitov, R.1    Janeway Jr., C.A.2
  • 24
    • 0033975869 scopus 로고    scopus 로고
    • Innate immune recognition: Mechanisms and pathways
    • DOI 10.1034/j.1600-065X.2000.917309.x
    • Medzhitov R, Janeway C, Jr. Innate immune recognition: Mechanisms and pathways. Immunol Rev 2000; 173:89-97. (Pubitemid 30095213)
    • (2000) Immunological Reviews , vol.173 , pp. 89-97
    • Medzhitov, R.1    Janeway Jr., C.2
  • 25
    • 64149116678 scopus 로고    scopus 로고
    • A novel peptidoglycan recognition protein containing a goose-type lysozyme domain from the Pacific oyster, Crassostrea gigas
    • Itoh N, Takahashi KG. A novel peptidoglycan recognition protein containing a goose-type lysozyme domain from the Pacific oyster, Crassostrea gigas. Mol Immunol 2009; 46:1768-1774.
    • (2009) Mol Immunol , vol.46 , pp. 1768-1774
    • Itoh, N.1    Takahashi, K.G.2
  • 26
    • 33846235195 scopus 로고    scopus 로고
    • Molecular cloning and mRNA expression of peptidoglycan recognition protein (PGRP) gene in bay scallop (Argopecten irradians, Lamarck 1819)
    • DOI 10.1016/j.dci.2006.09.001, PII S0145305X06001674
    • Ni D, Song L, Wu L et al. Molecular cloning and mRNA expression of peptidoglycan recognition protein (PGRP) gene in bay scallop (Argopecten irradians, Lamarck 1819). Dev Comp Immunol 2007; 31:548-558. (Pubitemid 46109040)
    • (2007) Developmental and Comparative Immunology , vol.31 , Issue.6 , pp. 548-558
    • Ni, D.1    Song, L.2    Wu, L.3    Chang, Y.4    Yu, Y.5    Qiu, L.6    Wang, L.7
  • 27
    • 67349265232 scopus 로고    scopus 로고
    • Expressed sequence tags from the zhikong scallop (Chlamys farreri): Discovery and annotation of host-defense genes
    • Wang L, Song L, Zhao J et al. Expressed sequence tags from the zhikong scallop (Chlamys farreri): Discovery and annotation of host-defense genes. Fish Shellfish Immunol 2009; 26:744-750.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 744-750
    • Wang, L.1    Song, L.2    Zhao, J.3
  • 28
    • 0037020201 scopus 로고    scopus 로고
    • Immunity-related genes and gene families in Anopheles gambiae
    • Christophides GK, Zdobnov E, Barillas-Mury C et al. Immunity-related genes and gene families in Anopheles gambiae. Science 2002; 298:159-165.
    • (2002) Science , vol.298 , pp. 159-165
    • Christophides, G.K.1    Zdobnov, E.2    Barillas-Mury, C.3
  • 29
    • 43049153222 scopus 로고    scopus 로고
    • Isolation, purification and characterization of beta-1,3-glucan binding protein from the plasma of marine mussel Perna viridis
    • Jayaraj SS, Thiagarajan R, Arumugam M et al. Isolation, purification and characterization of beta-1,3-glucan binding protein from the plasma of marine mussel Perna viridis. Fish Shellfish Immunol 2008; 24:715-725.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 715-725
    • Jayaraj, S.S.1    Thiagarajan, R.2    Arumugam, M.3
  • 30
    • 29144452851 scopus 로고    scopus 로고
    • The C-type lectin-like domain superfamily
    • DOI 10.1111/j.1742-4658.2005.05031.x
    • Zelensky AN, Gready JE. The C-type lectin-like domain superfamily. FEBS J 2005; 272:6179-6217. (Pubitemid 41815610)
    • (2005) FEBS Journal , vol.272 , Issue.24 , pp. 6179-6217
    • Zelensky, A.N.1    Gready, J.E.2
  • 31
    • 36749079907 scopus 로고    scopus 로고
    • Identification and tissue expression analysis of C-type lectin and galectin in the Pacific oyster, Crassostrea gigas
    • DOI 10.1016/j.cbpb.2007.09.004, PII S1096495907003533
    • Yamaura K, Takahashi KG, Suzuki T. Identification and tissue expression analysis of C-type lectin and galectin in the Pacific oyster, Crassostrea gigas. Comp Biochem Physiol B Biochem Mol Biol 2008; 149:168-175. (Pubitemid 350217044)
    • (2008) Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology , vol.149 , Issue.1 , pp. 168-175
    • Yamaura, K.1    Takahashi, K.G.2    Suzuki, T.3
  • 32
    • 33749147438 scopus 로고    scopus 로고
    • Characterization of a novel C-type lectin, Bombyx mori multibinding protein, from the B. mori hemolymph: Mechanism of wide-range microorganism recognition and role in immunity
    • Watanabe A, Miyazawa S, Kitami M et al. Characterization of a novel C-type lectin, Bombyx mori multibinding protein, from the B. mori hemolymph: Mechanism of wide-range microorganism recognition and role in immunity. J Immunol 2006; 177:4594-4604. (Pubitemid 44469791)
    • (2006) Journal of Immunology , vol.177 , Issue.7 , pp. 4594-4604
    • Watanabe, A.1    Miyazawa, S.2    Kitami, M.3    Tabunoki, H.4    Ueda, K.5    Sato, R.6
  • 33
    • 54849419068 scopus 로고    scopus 로고
    • Characterization, tissue expression and immunohistochemical localization of MCL3, a C-type lectin produced by Perkinsus olseni-infected Manila clams (Rudi tapes philippinarum)
    • Kim JY, Adhya M, Cho SK et al. Characterization, tissue expression and immunohistochemical localization of MCL3, a C-type lectin produced by Perkinsus olseni-infected Manila clams (Rudi tapes philippinarum). Fish Shellfish Immunol 2008; 25:598-603.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 598-603
    • Kim, J.Y.1    Adhya, M.2    Cho, S.K.3
  • 34
    • 41549145208 scopus 로고    scopus 로고
    • Purification and antibacterial characterization of a novel isoform of the Manila clam lectin (MCL-4) from the plasma of the Manila clam Ruditapes philippinarum
    • Takahashi KG, Kuroda T, Muroga K. Purification and antibacterial characterization of a novel isoform of the Manila clam lectin (MCL-4) from the plasma of the Manila clam, Ruditapes philippinarum. Comp Biochem Physiol B Biochem Mol Biol 2008; 150:45-52.
