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Volumn 8, Issue 8, 2013, Pages

A Double WAP Domain-Containing Protein Es-DWD1 from Eriocheir sinensis Exhibits Antimicrobial and Proteinase Inhibitory Activities

Author keywords

[No Author keywords available]

Indexed keywords

AGAROSE; COMPLEMENTARY DNA; DOUBLE WHEY ACIDIC PROTEIN DOMAIN CONTAINING PROTEIN; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEINASE INHIBITOR; SIGNAL PEPTIDE; UNCLASSIFIED DRUG;

EID: 84881510926     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0073563     Document Type: Article
Times cited : (52)

References (62)
  • 1
    • 0028933794 scopus 로고
    • Peptide antibiotics and their role in innate immunity
    • doi:10.1146/annurev.iy.13.040195.000425
    • Boman HG, (1995) Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 13: 61-92. doi:10.1146/annurev.iy.13.040195.000425. PubMed: 7612236.
    • (1995) Annu Rev Immunol , vol.13 , pp. 61-92
    • Boman, H.G.1
  • 2
    • 1642545489 scopus 로고    scopus 로고
    • Anti-microbial peptides: from invertebrates to vertebrates
    • doi:10.1111/j.0105-2896.2004.0124.x
    • Bulet P, Stöcklin R, Menin L, (2004) Anti-microbial peptides: from invertebrates to vertebrates. Immunol Rev 198: 169-184. doi:10.1111/j.0105-2896.2004.0124.x. PubMed: 15199962.
    • (2004) Immunol Rev , vol.198 , pp. 169-184
    • Bulet, P.1    Stöcklin, R.2    Menin, L.3
  • 3
    • 40849102419 scopus 로고    scopus 로고
    • Crustins: enigmatic WAP domain-containing antibacterial proteins from crustaceans
    • doi:10.1016/j.dci.2007.12.002
    • Smith VJ, Fernandes JM, Kemp GD, Hauton C, (2008) Crustins: enigmatic WAP domain-containing antibacterial proteins from crustaceans. Dev Comp Immunol 32: 758-772. doi:10.1016/j.dci.2007.12.002. PubMed: 18222540.
    • (2008) Dev Comp Immunol , vol.32 , pp. 758-772
    • Smith, V.J.1    Fernandes, J.M.2    Kemp, G.D.3    Hauton, C.4
  • 4
    • 0000056632 scopus 로고    scopus 로고
    • The whey acidic protein family: a new signature motif and three dimensional structure by comparative modeling
    • doi:10.1016/S1093-3263(99)00023-6
    • Ranganathan S, Simpson KJ, Shaw DC, Nicholas K, (1999) The whey acidic protein family: a new signature motif and three dimensional structure by comparative modeling. J Mol Graph Modell 17: 106-113. doi:10.1016/S1093-3263(99)00023-6.
    • (1999) J Mol Graph Modell , vol.17 , pp. 106-113
    • Ranganathan, S.1    Simpson, K.J.2    Shaw, D.C.3    Nicholas, K.4
  • 5
    • 0020489775 scopus 로고
    • Mouse whey acidic protein is a novel member of the family of 'four-disulfi{ligature}de core' proteins
    • doi:10.1093/nar/10.8.2677
    • Hennighausen LG, Sippel AE, (1982) Mouse whey acidic protein is a novel member of the family of 'four-disulfi{ligature}de core' proteins. Nucleic Acids Res 10: 2677-2684. doi:10.1093/nar/10.8.2677. PubMed: 6896234.
    • (1982) Nucleic Acids Res , vol.10 , pp. 2677-2684
    • Hennighausen, L.G.1    Sippel, A.E.2
  • 6
    • 0036547750 scopus 로고    scopus 로고
    • Antimicrobial activity of antiproteinases
    • Sallenave JM, (2002) Antimicrobial activity of antiproteinases. Biochem Soc Trans 30: 111-115. PubMed: 12023836.
    • (2002) Biochem Soc Trans , vol.30 , pp. 111-115
    • Sallenave, J.M.1
  • 7
    • 73049108425 scopus 로고    scopus 로고
    • A single WAP domain (SWD)-containing protein with antipathic relevance in red swamp crayfish, Procambarus clarkii
    • doi:10.1016/j.fsi.2009.10.009
    • Du ZQ, Li XC, Wang ZH, Zhao XF, Wang JX, (2010) A single WAP domain (SWD)-containing protein with antipathic relevance in red swamp crayfish, Procambarus clarkii. Fish Shellfish Immunol 28: 134-142. doi:10.1016/j.fsi.2009.10.009. PubMed: 19840856.
