메뉴 건너뛰기




Volumn 708, Issue , 2010, Pages 239-259

Crustacean immunity

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; LECTIN; MESSENGER RNA; MONOPHENOL MONOOXYGENASE; PATTERN RECOGNITION RECEPTOR; PROPHENOL OXIDASE; UNCLASSIFIED DRUG;

EID: 79960731799     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-8059-5_13     Document Type: Article
Times cited : (141)

References (143)
  • 1
    • 33646495280 scopus 로고    scopus 로고
    • Cell-mediated immunity in arthropods: Hematopoiesis, coagulation and opsonization
    • Jiravanichpaisal P, Lee BL, Söderhäll K. Cell-mediated immunity in arthropods: Hematopoiesis, coagulation and opsonization. Immunobiol 2006; 211:213-236.
    • (2006) Immunobiol , vol.211 , pp. 213-236
    • Jiravanichpaisal, P.1    Lee, B.L.2    Söderhäll, K.3
  • 2
    • 0036076660 scopus 로고    scopus 로고
    • Early events in crustacean innate immunity
    • DOI 10.1006/fsim.2002.0420
    • Lee SY, Soderhall K. Early events in crustacean innate immunity. Fish Shellfish Immunol 2002: 12:421-437. (Pubitemid 34800929)
    • (2002) Fish and Shellfish Immunology , vol.12 , Issue.5 , pp. 421-437
    • Young Lee, S.1    Soderhall, K.2
  • 3
    • 40849102419 scopus 로고    scopus 로고
    • Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans
    • Smith VJ, Fernandes JMO, Kemp GD et al. Crustins: Enigmatic WAP domain-containing antibacterial proteins from crustaceans. Dev Comp Immunol 2008; 32:758-772.
    • (2008) Dev Comp Immunol , vol.32 , pp. 758-772
    • Smith, V.J.1    Fernandes, J.M.O.2    Kemp, G.D.3
  • 6
    • 52549093726 scopus 로고    scopus 로고
    • Sensing of dangersignals and pathogen-associated molecular patterns defines binary signaling pathways upstream of Toll
    • Chamy LE, Leclerc V, Caldelari I et al. Sensing of dangersignals and pathogen-associated molecular patterns defines binary signaling pathways upstream of Toll. Nature Immunol 2008; 9:1165-1170.
    • (2008) Nature Immunol , vol.9 , pp. 1165-1170
    • Chamy, L.E.1    Leclerc, V.2    Caldelari, I.3
  • 7
    • 0025351924 scopus 로고
    • Purification and characterization of a beta-1,3-Glucan binding-protein from plasma of the crayfish Pacifastacus leniusculus
    • Duvic B, Soderhall K. Purification and characterization of a beta-1,3-Glucan binding-protein from plasma of the crayfish Pacifastacus leniusculus. J Biol Chem 1990; 265:9327-9332.
    • (1990) J Biol Chem , vol.265 , pp. 9327-9332
    • Duvic, B.1    Soderhall, K.2
  • 8
    • 0028077775 scopus 로고    scopus 로고
    • Structure and biological activity of a 1,3-beta-D-glucan-binding protein in crustacean blood
    • Cerenius L, Liang ZC, Duvic B et al. Structure and biological activity of a 1,3-beta-D-glucan-binding protein in crustacean blood. J Biol Chem 2004; 269:29462-29467.
    • (2004) J Biol Chem , vol.269 , pp. 29462-29467
    • Cerenius, L.1    Liang, Z.C.2    Duvic, B.3
  • 9
    • 0343415656 scopus 로고    scopus 로고
    • A lipopolysaccharide- and β-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus. Purification, characterization, and cDNA cloning
    • DOI 10.1074/jbc.275.2.1337
    • Lee SY, Wang RG, Söderhäll K. A lipopolysaccharide- and beta-1,3-glucan-binding protein from hemocytes of the freshwater crayfish Pacifastacus leniusculus-Purification, characterization and cDNA cloning. J Biol Chem 2000; 275:1337-1343. (Pubitemid 30051190)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.2 , pp. 1337-1343
    • Lee, S.Y.1    Wang, R.2    Soderhall, K.3
  • 10
    • 0034616025 scopus 로고    scopus 로고
    • A cell adhesion protein from the crayfish Pacifastacus leniusculus, a serine proteinase homologue similar to Drosophila masquerade
    • DOI 10.1074/jbc.275.14.9996
    • Huang TS, Wang HY, Lee SY et al. A cell adhesion protein from the crayfish Pacifastacus leniusculus, a serine proteinase homologue similar to Drosophila masquerade. J Biol Chem 2000; 275:9996-10001. (Pubitemid 30202046)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 9996-10001
    • Huang, T.-S.1    Wang, H.2    Lee, S.Y.3    Johansson, M.W.4    Soderhall, K.5    Cerenius, L.6
  • 11
    • 0035877242 scopus 로고    scopus 로고
    • Characterization of a pattern recognition protein, a masquerade-like protein, in the freshwater crayfish Pacifastacus leniusculus
    • Lee SY, Söderhäll K. Characterization of a pattern recognition protein, a masquerade-like protein, in the freshwater crayfish Pacifastacus leniusculus. J Immunol 2001; 166:7319-7326. (Pubitemid 32525607)
    • (2001) Journal of Immunology , vol.166 , Issue.12 , pp. 7319-7326
    • Lee, S.Y.1    Soderhall, K.2
  • 12
    • 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
  • 13
    • 66149091989 scopus 로고    scopus 로고
    • The components of the Daphnia pulex immune system as revealed by complete genome sequencing
    • McTaggart SJ, Conlon C, Colbourne JKK et al. The components of the Daphnia pulex immune system as revealed by complete genome sequencing. BMC Genomics 2009; 10:175.
    • (2009) BMC Genomics , vol.10 , pp. 175
    • McTaggart, S.J.1    Conlon, C.2    Colbourne, J.K.K.3
  • 14
    • 55949135771 scopus 로고    scopus 로고
    • Gene expression profile of hemocytes of kuruma shrimp, Marsupenaeus japonicus following peptidoglycan stimulation
    • Fagutao FF, Yasuike M, Caipang CM et al. Gene expression profile of hemocytes of kuruma shrimp, Marsupenaeus japonicus following peptidoglycan stimulation Mar Biotech 2008; 10:731-740.
    • (2008) Mar Biotech , vol.10 , pp. 731-740
    • Fagutao, F.F.1    Yasuike, M.2    Caipang, C.M.3
  • 15
    • 1642463826 scopus 로고    scopus 로고
    • The prophenoloxidase activating system in invertebrates
    • Cerenius L, Söderhäll K. The prophenoloxidase activating system in invertebrates. Immunol Rev 2004; 198:72-82.
    • (2004) Immunol Rev , vol.198 , pp. 72-82
    • Cerenius, L.1    Söderhäll, K.2
  • 16
    • 67349234897 scopus 로고    scopus 로고
    • Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus monodon
    • Jitvaropas R, Amparyup P, Gross PS et al. Functional characterization of a masquerade-like serine proteinase homologue from the black tiger shrimp Penaeus monodon. Comp Biochem Physiol B 2009; 153:236-243.
    • (2009) Comp Biochem Physiol B , vol.153 , pp. 236-243
    • Jitvaropas, R.1    Amparyup, P.2    Gross, P.S.3
  • 17
    • 11544358874 scopus 로고    scopus 로고
    • Lectins: Carbohydrate-specific proteins that mediate cellular recognition
    • Lis H, Sharon N. Lectins: Carbohydrate-specific proteins that mediate cellular recognition. Chem Rev 1998; 98:1283-1297.
    • (1998) Chem Rev , vol.98 , pp. 1283-1297
    • Lis, H.1    Sharon, N.2
  • 18
    • 0037020201 scopus 로고    scopus 로고
    • Immunity-related genes and genes families in Anopheles gambiae
    • Christophides GK, Zdobnov E, Barillas-Mury C et al. Immunity-related genes and genes 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
  • 19
    • 2942617149 scopus 로고    scopus 로고
    • Immulectin-2, a pattern recognition receptor that stimulates hemocyte encapsulation and melanization in the tobacco hornworm, Manduca sexta
    • DOI 10.1016/j.dci.2004.02.005, PII S0145305X04000540
    • YuXQ, Kanost MR. Immulectin-2, apattern recognition receptor that stimulates haemocyte encapsulation and melanization in the tobacco hornworm, Manduca sexta. Dev Comp Immunol 2004; 28:891-900. (Pubitemid 38746429)
    • (2004) Developmental and Comparative Immunology , vol.28 , Issue.9 , pp. 891-900
    • Yu, X.-Q.1    Kanost, M.R.2
  • 20
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J Biol Chem 1988; 263:9557-9560.
