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Volumn 34, Issue 4, 2013, Pages 968-972

Molecular mechanisms of the shrimp clotting system

Author keywords

Clotting protein; Clotting system; Shrimp; Transglutaminase

Indexed keywords

ASTACOIDEA; DECAPODA (CRUSTACEA); INVERTEBRATA; MEROSTOMATA;

EID: 84875379291     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2012.09.018     Document Type: Article
Times cited : (68)

References (70)
  • 2
    • 79955947017 scopus 로고    scopus 로고
    • Fosmid library end sequencing reveals a rarely known genome structure of marine shrimp
    • Huang S.W., Lin Y.Y., You E.M., Liu T.T., Shu H.Y., Wu K.M., et al. Fosmid library end sequencing reveals a rarely known genome structure of marine shrimp. BMC Genomics 2011, 12:242-261.
    • (2011) BMC Genomics , vol.12 , pp. 242-261
    • Huang, S.W.1    Lin, Y.Y.2    You, E.M.3    Liu, T.T.4    Shu, H.Y.5    Wu, K.M.6
  • 3
    • 77949352365 scopus 로고    scopus 로고
    • Hyper-expansion of large DNA segments in the genome of kuruma shrimp, Marsupenaeus japonicus
    • Koyama T., Asakawa S., Katagiri T., Shimizu A., Fagutao F.F., Mavichak R., et al. Hyper-expansion of large DNA segments in the genome of kuruma shrimp, Marsupenaeus japonicus. BMC Genomics 2010, 1:141-152.
    • (2010) BMC Genomics , vol.1 , pp. 141-152
    • Koyama, T.1    Asakawa, S.2    Katagiri, T.3    Shimizu, A.4    Fagutao, F.F.5    Mavichak, R.6
  • 4
    • 0002916432 scopus 로고
    • Meiotic chromosome complements and nuclear DNA contents of four species of shrimps of the genus Penaeus
    • Chow S., Dougherty W.J., Sandifer P.A. Meiotic chromosome complements and nuclear DNA contents of four species of shrimps of the genus Penaeus. J Crustacean Biol 1990, 10:29-36.
    • (1990) J Crustacean Biol , vol.10 , pp. 29-36
    • Chow, S.1    Dougherty, W.J.2    Sandifer, P.A.3
  • 5
    • 0015937516 scopus 로고
    • Nuclear DNA amounts in pacific Crustacea
    • Bachmann K., Rheinsmith E.L. Nuclear DNA amounts in pacific Crustacea. Chromosoma 1973, 43:225-236.
    • (1973) Chromosoma , vol.43 , pp. 225-236
    • Bachmann, K.1    Rheinsmith, E.L.2
  • 6
    • 33746237725 scopus 로고    scopus 로고
    • Development of polymorphic expressed sequence tag-derived microsatellites for the extension of the genetic linkage map of the black tiger shrimp (Penaeus monodon)
    • Maneeruttanarungroj C., Pongsomboon S., Wuthisuthimethavee S., Klinbunga S., Wilson K.J., Swan J., et al. Development of polymorphic expressed sequence tag-derived microsatellites for the extension of the genetic linkage map of the black tiger shrimp (Penaeus monodon). Anim Genet 2006, 37:363-368.
    • (2006) Anim Genet , vol.37 , pp. 363-368
    • Maneeruttanarungroj, C.1    Pongsomboon, S.2    Wuthisuthimethavee, S.3    Klinbunga, S.4    Wilson, K.J.5    Swan, J.6
  • 7
    • 0035321067 scopus 로고    scopus 로고
    • The evolution and genetics of innate immunity
    • Kimbrell D.A., Beutler B. The evolution and genetics of innate immunity. Nat Rev Genet 2001, 2:256-267.
    • (2001) Nat Rev Genet , vol.2 , pp. 256-267
    • Kimbrell, D.A.1    Beutler, B.2
  • 8
    • 78650515757 scopus 로고    scopus 로고
    • Coagulation systems of invertebrates and vertebrates and their roles in innate immunity: the same side of two coins?
    • Loof T.G., Schmidt O., Herwald H., Theopold U. Coagulation systems of invertebrates and vertebrates and their roles in innate immunity: the same side of two coins?. J Innate Immun 2011, 3:34-40.