    • (2010) Fish Shellfish Immunol , vol.28 , pp. 134-142
    • Du, Z.Q.1    Li, X.C.2    Wang, Z.H.3    Zhao, X.F.4    Wang, J.X.5
  • 8
    • 49949095079 scopus 로고    scopus 로고
    • Mj-DWD, a double WAP domain-containing protein with antiviral relevance in Marsupenaeus japonicus
    • doi:10.1016/j.fsi.2008.02.017
    • Chen D, He N, Xu X, (2008) Mj-DWD, a double WAP domain-containing protein with antiviral relevance in Marsupenaeus japonicus. Fish Shellfish Immunol 25: 775-781. doi:10.1016/j.fsi.2008.02.017. PubMed: 18974012.
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 775-781
    • Chen, D.1    He, N.2    Xu, X.3
  • 9
    • 80053366469 scopus 로고    scopus 로고
    • Phylogeny of whey acidic protein (WAP) four-disulfide core proteins and their role in lower vertebrates and invertebrates
    • doi:10.1042/BST0391403
    • Smith VJ, (2011) Phylogeny of whey acidic protein (WAP) four-disulfide core proteins and their role in lower vertebrates and invertebrates. Biochem Soc Trans 39: 1403-1408. doi:10.1042/BST0391403. PubMed: 21936823.
    • (2011) Biochem Soc Trans , vol.39 , pp. 1403-1408
    • Smith, V.J.1
  • 10
    • 0037442202 scopus 로고    scopus 로고
    • Mouse SWAM1 and SWAM2 are antibacterial proteins composed of a single whey acidic protein motif
    • Hagiwara K, Kikuchi T, Endo Y, Huqun Usui K, Takahashi M, et al. (2003) Mouse SWAM1 and SWAM2 are antibacterial proteins composed of a single whey acidic protein motif. J Immunol 170: 1973-1979. PubMed: 12574366.
    • (2003) J Immunol , vol.170 , pp. 1973-1979
    • Hagiwara, K.1    Kikuchi, T.2    Endo, Y.3    Huqun Usui, K.4    Takahashi, M.5
  • 13
    • 27944505171 scopus 로고    scopus 로고
    • The novel avian protein, AWAK, contains multiple domains with homology to protease inhibitory modules
    • doi:10.1016/j.molimm.2005.02.015
    • Nile CJ, Townes CL, Hirst BH, Hall J, (2006) The novel avian protein, AWAK, contains multiple domains with homology to protease inhibitory modules. Mol Immunol 43: 388-394. doi:10.1016/j.molimm.2005.02.015. PubMed: 16310052.
    • (2006) Mol Immunol , vol.43 , pp. 388-394
    • Nile, C.J.1    Townes, C.L.2    Hirst, B.H.3    Hall, J.4
  • 15
    • 0027980413 scopus 로고
    • Purification and cDNA cloning of a four-domain Kazal proteinase inhibitor from crayfish blood cells
    • doi:10.1111/j.1432-1033.1994.tb19005.x
    • Johansson MW, Keyser P, Söderhäll K, (1994) Purification and cDNA cloning of a four-domain Kazal proteinase inhibitor from crayfish blood cells. Eur J Biochem 223: 389-394. doi:10.1111/j.1432-1033.1994.tb19005.x. PubMed: 8055907.
    • (1994) Eur J Biochem , vol.223 , pp. 389-394
    • Johansson, M.W.1    Keyser, P.2    Söderhäll, K.3
  • 16
    • 13544251554 scopus 로고    scopus 로고
    • A four-Kazal domain protein in Litopenaeus vannamei hemocytes
    • doi:10.1016/j.dci.2004.10.001
    • Jiménez-Vega F, Vargas-Albores F, (2005) A four-Kazal domain protein in Litopenaeus vannamei hemocytes. Dev Comp Immunol 29: 385-391. doi:10.1016/j.dci.2004.10.001. PubMed: 15707660.
    • (2005) Dev Comp Immunol , vol.29 , pp. 385-391
    • Jiménez-Vega, F.1    Vargas-Albores, F.2
  • 17
    • 0036755716 scopus 로고    scopus 로고
    • Identification of immune-related genes in hemocytes of black tiger shrimp (Penaeus monodon)
    • doi:10.1007/s10126-002-0043-8
    • Supungul P, Klinbunga S, Pichyangkura R, Jitrapakdee S, Hirono I, Aoki T, et al. (2002) Identification of immune-related genes in hemocytes of black tiger shrimp (Penaeus monodon). Mar Biotechnol 4: 487-494. doi:10.1007/s10126-002-0043-8. PubMed: 14961242.