    • (1988) J Biol Chem , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 21
    • 0026342025 scopus 로고
    • Structure of the calcium-binding protein determined by MAD phasing
    • Weis WI, Kahn R, Fourme R et al. Structure of the calcium-binding protein determined by MAD phasing. Science 1991; 254:1608-1615.
    • (1991) Science , vol.254 , pp. 1608-1615
    • Weis, W.I.1    Kahn, R.2    Fourme, R.3
  • 23
    • 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
  • 25
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • DOI 10.1111/j.1600-065X.1998.tb01185.x
    • Weis WI, Taylor ME, Drickamer K. The C-type lectin superfamily in the immune system. Immunol Rev 1998; 163:19-34. (Pubitemid 28327859)
    • (1998) Immunological Reviews , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 26
    • 41649104468 scopus 로고    scopus 로고
    • Specificity of the innate immune system and diversity of C-type lectin domain (CTLD) proteins in the nematode Caenorhabditis elegans
    • Schulenburg H, Hoeppner MP, Weiner III J et al. Specificity of the innate immune system and diversity of C-type lectin domain (CTLD) proteins in the nematode Caenorhabditis elegans. Immunol 2008; 213:237-250.
    • (2008) Immunol , vol.213 , pp. 237-250
    • Schulenburg, H.1    Hoeppner, M.P.2    Weiner III, J.3
  • 27
    • 0034927549 scopus 로고    scopus 로고
    • Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei, and the Atlantic White Shrimp, L. setiferus
    • DOI 10.1016/S0145-305X(01)00018-0, PII S0145305X01000180
    • Gross PS, Bartlett TC, Browdy L et al. Immune gene discovery by expressed sequence tag analysis of hemocytes and hepatopancreas in the Pacific White Shrimp, Litopenaeus vannamei and the Atlantic White shrimp, L. setiferus. Dev Comp Immunol 2001; 25:565-577. (Pubitemid 32694666)
    • (2001) Developmental and Comparative Immunology , vol.25 , Issue.7 , pp. 565-577
    • Gross, P.S.1    Bartlett, T.C.2    Browdy, C.L.3    Chapman, R.W.4    Warr, G.W.5
  • 28
    • 0034920428 scopus 로고    scopus 로고
    • Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity
    • Dodd RB, Drickamer K. Lectin-like proteins in model organisms: Implications for evolution of carbohydrate-binding activity. Glycobiol 2001; 11:71R-79R. (Pubitemid 32685209)
    • (2001) Glycobiology , vol.11 , Issue.5
    • Dodd, R.B.1    Drickamer, K.2
  • 29
    • 65549153845 scopus 로고    scopus 로고
    • C-type lectins and phagocytosis
    • Kerrigan AM, Brown GD. C-type lectins and phagocytosis. Immunobiol 2009; 214:562-575.
    • (2009) Immunobiol , vol.214 , pp. 562-575
    • Kerrigan, A.M.1    Brown, G.D.2
  • 30
    • 0034535375 scopus 로고    scopus 로고
    • Immulectin-2, a lipopolysaccharide-specific lectin from an insect, Manduca sexta, is induced in response to Gram-negative bacteria
    • DOI 10.1074/jbc.M003021200
    • Yu XQ, Kanost MR. Immulectin-2, a lipopolysaccharide-specific lectin from an insect, manduca sexta, is induced in response to gram-negative bacteria. J Biol Chem 2000; 275:37373-37381. (Pubitemid 32004840)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.48 , pp. 37373-37381
    • Yu, X.-Q.1    Kanost, M.R.2
  • 31
    • 0033166017 scopus 로고    scopus 로고
    • Immulectin, an inducible C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenol oxidase
    • DOI 10.1016/S0965-1748(99)00036-3, PII S0965174899000363
    • Yu XQ, Gan H, Kanost MR. Immulectin, an induction C-type lectin from an insect, Manduca sexta, stimulates activation of plasma prophenoloxidase. Insect Biochem Mol Biol 1999; 29:585-597. (Pubitemid 29336938)
    • (1999) Insect Biochemistry and Molecular Biology , vol.29 , Issue.7 , pp. 585-597
    • Yu, X.-Q.1    Gan, H.2    Kanost, M.R.3
  • 32
    • 14844282115 scopus 로고    scopus 로고
    • A novel C-type immulectin-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes
    • DOI 10.1016/j.ibmb.2005.01.004
    • Yu XQ, Tracy ME, Ling E et al. A novel C-type immulectin-3 from Manduca sexta is translocated from hemolymph into the cytoplasm of hemocytes. Insect Biochem Mol Biol 2005; 35:285-295. (Pubitemid 40335940)
    • (2005) Insect Biochemistry and Molecular Biology , vol.35 , Issue.4 , pp. 285-295
    • Yu, X.-Q.1    Tracy, M.E.2    Ling, E.3    Scholz, F.R.4    Trenczek, T.5
  • 33
    • 27644578820 scopus 로고    scopus 로고
    • Cellular encapsulation and melanization are enhanced by immulectins, pattern recognition receptors from the tobacco hornworm Manduca sexta
    • DOI 10.1016/j.dci.2005.05.005, PII S0145305X05000911
    • Ling E, Yu XQ. Cellular encapsulation and melanization are enhanced by immulectins, pattern recognition receptors from the tobacco hornworm Manduca sexta. Dev Comp Immunol 2006; 30:289-299. (Pubitemid 41571269)
    • (2006) Developmental and Comparative Immunology , vol.30 , Issue.3 , pp. 289-299
    • Ling, E.1    Yu, X.-Q.2
  • 34
    • 0032993577 scopus 로고    scopus 로고
    • The lipopolysaccharide-binding protein participating in hemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains
    • DOI 10.1016/S0014-5793(98)01701-3, PII S0014579398017013
    • Koizumi N, Imamura M, Kadotani T et al. The lipopolysaccharide- bindingproteinparticipating in haemocyte nodule formation in the silkworm Bombyx mori is a novel member of the C-type lectin superfamily with two different tandem carbohydrate-recognition domains. FEBS Lett 1999; 443:139-143. (Pubitemid 29078619)
    • (1999) FEBS Letters , vol.443 , Issue.2 , pp. 139-143
    • Koizumi, N.1    Imamura, M.2    Kadotani, T.3    Yaoi, K.4    Iwahana, H.5    Sato, R.6
  • 35
    • 0026516931 scopus 로고
    • Functional of the lipopolysaccharide-binding protein of Periplaneta americana as an opsonin
    • Jomori T, Natori S. Functional of the lipopolysaccharide-binding protein of Periplaneta americana as an opsonin. FEBS Lett 1992; 283-286.
    • (1992) FEBS Lett , pp. 283-286
    • Jomori, T.1    Natori, S.2
  • 37
    • 37849045813 scopus 로고    scopus 로고
    • C-type lectin receptors in antifungal immunity
    • Willment JA, Brown GD. C-type lectin receptors in antifungal immunity. Trends Microbiol 2008; 16:27-32.
    • (2008) Trends Microbiol , vol.16 , pp. 27-32
    • Willment, J.A.1    Brown, G.D.2
  • 38
    • 50149101714 scopus 로고    scopus 로고
    • Molecular cloning and immune responsive expression of a novel C-type lectin gene from bay scallop Argopecten irradians
    • Zhu L, Song LS, Xu W et al. Molecular cloning and immune responsive expression of a novel C-type lectin gene from bay scallop Argopecten irradians. Fish Shellfish Immunol 2008; 25:231-238.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 231-238
    • Zhu, L.1    Song, L.S.2    Xu, W.3
  • 39
    • 0034694384 scopus 로고    scopus 로고
    • Lectins as nonself recognition factors, in crustaceans
    • Marques MRF, Barracco MA. Lectins as nonself recognition factors, in crustaceans. Aquaculture 2000; 191:23-44.
