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Volumn 33, Issue 1, 2014, Pages 1-10

Characterization and structural analysis of hepcidin like antimicrobial peptide from schizothorax richardsonii (Gray)

Author keywords

Antimicrobial peptides; Hepcidin; Infectious agents; Innate immunity; Schizothorax richardsonii

Indexed keywords

COMPLEMENTARY DNA; CYSTINE; HEPCIDIN; POLYPEPTIDE ANTIBIOTIC AGENT; SIGNAL PEPTIDE;

EID: 84898596796     PISSN: 15723887     EISSN: 15734943     Source Type: Journal    
DOI: 10.1007/s10930-013-9530-1     Document Type: Article
Times cited : (17)

References (68)
  • 1
    • 34247117757 scopus 로고    scopus 로고
    • Cationic host defence peptides: Innate immune regulatory peptides as a novel approach for treating infections
    • Mookherjee N, Hancock REW (2007) Cationic host defence peptides: innate immune regulatory peptides as a novel approach for treating infections. Cell Mol Life Sci Rev 64:922-933
    • (2007) Cell Mol Life Sci Rev , vol.64 , pp. 922-933
    • Mookherjee, N.1    Hancock, R.E.W.2
  • 3
    • 22844435410 scopus 로고    scopus 로고
    • Innate immunity of fish (overview)
    • Magnadottir B (2006) Innate immunity of fish (overview). Fish Shellfish Immunol 20:137-151
    • (2006) Fish Shellfish Immunol , vol.20 , pp. 137-151
    • Magnadottir, B.1
  • 4
    • 40149102505 scopus 로고    scopus 로고
    • The antimicrobial peptide hepcidin exerts an important role in the innate immunity against bacteria in the bony fish gilthead seabream
    • Cuesta A, Mesegure J, Esteban MA (2008) The antimicrobial peptide hepcidin exerts an important role in the innate immunity against bacteria in the bony fish gilthead seabream. Mol Immunol 45:2333-2342
    • (2008) Mol Immunol , vol.45 , pp. 2333-2342
    • Cuesta, A.1    Mesegure, J.2    Esteban, M.A.3
  • 5
    • 33746021126 scopus 로고    scopus 로고
    • Hepcidins in amphibians and fishes: Antimicrobial peptides or iron-regulatory hormones?
    • Shi J, Camus AC (2006) Hepcidins in amphibians and fishes: antimicrobial peptides or iron-regulatory hormones? Dev Comp Immunol 30:746-755
    • (2006) Dev Comp Immunol , vol.30 , pp. 746-755
    • Shi, J.1    Camus, A.C.2
  • 6
    • 34548501544 scopus 로고    scopus 로고
    • Genomic organization and tissue expression analysis of hepcidin-like genes from black porgy (Acanthopagrus schlegelii B.)
    • Yang M, Wang KL, Chen JH, Qu HD, Li SJ (2007) Genomic organization and tissue expression analysis of hepcidin-like genes from black porgy (Acanthopagrus schlegelii B.). Fish Shellfish Immunol 23:1060-1071
    • (2007) Fish Shellfish Immunol , vol.23 , pp. 1060-1071
    • Yang, M.1    Wang, K.L.2    Chen, J.H.3    Qu, H.D.4    Li, S.J.5
  • 7
    • 34848901649 scopus 로고    scopus 로고
    • Expression and antiviral activity of a beta-defensin-like peptide identified in the rainbow trout (Oncorhynchus mykiss) EST sequences
    • Falco A, Chico V, Marroqui L, Perez L, Coll JM, Estepa A (2008) Expression and antiviral activity of a beta-defensin-like peptide identified in the rainbow trout (Oncorhynchus mykiss) EST sequences. Mol Immunol 45:757-765
    • (2008) Mol Immunol , vol.45 , pp. 757-765
    • Falco, A.1    Chico, V.2    Marroqui, L.3    Perez, L.4    Coll, J.M.5    Estepa, A.6
  • 8
    • 0028085937 scopus 로고
    • Improvement of outer membrane-permeabilizing and lipopolysaccharide- binding activities of an antimicrobial cationic peptide by C-terminal modification
    • Piers KL, Brown MH, Hancock RE (1994) Improvement of outer membrane-permeabilizing and lipopolysaccharide-binding activities of an antimicrobial cationic peptide by C-terminal modification. Antimicrob Agents Chemother 38:2311-2316