    • (2008) Comp Biochem Physiol B Biochem Mol Biol , vol.150 , pp. 45-52
    • Takahashi, K.G.1    Kuroda, T.2    Muroga, K.3
  • 35
    • 4143112349 scopus 로고    scopus 로고
    • Isolation and partial characterization of a calcium-dependent lectin (chiletin) from the haemolymph of the flat oyster, Ostrea chilensis
    • DOI 10.1016/j.fsi.2004.05.001, PII S1050464804000506
    • Minamikawa M, Hine M, Russell S et al. Isolation and partial characterization of a calcium-dependent lectin (chiletin) from the haemolymph of the flat oyster, Ostrea chilensis. Fish Shellfish Immunol 2004; 17:463-476. (Pubitemid 39081819)
    • (2004) Fish and Shellfish Immunology , vol.17 , Issue.5 , pp. 463-476
    • Minamikawa, M.1    Hine, M.2    Russell, S.3    Huber, P.4    Duignan, P.5    Lumsden, J.S.6
  • 36
    • 57649158620 scopus 로고    scopus 로고
    • High affinity interaction between a bivalve C-type lectin and a biantennary complex-type N-glycan revealed by crystallography and microcalorimetry
    • Gourdine JP, Cioci G, Miguet L et al. High affinity interaction between a bivalve C-type lectin and a biantennary complex-type N-glycan revealed by crystallography and microcalorimetry. J Biol Chem 2008; 283:30112-30120.
    • (2008) J Biol Chem , vol.283 , pp. 30112-30120
    • Gourdine, J.P.1    Cioci, G.2    Miguet, L.3
  • 37
    • 35548934271 scopus 로고    scopus 로고
    • A galectin of unique domain organization from hemocytes of the Eastern oyster (Crassostrea virginica) is a receptor for the protistan parasite Perkinsus marinus
    • Tasumi S, Vasta GR. A galectin of unique domain organization from hemocytes of the Eastern oyster (Crassostrea virginica) is a receptor for the protistan parasite Perkinsus marinus. J Immunol 2007; 179:3086-3098.
    • (2007) J Immunol , vol.179 , pp. 3086-3098
    • Tasumi, S.1    Vasta, G.R.2
  • 38
    • 74649085824 scopus 로고    scopus 로고
    • An immune responsive multidomain galectin from bay scallop Argopectens irradians
    • In Press, Corrected Proof
    • Song X, Zhang H, Zhao J et al. An immune responsive multidomain galectin from bay scallop Argopectens irradians. Fish and Shellfish Immunology 2010;In Press, Corrected Proof.
    • (2010) Fish and Shellfish Immunology
    • Song, X.1    Zhang, H.2    Zhao, J.3
  • 39
    • 46549085873 scopus 로고    scopus 로고
    • Noble tandem-repeat galectin of Manila clam Ruditapes philippinarum is induced upon infection with the protozoan parasite Perkinsus olseni
    • Kim JY, Kim YM, Cho SK et al. Noble tandem-repeat galectin of Manila clam Ruditapes philippinarum is induced upon infection with the protozoan parasite Perkinsus olseni. Dev Comp Immunol 2008; 32:1131-1141.
    • (2008) Dev Comp Immunol , vol.32 , pp. 1131-1141
    • Kim, J.Y.1    Kim, Y.M.2    Cho, S.K.3
  • 40
    • 0346157328 scopus 로고    scopus 로고
    • Thioester-containing proteins and insect immunity
    • DOI 10.1016/j.molimm.2003.10.010
    • Blandin S, Levashina EA. Thioester-containing proteins and insect immunity. Mol Immunol 2004; 40:903-908. (Pubitemid 38032813)
    • (2004) Molecular Immunology , vol.40 , Issue.12 , pp. 903-908
    • Blandin, S.1    Levashina, E.A.2
  • 41
    • 60649110212 scopus 로고    scopus 로고
    • Characterization of a C3 and a factor B-like in the carpet-shell clam, Ruditapes decussatus
    • Prado-Alvarez M, Rotllant J, Gestal C et al. Characterization of a C3 and a factor B-like in the carpet-shell clam, Ruditapes decussatus. Fish Shellfish Immunol 2009; 26:305-315.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 305-315
    • Prado-Alvarez, M.1    Rotllant, J.2    Gestal, C.3
  • 42
    • 34248582388 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a thioester-containing protein from Zhikong scallop Chlamys farreri
    • DOI 10.1016/j.molimm.2007.03.008, PII S0161589007001204
    • Zhang H, Song L, Li C et al. Molecular cloning and characterization of a thioester-containing protein from Zhikong scallop Chlamys farreri. Mol Immunol 2007; 44:3492-3500. (Pubitemid 46754439)
    • (2007) Molecular Immunology , vol.44 , Issue.14 , pp. 3492-3500
    • Zhang, H.1    Song, L.2    Li, C.3    Zhao, J.4    Wang, H.5    Gao, Q.6    Xu, W.7
  • 43
    • 25844487754 scopus 로고    scopus 로고
    • Characterization of a C3-like cDNA in a coral: Phylogenetic implications
    • DOI 10.1007/s00251-005-0005-1
    • Dishaw LJ, Smith SL, Bigger CH. Characterization of a C3-like cDNA in a coral: Phylogenetic implications. Immunogenetics 2005; 57:535-548. (Pubitemid 41397192)
    • (2005) Immunogenetics , vol.57 , Issue.7 , pp. 535-548
    • Dishaw, L.J.1    Smith, S.L.2    Bigger, C.H.3
  • 44
    • 67650220906 scopus 로고    scopus 로고
    • The genomic structure, alternative splicing and immune response of Chlamys farreri thioester-containing protein
    • Zhang H, Wang L, Song L et al. The genomic structure, alternative splicing and immune response of Chlamys farreri thioester-containing protein. Dev Comp Immunol 2009.