    • (2000) Aquaculture , vol.191 , pp. 23-44
    • Marques, M.R.F.1    Barracco, M.A.2
  • 41
    • 64149094067 scopus 로고    scopus 로고
    • A novel C-type lectin with two CRD domains from Chinese shrimp Fenneropenaeus chinensis functions as a pattern recognition protein
    • Zhang X-W, Xu W-T, Wang X-W et al. A novel C-type lectin with two CRD domains from Chinese shrimp Fenneropenaeus chinensis functions as a pattern recognition protein. Mol Immunol 2009; 46:1626-1637.
    • (2009) Mol Immunol , vol.46 , pp. 1626-1637
    • Zhang, X.-W.1    Xu, W.-T.2    Wang, X.-W.3
  • 42
    • 67349183990 scopus 로고    scopus 로고
    • A novel C-type lectin (FcLec4) facilitates the clearance of Vibrio anguillarum in vivo in Chinese white shrimp
    • Wang X-W, Zhang X-W, Xu W-T et al. A novel C-type lectin (FcLec4) facilitates the clearance of Vibrio anguillarum in vivo in Chinese white shrimp. Dev Comp Immunol 2009; 33:1039-1047.
    • (2009) Dev Comp Immunol , vol.33 , pp. 1039-1047
    • Wang, X.-W.1    Zhang, X.-W.2    Xu, W.-T.3
  • 43
    • 33747818004 scopus 로고    scopus 로고
    • Molecular cloning, characterization and expression analysis of a putative C-type lectin (Fclectin) gene in Chinese shrimp Fenneropenaeus chinensis
    • DOI 10.1016/j.molimm.2006.01.015, PII S0161589006000265
    • Liu Y-H, Li F-H, Dong B et al. Molecular cloning, characterization and expression analysis of a putative C-type lectin (Fclectin) gene in Chinese shrimp Fenneropenaeus chinensis. Mol Immunol 2007; 44:598-607. (Pubitemid 44287040)
    • (2007) Molecular Immunology , vol.44 , Issue.4 , pp. 598-607
    • Liu, Y.-C.1    Li, F.-H.2    Dong, B.3    Wang, B.4    Luan, W.5    Zhang, X.-J.6    Zhang, L.-S.7    Xiang, J.-H.8
  • 44
    • 33645404551 scopus 로고    scopus 로고
    • Purification, characterization and cDNA cloning of a novel lipopolysaccharide-binding lectin from the shrimp Penaeus monodon
    • Luo T, Yang H, Li F et al. Purification, characterization and cDNA cloning of a novel lipopolysaccharide-binding lectin from the shrimp Penaeus monodon. Dev Comp Immunol 2006; 30:607-617.
    • (2006) Dev Comp Immunol , vol.30 , pp. 607-617
    • Luo, T.1    Yang, H.2    Li, F.3
  • 45
    • 59349085737 scopus 로고    scopus 로고
    • Cloning and characterization of a novel C-type lectin gene from shrimp Litopenaeus vannamei
    • Zhang Y, Qui L, Song L et al. Cloning and characterization of a novel C-type lectin gene from shrimp Litopenaeus vannamei. Fish Shellfish Immunol 2009; 26:183-192.
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 183-192
    • Zhang, Y.1    Qui, L.2    Song, L.3
  • 46
    • 54849425522 scopus 로고    scopus 로고
    • PmLT, a C-type lectin specific to hepatopancreas is involved in the innate defense of the shrimp Penaeus monodon
    • Ma TH-T, Benzie JAH, He JG et al. PmLT, a C-type lectin specific to hepatopancreas is involved in the innate defense of the shrimp Penaeus monodon. J Invertebr Pathol 2008; 99:332-341.
    • (2008) J Invertebr Pathol , vol.99 , pp. 332-341
    • Ma, T.H.-T.1    Benzie, J.A.H.2    He, J.G.3
  • 47
    • 34548287510 scopus 로고    scopus 로고
    • A hepatopancreas-specific C-type lectin from the Chinese shrimp Fenneropenaeus chinensis exhibits antimicrobial activity
    • DOI 10.1016/j.molimm.2007.06.355, PII S0161589007004099
    • Sun Y-D, Fu L-D, Jia Y-P et al. A hepatopancreas-specific C-type lectin from the Chinese shrimp Fenneropenaeus chinensis exhibits antimicrobial activity. Mol Immunol 2008; 45:348-361. (Pubitemid 47332646)
    • (2008) Molecular Immunology , vol.45 , Issue.2 , pp. 348-361
    • Sun, Y.-D.1    Fu, L.-D.2    Jia, Y.-P.3    Du, X.-J.4    Wang, Q.5    Wang, Y.-H.6    Zhao, X.-F.7    Yu, X.-Q.8    Wang, J.-X.9
  • 48
    • 58149380770 scopus 로고    scopus 로고
    • A novel C-type lectin from the shrimp Litopenaeus vannamei possesses anti-white spot syndrome virus activity
    • Zhao Z-Y, Yin Z-X, Xu X-P et al. A novel C-type lectin from the shrimp Litopenaeus vannamei possesses anti-white spot syndrome virus activity. J Virol 2009; 83:347-356.
    • (2009) J Virol , vol.83 , pp. 347-356
    • Zhao, Z.-Y.1    Yin, Z.-X.2    Xu, X.-P.3
  • 49
    • 70049111368 scopus 로고    scopus 로고
    • A C-type lectin is involved in the innate immune response of Chinese white shrimp
    • Wang X-W, Xu W-T, Zhang X-W et al. A C-type lectin is involved in the innate immune response of Chinese white shrimp. Fish Shellfish Immunol 2009; 27:556-562.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 556-562
    • Wang, X.-W.1    Xu, W.-T.2    Zhang, X.-W.3
  • 50
    • 0142039042 scopus 로고    scopus 로고
    • PmAV, a novel gene involved in virus resistance of shrimp Penaeus monodon
    • DOI 10.1016/S0014-5793(03)00891-3
    • Luo T, Zhang X, Shao Z et al. PmAV, a novel gene involved in virus resistance of shrimp Penaeus monodon. FEBS Lett 2003; 551:53-57. (Pubitemid 37281327)
    • (2003) FEBS Letters , vol.551 , Issue.1-3 , pp. 53-57
    • Luo, T.1    Zhang, X.2    Shao, Z.3    Xu, X.4
  • 51
    • 70349985733 scopus 로고    scopus 로고
    • Expression of immune-related genes in the digestive organ of shrimp, Penaeus monodon, after an oral infection by Vibrio harveyi
    • Soonthornchai W, Rungrassamee W, Karoonuthaisiri N et al. Expression of immune-related genes in the digestive organ of shrimp, Penaeus monodon, after an oral infection by Vibrio harveyi. Dev Comp Immunol 2010; 34:19-28.
    • (2010) Dev Comp Immunol , vol.34 , pp. 19-28
    • Soonthornchai, W.1    Rungrassamee, W.2    Karoonuthaisiri, N.3
  • 52
    • 0023941580 scopus 로고
    • Isolation and purification of a cell adhesion factor from crayfish blood cells
    • Johansson MW, Soderhall K. Isolation and purification of a cell adhesion factor from crayfish blood cells. J Cell Biol 1988; 106:1795-1803.
    • (1988) J Cell Biol , vol.106 , pp. 1795-1803
    • Johansson, M.W.1    Soderhall, K.2
  • 53
    • 0028863268 scopus 로고
    • Peroxinectin, a novel cell-adhesion protein from crayfish blood
    • Johansson MW, Lind MI, Holmblad T et al. Peroxinectin, a novel cell-adhesion protein from crayfish blood. Biochem Biophys Res Com 1995; 216:1079-1097.
    • (1995) Biochem Biophys Res Com , vol.216 , pp. 1079-1097
    • Johansson, M.W.1    Lind, M.I.2    Holmblad, T.3
  • 54
    • 0002765899 scopus 로고
    • s Ratcliffe NA Rowley AF eds. Invertebrate Blood Cells. London and New York: Academic Press
    • Bauchau AG. Crustaceans. s Ratcliffe NA, Rowley AF, eds. Invertebrate Blood Cells. London and New York: Academic Press 1981, 385-420.