    • (2011) J Innate Immun , vol.3 , pp. 34-40
    • Loof, T.G.1    Schmidt, O.2    Herwald, H.3    Theopold, U.4
  • 10
  • 11
    • 33846226552 scopus 로고    scopus 로고
    • Functional consequences of blood clotting in insects
    • Haine E.R., Rolff J., Siva-Jothy M.T. Functional consequences of blood clotting in insects. Dev Comp Immunol 2007, 31:456-464.
    • (2007) Dev Comp Immunol , vol.31 , pp. 456-464
    • Haine, E.R.1    Rolff, J.2    Siva-Jothy, M.T.3
  • 12
    • 68549133224 scopus 로고    scopus 로고
    • Insect hemolymph clotting
    • Dushay M. Insect hemolymph clotting. Cell Mol Life Sci 2009, 66:2643-2650.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2643-2650
    • Dushay, M.1
  • 13
    • 84875380449 scopus 로고    scopus 로고
    • Insect hemolymph clotting: evidence for interaction between the coagulation system and the prohenoloxidase activating cascade
    • Li D., Schefer C., Korayem A.M., Zhao Z., Schmidt O., Theopold U. Insect hemolymph clotting: evidence for interaction between the coagulation system and the prohenoloxidase activating cascade. Insect Biochem Mol Biol 2002, 26:177-184.
    • (2002) Insect Biochem Mol Biol , vol.26 , pp. 177-184
    • Li, D.1    Schefer, C.2    Korayem, A.M.3    Zhao, Z.4    Schmidt, O.5    Theopold, U.6
  • 14
    • 0036467504 scopus 로고    scopus 로고
    • The molecular basis of innate immunity in the horseshoe crab
    • Iwanaga S. The molecular basis of innate immunity in the horseshoe crab. Curr Opin Immunol 2002, 14:87-95.
    • (2002) Curr Opin Immunol , vol.14 , pp. 87-95
    • Iwanaga, S.1
  • 15
    • 3042523021 scopus 로고    scopus 로고
    • Structure and function of coagulogen, a clottable protein in horseshoe crab
    • Osaki T., Kabawata S. Structure and function of coagulogen, a clottable protein in horseshoe crab. Cell Mol Life Sci 2004, 61:1257-1265.
    • (2004) Cell Mol Life Sci , vol.61 , pp. 1257-1265
    • Osaki, T.1    Kabawata, S.2
  • 16
    • 20444506858 scopus 로고    scopus 로고
    • Recent advances in the innate immunity of invertebrate animals
    • Iwanaga S., Lee B.L. Recent advances in the innate immunity of invertebrate animals. J Biochem.Mol Biol 2005, 38:128-150.
    • (2005) J Biochem.Mol Biol , vol.38 , pp. 128-150
    • Iwanaga, S.1    Lee, B.L.2
  • 17
    • 0029928757 scopus 로고    scopus 로고
    • The role of hemolymph coagulation in innate immunity
    • Muta T., Iwanaga S. The role of hemolymph coagulation in innate immunity. Curr Opin Immunol 1996, 8:41-47.
    • (1996) Curr Opin Immunol , vol.8 , pp. 41-47
    • Muta, T.1    Iwanaga, S.2
  • 18
    • 0034694375 scopus 로고    scopus 로고
    • The proPO and clotting system in crustaceans
    • Sritunyalucksana K., Söderhäll K. The proPO and clotting system in crustaceans. Aquaculture 2000, 101:53-69.
    • (2000) Aquaculture , vol.101 , pp. 53-69
    • Sritunyalucksana, K.1    Söderhäll, K.2
  • 19
    • 0036076660 scopus 로고    scopus 로고
    • Early events in crustacean innate immunity
    • Lee Y.S., Söderhäll K. Early events in crustacean innate immunity. Fish Shellfish Immunol 2002, 12:421-437.
    • (2002) Fish Shellfish Immunol , vol.12 , pp. 421-437
    • Lee, Y.S.1    Söderhäll, K.2
  • 20
    • 33646495280 scopus 로고    scopus 로고
    • Cell mediated review in arthropods: hematopoiesis, coagulation, melanization and opsonization
    • Jiravanichpaisal P., Lee B.L., Söderhäll K. Cell mediated review in arthropods: hematopoiesis, coagulation, melanization and opsonization. Immunobiology 2006, 211:213-236.