    • (2009) Dev Comp Immunol
    • Zhang, H.1    Wang, L.2    Song, L.3
  • 45
    • 4544382185 scopus 로고    scopus 로고
    • The role of scavenger receptors in pathogen recognition and innate immunity
    • DOI 10.1016/j.imbio.2004.02.004
    • Mukhopadhyay S, Gordon S. The role of scavenger receptors in pathogen recognition and innate immunity. Immunobiology 2004; 209:39-49. (Pubitemid 39255690)
    • (2004) Immunobiology , vol.209 , Issue.1-2 , pp. 39-49
    • Mukhopadhyay, S.1    Gordon, S.2
  • 46
    • 4143143353 scopus 로고    scopus 로고
    • Discovery of genes expressed in response to Perkinsus marinus challenge in Eastern (Crassostrea virginica) and Pacific (C. gigas) oysters
    • DOI 10.1016/j.gene.2004.05.019, PII S0378111904003105
    • Tanguy A, Guo X, Ford SE. Discovery of genes expressed in response to Perkinsus marinus challenge in Eastern (Crassostrea virginica) and Pacific (C. gigas) oysters. Gene 2004; 338:121-131. (Pubitemid 39092418)
    • (2004) Gene , vol.338 , Issue.1 , pp. 121-131
    • Tanguy, A.1    Guo, X.2    Ford, S.E.3
  • 47
    • 33646476745 scopus 로고    scopus 로고
    • Development of expressed sequence tags from the bay scallop Argopecten irradians irradians
    • Song L, Xu W, Li C et al. Development of expressed sequence tags from the bay scallop, Argopecten irradians irradians. Mar Biotechnol (NY) 2006; 8:161-169.
    • (2006) Mar Biotechnol (NY) , vol.8 , pp. 161-169
    • Song, L.1    Xu, W.2    Li, C.3
  • 48
    • 70349696510 scopus 로고    scopus 로고
    • Identification and expression of differentially expressed genes in the hard clam, Mercenaria mercenaria, in response to quahog parasite unknown (QPX)
    • Mickael Perrigault ATaBA.
    • Mickael Perrigault ATaBA. Identification and expression of differentially expressed genes in the hard clam, Mercenaria mercenaria, in response to quahog parasite unknown (QPX). BMC Genomics 2009; 10.
    • (2009) BMC Genomics , vol.10
  • 49
    • 33846561574 scopus 로고    scopus 로고
    • Molecular cloning and expression of a Toll receptor gene homologue from Zhikong Scallop, Chlamys farreri
    • DOI 10.1016/j.fsi.2006.05.003, PII S1050464806000878
    • Qiu L, Song L, Xu W et al. Molecular cloning and expression of a Toll receptor gene homologue from Zhikong Scallop, Chlamys farreri. Fish Shellfish Immunol 2007; 22:451-466. (Pubitemid 46176642)
    • (2007) Fish and Shellfish Immunology , vol.22 , Issue.5 , pp. 451-466
    • Qiu, L.1    Song, L.2    Xu, W.3    Ni, D.4    Yu, Y.5
  • 50
    • 27844487939 scopus 로고    scopus 로고
    • The NF-kappaB pathway
    • Moynagh PN. The NF-kappaB pathway. J Cell Sci 2005; 118:4589-4592.
    • (2005) J Cell Sci , vol.118 , pp. 4589-4592
    • Moynagh, P.N.1
  • 51
    • 0036781052 scopus 로고    scopus 로고
    • NF-kappaB regulation in the immune system
    • Li Q, Verma IM. NF-kappaB regulation in the immune system. Nat Rev Immunol 2002; 2:725-734.
    • (2002) Nat Rev Immunol , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 52
    • 36549033242 scopus 로고    scopus 로고
    • Cg-IκB, a new member of the IκB protein family characterized in the pacific oyster Crassostrea gigas
    • DOI 10.1016/j.dci.2007.06.001, PII S0145305X07000900
    • Montagnani C, Labreuche Y, Escoubas J. Cg-IĚB, anew member of the IĚB protein family characterized in the pacific oyster Crassostrea gigas. Developmental and Comparative Immunology 2008; 32:182-190. (Pubitemid 350180078)
    • (2008) Developmental and Comparative Immunology , vol.32 , Issue.3 , pp. 182-190
    • Montagnani, C.1    Labreuche, Y.2    Escoubas, J.M.3
  • 53
    • 34547225981 scopus 로고    scopus 로고
    • Pf-Rel, a rel/nuclear factor-κB homolog identified from the pearl oyster, pinctada fucata
    • DOI 10.1111/j.1745-7270.2007.00306.x
    • Wu X, Xiong X, Xie L et al. Pf-Rel, a Rel/nuclear factor-kappaB homolog identified from the pearl oyster, Pinctada fucata. Acta Biochim Biophys Sin (Shanghai) 2007; 39:533-539. (Pubitemid 47117603)
    • (2007) Acta Biochimica et Biophysica Sinica , vol.39 , Issue.7 , pp. 533-539
    • Wu, X.1    Xiong, X.2    Xie, L.3    Zhang, R.4
  • 54
    • 36349024341 scopus 로고    scopus 로고
    • Cloning and characterization of an IKK homologue from pearl oyster, Pinctada fucata
    • DOI 10.1016/j.dci.2007.03.013, PII S0145305X07000663
    • Xiong X, Feng Q, Chen L et al. Cloning and characterization of an IKKK homologue from pearl oyster, Pinctada fucata. Dev Comp Immunol 2008; 32:15-25. (Pubitemid 350160912)
    • (2008) Developmental and Comparative Immunology , vol.32 , Issue.1 , pp. 15-25
    • Xiong, X.1    Feng, Q.2    Chen, L.3    Xie, L.4    Zhang, R.5
  • 55
    • 59549084520 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of the IkappaB gene from pearl oyster Pinctada fucata
    • Zhang D, Jiang S, Qiu L et al. Molecular characterization and expression analysis of the IkappaB gene from pearl oyster Pinctada fucata. Fish Shellfish Immunol 2009; 26:84-90.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 84-90
    • Zhang, D.1    Jiang, S.2    Qiu, L.3
  • 56
    • 34249341697 scopus 로고    scopus 로고
    • Distinct signalling pathways promote phagocytosis of bacteria, latex beads and lipopolysaccharide in medfly haemocytes
    • DOI 10.1111/j.1365-2567.2007.02576.x
    • Lamprou I, Mamali I, Dallas K et al. Distinct signalling pathways promote phagocytosis of bacteria, latex beads and lipopolysaccharide in medfly haemocytes. Immunology 2007; 121:314-327. (Pubitemid 46817353)
    • (2007) Immunology , vol.121 , Issue.3 , pp. 314-327
    • Lamprou, I.1    Mamali, I.2    Dallas, K.3    Fertakis, V.4    Lampropoulou, M.5    Marmaras, V.J.6
  • 57
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK JNK and p38 protein kinases
    • Johnson G, Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK and p38 protein kinases. Science's STKE2002; 298:1911.