    • (2002) Mar Biotechnol , vol.4 , pp. 487-494
    • Supungul, P.1    Klinbunga, S.2    Pichyangkura, R.3    Jitrapakdee, S.4    Hirono, I.5    Aoki, T.6
  • 18
    • 0030917010 scopus 로고    scopus 로고
    • Pacifastin, a novel 155-kDa heterodimeric proteinase inhibitor containing a unique transferrin chain
    • doi:10.1073/pnas.94.13.6682
    • Liang Z, Sottrup-Jensen L, Aspán A, Hall M, Söderhäll K, (1997) Pacifastin, a novel 155-kDa heterodimeric proteinase inhibitor containing a unique transferrin chain. Proc Natl Acad Sci U S A 94: 6682-6687. doi:10.1073/pnas.94.13.6682. PubMed: 9192625.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6682-6687
    • Liang, Z.1    Sottrup-Jensen, L.2    Aspán, A.3    Hall, M.4    Söderhäll, K.5
  • 19
    • 0028788934 scopus 로고
    • Isolation of cDNA encoding a novel serpin of crayfish hemocytes
    • Liang Z, Söderhäll K, (1995) Isolation of cDNA encoding a novel serpin of crayfish hemocytes. Comp Biochem Physiol B Biochem Mol Biol 112: 384-391. PubMed: 7584865.
    • (1995) Comp Biochem Physiol B Biochem Mol Biol , vol.112 , pp. 384-391
    • Liang, Z.1    Söderhäll, K.2
  • 20
    • 0024980237 scopus 로고
    • Amino acid sequence around the thiolester of alpha 2-macroglobulin from plasma of the crayfish, Pacifastacus leniusculus
    • doi:10.1016/0014-5793(89)81019-1
    • Hall M, Söderhäll K, Sottrup-Jensen L, (1989) Amino acid sequence around the thiolester of alpha 2-macroglobulin from plasma of the crayfish, Pacifastacus leniusculus. FEBS Lett 254: 111-114. doi:10.1016/0014-5793(89)81019-1. PubMed: 2476331.
    • (1989) FEBS Lett , vol.254 , pp. 111-114
    • Hall, M.1    Söderhäll, K.2    Sottrup-Jensen, L.3
  • 22
    • 2442454655 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of alpha 2-macroglobulin in the kuruma shrimp, Marsupenaeus japonicus
    • doi:10.1016/j.fsi.2003.09.011
    • Rattanachai A, Hirono I, Ohira T, Takahashi T, Aoki T, (2004) Molecular cloning and expression analysis of alpha 2-macroglobulin in the kuruma shrimp, Marsupenaeus japonicus. Fish Shellfish Immunol 16: 599-611. doi:10.1016/j.fsi.2003.09.011. PubMed: 15110334.
    • (2004) Fish Shellfish Immunol , vol.16 , pp. 599-611
    • Rattanachai, A.1    Hirono, I.2    Ohira, T.3    Takahashi, T.4    Aoki, T.5
  • 23
    • 33748758437 scopus 로고    scopus 로고
    • Molecular cloning and characterisation of a proteinase inhibitor, alpha 2-macroglobulin (alpha2-M) from the haemocytes of tiger shrimp Penaeus monodon
    • doi:10.1016/j.molimm.2006.08.002
    • Lin YC, Vaseeharan B, Ko CF, Chiou TT, Chen JC, (2007) Molecular cloning and characterisation of a proteinase inhibitor, alpha 2-macroglobulin (alpha2-M) from the haemocytes of tiger shrimp Penaeus monodon. Mol Immunol 44: 1065-1074. doi:10.1016/j.molimm.2006.08.002. PubMed: 16982096.
    • (2007) Mol Immunol , vol.44 , pp. 1065-1074
    • Lin, Y.C.1    Vaseeharan, B.2    Ko, C.F.3    Chiou, T.T.4    Chen, J.C.5
  • 24
    • 37349103963 scopus 로고    scopus 로고
    • Molecular cloning and phylogenetic analysis on alpha2-macroglobulin (alpha2-M) of white shrimp Litopenaeusvannamei
    • doi:10.1016/j.dci.2007.07.002
    • Lin YC, Vaseeharan B, Chen JC, (2008) Molecular cloning and phylogenetic analysis on alpha2-macroglobulin (alpha2-M) of white shrimp Litopenaeusvannamei. Dev Comp Immunol 32: 317-329. doi:10.1016/j.dci.2007.07.002. PubMed: 17706773.
    • (2008) Dev Comp Immunol , vol.32 , pp. 317-329
    • Lin, Y.C.1    Vaseeharan, B.2    Chen, J.C.3
  • 25
    • 67651083312 scopus 로고    scopus 로고
    • A double WAP domain (DWD)- containing protein with proteinase inhibitory activity in Chinese white shrimp, Fenneropenaeus chinensis
    • doi:10.1016/j.cbpb.2009.06.004
    • Du ZQ, Ren Q, Zhao XF, Wang JX, (2009) A double WAP domain (DWD)- containing protein with proteinase inhibitory activity in Chinese white shrimp, Fenneropenaeus chinensis. Comp Biochem Physiol B Biochem Mol Biol 154: 203-210. doi:10.1016/j.cbpb.2009.06.004. PubMed: 19545640.