    • (2006) Immunobiology , vol.211 , pp. 213-236
    • Jiravanichpaisal, P.1    Lee, B.L.2    Söderhäll, K.3
  • 21
    • 0027405148 scopus 로고
    • Characterization of a clotting protein, isolated from plasma of the freshwater crayfish Pacifastacus leniusculus
    • Kopacek P., Hall M., Söderhäll K. Characterization of a clotting protein, isolated from plasma of the freshwater crayfish Pacifastacus leniusculus. Eur J Biochem 1993, 213:519-597.
    • (1993) Eur J Biochem , vol.213 , pp. 519-597
    • Kopacek, P.1    Hall, M.2    Söderhäll, K.3
  • 22
    • 0033514933 scopus 로고    scopus 로고
    • The crayfish plasma clotting protein: a vitellogenin-related protein responsible for clot formation in crustacean blood
    • Hall M., Ruigong W., Antwerpen R., Sottrup-Jensen V., Söderhäll K. The crayfish plasma clotting protein: a vitellogenin-related protein responsible for clot formation in crustacean blood. Proc Natl Acad Sci USA 1999, 96:1965-1970.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 1965-1970
    • Hall, M.1    Ruigong, W.2    Antwerpen, R.3    Sottrup-Jensen, V.4    Söderhäll, K.5
  • 23
    • 0035542684 scopus 로고    scopus 로고
    • A transglutaminase involved in the coagulation system of the freshwater crayfish, Pacifastacus leniusculus. Tissue localization and cDNA cloning
    • Wang R., Liang Z., Hall M., Söderhäll K. A transglutaminase involved in the coagulation system of the freshwater crayfish, Pacifastacus leniusculus. Tissue localization and cDNA cloning. Fish Shellfish Immunol 2011, 11:623-637.
    • (2011) Fish Shellfish Immunol , vol.11 , pp. 623-637
    • Wang, R.1    Liang, Z.2    Hall, M.3    Söderhäll, K.4
  • 24
    • 0345863449 scopus 로고    scopus 로고
    • Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase
    • Huang C.C., Sritunyalucksana K., Söderhäll K., Song Y.L. Molecular cloning and characterization of tiger shrimp (Penaeus monodon) transglutaminase. Dev Comp Immunol 2004, 28:279-294.
    • (2004) Dev Comp Immunol , vol.28 , pp. 279-294
    • Huang, C.C.1    Sritunyalucksana, K.2    Söderhäll, K.3    Song, Y.L.4
  • 25
    • 25444462044 scopus 로고    scopus 로고
    • A second type of transglutaminase is involved in shrimp coagulation
    • Chen M.Y., Hu K.Y., Huang C.C., Song Y.L. A second type of transglutaminase is involved in shrimp coagulation. Dev Comp Immunol 2005, 29:1003-1016.
    • (2005) Dev Comp Immunol , vol.29 , pp. 1003-1016
    • Chen, M.Y.1    Hu, K.Y.2    Huang, C.C.3    Song, Y.L.4
  • 26
    • 33846619676 scopus 로고    scopus 로고
    • A transglutaminase from Chinese shrimp (Fenneropenaeus chinensis), full-length cDNA cloning, tissue localization and expression profile after challenge
    • Liu Y.C., Li F.H., Wang B., Dong B., Zhang Q.L., Luan W., et al. A transglutaminase from Chinese shrimp (Fenneropenaeus chinensis), full-length cDNA cloning, tissue localization and expression profile after challenge. Fish Shellfish Immunol 2007, 22:576-588.
    • (2007) Fish Shellfish Immunol , vol.22 , pp. 576-588
    • Liu, Y.C.1    Li, F.H.2    Wang, B.3    Dong, B.4    Zhang, Q.L.5    Luan, W.6
  • 28
    • 37349060626 scopus 로고    scopus 로고
    • Essential function of transglutaminase and clotting protein in shrimp immunity
    • Maningas M.B.B., Kondo H., Hirono I., Saito-Taki T., Aoki T. Essential function of transglutaminase and clotting protein in shrimp immunity. Mol Immunol 2008, 45:1269-1275.
    • (2008) Mol Immunol , vol.45 , pp. 1269-1275
    • Maningas, M.B.B.1    Kondo, H.2    Hirono, I.3    Saito-Taki, T.4    Aoki, T.5
  • 29
    • 0019841763 scopus 로고
    • Fungal cell wall â-1, 3-glucans induce clotting and phenoloxidase attachment to foreign surfaces of crayfish hemocyte lysate
    • Söderhäll K. Fungal cell wall â-1, 3-glucans induce clotting and phenoloxidase attachment to foreign surfaces of crayfish hemocyte lysate. Dev Comp Immunol 1981, 5:565-573.