    • (2002) Science's STKE , vol.298 , pp. 1911
    • Johnson, G.1    Lapadat, R.2
  • 58
    • 0742288805 scopus 로고    scopus 로고
    • Tyrosine kinase-mediated cell signalling in the activation of Mytilus hemocytes: Possible role of STAT-like proteins
    • DOI 10.1016/j.biolcel.2003.09.006, PII S0248490003001308
    • Canesi L, Betti M, Ciacci C et al. Tyrosine kinase-mediated cell signalling in the activation of Mytilus hemocytes: Possible role of STAT-like proteins. Biol Cell 2003; 95:603-613. (Pubitemid 38145777)
    • (2003) Biology of the Cell , vol.95 , Issue.9 , pp. 603-613
    • Canesi, L.1    Betti, M.2    Ciacci, C.3    Citterio, B.4    Pruzzo, C.5    Gallo, G.6
  • 59
    • 33746283951 scopus 로고    scopus 로고
    • Analysis of EST and lectin expressions in hemocytes of Manila clams (Ruditapes philippinarum) (Bivalvia: Mollusca) infected with Perkinsus olseni
    • Kang YS, Kim YM, Park KI et al. Analysis of EST and lectin expressions in hemocytes of Manila clams (Ruditapes philippinarum) (Bivalvia: Mollusca) infected with Perkinsus olseni. Dev Comp Immunol 2006; 30:1119-1131.
    • (2006) Dev Comp Immunol , vol.30 , pp. 1119-1131
    • Kang, Y.S.1    Kim, Y.M.2    Park, K.I.3
  • 62
    • 34447264484 scopus 로고    scopus 로고
    • Identification and characterization of a myeloid differentiation factor 88 (MyD88) cDNA from Zhikong scallop Chlamys farreri
    • DOI 10.1016/j.fsi.2007.01.012, PII S1050464807000198
    • Qiu L, Song L, Yu Y et al. Identification and characterization of a myeloid differentiation factor 88 (MyD88) cDNA from Zhikong scallop Chlamys farreri. Fish Shellfish Immunol 2007; 23:614-623. (Pubitemid 47048739)
    • (2007) Fish and Shellfish Immunology , vol.23 , Issue.3 , pp. 614-623
    • Qiu, L.1    Song, L.2    Yu, Y.3    Xu, W.4    Ni, D.5    Zhang, Q.6
  • 64
    • 62749142959 scopus 로고    scopus 로고
    • Identification and expression of TRAF6 (TNF receptor-associated factor 6) gene in Zhikong scallop Chlamys farreri
    • Qiu L, Song L, Yu Y et al. Identification and expression of TRAF6 (TNF receptor-associated factor 6) gene in Zhikong scallop Chlamys farreri. Fish Shellfish Immunol 2009; 26:359-367.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 359-367
    • Qiu, L.1    Song, L.2    Yu, Y.3
  • 65
    • 58849084605 scopus 로고    scopus 로고
    • Analysis of genes isolated from plated hemocytes of the pacific oyster crassostreas gigas
    • Goetz SRGGSWF
    • Goetz SRGGSWF. Analysis of Genes Isolated from Plated Hemocytes of the Pacific Oyster, Crassostreas gigas. Mar Biotechnol (NY) 2009; 11:24-44.
    • (2009) Mar Biotechnol (NY) , vol.11 , pp. 24-44
  • 66
    • 79960705311 scopus 로고    scopus 로고
    • The human complement system in health and disease
    • Morgan BP. The Human Complement System in Health and Disease. Annals of the Rheumatic Diseases 1998; 57:581-581.
    • (1998) Annals of the Rheumatic Diseases , vol.57 , pp. 581-581
    • Morgan, B.P.1
  • 68
    • 60649110212 scopus 로고    scopus 로고
    • Characterization of a C3 and a factor B-like in the carpet-shell clam, Ruditapes decussatus
    • Prado-Alvarez M, Rotllant J, Gestal C et al. Characterization of a C3 and a factor B-like in the carpet-shell clam, Ruditapes decussatus. Fish and Shellfish Immunology 2009; 26:305-315.
    • (2009) Fish and Shellfish Immunology , vol.26 , pp. 305-315
    • Prado-Alvarez, M.1    Rotllant, J.2    Gestal, C.3
  • 69
    • 50149106793 scopus 로고    scopus 로고
    • A novel C1 q-domain-containing protein from Zhikong scallop Chlamys farreri with lipopolysaccharide binding activity
    • Zhang H, Song L, Li C et al. A novel C1 q-domain-containing protein from Zhikong scallop Chlamys farreri with lipopolysaccharide binding activity. Fish and Shellfish Immunology 2008.
    • (2008) Fish and Shellfish Immunology
    • Zhang, H.1    Song, L.2    Li, C.3
  • 70
    • 59349095036 scopus 로고    scopus 로고
    • A fibrinogen-related protein from bay scallop Argopecten irradians involved in innate immunity as pattern recognition receptor
    • Zhang H, Wang L, Song L et al. A fibrinogen-related protein from bay scallop Argopecten irradians involved in innate immunity as pattern recognition receptor. Fish Shellfish Immunol 2009; 26:56-64.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 56-64
    • Zhang, H.1    Wang, L.2    Song, L.3
  • 71
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: From invertebrates to vertebrates
    • DOI 10.1111/j.0105-2896.2004.0124.x
    • Bulet P, Stocklin R, Menin L. Anti-microbial peptides: From invertebrates to vertebrates. Immunol Rev 2004; 198:169-184. (Pubitemid 38406943)
    • (2004) Immunological Reviews , vol.198 , pp. 169-184
    • Bulet, P.1    Stocklin, R.2    Menin, L.3
  • 72
    • 70349146147 scopus 로고    scopus 로고
    • A review of advances in research on marine molluscan antimicrobial peptides and their potential application in aquaculture
    • Li C, Zhao J, Song L. A review of advances in research on marine molluscan antimicrobial peptides and their potential application in aquaculture. Molluscan Research 2009; 29:17-26.
    • (2009) Molluscan Research , vol.29 , pp. 17-26
    • Li, C.1    Zhao, J.2    Song, L.3
  • 73
    • 0034672657 scopus 로고    scopus 로고
    • Original involvement of antimicrobial peptides in mussel innate immunity
    • MittaG, Vandenbulcke F, Roch P. Original involvement of antimicrobial peptides in mussel innate immunity. FEBS Lett 2000; 486:185-190.
    • (2000) FEBS Lett , vol.486 , pp. 185-190
    • Mitta, G.1    VanDenbulcke, F.2    Roch, P.3
  • 74
    • 54849430925 scopus 로고    scopus 로고
    • Evidence of high individual diversity on myticin C in mussel (Mytilus galloprovincialis)
    • Costa MM, Dios S, Alonso-Gutierrez J et al. Evidence of high individual diversity on myticin C in mussel (Mytilus galloprovincialis). Dev Comp Immunol 2009; 33:162-170.