    • (2009) Comp Biochem Physiol B Biochem Mol Biol , vol.154 , pp. 203-210
    • Du, Z.Q.1    Ren, Q.2    Zhao, X.F.3    Wang, J.X.4
  • 26
    • 34548474857 scopus 로고    scopus 로고
    • A secretory leukocyte proteinase inhibitor (SLPI)-like protein from Litopenaeus vannamei haemocytes
    • doi:10.1016/j.fsi.2007.06.006
    • Jiménez-Vega F, Vargas-Albores F, (2007) A secretory leukocyte proteinase inhibitor (SLPI)-like protein from Litopenaeus vannamei haemocytes. Fish Shellfish Immunol 23: 1119-1126. doi:10.1016/j.fsi.2007.06.006. PubMed: 17664073.
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 1119-1126
    • Jiménez-Vega, F.1    Vargas-Albores, F.2
  • 27
    • 0035941480 scopus 로고    scopus 로고
    • A survey of genes in the Atlantic salmon (Salmo salar) as identifi{ligature}ed by expressed sequence tags
    • doi:10.1016/S0378-1119(00)00587-4
    • Davey GC, Caplice NC, Martin SA, Powell R, (2001) A survey of genes in the Atlantic salmon (Salmo salar) as identifi{ligature}ed by expressed sequence tags. Gene 263: 121-130. doi:10.1016/S0378-1119(00)00587-4. PubMed: 11223250.
    • (2001) Gene , vol.263 , pp. 121-130
    • Davey, G.C.1    Caplice, N.C.2    Martin, S.A.3    Powell, R.4
  • 28
    • 36248948251 scopus 로고    scopus 로고
    • Current trends of aquaculture roduction and sustainable development of Chinese mitten crab, Eriocheir sinensis
    • Yang WL, Zhang GH, (2005) Current trends of aquaculture roduction and sustainable development of Chinese mitten crab, Eriocheir sinensis. Chin J Freshwater Fish 35: 62-64.
    • (2005) Chin J Freshwater Fish , vol.35 , pp. 62-64
    • Yang, W.L.1    Zhang, G.H.2
  • 29
    • 4544358441 scopus 로고    scopus 로고
    • Morphology of spiroplasmas in the Chinese mitten crab Eriocheir sinensis associated with tremor disease
    • doi:10.1016/j.resmic.2004.04.010
    • Wang W, Chen J, Du K, Xu Z, (2004) Morphology of spiroplasmas in the Chinese mitten crab Eriocheir sinensis associated with tremor disease. Res Microbiol 155: 630-635. doi:10.1016/j.resmic.2004.04.010. PubMed: 15380550.
    • (2004) Res Microbiol , vol.155 , pp. 630-635
    • Wang, W.1    Chen, J.2    Du, K.3    Xu, Z.4
  • 30
    • 2542425009 scopus 로고    scopus 로고
    • Mass mortality of larval Eriocheir sinensis (Decapoda: Grapsidae) population bred under facility conditions: possible role of Zoothamnium sp. (Peritrichida: Vorticellidae) Epiphyte
    • doi:10.1016/j.jip.2004.03.010
    • Wu HX, Feng MG, (2004) Mass mortality of larval Eriocheir sinensis (Decapoda: Grapsidae) population bred under facility conditions: possible role of Zoothamnium sp. (Peritrichida: Vorticellidae) Epiphyte. J Invertebr Pathol 86: 59-60. doi:10.1016/j.jip.2004.03.010. PubMed: 15145254.
    • (2004) J Invertebr Pathol , vol.86 , pp. 59-60
    • Wu, H.X.1    Feng, M.G.2
  • 31
    • 2542502883 scopus 로고    scopus 로고
    • Preliminary studies on two strains of reovirus from crab Eriocheir sinensis
    • Zhang S, Zhang J, Huang C, Bonami JR, Shi Z, (2002) Preliminary studies on two strains of reovirus from crab Eriocheir sinensis. Virol Sin 17: 263-265.
    • (2002) Virol Sin , vol.17 , pp. 263-265
    • Zhang, S.1    Zhang, J.2    Huang, C.3    Bonami, J.R.4    Shi, Z.5
  • 32
    • 0020728304 scopus 로고
    • Separation of the haemocyte populations of Carcinus maenas and other marine decapods, and prophenoloxidase distribution
    • doi:10.1016/0145-305X(83)90004-6
    • Söderhäll K, Smith VJ, (1983) Separation of the haemocyte populations of Carcinus maenas and other marine decapods, and prophenoloxidase distribution. Dev Comp Immunol 7: 229-239. doi:10.1016/0145-305X(83)90004-6. PubMed: 6409683.
    • (1983) Dev Comp Immunol , vol.7 , pp. 229-239
    • Söderhäll, K.1    Smith, V.J.2
  • 33
    • 84964097788 scopus 로고
    • A physiological solution for freshwater crustaceans
    • Van Harreveld (1936) A physiological solution for freshwater crustaceans. Exp Biol Med 34: 428-432.