    • (1981) Dev Comp Immunol , vol.5 , pp. 565-573
    • Söderhäll, K.1
  • 30
    • 0028178005 scopus 로고
    • Crayfish alpha-2-macroglobulin as a substrate to for TGase
    • Hall M., Söderhäll K. Crayfish alpha-2-macroglobulin as a substrate to for TGase. Comp.Biochem.Physiol 1994, 108B:65-72.
    • (1994) Comp.Biochem.Physiol , vol.108 B , pp. 65-72
    • Hall, M.1    Söderhäll, K.2
  • 31
    • 0025790041 scopus 로고
    • Localization and roles of transglutaminase in hemolymph coahulation in decapods crustaceans
    • Martin G.G., Hose J.E., Omori S., Chong C., Hoodbhoy T., McKrell N. Localization and roles of transglutaminase in hemolymph coahulation in decapods crustaceans. Comp Biochem Physiol 1991, 3:517-522.
    • (1991) Comp Biochem Physiol , vol.3 , pp. 517-522
    • Martin, G.G.1    Hose, J.E.2    Omori, S.3    Chong, C.4    Hoodbhoy, T.5    McKrell, N.6
  • 32
    • 55349103779 scopus 로고    scopus 로고
    • Transglutaminase activity in the hematopoietic tissue of a crustacean, Pacifastacus leniusculus, importance in hemocyte homeostasis
    • Lin X., Söderhäll K., Söderhäll 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.1    Söderhäll, K.2    Söderhäll3
  • 33
    • 33746050656 scopus 로고    scopus 로고
    • Biochemical characterization and cloning of transglutaminases responsible for hemolymph clotting in Penaeus monodon and Marsupenaeus japonicus
    • Yeh M.S., Kao L.R., Huang C.J., Tsai I.H. Biochemical characterization and cloning of transglutaminases responsible for hemolymph clotting in Penaeus monodon and Marsupenaeus japonicus. Biochim Biophys Acta 2006, 1764:1167-1178.
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1167-1178
    • Yeh, M.S.1    Kao, L.R.2    Huang, C.J.3    Tsai, I.H.4
  • 34
    • 70350770824 scopus 로고    scopus 로고
    • CDNA cloning, identification, tissue localisation, and transcription profile of a transglutaminase from white shrimp, Litopenaeus vannamei, after infection by Vibrio alginolyticus
    • Yeh M.S., Liu C.H., Hung C.W., Cheng W. cDNA cloning, identification, tissue localisation, and transcription profile of a transglutaminase from white shrimp, Litopenaeus vannamei, after infection by Vibrio alginolyticus. Fish Shellfish Immunol 2009, 27(6):748-756.
    • (2009) Fish Shellfish Immunol , vol.27 , Issue.6 , pp. 748-756
    • Yeh, M.S.1    Liu, C.H.2    Hung, C.W.3    Cheng, W.4
  • 35
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminase: nature's biological glues
    • Griffin M., Casadio R., Bergamini C.M. Transglutaminase: nature's biological glues. Biochem J 2002, 368(Pt 2):377-396.
    • (2002) Biochem J , vol.368 , Issue.PART 2 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 36
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: crosslinking enzymes with pleiotropic functions
    • Lorand L., Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat Rev 2003, 4(2):140-156.
    • (2003) Nat Rev , vol.4 , Issue.2 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 37
    • 77649265237 scopus 로고    scopus 로고
    • Pathogen entrapment by transglutaminase-A conserved early innate immune mechanism
    • Wang Z., Wilhelmsson C., Hyrsl P., Loof T.G., Dobes P., Klupp M., et al. Pathogen entrapment by transglutaminase-A conserved early innate immune mechanism. PLoS Pathog 2010, 6(2):e1000763. 10.1371/journal.ppat.1000763.