    • (2009) Dev Comp Immunol , vol.33 , pp. 162-170
    • Costa, M.M.1    Dios, S.2    Alonso-Gutierrez, J.3
  • 75
    • 0029810861 scopus 로고    scopus 로고
    • Innate immunity: Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis
    • DOI 10.1074/jbc.271.36.21808
    • Charlet M, Chernysh S, Philippe H et al. Innate immunity. Isolation of several cysteine-rich antimicrobial peptides from the blood of a mollusc, Mytilus edulis. J Biol Chem 1996; 271:21808-21813. (Pubitemid 26303799)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.36 , pp. 21808-21813
    • Charlet, M.1    Chernysh, S.2    Philippe, H.3    Hetru, C.4    Hoffmann, J.A.5    Bulet, P.6
  • 77
    • 33747829917 scopus 로고    scopus 로고
    • Molecular cloning, expression of a big defensin gene from bay scallop Argopecten irradians and the antimicrobial activity of its recombinant protein
    • DOI 10.1016/j.molimm.2006.02.025, PII S0161589006000800
    • Zhao J, Song L, Li C et al. Molecular cloning, expression of a big defensin gene from bay scallop Argopecten irradians and the antimicrobial activity of its recombinant protein. Mol Immunol 2007; 44:360-368. (Pubitemid 44287059)
    • (2007) Molecular Immunology , vol.44 , Issue.4 , pp. 360-368
    • Zhao, J.1    Song, L.2    Li, C.3    Ni, D.4    Wu, L.5    Zhu, L.6    Wang, H.7    Xu, W.8
  • 78
    • 0029687175 scopus 로고    scopus 로고
    • Animal lysozymes c and g: An overview
    • Prager EM, Jolles P. Animal lysozymes c and g: An overview. EXS 1996; 75:9-31.
    • (1996) EXS , vol.75 , pp. 9-31
    • Prager, E.M.1    Jolles, P.2
  • 80
    • 33748862602 scopus 로고    scopus 로고
    • Molecular cloning of an invertebrate goose-type lysozyme gene from Chlamys farreri, and lytic activity of the recombinant protein
    • DOI 10.1016/j.molimm.2006.06.008, PII S0161589006002161
    • Zhao J, Song L, Li C et al. Molecular cloning of an invertebrate goose-type lysozyme gene from Chlamys farreri and lytic activity of the recombinant protein. Mol Immunol 2007; 44:1198-1208. (Pubitemid 44419577)
    • (2007) Molecular Immunology , vol.44 , Issue.6 , pp. 1198-1208
    • Zhao, J.1    Song, L.2    Li, C.3    Zou, H.4    Ni, D.5    Wang, W.6    Xu, W.7
  • 81
    • 0033402852 scopus 로고    scopus 로고
    • Protein purification and gene isolation of chlamysin, a cold-active lysozyme-like enzyme with antibacterial activity
    • DOI 10.1016/S0014-5793(99)01693-2, PII S0014579399016932
    • Nilsen IW, Overbo K, Sandsdalen E et al. Protein purification and gene isolation of chlamysin, a cold-active lysozyme-like enzyme with antibacterial activity. FEBS Lett 1999; 464:153-158. (Pubitemid 30017933)
    • (1999) FEBS Letters , vol.464 , Issue.3 , pp. 153-158
    • Nilsen, I.W.1    Overbo, K.2    Sandsdalen, E.3    Sandaker, E.4    Sletten, K.5    Myrnes, B.6
  • 82
    • 3142643627 scopus 로고    scopus 로고
    • Determination of the complete cDNA sequence, construction of expression systems, and elucidation of fibrinolytic activity for Tapes japonica lysozyme
    • DOI 10.1016/j.pep.2004.05.001, PII S1046592804001536
    • Takeshita K, Hashimoto Y, Thujihata Y et al. Determination of the complete cDNA sequence, construction of expression systems and elucidation of fibrinolytic activity for Tapes japonica lysozyme. Protein Expr Purif 2004; 36:254-262. (Pubitemid 38893163)
    • (2004) Protein Expression and Purification , vol.36 , Issue.2 , pp. 254-262
    • Takeshita, K.1    Hashimoto, Y.2    Thujihata, Y.3    So, T.4    Ueda, T.5    Iomoto, T.6
  • 85
    • 0020010099 scopus 로고
    • Characterization of the lysozyme of Mytilus edulis (L)
    • McHenery JG, Birkbeck TH. Characterization of the lysozyme of Mytilus edulis (L). Comp Biochem PhysiolB 1982; 71:583-589.
    • (1982) Comp Biochem PhysiolB , Issue.71 , pp. 583-589
    • McHenery, J.G.1    Birkbeck, T.H.2
  • 86
    • 1842844345 scopus 로고    scopus 로고
    • Purification and characterisation of a lectin isolated from the Manila clam Ruditapes philippinarum in Korea
    • DOI 10.1016/j.fsi.2003.08.006
    • Bulgakov AA, Park KI, Choi KS et al. Purification and characterisation of a lectin isolated from the Manila clam Ruditapes philippinarum in Korea. Fish Shellfish Immunol 2004; 16:487-499. (Pubitemid 38484977)
    • (2004) Fish and Shellfish Immunology , vol.16 , Issue.4 , pp. 487-499
    • Bulgakov, A.A.1    Park, K.-I.2    Choi, K.-S.3    Lim, H.-K.4    Cho, M.5
  • 87
    • 33846671423 scopus 로고    scopus 로고
    • Analysis of a cDNA-derived sequence of a novel mannose-binding lectin, codakine, from the tropical clam Codakia orbicularis
    • DOI 10.1016/j.fsi.2006.06.013, PII S1050464806001203
    • Gourdine JP, Smith-Ravin EJ. Analysis of a cDNA-derived sequence of a novel mannose-binding lectin, codakine, from the tropical clam Codakia orbicularis. Fish Shellfish Immunol 2007; 22:498-509. (Pubitemid 46188405)
    • (2007) Fish and Shellfish Immunology , vol.22 , Issue.5 , pp. 498-509
    • Gourdine, J.-P.1    Smith-Ravin, E.J.2
  • 88
    • 0026163409 scopus 로고
    • Agglutination of bacteria and erythrocytes by serum from six species of marine molluscs
    • Fisher WS, DiNuzzo AR. Agglutination of bacteria and erythrocytes by serum from six species of marine molluscs. J Invertebr Pathol 1991; 57:380-394.