    • (1936) Exp Biol Med , vol.34 , pp. 428-432
    • Van, H.1
  • 34
    • 84863347246 scopus 로고    scopus 로고
    • Transcriptome Profiling of Testis during Sexual Maturation Stages in Eriocheir sinensis Using Illumina Sequencing
    • He L, Wang Q, Jin X, Wang Y, Chen L, et al. Transcriptome Profiling of Testis during Sexual Maturation Stages in Eriocheir sinensis Using Illumina Sequencing. PLOS ONE. 20127: e33735.
    • PLOS ONE , vol.7
    • He, L.1    Wang, Q.2    Jin, X.3    Wang, Y.4    Chen, L.5
  • 35
    • 77955292449 scopus 로고    scopus 로고
    • Molecular Cloning and Gene Expression Analysis of the Leptin Receptor in the Chinese Mitten Crab Eriocheir sinensis
    • doi:10.1371/journal.pone.0011175
    • Jiang H, Ren F, Sun J, He L, Li W, et al. (2010) Molecular Cloning and Gene Expression Analysis of the Leptin Receptor in the Chinese Mitten Crab Eriocheir sinensis. PLOS ONE 5: e11175. doi:10.1371/journal.pone.0011175. PubMed: 20567508.
    • (2010) PLOS ONE , vol.5
    • Jiang, H.1    Ren, F.2    Sun, J.3    He, L.4    Li, W.5
  • 36
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2-ΔΔCT Method
    • doi:10.1006/meth.2001.1262
    • Livak KJ, Schmittgen TD, (2001) Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2-ΔΔCT Method. Methods 25: 402-408. doi:10.1006/meth.2001.1262. PubMed: 11846609.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 37
    • 70350786388 scopus 로고    scopus 로고
    • An acyl-CoA-binding protein (FcACBP) and a fatty acid binding protein (FcFABP) respond to microbial infection in Chinese white shrimp, Fenneropenaeus chinensis
    • doi:10.1016/j.fsi.2009.09.007
    • Ren Q, Du ZQ, Zhao XF, Wang JX, (2009) An acyl-CoA-binding protein (FcACBP) and a fatty acid binding protein (FcFABP) respond to microbial infection in Chinese white shrimp, Fenneropenaeus chinensis. Fish Shellfish Immunol 27: 739-747. doi:10.1016/j.fsi.2009.09.007. PubMed: 19766195.
    • (2009) Fish Shellfish Immunol , vol.27 , pp. 739-747
    • Ren, Q.1    Du, Z.Q.2    Zhao, X.F.3    Wang, J.X.4
  • 38
    • 40049083456 scopus 로고    scopus 로고
    • A Short-Form C-Type Lectin from Amphioxus Acts as a Direct Microbial Killing Protein via Interaction with Peptidoglycan and Glucan
    • Yu YH, Yu YC, Huang HQ, Feng KX, Xu AL, et al. (2007) A Short-Form C-Type Lectin from Amphioxus Acts as a Direct Microbial Killing Protein via Interaction with Peptidoglycan and Glucan. J Immunol 179: 8425-8434. PubMed: 18056389.
    • (2007) J Immunol , vol.179 , pp. 8425-8434
    • Yu, Y.H.1    Yu, Y.C.2    Huang, H.Q.3    Feng, K.X.4    Xu, A.L.5
  • 39
    • 52049098247 scopus 로고    scopus 로고
    • T-antigen binding lectin with antibacterial activity from marine invertebrate, sea cucumber (Holothuria scabra): Possible involvement in differential recognition of bacteria
    • doi:10.1016/j.jip.2008.04.003
    • Gowda NM, Goswami U, Islam Khan M, (2008) T-antigen binding lectin with antibacterial activity from marine invertebrate, sea cucumber (Holothuria scabra): Possible involvement in differential recognition of bacteria. J Invertebr Pathol 99: 141-145. doi:10.1016/j.jip.2008.04.003. PubMed: 18501924.
    • (2008) J Invertebr Pathol , vol.99 , pp. 141-145
    • Gowda, N.M.1    Goswami, U.2    Islam Khan, M.3
  • 40
    • 77956893368 scopus 로고    scopus 로고
    • An ancient C-type lectin in Chlamys farreri (CfLec-2) that mediate pathogen recognition and cellular adhesion
    • doi:10.1016/j.dci.2010.07.004
    • Yang J, Qiu L, Wei X, Wang L, Wang L, et al. (2010) An ancient C-type lectin in Chlamys farreri (CfLec-2) that mediate pathogen recognition and cellular adhesion. Dev Comp Immunol 34: 1274-1282. doi:10.1016/j.dci.2010.07.004. PubMed: 20638410.