    • (2010) PLoS Pathog , vol.6 , Issue.2
    • Wang, Z.1    Wilhelmsson, C.2    Hyrsl, P.3    Loof, T.G.4    Dobes, P.5    Klupp, M.6
  • 38
    • 0037380557 scopus 로고    scopus 로고
    • Haemolymph parameters of Pacific white shrimp (Litopenaeus vannamei) infected with Taura syndrome virus
    • Song Y.L., Yu C.I., Lien T.W., Huang C.C., Lin M.N. Haemolymph parameters of Pacific white shrimp (Litopenaeus vannamei) infected with Taura syndrome virus. Fish Shellfish Immunol 2003, 14(4):317-331.
    • (2003) Fish Shellfish Immunol , vol.14 , Issue.4 , pp. 317-331
    • Song, Y.L.1    Yu, C.I.2    Lien, T.W.3    Huang, C.C.4    Lin, M.N.5
  • 39
    • 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
    • Han-Ching Wang K., Tseng C.E., Lin H.Y., Chen I.T., Chen Y.H., Chen Y.M., 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(1):49-58.
    • (2010) Dev Comp Immunol , vol.34 , Issue.1 , pp. 49-58
    • Han-Ching Wang, K.1    Tseng, C.E.2    Lin, H.Y.3    Chen, I.T.4    Chen, Y.H.5    Chen, Y.M.6
  • 40
    • 79959385370 scopus 로고    scopus 로고
    • Crustacean hematopoiesis and the astakine cytokines
    • Lin X., Söderhäll I. Crustacean hematopoiesis and the astakine cytokines. Blood 2011, 117(24):6417-6424.
    • (2011) Blood , vol.117 , Issue.24 , pp. 6417-6424
    • Lin, X.1    Söderhäll, I.2
  • 41
    • 78149426519 scopus 로고    scopus 로고
    • Protein crosslinking by transglutaminase controls cuticle morphogenesis in drosophila
    • Shibata T., Ariki S., Shinzawa N., Miyaji R., Suyama H., Sako M., et al. Protein crosslinking by transglutaminase controls cuticle morphogenesis in drosophila. PLoS One 2010, 5(10):e13477. 10.1371/journal.pone.0013477.
    • (2010) PLoS One , vol.5 , Issue.10
    • Shibata, T.1    Ariki, S.2    Shinzawa, N.3    Miyaji, R.4    Suyama, H.5    Sako, M.6
  • 42
    • 0038272020 scopus 로고    scopus 로고
    • The evolution of vertebrate blood coagulation as viewed from a comparison of puffer fish and sea squirt genomes
    • Jiang Y., Doolittle R.F. The evolution of vertebrate blood coagulation as viewed from a comparison of puffer fish and sea squirt genomes. Proc Natl Acad Sci USA 2003, 100:7527-7532.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7527-7532
    • Jiang, Y.1    Doolittle, R.F.2
  • 44
    • 0032428456 scopus 로고    scopus 로고
    • The hemolymph clottable proteins of tiger shrimp, Penaeus monodon, and related species
    • Yeh M.S., Chen Y.L., Tsai I.H. The hemolymph clottable proteins of tiger shrimp, Penaeus monodon, and related species. Comp Biochem Physiol 1998, 121:169-176.
    • (1998) Comp Biochem Physiol , vol.121 , pp. 169-176
    • Yeh, M.S.1    Chen, Y.L.2    Tsai, I.H.3
  • 45
    • 0033485927 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a hemolymph clottable protein from tiger shrimp (Penaeus monodon)
    • Yeh M.S., Huang C.J., Leu J.H., Lee Y.C., Tsai I.H. Molecular cloning and characterization of a hemolymph clottable protein from tiger shrimp (Penaeus monodon). Eur J Biochem 1999, 266:624-633.
    • (1999) Eur J Biochem , vol.266 , pp. 624-633
    • Yeh, M.S.1    Huang, C.J.2    Leu, J.H.3    Lee, Y.C.4    Tsai, I.H.5
  • 47
    • 0035929165 scopus 로고    scopus 로고
    • Proteinase activity in the white shrimp (Penaeus vannamei) clotting protein
    • Reyes-Izquierdo T., Vargas-Albores F. Proteinase activity in the white shrimp (Penaeus vannamei) clotting protein. Biochem Biophys Res Comm 2001, 287:332-336.
    • (2001) Biochem Biophys Res Comm , vol.287 , pp. 332-336
    • Reyes-Izquierdo, T.1    Vargas-Albores, F.2
  • 48
    • 26844546722 scopus 로고    scopus 로고
    • Purification and partial characterization of the plasma clotting protein from pink shrimp Farfantepenaeus paulensis
    • Perazzolo L.M., Lorenzini D.M., Daffre S., Barracco M.A. Purification and partial characterization of the plasma clotting protein from pink shrimp Farfantepenaeus paulensis. Comp Biochem Physiol 2005, 142(3):302-307.