    • (1994) Antimicrob Agents Chemother , vol.38 , pp. 2311-2316
    • Piers, K.L.1    Brown, M.H.2    Hancock, R.E.3
  • 9
    • 0036900093 scopus 로고    scopus 로고
    • Antimicrobial peptides from amphibian skin: An expanding scenario
    • Rinaldi AC (2002) Antimicrobial peptides from amphibian skin: an expanding scenario. Curr Opin Bio 6:82-88
    • (2002) Curr Opin Bio , vol.6 , pp. 82-88
    • Rinaldi, A.C.1
  • 10
    • 67849121294 scopus 로고    scopus 로고
    • A fish antimicrobial peptide, tilapia hepcidin TH2-3, shows potent antitumor activity against human fibrosarcoma cells
    • Chen JY, Lin WJ, Lin TL (2009) A fish antimicrobial peptide, tilapia hepcidin TH2-3, shows potent antitumor activity against human fibrosarcoma cells. Peptides 30:1636-1642
    • (2009) Peptides , vol.30 , pp. 1636-1642
    • Chen, J.Y.1    Lin, W.J.2    Lin, T.L.3
  • 11
    • 78751644815 scopus 로고    scopus 로고
    • Tilipia (Oreochomis mossambicus) antimicrobial peptide, hepcidin 1-5, shows antitumor activity in cancer cells
    • Chang WT, Pan CY, Rajanbabu V, Cheng CW, Chen JY (2011) Tilipia (Oreochomis mossambicus) antimicrobial peptide, hepcidin 1-5, shows antitumor activity in cancer cells. Peptides 32:342-352
    • (2011) Peptides , vol.32 , pp. 342-352
    • Chang, W.T.1    Pan, C.Y.2    Rajanbabu, V.3    Cheng, C.W.4    Chen, J.Y.5
  • 12
    • 0142134356 scopus 로고    scopus 로고
    • Gone gene fishing: How to catch noval marine antimicrobials
    • Patrzykat A, Douglas SE (2003) Gone gene fishing: how to catch noval marine antimicrobials. Trends Biotechnol 21:362-369
    • (2003) Trends Biotechnol , vol.21 , pp. 362-369
    • Patrzykat, A.1    Douglas, S.E.2
  • 13
    • 27944467507 scopus 로고    scopus 로고
    • The catfish liver-expressed antimicrobial peptide 2 (LEAP-2) gene is expressed in a wide range of tissues and developmentally regulated
    • Bao B, Peatman E, Xu P, Li P, Zeng H, He C, Liu Z (2006) The catfish liver-expressed antimicrobial peptide 2 (LEAP-2) gene is expressed in a wide range of tissues and developmentally regulated. Mol Immonol 43:367-377
    • (2006) Mol Immonol , vol.43 , pp. 367-377
    • Bao, B.1    Peatman, E.2    Xu, P.3    Li, P.4    Zeng, H.5    He, C.6    Liu, Z.7
  • 15
    • 84880037398 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of liverexpressed antimicrobial peptide 1 (LEAP-1) and LEAP-2 genes in the blunt snout bream (Megalobrama amblycephala)
    • Liang T, Ji W, Zhang GR, Wei KJ, Feng K, Wang WM, Zou GW (2013) Molecular cloning and expression analysis of liverexpressed antimicrobial peptide 1 (LEAP-1) and LEAP-2 genes in the blunt snout bream (Megalobrama amblycephala). Fish Shellfish Immunol 35:553-563
    • (2013) Fish Shellfish Immunol , vol.35 , pp. 553-563
    • Liang, T.1    Ji, W.2    Zhang, G.R.3    Wei, K.J.4    Feng, K.5    Wang, W.M.6    Zou, G.W.7
  • 16
    • 0035896642 scopus 로고    scopus 로고
    • Hepcidin, a urinary antimicrobial peptide synthesized in the liver
    • Park CH, Valore EV, Waring AJ, Ganz T (2001) Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J Biol Chem 276:7806-7810
    • (2001) J Biol Chem , vol.276 , pp. 7806-7810
    • Park, C.H.1    Valore, E.V.2    Waring, A.J.3    Ganz, T.4
  • 17
    • 0037020241 scopus 로고    scopus 로고
    • The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis
    • Hunter HN, Fulton DB, Ganz T, Vogel HJ (2002) The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J Biol Chem 277:37597-37603
    • (2002) J Biol Chem , vol.277 , pp. 37597-37603
    • Hunter, H.N.1    Fulton, D.B.2    Ganz, T.3    Vogel, H.J.4
  • 19
    • 62749144992 scopus 로고    scopus 로고