    • (2010) Dev Comp Immunol , vol.34 , pp. 1274-1282
    • Yang, J.1    Qiu, L.2    Wei, X.3    Wang, L.4    Wang, L.5
  • 41
    • 33746321298 scopus 로고    scopus 로고
    • A fi{ligature}ve-domain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon and its inhibitory activities
    • doi:10.1016/j.dci.2006.01.004
    • Somprasong N, Rimphanitchayakit V, Tassanakajon A, (2006) A fi{ligature}ve-domain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon and its inhibitory activities. Dev Comp Immunol 30: 998-1008. doi:10.1016/j.dci.2006.01.004. PubMed: 16519941.
    • (2006) Dev Comp Immunol , vol.30 , pp. 998-1008
    • Somprasong, N.1    Rimphanitchayakit, V.2    Tassanakajon, A.3
  • 42
    • 0003632935 scopus 로고
    • Ames, IA: The Iowas State University Press
    • Snedecor G, [!(surname)!], (1971) Statistical methods. Ames, IA: The Iowas State University Press.
    • (1971) Statistical Methods
    • Snedecor, G.1
  • 43
    • 0029833464 scopus 로고    scopus 로고
    • Granular cells are required for encapsulation of foreign targets by insect haemocytes
    • Pech LL, Strand MR, (1996) Granular cells are required for encapsulation of foreign targets by insect haemocytes. J CellSci 109: 2053-2060. PubMed: 8856501.
    • (1996) J CellSci , vol.109 , pp. 2053-2060
    • Pech, L.L.1    Strand, M.R.2
  • 44
    • 33845643045 scopus 로고    scopus 로고
    • Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis
    • doi:10.1016/j.jbiotec.2006.08.013
    • Zhang J, Li F, Wang Z, Xiang J, (2007) Cloning and recombinant expression of a crustin-like gene from Chinese shrimp, Fenneropenaeus chinensis. J Biotechnol 127: 605-614. doi:10.1016/j.jbiotec.2006.08.013. PubMed: 16987562.
    • (2007) J Biotechnol , vol.127 , pp. 605-614
    • Zhang, J.1    Li, F.2    Wang, Z.3    Xiang, J.4
  • 45
    • 0035058194 scopus 로고    scopus 로고
    • Antimicrobial proteins in crustaceans
    • doi:10.1007/978-1-4615-1291-2_10
    • Smith VJ, Chisholm JR, (2001) Antimicrobial proteins in crustaceans. Adv Exp Med Biol 484: 95-112. doi:10.1007/978-1-4615-1291-2_10. PubMed: 11419011.
    • (2001) Adv Exp Med Biol , vol.484 , pp. 95-112
    • Smith, V.J.1    Chisholm, J.R.2
  • 46
    • 0023790003 scopus 로고
    • Differential expression of a novel gene, WDNM1, in nonmetastatic rat mammary adenocarcinoma cells
    • Dear TN, Ramshaw IA, Kefford RF, (1988) Differential expression of a novel gene, WDNM1, in nonmetastatic rat mammary adenocarcinoma cells. Cancer Res 48: 5203-5209. PubMed: 3136918.
    • (1988) Cancer Res , vol.48 , pp. 5203-5209
    • Dear, T.N.1    Ramshaw, I.A.2    Kefford, R.F.3
  • 47
    • 0024453999 scopus 로고
    • Novel peptide inhibitor (SPAI) of Na+,K+-ATPase from porcine intestine
    • doi:10.1016/0006-291X(89)91747-6
    • Araki K, Kuroki J, Ito O, Kuwada M, Tachibana S, (1989) Novel peptide inhibitor (SPAI) of Na+,K+-ATPase from porcine intestine. Biochem Biophys Res Commun 164: 496-502. doi:10.1016/0006-291X(89)91747-6. PubMed: 2553020.
    • (1989) Biochem Biophys Res Commun , vol.164 , pp. 496-502
    • Araki, K.1    Kuroki, J.2    Ito, O.3    Kuwada, M.4    Tachibana, S.5
  • 48
    • 0025218417 scopus 로고
    • Purification and structure of caltrin-like proteins from seminal vesicle of the guinea pig
    • Coronel CE, San Agustin J, Lardy HA, (1990) Purification and structure of caltrin-like proteins from seminal vesicle of the guinea pig. J Biol Chem 265: 6854-6859. PubMed: 2324101.
    • (1990) J Biol Chem , vol.265 , pp. 6854-6859
    • Coronel, C.E.1    San Agustin, J.2    Lardy, H.A.3
  • 49
    • 33644829821 scopus 로고    scopus 로고
    • Cloning of a crustin- like, single whey-acidic-domain, antibacterial peptide from the haemocytes of the European lobster, Homarus gammarus, and its response to infection with bacteria
    • doi:10.1016/j.molimm.2005.07.029
    • Hauton C, Brockton V, Smith VJ, (2006) Cloning of a crustin- like, single whey-acidic-domain, antibacterial peptide from the haemocytes of the European lobster, Homarus gammarus, and its response to infection with bacteria. Mol Immunol 43: 1490-1496. doi:10.1016/j.molimm.2005.07.029. PubMed: 16144710.