    • (1981) Crustaceans , pp. 385-420
    • Bauchau, A.G.1
  • 56
    • 0020728304 scopus 로고
    • Separation of hemocyte population of Carcinus maenas and other marine decapods and prophenoloxidase distribution
    • Söderhäll K, Smith VJ. Separation of hemocyte population of Carcinus maenas and other marine decapods and prophenoloxidase distribution. Dev Comp Immunol 1983; 7:229-239.
    • (1983) Dev Comp Immunol , vol.7 , pp. 229-239
    • Söderhäll, K.1    Smith, V.J.2
  • 57
    • 25444468112 scopus 로고    scopus 로고
    • Exocytosis and proteomic analysis of the vesicle content of granular hemocytes from a crayfish
    • DOI 10.1016/j.dci.2005.03.010, PII S0145305X05000820
    • Sricharoen S, Kim JJ, Tunkijanukij S et al. Exocytosis and proteomic analysis of the vesicle content of granular hemocytes from a crayfish. Dev Comp Immunol 2005; 29:1017-1031. (Pubitemid 41375730)
    • (2005) Developmental and Comparative Immunology , vol.29 , Issue.12 , pp. 1017-1031
    • Sricharoen, S.1    Jeong, J.K.2    Tunkijjanukij, S.3    Soderhall, I.4
  • 58
    • 0036784566 scopus 로고    scopus 로고
    • Insect hemocytes and their role in immunity
    • Lavine MD, Strand MR. Insect hemocytes and their role in immunity. Insect Biochem Mol Biol 2002; 32:1295-1309.
    • (2002) Insect Biochem Mol Biol , vol.32 , pp. 1295-1309
    • Lavine, M.D.1    Strand, M.R.2
  • 59
  • 60
    • 0003158203 scopus 로고
    • The haemopoietic cells of the freshwater crayfish, Pacifastacus leniusculus
    • Chaga O, Lignell M, Soderhall K. The haemopoietic cells of the freshwater crayfish, Pacifastacus leniusculus. Anim Biol 1995; 4:57-70.
    • (1995) Anim Biol , vol.4 , pp. 57-70
    • Chaga, O.1    Lignell, M.2    Soderhall, K.3
  • 61
    • 0038546825 scopus 로고    scopus 로고
    • Hemocyte production and maturation in an invertebrate animal; proliferation and gene expression in hematopoietic stem cells of Pacifastacus leniusculus
    • DOI 10.1016/S0145-305X(03)00039-9
    • Söderhäll I, Bangyeekhun E, Mayo S et al. Hemocyte production and maturation in an invertebrate animal: Proliferation and gene expression in hematopoietic stem cells of Pacifastacus leniusculus. Dev Comp Immunol 2003; 27:661-672. (Pubitemid 36683068)
    • (2003) Developmental and Comparative Immunology , vol.27 , Issue.8 , pp. 661-672
    • Soderhall, I.1    Bangyeekhun, E.2    Mayo, S.3    Soderhall, K.4
  • 63
    • 55349103779 scopus 로고    scopus 로고
    • Transglutaminase activity in the hematopoietic tissue of a crustacean, Pacifastacus leniusculus, importance in hemocyte homeostasis
    • Lin XH, Söderhäll K, Söderhäll I. Transglutaminase activity in the hematopoietic tissue of a crustacean, Pacifastacus leniusculus, importance in hemocyte homeostasis. BMC Immunol 2008; 9:58.
    • (2008) BMC Immunol , vol.9 , pp. 58
    • Lin, X.H.1    Söderhäll, K.2    Söderhäll, I.3
  • 64
    • 55749112809 scopus 로고    scopus 로고
    • Hemocyte-lineage marker proteins in a crustacean, the freshwater crayfish, Pacifastacus leniusculus
    • Wu CL, Söderhäll I, Kim YA et al. Hemocyte-lineage marker proteins in a crustacean, the freshwater crayfish, Pacifastacus leniusculus. Proteomics 2008; 8:4226-4235.
    • (2008) Proteomics , vol.8 , pp. 4226-4235
    • Wu, C.L.1    Söderhäll, I.2    Kim, Y.A.3
  • 65
    • 63249107450 scopus 로고    scopus 로고
    • Identification and properties of a receptor for the invertebrate cytokine astakine, involved in hematopoiesis
    • Lin XH, Kim YA, Lee BL et al. Identification and properties of a receptor for the invertebrate cytokine astakine, involved in hematopoiesis. Exp Cell Res 2009; 315:1171-1180.
    • (2009) Exp Cell Res , vol.315 , pp. 1171-1180
    • Lin, X.H.1    Kim, Y.A.2    Lee, B.L.3
  • 66
    • 79960724175 scopus 로고
    • The renal organs of certain decapod crustacea
    • Weldon WFR. The renal organs of certain decapod crustacea. Quart J Micr Sci 1891; 32:279-291.
    • (1891) Quart J Micr Sci , vol.32 , pp. 279-291
    • Weldon, W.F.R.1
  • 67
    • 79960703022 scopus 로고
    • Nephridia and body-cavity of some decapod crustacea
    • Allen EJ. Nephridia and body-cavity of some decapod crustacea. Quart J Micr Sci 1893; 34:403-426.
    • (1893) Quart J Micr Sci , vol.34 , pp. 403-426
    • Allen, E.J.1
  • 69
    • 0000957879 scopus 로고
    • A handbook of normal penaeid shrimp histology
    • Kansas: Allen Press
    • Bell T, Lightner DV. A handbook of normal penaeid shrimp histology. World Aquaculture Society. Kansas: Allen Press, 1988: 114.
    • (1988) World Aquaculture Society , vol.114
    • Bell, T.1    Lightner, D.V.2
  • 70
    • 85008030099 scopus 로고
    • Studies on Penaeus orientalis Kishinouye. VIII. Structure of newly found lymphoid organ
    • Oka M. Studies on Penaeus orientalis Kishinouye. VIII. Structure of newly found lymphoid organ. Bull Jpn Soc Sei Fish 1969; 35:245-250.
    • (1969) Bull Jpn Soc Sei Fish , vol.35 , pp. 245-250
    • Oka, M.1
  • 71
    • 0000771005 scopus 로고
    • Patterns of hemocyte production and release throughout the molt cycle in the penaeid shrimp Sicyonia ingentis
    • Hose JE, Martin GG, Tiu S et al. Patterns of hemocyte production and release throughout the molt cycle in the penaeid shrimp Sicyonia ingentis. Biol Bull 1992; 183:185-199.
    • (1992) Biol Bull , vol.183 , pp. 185-199
    • Hose, J.E.1    Martin, G.G.2    Tiu, S.3
  • 73
    • 24544476680 scopus 로고
    • L'organe phagocytaire des Crustacés Décapodes
    • Cuénot L. L'organe phagocytaire des Crustacés Décapodes. Arch Zool Exp Gen 1905; 4:1-16.
    • (1905) Arch Zool Exp Gen , vol.4 , pp. 1-16
    • Cuénot, L.1
  • 74
    • 0017758547 scopus 로고
    • Hemopoiesis in crustacea decapoda: Origin and evolution of hemocytes and cyanocytes of Carcinus maenas
    • DOI 10.1016/0045-6039(77)90014-8
    • Ghiretti-Magaldi A, Milanesi C, Tognon G. Hemopoiesis in crustacea decapoda: Origin and evolution of hemocytes and cyanocytes of Carcinus maenas. Cell Differ 1977; 6:167-186. (Pubitemid 8186234)
    • (1977) Cell Differentiation , vol.6 , Issue.3-4 , pp. 167-186
    • Ghiretti-Magaldi, A.1    Milanesi, C.2    Tognon, G.3
  • 75
    • 84856031254 scopus 로고
    • Ultrastructure de l 'organe hématopolétique chez le crabe Carcinus maenas (L.)
    • Bazin F. Ultrastructure de l 'organe hématopolétique chez le crabe Carcinus maenas (L.) Arch Anat Microsc Morphol Exp 1979; 68:142-157.