    • Cloning and expression of a hepcidin gene from a marine fish (Pseudosciaena crocea) and the antimicrobial activity of its synthetic peptide
    • Wang KJ, Cai JJ, Cai L, Qu HD, Yang M, Zhang M (2009) Cloning and expression of a hepcidin gene from a marine fish (Pseudosciaena crocea) and the antimicrobial activity of its synthetic peptide. Peptides 30:638-646
    • (2009) Peptides , vol.30 , pp. 638-646
    • Wang, K.J.1    Cai, J.J.2    Cai, L.3    Qu, H.D.4    Yang, M.5    Zhang, M.6
  • 20
    • 67349265607 scopus 로고    scopus 로고
    • Isolation and characterization of a hepcidin peptide from the head kidney of large yellow croaker, Pseudosciaena crocea
    • Zhang J, Yan Q, Ji R, Zou W, Guo G (2009) Isolation and characterization of a hepcidin peptide from the head kidney of large yellow croaker, Pseudosciaena crocea. Fish Shellfish Immunol 26:864-870
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 864-870
    • Zhang, J.1    Yan, Q.2    Ji, R.3    Zou, W.4    Guo, G.5
  • 21
    • 27144471911 scopus 로고    scopus 로고
    • Two different types of hepcidins from the Japanese flounder Paralichthys olivaceus
    • Hirono I, Hwang JY, Ono Y, Kurobe T, Ohira T, Nozaki R, Aoki T (2005) Two different types of hepcidins from the Japanese flounder Paralichthys olivaceus. FEBS J 2272:5257-5264
    • (2005) FEBS J , vol.2272 , pp. 5257-5264
    • Hirono, I.1    Hwang, J.Y.2    Ono, Y.3    Kurobe, T.4    Ohira, T.5    Nozaki, R.6    Aoki, T.7
  • 22
    • 34250824283 scopus 로고    scopus 로고
    • Three different hepcidins from tilapia oreochromis mossambicus: Analysis of their expressions and biological functions
    • Huang PH, Chen JY, Kuo CM(2007) Three different hepcidins from tilapia, Oreochromis mossambicus: analysis of their expressions and biological functions. Mol Immunol 44:1922-1934
    • (2007) Mol Immunol , vol.44 , pp. 1922-1934
    • Huang, P.H.1    Chen, J.Y.2    Kuo, C.M.3
  • 24
    • 78650176057 scopus 로고    scopus 로고
    • Molecular characterization of hepcidin AS-hepc2 and AS-hepc6 in black porgy (Acanthopagrus schlegelii): Expression pattern responded to bacterial challenge and in vitro antimicrobial activity
    • Yang M, Chen B, Cai JJ, Peng H, Ling C, Yuan JJ, Wang KJ (2011) Molecular characterization of hepcidin AS-hepc2 and AS-hepc6 in black porgy (Acanthopagrus schlegelii): expression pattern responded to bacterial challenge and in vitro antimicrobial activity. Comp Biochem Physiol B: Biochem Mol Biol 158:155-163
    • (2011) Comp Biochem Physiol B: Biochem Mol Biol , vol.158 , pp. 155-163
    • Yang, M.1    Chen, B.2    Cai, J.J.3    Peng, H.4    Ling, C.5    Yuan, J.J.6    Wang, K.J.7
  • 25
    • 83555177242 scopus 로고    scopus 로고
    • Recombinant medaka (Oryzias melastigmus) pro-hepcidin: Multifunctional characterization
    • Cai L, Cai JJ, Liu HP, Fan DQ, Peng H, Wang KJ (2012) Recombinant medaka (Oryzias melastigmus) pro-hepcidin: multifunctional characterization. Comp Biochem Physiol B 161:140-147
    • (2012) Comp Biochem Physiol B , vol.161 , pp. 140-147
    • Cai, L.1    Cai, J.J.2    Liu, H.P.3    Fan, D.Q.4    Peng, H.5    Wang, K.J.6
  • 26
    • 47749113635 scopus 로고    scopus 로고
    • Expression, purification and structural characterization of recombinant hepcidin, an antimicrobial peptide identified in Japanese flounder, Paralichthys olivaceus
    • Srinivasulu B, Syvitski R, Seo JK, Mattatall NR, Knickle LC, Douglas SE (2008) Expression, purification and structural characterization of recombinant hepcidin, an antimicrobial peptide identified in Japanese flounder, Paralichthys olivaceus. Protein Expr Purif 61:36-44
    • (2008) Protein Expr Purif , vol.61 , pp. 36-44