    • (2006) Mol Immunol , vol.43 , pp. 1490-1496
    • Hauton, C.1    Brockton, V.2    Smith, V.J.3
  • 50
    • 35649028748 scopus 로고    scopus 로고
    • Molecular cloning, genomic organization and recombinant expression of a crustin-like antimicrobial peptide from black tiger shrimp Penaeus monodon
    • doi:10.1016/j.molimm.2007.07.031
    • Amparyup P, Kondo H, Hirono I, Aoki T, Tassanakajon A, (2008b) Molecular cloning, genomic organization and recombinant expression of a crustin-like antimicrobial peptide from black tiger shrimp Penaeus monodon. Mol Immunol 45: 1085-1093. doi:10.1016/j.molimm.2007.07.031.
    • (2008) Mol Immunol , vol.45 , pp. 1085-1093
    • Amparyup, P.1    Kondo, H.2    Hirono, I.3    Aoki, T.4    Tassanakajon, A.5
  • 51
    • 77951499021 scopus 로고    scopus 로고
    • Molecular characterization and expression of a crustin-like gene from Chinese mitten crab, Eriocheir sinensis
    • doi:10.1016/j.dci.2010.02.001
    • Mu C, Zheng P, Zhao J, Wang L, Zhang H, et al. (2010) Molecular characterization and expression of a crustin-like gene from Chinese mitten crab, Eriocheir sinensis. Dev Comp Immunol 34: 734-740. doi:10.1016/j.dci.2010.02.001. PubMed: 20144896.
    • (2010) Dev Comp Immunol , vol.34 , pp. 734-740
    • Mu, C.1    Zheng, P.2    Zhao, J.3    Wang, L.4    Zhang, H.5
  • 52
    • 79957853129 scopus 로고    scopus 로고
    • A novel type III crustin (CrusEs2) identified from Chinese mitten crab Eriocheir sinensis
    • doi:10.1016/j.fsi.2011.04.013
    • Mu C, Zheng P, Zhao J, Wang L, Qiu L, et al. (2011) A novel type III crustin (CrusEs2) identified from Chinese mitten crab Eriocheir sinensis. Fish Shellfish Immunol 31: 142-147. doi:10.1016/j.fsi.2011.04.013. PubMed: 21549196.
    • (2011) Fish Shellfish Immunol , vol.31 , pp. 142-147
    • Mu, C.1    Zheng, P.2    Zhao, J.3    Wang, L.4    Qiu, L.5
  • 53
    • 80054908401 scopus 로고    scopus 로고
    • A double WAP domain-containing protein from Chinese mitten crab Eriocheir sinensis with antimicrobial activities against Gram-negative bacteria and yeast
    • Li FM, Wang LL, Qiu LM, Zhang H, Gai YC, et al. (2011) A double WAP domain-containing protein from Chinese mitten crab Eriocheir sinensis with antimicrobial activities against Gram-negative bacteria and yeast. Dev Comp Immunol 36: 183-190. PubMed: 21798281.
    • (2011) Dev Comp Immunol , vol.36 , pp. 183-190
    • Li, F.M.1    Wang, L.L.2    Qiu, L.M.3    Zhang, H.4    Gai, Y.C.5
  • 54
    • 0000463507 scopus 로고    scopus 로고
    • Antileukoprotease: an endogenous protein in the innate mucosal defense against fungi
    • doi:10.1086/514098
    • Tomee JFC, Hiemstra PS, Heinzel-Wieland R, Kauffman HF, (1997) Antileukoprotease: an endogenous protein in the innate mucosal defense against fungi. J Infect Dis 176: 740-747. doi:10.1086/514098. PubMed: 9291323.
    • (1997) J Infect Dis , vol.176 , pp. 740-747
    • Tomee, J.F.C.1    Hiemstra, P.S.2    Heinzel-Wieland, R.3    Kauffman, H.F.4
  • 55
    • 0037442202 scopus 로고    scopus 로고
    • Mouse SWAM1 and SWAM2 are antibacterial proteins composed of a single whey acidic protein motif
    • Hagiwara K, Kikuchi T, Endo Y, (2003) Mouse SWAM1 and SWAM2 are antibacterial proteins composed of a single whey acidic protein motif. J Immunol 170: 1973-1979. PubMed: 12574366.
    • (2003) J Immunol , vol.170 , pp. 1973-1979
    • Hagiwara, K.1    Kikuchi, T.2    Endo, Y.3
  • 56
    • 6344253094 scopus 로고    scopus 로고
    • Antimicrobial activity of human EPPIN, an androgen-regulated, sperm-bound protein with a whey acidic protein motif
    • doi:10.1095/biolreprod.104.031567
    • Yenugu S, Richardson RT, Sivashanmugam P, Wang Z, O'Rand MG, et al. (2004) Antimicrobial activity of human EPPIN, an androgen-regulated, sperm-bound protein with a whey acidic protein motif. Biol Reprod 71: 1484-1490. doi:10.1095/biolreprod.104.031567. PubMed: 15229136.