    • (1979) Arch Anat Microsc Morphol Exp , vol.68 , pp. 142-157
    • Bazin, F.1
  • 76
    • 84986651425 scopus 로고
    • Structure of hematopoietic nodules in the ridgeback prawn, Sicyonia ingentis: Light and electron microscopic observations
    • Martin GG, Hose JE, Kim JJ. Structure of hematopoietic nodules in the ridgeback prawn, Sicyonia ingentis: Light and electron microscopic observations. J Morphol 1987; 192:193-204.
    • (1987) J Morphol , vol.192 , pp. 193-204
    • Martin, G.G.1    Hose, J.E.2    Kim, J.J.3
  • 77
    • 84993908976 scopus 로고
    • Organization of hematopoietic tissue in the intermolt lobster, Homarus americanus
    • Martin GG, Hose JE, Chou M et al. Organization of hematopoietic tissue in the intermolt lobster, Homarus americanus. J Morphol 1993; 216:65-78.
    • (1993) J Morphol , vol.216 , pp. 65-78
    • Martin, G.G.1    Hose, J.E.2    Chou, M.3
  • 79
    • 8644278673 scopus 로고    scopus 로고
    • Manganese induced immune suppression of the lobster, Nephrops norvegicus
    • DOI 10.1016/j.aquatox.2004.09.004, PII S0166445X04002577
    • Hernroth B, Baden SP, Holm K et al. Manganese induced immune suppression of the lobster, Nephrops norvegicus. Aquat Toxicol 2004; 70:223-231. (Pubitemid 39506832)
    • (2004) Aquatic Toxicology , vol.70 , Issue.3 , pp. 223-231
    • Hernroth, B.1    Baden, S.P.2    Holm, K.3    Andre, T.4    Soderhall, I.5
  • 80
    • 73049105329 scopus 로고    scopus 로고
    • A long form of shrimp astakine transcript: Molecular cloning, characterization and functional elucidation in promoting hematopoiesis
    • Hsiao CY, Song YL. A long form of shrimp astakine transcript: Molecular cloning, characterization and functional elucidation in promoting hematopoiesis. Fish Shellfish Immunol 2010; 28:77-86.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 77-86
    • Hsiao, C.Y.1    Song, Y.L.2
  • 81
    • 79960723221 scopus 로고    scopus 로고
    • Function of crayfish astakines in hemocyte lineage determination
    • Epub ahead of print, PMID 2059 2028
    • Lin X, Novotny M, Soderhall K et al. Function of crayfish astakines in hemocyte lineage determination. J Biol Chem 2010; Epub ahead of print, PMID 2059 2028.
    • (2010) J Biol Chem
    • Lin, X.1    Novotny, M.2    Soderhall, K.3
  • 83
    • 60549110465 scopus 로고    scopus 로고
    • Contributions of functional genomics and proteomics to the study of immune responses in the Pacific white leg shrimp Litopenaeus vannamei
    • Robalino J, Carnegie RB, O'Leary N et al. Contributions of functional genomics and proteomics to the study of immune responses in the Pacific white leg shrimp Litopenaeus vannamei. Vet Immunol Immunopathol 2009; 128:110-118.
    • (2009) Vet Immunol Immunopathol , vol.128 , pp. 110-118
    • Robalino, J.1    Carnegie, R.B.2    O'Leary, N.3
  • 84
    • 0033740453 scopus 로고    scopus 로고
    • Broad antiviral activity in tissues of crustaceans
    • Pan J, Kurosky A, Xu B et al. Broad antiviral activity in tissues of crustaceans. Antiviral Res 2000; 48:39-47.
    • (2000) Antiviral Res , vol.48 , pp. 39-47
    • Pan, J.1    Kurosky, A.2    Xu, B.3
  • 85
    • 0022887258 scopus 로고
    • Primary structure of limulus anticoagulant anti-lipopolysaccharide factor
    • Aketagawa J, Miyata T, Ohtsubo S et al. Primary structure of limulus anticoagulant anti-lipopolysaccharide factor. J Biol Chem 1986; 261:7357-7365. (Pubitemid 17224737)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.16 , pp. 7357-7365
    • Aketegawa, J.1    Miyata, T.2    Ohtsubo, S.3
  • 86
    • 39149087407 scopus 로고    scopus 로고
    • Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF): A broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection
    • de la Vega E, O'Leary NA, Shockey JE et al. Anti-lipopolysaccharide factor in Litopenaeus vannamei (LvALF): A broad spectrum antimicrobial peptide essential for shrimp immunity against bacterial and fungal infection. Mol Immunol 2008; 45:1916-1925.
    • (2008) Mol Immunol , vol.45 , pp. 1916-1925
    • De La Vega, E.1    O'Leary, N.A.2    Shockey, J.E.3
  • 88
    • 33750306792 scopus 로고    scopus 로고
    • Antilipopolysaccharide factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus
    • DOI 10.1128/JVI.01101-06
    • Liu H, Jiravanichpaisal P, Söderhäll I et al. Antilipopolysaccharide Factor interferes with white spot syndrome virus replication in vitro and in vivo in the crayfish Pacifastacus leniusculus. J Virol 2006: 80:10365-10371. (Pubitemid 44628884)
    • (2006) Journal of Virology , vol.80 , Issue.21 , pp. 10365-10371
    • Liu, H.1    Jiravanichpaisal, P.2    Soderhall, I.3    Cerenius, L.4    Soderhall, K.5
  • 89
    • 67649197704 scopus 로고    scopus 로고
    • Role of antilipopolysaccharide factor from the black tiger shrimp, Penaeus monodon, in protection from white spot syndrome virus infection
    • Tharntada S, Ponprateep S, Somboonwiwat K et al. Role of antilipopolysaccharide factor from the black tiger shrimp, Penaeus monodon, in protection from white spot syndrome virus infection. J Gen Virol 2009; 90:1491-1498.
    • (2009) J Gen Virol , vol.90 , pp. 1491-1498
    • Tharntada, S.1    Ponprateep, S.2    Somboonwiwat, K.3
  • 91
    • 33846478653 scopus 로고    scopus 로고
    • White spot syndrome virus annexes a shrimp STAT to enhance expression of the immediate-early gene ie1
    • DOI 10.1128/JVI.01880-06
    • Liu WJ, Chang YS, Wang AH et al. White spot syndrome virus annexes a shrimp STAT to enhance expression of the immediate-early gene ie1. J Virol 2007; 81:1461-1471. (Pubitemid 46167867)
    • (2007) Journal of Virology , vol.81 , Issue.3 , pp. 1461-1471
    • Liu, W.-J.1    Chang, Y.-S.2    Wang, A.H.-J.3    Kou, G.-H.4    Lo, C.-F.5
  • 92
    • 46549084448 scopus 로고    scopus 로고
    • WSSV infection activates STAT in shrimp
    • Chen WY, Ho KC, Leu JH et al. WSSV infection activates STAT in shrimp. Dev Comp Immunol 2008; 32:1142-1150.
    • (2008) Dev Comp Immunol , vol.32 , pp. 1142-1150
    • Chen, W.Y.1    Ho, K.C.2    Leu, J.H.3
  • 93
    • 55549111874 scopus 로고    scopus 로고
    • Transactivation, dimerization and DNA-binding activity of White spot syndrome virus immediate early protein IE1
    • Liu WJ, Chang YS, Wang HC et al. Transactivation, dimerization and DNA-binding activity of White spot syndrome virus immediate early protein IE1. J Virol 2008; 82:11362-11373.
    • (2008) J Virol , vol.82 , pp. 11362-11373
    • Liu, W.J.1    Chang, Y.S.2    Wang, H.C.3
  • 95
    • 64149098051 scopus 로고    scopus 로고
    • Lack of evidence for Litopenaeus vannamei Toll receptor (lToll) involvement in activation of sequence-independent antiviral immunity in shrimp
    • Labreuche Y, O'Leary NA, de la Vega E et al. Lack of evidence for Litopenaeus vannamei Toll receptor (lToll) involvement in activation of sequence-independent antiviral immunity in shrimp. Dev Comp Immunol 2009; 33:806-810.
    • (2009) Dev Comp Immunol , vol.33 , pp. 806-810
    • Labreuche, Y.1    O'Leary, N.A.2    De La Vega, E.3
  • 96
    • 77951666097 scopus 로고    scopus 로고
    • Mechanisms of apoptosis in Crustacea: What conditions induce versus suppress cell death?