    • (2005) Comp Biochem Physiol , vol.142 , Issue.3 , pp. 302-307
    • Perazzolo, L.M.1    Lorenzini, D.M.2    Daffre, S.3    Barracco, M.A.4
  • 49
    • 0028839529 scopus 로고
    • Identification of the major lipoproteins in crayfish hemolymph as proteins involved in immune recognition and clotting
    • Hall M., van Heusden M.C., Söderhäll K. Identification of the major lipoproteins in crayfish hemolymph as proteins involved in immune recognition and clotting. Biophys Res Commun 1995, 216:939-946.
    • (1995) Biophys Res Commun , vol.216 , pp. 939-946
    • Hall, M.1    van Heusden, M.C.2    Söderhäll, K.3
  • 51
    • 34248375582 scopus 로고    scopus 로고
    • Tissue-specific expression and regulation of the hemolymph clottable protein of tiger shrimp (Penaeus monodon)
    • Yeh M.S., Huang C.J., Cheng J.H., Tsai I.H. Tissue-specific expression and regulation of the hemolymph clottable protein of tiger shrimp (Penaeus monodon). Fish Shellfish Immunol 2007, 23:272-279.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 272-279
    • Yeh, M.S.1    Huang, C.J.2    Cheng, J.H.3    Tsai, I.H.4
  • 52
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: from invertebrates to vertebrates
    • Bulet P., Stöcklin R., Menin L. Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 2004, 198:169-184.
    • (2004) Immunol Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stöcklin, R.2    Menin, L.3
  • 53
    • 77649237880 scopus 로고    scopus 로고
    • Antimicrobial peptides: general overview and clinical implications in human health and disease
    • Guaní-Guerra E., Santos-Mendoza T., Lugo-Reyes S.O., Terán L.M. Antimicrobial peptides: general overview and clinical implications in human health and disease. Clin Immunol 2010, 135:1-11.
    • (2010) Clin Immunol , vol.135 , pp. 1-11
    • Guaní-Guerra, E.1    Santos-Mendoza, T.2    Lugo-Reyes, S.O.3    Terán, L.M.4
  • 54
    • 0042381670 scopus 로고    scopus 로고
    • Novel properties of antimicrobial peptides
    • Kamysz W., Okroj M., Lukasiak J. Novel properties of antimicrobial peptides. Acta Biochim Pol 2003, 50:461-469.
    • (2003) Acta Biochim Pol , vol.50 , pp. 461-469
    • Kamysz, W.1    Okroj, M.2    Lukasiak, J.3
  • 55
    • 61349169039 scopus 로고    scopus 로고
    • AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense
    • Lai Y., Gallo R.L. AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol 2009, 30:131-141.
    • (2009) Trends Immunol , vol.30 , pp. 131-141
    • Lai, Y.1    Gallo, R.L.2
  • 57
    • 1642422727 scopus 로고    scopus 로고
    • Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Craccostrea gigas
    • Bachere E., Gueguen Y., de Lorgeni J., Gamier J., Romestand B. Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Craccostrea gigas. Immunol Rev 2004, 198:149-168.
    • (2004) Immunol Rev , vol.198 , pp. 149-168
    • Bachere, E.1    Gueguen, Y.2    de Lorgeni, J.3    Gamier, J.4    Romestand, B.5
  • 58
    • 0030692830 scopus 로고    scopus 로고
    • Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (decapoda)
    • Destoumieux D., Bulet P., Loew D., VanDorsselaer A., Rodriguez J., Bachere E. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (decapoda). J Biol Chem 1997, 272:28398-28406.
    • (1997) J Biol Chem , vol.272 , pp. 28398-28406
    • Destoumieux, D.1    Bulet, P.2    Loew, D.3    VanDorsselaer, A.4    Rodriguez, J.5    Bachere, E.6
  • 60
    • 79960901109 scopus 로고    scopus 로고
    • Antimicrobial peptides in crustaceans
    • Barracco
    • Rosa R.D., Barracco Antimicrobial peptides in crustaceans. Inv Surv J 2010, 7:262-284.