    • (1991) J Invertebr Pathol , vol.57 , pp. 380-394
    • Fisher, W.S.1    DiNuzzo, A.R.2
  • 89
    • 0026639046 scopus 로고
    • Agglutinin activity in Pacific oyster (Crassostrea gigas) hemolymph following in vivo Vibrio anguillarum challenge
    • Olafsen JA, Fletcher TC, Grant PT. Agglutinin activity in Pacific oyster (Crassostrea gigas) hemolymph following in vivo Vibrio anguillarum challenge. Dev Comp Immunol 1992; 16:123-138.
    • (1992) Dev Comp Immunol , vol.16 , pp. 123-138
    • Olafsen, J.A.1    Fletcher, T.C.2    Grant, P.T.3
  • 90
    • 67349154111 scopus 로고    scopus 로고
    • Purification and characterization of an N-acetylglucosamine specific lectin from marine bivalve Macoma birmanica
    • Adhya M, Singha B, Chatterjee BP. Purification and characterization of an N-acetylglucosamine specific lectin from marine bivalve Macoma birmanica. Fish Shellfish Immunol 2009; 27:1-8.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 1-8
    • Adhya, M.1    Singha, B.2    Chatterjee, B.P.3
  • 91
    • 41949142619 scopus 로고    scopus 로고
    • Rapid accumulation of an interleukin 17 homolog transcript in Crassostrea gigas hemocytes following bacterial exposure
    • Roberts S, Gueguen Y, de Lorgeril J et al. Rapid accumulation of an interleukin 17 homolog transcript in Crassostrea gigas hemocytes following bacterial exposure. Dev Comp Immunol 2008; 32:1099-1104.
    • (2008) Dev Comp Immunol , vol.32 , pp. 1099-1104
    • Roberts, S.1    Gueguen, Y.2    De Lorgeril, J.3
  • 92
    • 0025321965 scopus 로고
    • Interaction of immunoactive monokines (interleukin 1 and tumor necrosis factor) in the bivalve mollusc Mytilus edulis
    • Hughes TK, Jr., Smith EM, Chin R et al. Interaction of immunoactive monokines (interleukin 1 and tumor necrosis factor) in the bivalve mollusc Mytilus edulis. Proc Natl Acad Sci USA 1990; 87:4426-4429.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4426-4429
    • Hughes Jr., T.K.1    Smith, E.M.2    Chin, R.3
  • 93
    • 1842841276 scopus 로고    scopus 로고
    • Invertebrate humoral factors: Cytokines as mediators of cell survival
    • Ottaviani E, Malagoli D, Franchini A. Invertebrate humoral factors: Cytokines as mediators of cell survival. Prog Mol Subcell Biol 2004; 34:1-25.
    • (2004) Prog Mol Subcell Biol , vol.34 , pp. 1-25
    • Ottaviani, E.1    Malagoli, D.2    Franchini, A.3
  • 95
    • 70350128771 scopus 로고    scopus 로고
    • First molluscan TNFRR homologue in Zhikong scallop: Molecular characterization and expression analysis
    • Li L, Qiu L, Song L et al. First molluscan TNFRR homologue in Zhikong scallop: Molecular characterization and expression analysis. Fish Shellfish Immunol 2009; 27:625-632.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 625-632
    • Li, L.1    Qiu, L.2    Song, L.3
  • 96
    • 16244414843 scopus 로고    scopus 로고
    • Structural and functional evidences for a type 1 TGF-β sensu stricto receptor in the lophotrochozoan Crassostrea gigas suggest conserved molecular mechanisms controlling mesodermal patterning across bilateria
    • DOI 10.1016/j.mod.2004.12.004
    • Herpin CLA, Becker T, Rosa FM et al. Structural and functional evidences for a type 1 TGF-p sensu stricto receptor in the lophotrochozoan Crassostrea gigas suggest conserved molecular mechanisms controlling mesodermal patterning across bilateria. Mechanisms of Development 2005; 122:695-705. (Pubitemid 40462516)
    • (2005) Mechanisms of Development , vol.122 , Issue.5 , pp. 695-705
    • Herpin, A.1    Lelong, C.2    Becker, T.3    Rosa, F.M.4    Favrel, P.5    Cunningham, C.6
  • 97
    • 0034997645 scopus 로고    scopus 로고
    • The ancestral complement system in sea urchins
    • DOI 10.1034/j.1600-065X.2001.1800102.x
    • Smith LC, Clow LA, Terwilliger DP. The ancestral complement system in sea urchins. Immunol Rev 2001; 180:16-34. (Pubitemid 32472849)
    • (2001) Immunological Reviews , vol.180 , pp. 16-34
    • Smith, L.C.1    Clow, L.A.2    Terwilliger, D.P.3
  • 98
    • 14644437730 scopus 로고    scopus 로고
    • Reactive oxygen species and development in microbial eukaryotes
    • DOI 10.1016/j.tim.2005.01.007
    • Aguirre J MM, Hewitt D, Hansberg W. Reactive oxygen species and development in microbial eukaryotes. Trends Microbiol 2005; 13:111-118. (Pubitemid 40311893)
    • (2005) Trends in Microbiology , vol.13 , Issue.3 , pp. 111-118
    • Aguirre, J.1    Rios-Momberg, M.2    Hewitt, D.3    Hansberg, W.4
  • 99
    • 0025805767 scopus 로고
    • Oxidants and antioxidants in aquatic animals
    • Winston GW. Oxidants and antioxidants in aquatic animals. Comp Biochem Physiol C 1991; 100:173-176.