    • Menze MA, Fortner G, Nag S et al. Mechanisms of apoptosis in Crustacea: What conditions induce versus suppress cell death? Apoptosis 2010; 15:293-312.
    • (2010) Apoptosis , vol.15 , pp. 293-312
    • Menze, M.A.1    Fortner, G.2    Nag, S.3
  • 97
    • 39049084854 scopus 로고    scopus 로고
    • Requirement for shrimp caspase in apoptosis against virus infection
    • Wang L, Zhi B, Wu W et al. Requirement for shrimp caspase in apoptosis against virus infection. Dev Comp Immunol 2008; 32:706-715.
    • (2008) Dev Comp Immunol , vol.32 , pp. 706-715
    • Wang, L.1    Zhi, B.2    Wu, W.3
  • 98
    • 39149109572 scopus 로고    scopus 로고
    • Knocking down caspase-3 by RNAi reduces mortality in Pacific white shrimp Penaeus (Litopenaeus) vannamei challenged with a low dose of white-spot syndrome virus
    • Rijiravanich A, Browdy CL, Withyachumnarnkul B. Knocking down caspase-3 by RNAi reduces mortality in Pacific white shrimp Penaeus (Litopenaeus) vannamei challenged with a low dose of white-spot syndrome virus. Fish Shellfish Immunol 2008; 24:308-313.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 308-313
    • Rijiravanich, A.1    Browdy, C.L.2    Withyachumnarnkul, B.3
  • 99
    • 44749086663 scopus 로고    scopus 로고
    • Up-regulation of ribophorin I after yellow head virus (YHV) challenge in black tiger shrimp Penaeus monodon
    • Molthathong S, Buaklin A, Senapin S et al. Up-regulation of ribophorin I after yellow head virus (YHV) challenge in black tiger shrimp Penaeus monodon. Fish Shellfish Immunol 2008; 25:40-46.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 40-46
    • Molthathong, S.1    Buaklin, A.2    Senapin, S.3
  • 100
    • 38349003352 scopus 로고    scopus 로고
    • Down-regulation of defender against apoptotic death (DAD 1) after yellow head virus (YHV) challenge in black tiger shrimp Penaeus monodon
    • Molthathong S, Senapin S, Klinbunga S et al. Down-regulation of defender against apoptotic death (DAD 1) after yellow head virus (YHV) challenge in black tiger shrimp Penaeus monodon. Fish Shellfish Immunol 2008; 24:173-179.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 173-179
    • Molthathong, S.1    Senapin, S.2    Klinbunga, S.3
  • 101
    • 70450162312 scopus 로고    scopus 로고
    • RNA interference-based therapeutics for shrimp viral diseases
    • Krishnan P, Gireesh-Babu P, Rajendran KV et al. RNA interference-based therapeutics for shrimp viral diseases. Dis Aquat Org 2009; 86:263-272.
    • (2009) Dis Aquat Org , vol.86 , pp. 263-272
    • Krishnan, P.1    Gireesh-Babu, P.2    Rajendran, K.V.3
  • 102
    • 33846368080 scopus 로고    scopus 로고
    • Double-stranded RNA and antiviral immunity in marine shrimp: Inducible host mechanisms and evidence for the evolution of viral counter-responses
    • DOI 10.1016/j.dci.2006.08.011, PII S0145305X06001698
    • Robalino J, Bartlett TC, Chapman RW et al. Double-stranded RNA and antiviral immunity in marine shrimp: Inducible host mechanisms and evidence for the evolution of viral counter-responses. Dev Comp Immunol 2007; 31:539-547. (Pubitemid 46127707)
    • (2007) Developmental and Comparative Immunology , vol.31 , Issue.6 , pp. 539-547
    • Robalino, J.1    Bartlett, T.C.2    Chapman, R.W.3    Gross, P.S.4    Browdy, C.L.5    Warr, G.W.6
  • 103
    • 38349035712 scopus 로고    scopus 로고
    • A key gene of the RNA interference pathway in the black tiger shrimp, Penaeus monodon: Identification and functional characterisation of Dicer-1
    • Su J, Oanh DT, Lyons RE et al. A key gene of the RNA interference pathway in the black tiger shrimp, Penaeus monodon: Identification and functional characterisation of Dicer-1. Fish Shellfish Immunol 2008; 24:223-233.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 223-233
    • Su, J.1    Oanh, D.T.2    Lyons, R.E.3
  • 105
    • 74449085558 scopus 로고    scopus 로고
    • Protective immunity induced by CpG ODNs against white spot syndrome virus (WSSV) via intermediation of virus replication indirectly in Litopenaeus vannamei
    • Zhang Y, Song L, Zhao J et al. Protective immunity induced by CpG ODNs against white spot syndrome virus (WSSV) via intermediation of virus replication indirectly in Litopenaeus vannamei. Dev Comp Immunol 2010; 34:418-424.
    • (2010) Dev Comp Immunol , vol.34 , pp. 418-424
    • Zhang, Y.1    Song, L.2    Zhao, J.3
  • 106
    • 66949167063 scopus 로고    scopus 로고
    • TRBP homolog interacts with eukaryotic initiation factor 6 (eIF6) in Fenneropenaeus chinensis
    • Wang S, Liu N, Chen A-J et al. TRBP homolog interacts with eukaryotic initiation factor 6 (eIF6) in Fenneropenaeus chinensis. J Immunol 2009; 182:5250-5258.
    • (2009) J Immunol , vol.182 , pp. 5250-5258
    • Wang, S.1    Liu, N.2    Chen, A.-J.3
  • 107
    • 0038546825 scopus 로고    scopus 로고
    • Hemocyte production and maturation in an invertebrate animal; proliferation and gene expression in hematopoietic stem cells of Pacifastacus leniusculus
    • DOI 10.1016/S0145-305X(03)00039-9
    • Söderhäll I, Bangyeekhun E, Mayo S et al. Hemocyte production and maturation in an invertebrate animal; proliferation and gene expression in hematopoietic stem cells of Pacifastacus leniusculus. Dev Comp Immunol 2003; 27:661-672. (Pubitemid 36683068)
    • (2003) Developmental and Comparative Immunology , vol.27 , Issue.8 , pp. 661-672
    • Soderhall, I.1    Bangyeekhun, E.2    Mayo, S.3    Soderhall, K.4
  • 108
    • 33645543215 scopus 로고    scopus 로고
    • Characterization of white spot syndrome virus replication in vitro-cultured haematopoietic stem cells of freshwater crayfish, Pacifastacus leniusculus
    • Jiravanichpaisal P, Söderhäll K, Söderhäll I. Characterization of white spot syndrome virus replication in vitro-cultured haematopoietic stem cells of freshwater crayfish, Pacifastacus leniusculus. J Gen Virol 2006; 87:847-854.
    • (2006) J Gen Virol , vol.87 , pp. 847-854
    • Jiravanichpaisal, P.1    Söderhäll, K.2    Söderhäll, I.3
  • 109
    • 0027405148 scopus 로고
    • Characterization of a clotting protein, isolated from plasma of the freshwater crayfish Pacifastacus leniusculus
    • Kopácek P, Hall M, Söderhäll K. Characterization of a clotting protein, isolated from plasma of the crayfish Pacifastacus leniusculus. Eur J Biochem 1993; 213:591-597. (Pubitemid 23106094)
    • (1993) European Journal of Biochemistry , vol.213 , Issue.1 , pp. 591-597
    • Kopacek, P.1    Hall, M.2    Soderhall, K.3
  • 111
    • 1842800032 scopus 로고    scopus 로고
    • Coagulation in arthropods: Defence, wound closure and healing
    • DOI 10.1016/j.it.2004.03.004, PII S1471490604000912
    • Theopold U, Schmidt O, Söderhäll K et al. Coagulation in arthropods: Defence, wound closure and healing. Trends Immunol 2004; 25:289-294. (Pubitemid 38610352)
    • (2004) Trends in Immunology , vol.25 , Issue.6 , pp. 289-294
    • Theopold, U.1    Schmidt, O.2    Soderhall, K.3    Dushay, M.S.4
  • 112
    • 37349060626 scopus 로고    scopus 로고
    • Essential function of transglutaminase and clotting protein in shrimp immunity
    • DOI 10.1016/j.molimm.2007.09.016, PII S0161589007007511
    • Maningas MBB, Kondo H, Hirono I et al. Essential function of transglutaminase and clotting protein in shrimp immunity. Mol Immunol 2008; 45:1269-1275. (Pubitemid 350299488)
    • (2008) Molecular Immunology , vol.45 , Issue.5 , pp. 1269-1275
    • Maningas, M.B.B.1    Kondo, H.2    Hirono, I.3    Saito-Taki, T.4    Aoki, T.5
  • 113
    • 67650578608 scopus 로고    scopus 로고
    • Hyastatin, a glycine-rich muti-domain antimicrobial peptide isolated from the spider crab (Hyas araneus) hemocytes
    • Spersted SV, Haug T, Vasskog T et al. Hyastatin, a glycine-rich muti-domain antimicrobial peptide isolated from the spider crab (Hyas araneus) hemocytes. Mol Immunol 2009; 46:2604-2612.