    • (2010) Inv Surv J , vol.7 , pp. 262-284
    • Rosa, R.D.1
  • 62
    • 73049097239 scopus 로고    scopus 로고
    • The antimicrobial peptides of the immune response of shrimp
    • Zhao X.F., Wang J.X. The antimicrobial peptides of the immune response of shrimp. Inv Surv J 2008, 5:162-179.
    • (2008) Inv Surv J , vol.5 , pp. 162-179
    • Zhao, X.F.1    Wang, J.X.2
  • 63
    • 44749090947 scopus 로고    scopus 로고
    • A relationship between antimicrobial peptide gene expression and capacity of a selected shrimp line to survive a Vibrio infection
    • de Lorgeril J., Gueguen Y., Goarant C., Goyard E., Mugnier C., Fievet J., et al. A relationship between antimicrobial peptide gene expression and capacity of a selected shrimp line to survive a Vibrio infection. Mol Immunol 2008, 45(12):3438-3445.
    • (2008) Mol Immunol , vol.45 , Issue.12 , pp. 3438-3445
    • de Lorgeril, J.1    Gueguen, Y.2    Goarant, C.3    Goyard, E.4    Mugnier, C.5    Fievet, J.6
  • 64
    • 84455161739 scopus 로고    scopus 로고
    • Functional analysis of C-type lysozyme in Penaeid shrimp
    • Kaizu A., Fagutao F.F., Kondo H., Aoki T., Hirono I. Functional analysis of C-type lysozyme in Penaeid shrimp. J Biol Chem 2011, 286(52):44344-44349.
    • (2011) J Biol Chem , vol.286 , Issue.52 , pp. 44344-44349
    • Kaizu, A.1    Fagutao, F.F.2    Kondo, H.3    Aoki, T.4    Hirono, I.5
  • 65
    • 84883623045 scopus 로고    scopus 로고
    • Antimicrobial peptides from the black tiger shrimp Penaeus monodon - a review
    • Tassanakajon A., Somboonwiwat K. Antimicrobial peptides from the black tiger shrimp Penaeus monodon - a review. Diseases in Asian aquaculture 2011, vol. VII:229-240.
    • (2011) Diseases in Asian aquaculture , vol.8 , pp. 229-240
    • Tassanakajon, A.1    Somboonwiwat, K.2
  • 66
    • 0027050777 scopus 로고
    • A common domain within the pro-enzyme regions of the Drosophila snake and easter proteins and Tachypleus pro-clotting enzymes defines a new subfamily of serine proteases
    • Smith C.L., De Lotto R. A common domain within the pro-enzyme regions of the Drosophila snake and easter proteins and Tachypleus pro-clotting enzymes defines a new subfamily of serine proteases. Protein Sci 1992, 1:1225-1226.
    • (1992) Protein Sci , vol.1 , pp. 1225-1226
    • Smith, C.L.1    De Lotto, R.2
  • 67
    • 0035059407 scopus 로고    scopus 로고
    • Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus
    • Wang R., Lee S.Y., Cerenius L., Söderhäll K. Properties of the prophenoloxidase activating enzyme of the freshwater crayfish, Pacifastacus leniusculus. Eur J Biochem 2001, 268:895-902.
    • (2001) Eur J Biochem , vol.268 , pp. 895-902
    • Wang, R.1    Lee, S.Y.2    Cerenius, L.3    Söderhäll, K.4
  • 68
    • 0036470428 scopus 로고    scopus 로고
    • Evolution of enzyme cascades from embryonic development to blood coagulation
    • Krem M.M., Cera E.D. Evolution of enzyme cascades from embryonic development to blood coagulation. Trends Biochem Sci 2002, 27:67-74.
    • (2002) Trends Biochem Sci , vol.27 , pp. 67-74
    • Krem, M.M.1    Cera, E.D.2
  • 69
    • 33746619204 scopus 로고    scopus 로고
    • The interaction between pathogens and the host coagulation system
    • Sun H. The interaction between pathogens and the host coagulation system. Physiology 2005, 21:281-288.
    • (2005) Physiology , vol.21 , pp. 281-288
    • Sun, H.1
  • 70
    • 33644801469 scopus 로고    scopus 로고
    • The interactions between inflammation and coagulation
    • Esmon C.T. The interactions between inflammation and coagulation. Br J Haematol 2005, 131:417-430.
    • (2005) Br J Haematol , vol.131 , pp. 417-430
    • Esmon, C.T.1


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