    • Srinivasulu, B.1    Syvitski, R.2    Seo, J.K.3    Mattatall, N.R.4    Knickle, L.C.5    Douglas, S.E.6
  • 28
    • 0037409525 scopus 로고    scopus 로고
    • Identification and expression analysis of hepcidin-like antimicrobial peptides in bony fish
    • Douglas SE, Gallant JW, Liebscher RS, Dacanay A, Tosi SCM (2003) Identification and expression analysis of hepcidin-like antimicrobial peptides in bony fish. Dev Comp Immunol 27: 598-601
    • (2003) Dev Comp Immunol , vol.27 , pp. 598-601
    • Douglas, S.E.1    Gallant, J.W.2    Liebscher, R.S.3    Dacanay, A.4    Tosi, S.C.M.5
  • 29
    • 1642386686 scopus 로고    scopus 로고
    • Organization and expression analysis of the zebrafish hepcidin gene, an antimicrobial peptide gene conserved among vertebrates
    • Shike H, Shimizu C, Lauth X, Burns JC (2004) Organization and expression analysis of the zebrafish hepcidin gene, an antimicrobial peptide gene conserved among vertebrates. Dev Comp Immunol 28:747-754
    • (2004) Dev Comp Immunol , vol.28 , pp. 747-754
    • Shike, H.1    Shimizu, C.2    Lauth, X.3    Burns, J.C.4
  • 30
    • 23944470428 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of two hepcidin genes from olive flounder (Paralichthys olivaceus)
    • Kim YO, Hong S, Nam BH, Lee JH, Kim KK, Lee SJ (2005) Molecular cloning and expression analysis of two hepcidin genes from olive flounder (Paralichthys olivaceus). Biosci Biotechnol Biochem 69(7):1411-1414
    • (2005) Biosci Biotechnol Biochem , vol.69 , Issue.7 , pp. 1411-1414
    • Kim, Y.O.1    Hong, S.2    Nam, B.H.3    Lee, J.H.4    Kim, K.K.5    Lee, S.J.6
  • 31
    • 16244395125 scopus 로고    scopus 로고
    • Cloning, characterization, and expression analysis of hepcidin gene from red sea bream (Chrysophrys major)
    • Chen SL, Xu MY, Ji XS, Yu GC, Liu Y (2005) Cloning, characterization, and expression analysis of hepcidin gene from red sea bream (Chrysophrys major). Antimicrob Agents Chemother 49:1608-1612
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 1608-1612
    • Chen, S.L.1    Xu, M.Y.2    Ji, X.S.3    Yu, G.C.4    Liu, Y.5
  • 32
    • 21444448913 scopus 로고    scopus 로고
    • Catfish hepcidin gene is expressed in a wide range of tissues and exhibits tissuespecific upregulation after bacterial infection
    • Bao B, Peatman E, Li P, He C, Liu Z (2005) Catfish hepcidin gene is expressed in a wide range of tissues and exhibits tissuespecific upregulation after bacterial infection. Dev Comp Immunol 29:939-950
    • (2005) Dev Comp Immunol , vol.29 , pp. 939-950
    • Bao, B.1    Peatman, E.2    Li, P.3    He, C.4    Liu, Z.5
  • 33
    • 33644507399 scopus 로고    scopus 로고
    • NK-lysin of channel catfish: Gene triplication, sequence variation, and expression analysis
    • Wang Q, Wang Y, Xu P, Liu Z (2006) NK-lysin of channel catfish: gene triplication, sequence variation, and expression analysis. Mol Immunol 43:1676-1686
    • (2006) Mol Immunol , vol.43 , pp. 1676-1686
    • Wang, Q.1    Wang, Y.2    Xu, P.3    Liu, Z.4
  • 34
    • 33947583828 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of a hepcidin antimicrobial peptide gene from turbot (Scophthalmus maximus)
    • Chen SL, Li W, Meng L, Sha ZX, Wang ZJ, Ren GC (2007) Molecular cloning and expression analysis of a hepcidin antimicrobial peptide gene from turbot (Scophthalmus maximus). Fish Shellfish Immunol 22:172-181
    • (2007) Fish Shellfish Immunol , vol.22 , pp. 172-181
    • Chen, S.L.1    Li, W.2    Meng, L.3    Sha, Z.X.4    Wang, Z.J.5    Ren, G.C.6
  • 35
    • 50149110932 scopus 로고    scopus 로고
    • Identification, cloning and expression analysis of a hepcidin cDNA of the Atlantic cod (Gadus morhua L.)