    • (2009) Mol Immunol , vol.46 , pp. 2604-2612
    • Spersted, S.V.1    Haug, T.2    Vasskog, T.3
  • 114
    • 67651083312 scopus 로고    scopus 로고
    • A double WAP domain (DWD)-containing protein with proteinase inhibitory activity in Chinese white shrimp, Fenneropenaeus chinensis
    • Du ZQ, Ren Q, Zhao XF et al. A double WAP domain (DWD)-containing protein with proteinase inhibitory activity in Chinese white shrimp, Fenneropenaeus chinensis. Comp Biochem Physiol B 2009; 154:203-210.
    • (2009) Comp Biochem Physiol B , vol.154 , pp. 203-210
    • Du, Z.Q.1    Ren, Q.2    Zhao, X.F.3
  • 115
    • 0035861645 scopus 로고    scopus 로고
    • Crustacean immunity-Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge
    • Destoumieux-Garzon D, Saulnier D, Garnier J et al. Crustacean immunity-Antifungal peptides are generated from the C terminus of shrimp hemocyanin in response to microbial challenge. J Biol Chem 2001; 276:47070-47077.
    • (2001) J Biol Chem , vol.276 , pp. 47070-47077
    • Destoumieux-Garzon, D.1    Saulnier, D.2    Garnier, J.3
  • 116
    • 0037424354 scopus 로고    scopus 로고
    • Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus
    • DOI 10.1074/jbc.M209239200
    • Lee SY, Lee BL, Söderhäll K. Processing of an antibacterial peptide from hemocyanin of the freshwater crayfish Pacifastacus leniusculus. J Biol Chem 2003; 278:7927-7933. (Pubitemid 36800529)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7927-7933
    • Lee, S.Y.1    Lee, B.L.2    Soderhall, K.3
  • 117
    • 70349988796 scopus 로고    scopus 로고
    • RNAi knock-down of the Litopenaeus vannamei Toll gene (LvToll) significantly increases mortality and reduces bacterial clearance after challenge with Vibrio harveyi
    • Wang KCHC, Tseng CW, Lin HY et al. RNAi knock-down of the Litopenaeus vannamei Toll gene (LvToll) significantly increases mortality and reduces bacterial clearance after challenge with Vibrio harveyi. Dev Comp Immunol 2010; 34:49-58.
    • (2010) Dev Comp Immunol , vol.34 , pp. 49-58
    • Wang, K.C.H.C.1    Tseng, C.W.2    Lin, H.Y.3
  • 119
    • 38349096821 scopus 로고    scopus 로고
    • Identification of cDNA encoding Toll receptor, MjToll gene from kuruma shrimp, Marsupenaeus japonicus
    • Mekata T, Kono T, Yoshida T et al. Identification of cDNA encoding Toll receptor, MjToll gene from kuruma shrimp, Marsupenaeus japonicus. Fish Shellfish Immunol 2008; 24:122-133.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 122-133
    • Mekata, T.1    Kono, T.2    Yoshida, T.3
  • 120
    • 41949106759 scopus 로고    scopus 로고
    • A Toll receptor from Chinese shrimp Fenneropenaeus chinensis is responsive to Vibrio anguillarum infection
    • Yang, C, Zhang J, Li F et al. A Toll receptor from Chinese shrimp Fenneropenaeus chinensis is responsive to Vibrio anguillarum infection. Fish Shellfish Immunol 2008; 24:564-574.
    • (2008) Fish Shellfish Immunol , vol.24 , pp. 564-574
    • Yang, C.1    Zhang, J.2    Li, F.3
  • 121
    • 70350128774 scopus 로고    scopus 로고
    • Identification and molecular characterization of a Spatzle-like protein from Chinese shrimp (Fenneropenaeus chinensis)
    • Shi XZ, Zhang RR, Jia YP et al. Identification and molecular characterization of a Spatzle-like protein from Chinese shrimp (Fenneropenaeus chinensis). Fish Shellfish Immunol 2009; 27:610-617.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 610-617
    • Shi, X.Z.1    Zhang, R.R.2    Jia, Y.P.3
  • 122
    • 67650395264 scopus 로고    scopus 로고
    • Identification and functional study of a shrimp Relish homologue
    • Huang XD, Yin ZX, Liao JX et al. Identification and functional study of a shrimp Relish homologue. Fish Shellfish Immunol 2009; 27:230-238.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 230-238
    • Huang, X.D.1    Yin, Z.X.2    Liao, J.X.3
  • 123
    • 67650260332 scopus 로고    scopus 로고
    • Identification of a novel relish homolog in Chinese shrimp Fenneropenaeus chinensis and its function in regulating the transcription of antimicrobial peptides
    • Li FH, Yan H, Wang DD et al. Identification of a novel relish homolog in Chinese shrimp Fenneropenaeus chinensis and its function in regulating the transcription of antimicrobial peptides. Dev Comp Immunol 2009; 33:1093-1101.
    • (2009) Dev Comp Immunol , vol.33 , pp. 1093-1101
    • Li, F.H.1    Yan, H.2    Wang, D.D.3
  • 124
    • 70450224674 scopus 로고    scopus 로고
    • Identification and functional study of a shrimp Dorsal homologue
    • Huang XD, Yin ZX, Jia XT et al. Identification and functional study of a shrimp Dorsal homologue. Dev Comp Immunol 2010; 34:107-113.
    • (2010) Dev Comp Immunol , vol.34 , pp. 107-113
    • Huang, X.D.1    Yin, Z.X.2    Jia, X.T.3
  • 125
    • 59349111922 scopus 로고    scopus 로고
    • The role of crustins in Litopenaeus vannamei in response to infection with shrimp pathogens: An in vivo approach
    • Shockey JE, O'Leary NA, de la Vega E et al. The role of crustins in Litopenaeus vannamei in response to infection with shrimp pathogens: An in vivo approach. Dev Comp Immunol 2009; 33:668-673.
    • (2009) Dev Comp Immunol , vol.33 , pp. 668-673
    • Shockey, J.E.1    O'Leary, N.A.2    De La Vega, E.3
  • 126
    • 64149102098 scopus 로고    scopus 로고
    • An immune deficiency homolog from the white shrimp, Litopenaeus vannamei, activates antimicrobial peptide genes
    • Wang PH, Gu ZH, Huang XD et al. An immune deficiency homolog from the white shrimp, Litopenaeus vannamei, activates antimicrobial peptide genes. Mol Immunol 2009; 46:1897-1904.
    • (2009) Mol Immunol , vol.46 , pp. 1897-1904
    • Wang, P.H.1    Gu, Z.H.2    Huang, X.D.3
  • 127
    • 0032005367 scopus 로고    scopus 로고
    • Role of the prophenoloxidase-activating system in invertebrate immunity
    • DOI 10.1016/S0952-7915(98)80026-5
    • Söderhäll K, Cerenius L. Role of the prophenoloxidase- activating system in invertebrate immunity. Cur Op Immunol 1998; 10:23-28. (Pubitemid 28112074)
    • (1998) Current Opinion in Immunology , vol.10 , Issue.1 , pp. 23-28
    • Soderhall, K.1    Cerenius, L.2
  • 128
    • 44649197623 scopus 로고    scopus 로고
    • The proPO-system: Pros and cons for its role in invertebrate immunity
    • Cerenius L, Lee BL, Söderhäll K. The proPO-system: Pros and cons for its role in invertebrate immunity. Trends Immunol 2008; 29:263-271.