    • (2004) Biol Reprod , vol.71 , pp. 1484-1490
    • Yenugu, S.1    Richardson, R.T.2    Sivashanmugam, P.3    Wang, Z.4    O'Rand, M.G.5
  • 57
    • 54049111337 scopus 로고    scopus 로고
    • A single whey acidic protein domain (SWD)-containing peptide from fleshy prawn with antimicrobial and proteinase inhibitory activities
    • doi:10.1016/j.aquaculture.2008.07.046
    • Jia YP, Sun YD, Wang ZH, Wang Q, Wang XW, et al. (2008) A single whey acidic protein domain (SWD)-containing peptide from fleshy prawn with antimicrobial and proteinase inhibitory activities. Aquaculture 284: 246-259. doi:10.1016/j.aquaculture.2008.07.046.
    • (2008) Aquaculture , vol.284 , pp. 246-259
    • Jia, Y.P.1    Sun, Y.D.2    Wang, Z.H.3    Wang, Q.4    Wang, X.W.5
  • 58
    • 58649108749 scopus 로고    scopus 로고
    • Characterization of crustins from the hemocytes of the spider crab, Hyas araneus, and the red king crab, Paralithodes camtschaticus
    • doi:10.1016/j.dci.2008.10.010
    • Sperstad SV, Haug T, Paulsen V, Rode TM, Strandskog G, Solem ST, Styrvold OB, Stensvåg K, (2009) Characterization of crustins from the hemocytes of the spider crab, Hyas araneus, and the red king crab, Paralithodes camtschaticus. Dev Comp Immunol 33: 583-591. doi:10.1016/j.dci.2008.10.010. PubMed: 19041340.
    • (2009) Dev Comp Immunol , vol.33 , pp. 583-591
    • Sperstad, S.V.1    Haug, T.2    Paulsen, V.3    Rode, T.M.4    Strandskog, G.5    Solem, S.T.6    Styrvold, O.B.7    Stensvåg, K.8
  • 59
    • 0003174699 scopus 로고
    • Electrokinetic studies on bacterial surfaces I: effects of surface-active agents on electrophoretic mobilities of bacteria
    • Dyar MT, Ordal EJ, (1946) Electrokinetic studies on bacterial surfaces I: effects of surface-active agents on electrophoretic mobilities of bacteria. J Bacteriol 51: 149-167.
    • (1946) J Bacteriol , vol.51 , pp. 149-167
    • Dyar, M.T.1    Ordal, E.J.2
  • 60
    • 80054880794 scopus 로고
    • Relation between changes in the stability of Pasteurella tularensis suspensions and in its bacterial population. I. the stability of suspensions of Pasteurella tularensis in the presence of electrolytes
    • Avi-Dor Y, Yaniv H, (1953) Relation between changes in the stability of Pasteurella tularensis suspensions and in its bacterial population. I. the stability of suspensions of Pasteurella tularensis in the presence of electrolytes. J Bacteriol 66: 1-5. PubMed: 13069457.
    • (1953) J Bacteriol , vol.66 , pp. 1-5
    • Avi-Dor, Y.1    Yaniv, H.2
  • 61
    • 80054964201 scopus 로고    scopus 로고
    • A comparative study of antimicrobial properties of crustinPm1 and crustinPm7 from the black tiger shrimp Penaeus monodon
    • doi:10.1016/j.dci.2011.08.002
    • Krusong K, Poolpipat P, Supungul P, Tassanakajon A, (2012) A comparative study of antimicrobial properties of crustinPm1 and crustinPm7 from the black tiger shrimp Penaeus monodon. Dev Comp Immunol 36: 208-215. doi:10.1016/j.dci.2011.08.002. PubMed: 21855569.
    • (2012) Dev Comp Immunol , vol.36 , pp. 208-215
    • Krusong, K.1    Poolpipat, P.2    Supungul, P.3    Tassanakajon, A.4
  • 62
    • 49949092690 scopus 로고    scopus 로고
    • Shrimp single WAP domain (SWD)-containing protein exhibits proteinase inhibitory and antimicrobial activities
    • doi:10.1016/j.dci.2008.06.005
    • Amparyup, Piti, Donpudsa Suchao, Tassanakajon Anchalee (2008) Shrimp single WAP domain (SWD)-containing protein exhibits proteinase inhibitory and antimicrobial activities. Dev Comp Immunol 32: 1497-1509. doi:10.1016/j.dci.2008.06.005. PubMed: 18602420.
    • (2008) Dev Comp Immunol , vol.32 , pp. 1497-1509
    • Amparyup1


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