    • (1991) Comp Biochem Physiol C , vol.100 , pp. 173-176
    • Winston, G.W.1
  • 100
    • 51249098717 scopus 로고    scopus 로고
    • The manganese superoxide dismutase gene in bay scallop Argopecten irradians: Cloning, 3D modelling and mRNA expression
    • Bao Y, Li L, Zhang G. The manganese superoxide dismutase gene in bay scallop Argopecten irradians: Cloning, 3D modelling and mRNA expression. Fish Shellfish Immunol 2008; 25:425-432.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 425-432
    • Bao, Y.1    Li, L.2    Zhang, G.3
  • 101
    • 34848825900 scopus 로고    scopus 로고
    • Effects of the toxic dinoflagellate, Gymnodinium catenatum on hydrolytic and antioxidant enzymes, in tissues of the giant lions-paw scallop Nodipecten subnodosus
    • DOI 10.1016/j.cbpc.2007.06.003, PII S1532045607001445
    • Estrada N, de Jesus Romero M, Campa-Cordova A et al. Effects of the toxic dinoflagellate, Gymnodinium catenatum on hydrolytic and antioxidant enzymes, in tissues of the giant lions-paw scallop Nodipecten subnodosus. Comp Biochem Physiol C Toxicol Pharmacol 2007; 146:502-510. (Pubitemid 47500150)
    • (2007) Comparative Biochemistry and Physiology - C Toxicology and Pharmacology , vol.146 , Issue.4 , pp. 502-510
    • Estrada, N.1    De Jesus Romero, M.2    Campa-Cordova, A.3    Luna, A.4    Ascencio, F.5
  • 102
    • 55949101724 scopus 로고    scopus 로고
    • Variations of enzyme activities in the haemocytes of scallop Chlamys farreri after infection with the acute virus necrobiotic virus (AVNV)
    • Xing J, Lin T, Zhan W. Variations of enzyme activities in the haemocytes of scallop Chlamys farreri after infection with the acute virus necrobiotic virus (AVNV). Fish Shellfish Immunol 2008; 25:847-852.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 847-852
    • Xing, J.1    Lin, T.2    Zhan, W.3
  • 103
    • 35348911184 scopus 로고    scopus 로고
    • Integrated use of biomarkers (superoxide dismutase, catalase and lipidperoxidation) in mussels Mytilus galloprovincialis for assessing heavy metals' pollution in coastal areas from the Saronikos Gulf of Greece
    • Vlahogianni T, Dassenakis M, Scoullos MJ et al. Integrated use of biomarkers (superoxide dismutase, catalase and lipidperoxidation) in mussels Mytilus galloprovincialis for assessing heavy metals' pollution in coastal areas from the Saronikos Gulf of Greece. Mar Pollut Bull 2007; 54:1361-1371.
    • (2007) Mar Pollut Bull , vol.54 , pp. 1361-1371
    • Vlahogianni, T.1    Dassenakis, M.2    Scoullos, M.J.3
  • 104
    • 60649083146 scopus 로고    scopus 로고
    • Investigation of EROD CYP1A immunopositive proteins and SOD in haemocytes of Chamelea gallina and their role in response to B[a]P
    • Monari M, Foschi J, Matozzo V et al. Investigation of EROD, CYP1A immunopositive proteins and SOD in haemocytes of Chamelea gallina and their role in response to B[a]P. Comp Biochem Physiol C Toxicol Pharmacol 2009; 149:382-392.
    • (2009) Comp Biochem Physiol C Toxicol Pharmacol , vol.149 , pp. 382-392
    • Monari, M.1    Foschi, J.2    Matozzo, V.3
  • 105
    • 33750091061 scopus 로고    scopus 로고
    • Effects of high temperatures on functional responses of haemocytes in the clam Chamelea gallina
    • DOI 10.1016/j.fsi.2006.03.016, PII S1050464806000611
    • Monari M, Matozzo V, Foschi J et al. Effects of high temperatures on functional responses of haemocytes in the clam Chamelea gallina. Fish Shellfish Immunol 2007; 22:98-114. (Pubitemid 44584743)
    • (2007) Fish and Shellfish Immunology , vol.22 , Issue.1 , pp. 98-114
    • Monari, M.1    Matozzo, V.2    Foschi, J.3    Cattani, O.4    Serrazanetti, G.P.5    Marin, M.G.6
  • 107
    • 0842309140 scopus 로고    scopus 로고
    • Diversity of structures and properties among catalases
    • DOI 10.1007/s00018-003-3206-5
    • Chelikani P, Fita I, Loewen PC. Diversity of structures and properties among catalases. Cell Mol Life Sci 2004; 61:192-208. (Pubitemid 38183572)
    • (2004) Cellular and Molecular Life Sciences , vol.61 , Issue.2 , pp. 192-208
    • Chelikani, P.1    Fita, I.2    Loewen, P.C.3
  • 108
    • 0022179287 scopus 로고
    • The active center of catalase
    • DOI 10.1016/0022-2836(85)90180-9
    • Fita I, Rossmann MG. The active center of catalase. J Mol Biol 1985; 185:21-37. (Pubitemid 16250043)
    • (1985) Journal of Molecular Biology , vol.185 , Issue.1 , pp. 21-37
    • Fita, I.1    Rossmann, M.G.2
  • 109
    • 58649108537 scopus 로고    scopus 로고
    • Tidal height influences the levels of enzymatic antioxidant defences in Mytilus edulis
    • Letendre J, Chouquet B, Manduzio H et al. Tidal height influences the levels of enzymatic antioxidant defences in Mytilus edulis. Mar Environ Res 2009; 67:69-74.
    • (2009) Mar Environ Res , vol.67 , pp. 69-74
    • Letendre, J.1    Chouquet, B.2    Manduzio, H.3
  • 110
    • 67651232616 scopus 로고    scopus 로고
    • Biotransformation and antioxidant enzymes of Dreissena polymorpha for detection of site impact in watercourses of Berlin
    • Contardo-Jara V, Krueger A, Exner HJ et al. Biotransformation and antioxidant enzymes of Dreissena polymorpha for detection of site impact in watercourses of Berlin. J Environ Monit 2009; 11:1147-1156.
    • (2009) J Environ Monit , vol.11 , pp. 1147-1156
    • Contardo-Jara, V.1    Krueger, A.2    Exner, H.J.3
  • 112
    • 38349165108 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a catalase gene from Zhikong scallop Chlamys farreri
    • Li C, Ni D, Song L et al. Molecular cloning and characterization of a catalase gene from Zhikong scallop Chlamys farreri. Fish Shellfish Immunol 2008; 24:26-34.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 26-34
    • Li, C.1    Ni, D.2    Song, L.3
  • 113
    • 54949086680 scopus 로고    scopus 로고
    • Metallothionein coding sequence identification and seasonal mRNA expression of detoxification genes in the bivalve Corbicula fluminea
    • Bigot A, Doyen P, Vasseur P et al. Metallothionein coding sequence identification and seasonal mRNA expression of detoxification genes in the bivalve Corbicula fluminea. Ecotoxicol Environ Saf 2009: 72:382-387.
    • (2009) Ecotoxicol Environ Saf , vol.72 , pp. 382-387
    • Bigot, A.1    Doyen, P.2    Vasseur, P.3
  • 114
    • 63449109865 scopus 로고    scopus 로고
    • Antioxidant response of the bivalve Pinna nobilis colonised by invasive red macroalgae Lophocladia lallemandii
    • Box A, Sureda A, Deudero S. Antioxidant response of the bivalve Pinna nobilis colonised by invasive red macroalgae Lophocladia lallemandii. Comp Biochem Physiol C Toxicol Pharmacol 2009; 149:456-460.