    • (2008) Trends Immunol , vol.29 , pp. 263-271
    • Cerenius, L.1    Lee, B.L.2    Söderhäll, K.3
  • 129
    • 36348951621 scopus 로고    scopus 로고
    • Phenoloxidase is an important component of the defense against Aeromonas hydrophila infection in a crustacean, Pacifastacus leniusculus
    • DOI 10.1074/jbc.M706113200
    • Liu HP, Jiravanichpaisal P, Cerenius L et al. Phenoloxidase is an important component of the defense against Aeromonas hydrophila infection in a crustacean, Pacifastacus leniusculus. J Biol Chem 2007; 282:33593-33598. (Pubitemid 350159517)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33593-33598
    • Liu, H.1    Jiravanichpaisal, P.2    Cerenius, L.3    Bok, L.L.4    Soderhall, I.5    Soderhall, K.6
  • 130
    • 72049112296 scopus 로고    scopus 로고
    • In vitro effects on bacterial growth of phenoloxidase reaction products
    • Cerenius L, Ramesh B, Söderhäll K et al. In vitro effects on bacterial growth of phenoloxidase reaction products. J Invertebr Pathol 2010; 103:21-23.
    • (2010) J Invertebr Pathol , vol.103 , pp. 21-23
    • Cerenius, L.1    Ramesh, B.2    Söderhäll, K.3
  • 131
    • 64549105261 scopus 로고    scopus 로고
    • Gene silencing of a prophenoloxidase activating enzyme in the shrimp, Penaeus monodon, increases susceptibility to Vibrio harveyi infection
    • Charoensapsri W, Amparyup P, Hirono I et al. Gene silencing of a prophenoloxidase activating enzyme in the shrimp, Penaeus monodon, increases susceptibility to Vibrio harveyi infection. Dev Comp Immunol 2009; 33:811-820.
    • (2009) Dev Comp Immunol , vol.33 , pp. 811-820
    • Charoensapsri, W.1    Amparyup, P.2    Hirono, I.3
  • 132
    • 84954358612 scopus 로고    scopus 로고
    • Two prophenoloxidases are important for the survival of Vibrio harveyi challenged shrimp Penaeus monodon
    • Amparyup P, Charoensapsri W, Tassanakajon A. Two prophenoloxidases are important for the survival of Vibrio harveyi challenged shrimp Penaeus monodon. Dev Comp Immunol 2009; 33:247-256.
    • (2009) Dev Comp Immunol , vol.33 , pp. 247-256
    • Amparyup, P.1    Charoensapsri, W.2    Tassanakajon, A.3
  • 133
    • 69449097951 scopus 로고    scopus 로고
    • Increased bacterial load in shrimp hemolymph in the absence of prophenoloxidase
    • Fagutao FF, Koyama T, Kaizu A et al. Increased bacterial load in shrimp hemolymph in the absence of prophenoloxidase. FEBS J 2009; 276:5298-5306.
    • (2009) FEBS J , vol.276 , pp. 5298-5306
    • Fagutao, F.F.1    Koyama, T.2    Kaizu, A.3
  • 134
    • 74449087251 scopus 로고    scopus 로고
    • Structure and function of invertebrate Kazal-type serine proteinase inhibitors
    • Rimphanitchayakit V, Tassanakajon A. Structure and function of invertebrate Kazal-type serine proteinase inhibitors. Dev Comp Immunol 2010; 34:377-386.
    • (2010) Dev Comp Immunol , vol.34 , pp. 377-386
    • Rimphanitchayakit, V.1    Tassanakajon, A.2
  • 135
    • 70349998712 scopus 로고    scopus 로고
    • High sequence variability among hemocyte-specific Kazal-type proteinase inhibitors in decapod crustaceans
    • Cerenius L, Liu HP, Zhang YJ et al. High sequence variability among hemocyte-specific Kazal-type proteinase inhibitors in decapod crustaceans. Dev Comp Immunol 2010; 34:69-75.
    • (2010) Dev Comp Immunol , vol.34 , pp. 69-75
    • Cerenius, L.1    Liu, H.P.2    Zhang, Y.J.3
  • 136
    • 77649337450 scopus 로고    scopus 로고
    • Multiple forms of alpha-2 macroglobulin in shrimp Fenneropenaeus chinensis and their transcriptional response to WSS V or Vibrio pathogen infection
    • Ma H, Wang B, Zhan J et al. Multiple forms of alpha-2 macroglobulin in shrimp Fenneropenaeus chinensis and their transcriptional response to WSS V or Vibrio pathogen infection. Dev Comp Immunol 2010; 34:677-684.
    • (2010) Dev Comp Immunol , vol.34 , pp. 677-684
    • Ma, H.1    Wang, B.2    Zhan, J.3
  • 137
    • 65249161204 scopus 로고    scopus 로고
    • A novel protein acts as a negative regulator of prophenoloxidase activation and melanization in the freshwater crayfish Pacifastacus leniusculus
    • Söderhäll I, Wu CL, Novotny M et al. A novel protein acts as a negative regulator of prophenoloxidase activation and melanization in the freshwater crayfish Pacifastacus leniusculus. J Biol Chem 2009: 284:6301-6310.
    • (2009) J Biol Chem , vol.284 , pp. 6301-6310
    • Söderhäll, I.1    Wu, C.L.2    Novotny, M.3
  • 139
    • 54449085542 scopus 로고    scopus 로고
    • Molecular control of phenoloxidase-induced melanin synthesis in an insect
    • Kan H, Kim CH, Kwon HM et al. Molecular control of phenoloxidase-induced melanin synthesis in an insect. J Biol Chem 2008; 283:25316-25323.
    • (2008) J Biol Chem , vol.283 , pp. 25316-25323
    • Kan, H.1    Kim, C.H.2    Kwon, H.M.3
  • 140
    • 74549187641 scopus 로고    scopus 로고
    • Distinct melanization pathways in the mosquito Aedes aegyptii
    • Zhou Z, Shin SW, Alvarez KS et al. Distinct melanization pathways in the mosquito Aedes aegyptii. Immunity 2010; 32:41-53.
    • (2010) Immunity , vol.32 , pp. 41-53
    • Zhou, Z.1    Shin, S.W.2    Alvarez, K.S.3
  • 141
    • 0346305961 scopus 로고    scopus 로고
    • Identification of differentially expressed genes in shrimp (Penaeus stylirostris) infected with White spot syndrome virus by cDNA microarrays
    • DOI 10.1007/s00705-003-0172-z
    • Dhar AK, Dettori A, Roux MM et al. Identification of differentially expressed genes in shrimp (Penaeus stylirostris) infected with White spot syndrome virus by cDNA microarrays. Arch Virol 2003; 148:2381-2396. (Pubitemid 38038990)
    • (2003) Archives of Virology , vol.148 , Issue.12 , pp. 2381-2396
    • Dhar, A.K.1    Dettori, A.2    Roux, M.M.3    Klimpel, K.R.4    Read, B.5
  • 142
    • 34248195025 scopus 로고    scopus 로고
    • Molecular cloning of a C-type lectin (LvLT) from the shrimp Litopenaeus vannamei: Early gene down-regulation after WSSV infection
    • DOI 10.1016/j.fsi.2006.12.005, PII S1050464806002452
    • Ma THT, Tiu SHK, He J-G, Chan S-M. Molecular cloning of a C-type lectin (LvLT) from the shrimp Litopenaeus vannamei: Early gene down-regulation after WSSV infection. Fish Shellfish Immunol 2007; 23:430-437. (Pubitemid 46720010)
    • (2007) Fish and Shellfish Immunology , vol.23 , Issue.2 , pp. 430-437
    • Ma, T.H.T.1    Tiu, S.H.K.2    He, J.-G.3    Chan, S.-M.4
  • 143
    • 50349086301 scopus 로고    scopus 로고
    • A C-type like-domain (CTLD)-containing protein (PtLD) from the swimming crab Portunus trituberculatus
    • Kong H-J, Park E-M, Nam B-H et al. A C-type like-domain (CTLD)-containing protein (PtLD) from the swimming crab Portunus trituberculatus. Fish Shellfish Immunol 2008; 25:311-314.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 311-314
    • Kong, H.-J.1    Park, E.-M.2    Nam, B.-H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.