    • (2009) Comp Biochem Physiol C Toxicol Pharmacol , vol.149 , pp. 456-460
    • Box, A.1    Sureda, A.2    Deudero, S.3
  • 115
    • 34548702054 scopus 로고    scopus 로고
    • Antioxidant enzyme complex of tissues of the bivalve Mytilus galloprovincialis Lam. under normal and oxidative-stress conditions: A review
    • Soldatov AA, Gostiukhina OL, Golovina IV. [Antioxidant enzyme complex of tissues of the bivalve Mytilus galloprovincialis Lam. under normal and oxidative-stress conditions: A review]. Prikl Biokhim Mikrobiol 2007; 43:621-628.
    • (2007) Prikl Biokhim Mikrobiol , vol.43 , pp. 621-628
    • Soldatov, A.A.1    Gostiukhina, O.L.2    Golovina, I.V.3
  • 116
    • 0036042619 scopus 로고    scopus 로고
    • Purification and partial characterization of seven glutathione S-transferase isoforms from the clam Ruditapes decussatus
    • DOI 10.1046/j.1432-1033.2002.03141.x
    • Hoarau P, Garello G, Gnassia-Barelli M et al. Purification and partial characterization of seven glutathione S-transferase isoforms from the clam Ruditapes decussatus. Eur J Biochem 2002; 269:4359-4366. (Pubitemid 35026022)
    • (2002) European Journal of Biochemistry , vol.269 , Issue.17 , pp. 4359-4366
    • Hoarau, P.1    Garello, G.2    Gnassia-Barelli, M.3    Romeo, M.4    Girard, J.-P.5
  • 117
    • 21044439424 scopus 로고    scopus 로고
    • The use of Mytilus Galloprovincialis acetylcholinesterase and glutathione S-transferases activities as biomarkers of environmental contamination along the northwest Portuguese coast
    • DOI 10.1007/s10661-005-3854-z
    • Moreira SM, Guilhermino L. The use of Mytilus galloprovincialis acetylcholinesterase and glutathione S-transferases activities as biomarkers of environmental contamination along the northwest Portuguese coast. Environ Monit Assess 2005; 105:309-325. (Pubitemid 40872334)
    • (2005) Environmental Monitoring and Assessment , vol.105 , Issue.1-3 , pp. 309-325
    • Moreira, S.M.1    Guilhermino, L.2
  • 118
    • 0037866875 scopus 로고    scopus 로고
    • Induction of glutathione-S-transferases in primary cultured digestive gland acini from the mollusk bivalve Pecten maximus (L.): Application of a new cellular model in biomonitoring studies
    • DOI 10.1016/S0166-445X(03)00041-9
    • Le Pennec G, Le Pennec M. Induction of glutathione-S-transferases in primary cultured digestive gland acini from the mollusk bivalve Pecten maximus (L.): Application of a new cellular model in biomonitoring studies. Aquat Toxicol 2003; 64:131-142. (Pubitemid 36683214)
    • (2003) Aquatic Toxicology , vol.64 , Issue.2 , pp. 131-142
    • Le Pennec, G.1    Le Pennec, M.2
  • 119
    • 40149107404 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression of heat shock protein 90 gene in the haemocytes of bay scallop Argopecten irradians
    • Gao Q, Zhao J, Song L et al. Molecular cloning, characterization and expression of heat shock protein 90 gene in the haemocytes of bay scallop Argopecten irradians. Fish Shellfish Immunol 2008: 24:379-385.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 379-385
    • Gao, Q.1    Zhao, J.2    Song, L.3
  • 120
    • 58649096133 scopus 로고    scopus 로고
    • Effects of elevated temperature and cadmium exposure on stress protein response in eastern oysters Crassostrea virginica (Gmelin)
    • Ivanina AV, Taylor C, Sokolova IM. Effects of elevated temperature and cadmium exposure on stress protein response in eastern oysters Crassostrea virginica (Gmelin). Aquat Toxicol 2009; 91:245-254.
    • (2009) Aquat Toxicol , vol.91 , pp. 245-254
    • Ivanina, A.V.1    Taylor, C.2    Sokolova, I.M.3
  • 121
    • 58149314027 scopus 로고    scopus 로고
    • Isolation and characterization of two cytoplasmic hsp90s from Mytilus galloprovincialis (Mollusca: Bivalvia) that contain a complex promoter with a p53 binding site
    • Pantzartzi CN, Kourtidis A, Drosopoulou E et al. Isolation and characterization of two cytoplasmic hsp90s from Mytilus galloprovincialis (Mollusca: Bivalvia) that contain a complex promoter with a p53 binding site. Gene 2009; 431:47-54.
    • (2009) Gene , vol.431 , pp. 47-54
    • Pantzartzi, C.N.1    Kourtidis, A.2    Drosopoulou, E.3
  • 123
    • 33750997854 scopus 로고    scopus 로고
    • Challenging the model for induction of metallothionein gene expression
    • DOI 10.1016/j.biochi.2006.07.021, PII S0300908406001659
    • Bourdineaud JP, Baudrimont M, Gonzalez P et al. Challenging the model for induction of metallothionein gene expression. Biochimie 2006; 88:1787-1792. (Pubitemid 44751342)
    • (2006) Biochimie , vol.88 , Issue.11 , pp. 1787-1792
    • Bourdineaud, J.-P.1    Baudrimont, M.2    Gonzalez, P.3    Moreau, J.-L.4
  • 124
    • 43049153212 scopus 로고    scopus 로고
    • Expression of metallothionein mRNAs by in situ hybridization in the gills of Mytilus galloprovincialis, from natural polluted environments
    • Fasulo S, Mauceri A, Giannetto A et al. Expression of metallothionein mRNAs by in situ hybridization in the gills of Mytilus galloprovincialis, from natural polluted environments. Aquat Toxicol 2008; 88:62-68.
    • (2008) Aquat Toxicol , vol.88 , pp. 62-68
    • Fasulo, S.1    Mauceri, A.2    Giannetto, A.3
  • 125
    • 56949088291 scopus 로고    scopus 로고
    • Alteration of metallothionein mRNA in bay scallop Argopecten irradians under cadmium exposure and bacteria challenge
    • Wang L, Song L, Ni D et al. Alteration of metallothionein mRNA in bay scallop Argopecten irradians under cadmium exposure and bacteria challenge. Comp Biochem Physiol C Toxicol Pharmacol 2009; 149:50-57.
    • (2009) Comp Biochem Physiol C Toxicol Pharmacol , vol.149 , pp. 50-57
    • Wang, L.1    Song, L.2    Ni, D.3


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