    • Solstad T, Larsen AN, Seppola M, Jorgensen TO (2008) Identification, cloning and expression analysis of a hepcidin cDNA of the Atlantic cod (Gadus morhua L.). Fish Shellfish Immunol 25: 298-310
    • (2008) Fish Shellfish Immunol , vol.25 , pp. 298-310
    • Solstad, T.1    Larsen, A.N.2    Seppola, M.3    Jorgensen, T.O.4
  • 36
    • 33746312646 scopus 로고    scopus 로고
    • Dual function of fish hepcidin: Response to experimental iron overload and bacterial infection in sea bass (Dicentrarchus labrax)
    • Rodrigues PN, Vazquez-Dorado S, Neves JV, Wilson JM (2006 Dual function of fish hepcidin: response to experimental iron overload and bacterial infection in sea bass (Dicentrarchus labrax). Dev Comp Immunol 30:1156-1167
    • (2006) Dev Comp Immunol , vol.30 , pp. 1156-1167
    • Rodrigues, P.N.1    Vazquez-Dorado, S.2    Neves, J.V.3    Wilson, J.M.4
  • 37
    • 0035896581 scopus 로고    scopus 로고
    • A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload
    • Pigeon C, Ilyin B, Courselaud P, Leroyer P, Turlin B, Brissot P, Loreal O (2001) A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is overexpressed during iron overload. J Biol Chem 276:7811-7819
    • (2001) J Biol Chem , vol.276 , pp. 7811-7819
    • Pigeon, C.1    Ilyin, B.2    Courselaud, P.3    Leroyer, P.4    Turlin, B.5    Brissot, P.6    Loreal, O.7
  • 38
    • 0036831170 scopus 로고    scopus 로고
    • The role of hepcidin in iron sequestration during infections and in the pathogenesis of anemia of chronic disease
    • Ganz T (2002) The role of hepcidin in iron sequestration during infections and in the pathogenesis of anemia of chronic disease. IMAJ 4:1043-1045
    • (2002) IMAJ , vol.4 , pp. 1043-1045
    • Ganz, T.1
  • 39
    • 84882836749 scopus 로고    scopus 로고
    • Molecular characterization of hepcidin gene in common carp (Cyprinus carpio L.) and its expression pattern responding to bacterial challenge
    • Li H, Zhang F, Guo H, Zhu Y, Yuan J, Yang G, An L (2013) Molecular characterization of hepcidin gene in common carp (Cyprinus carpio L.) and its expression pattern responding to bacterial challenge. Fish Shellfish Immunol 35:1030-1038
    • (2013) Fish Shellfish Immunol , vol.35 , pp. 1030-1038
    • Li, H.1    Zhang, F.2    Guo, H.3    Zhu, Y.4    Yuan, J.5    Yang, G.6    An, L.7
  • 40
    • 10844258104 scopus 로고    scopus 로고
    • Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization
    • Nemeth E, Tuttle MS, Powelson J, Vaughn MB, Donovan A, Ward DM, Ganz T, Kaplan J (2004) Hepcidin regulates cellular iron efflux by binding to ferroportin and inducing its internalization. Science 306(5704):2090-2093
    • (2004) Science , vol.306 , Issue.5704 , pp. 2090-2093
    • Nemeth, E.1    Tuttle, M.S.2    Powelson, J.3    Vaughn, M.B.4    Donovan, A.5    Ward, D.M.6    Ganz, T.7    Kaplan, J.8
  • 41
    • 0344420199 scopus 로고    scopus 로고
    • Hepcidin: The missing link between hemochromatosis and infections
    • Ashrafian H (2003) Hepcidin: the missing link between hemochromatosis and infections. Infect Immun 71:6693-6700
    • (2003) Infect Immun , vol.71 , pp. 6693-6700
    • Ashrafian, H.1
  • 42
    • 33748581212 scopus 로고    scopus 로고
    • Hepcidin- The iron regulatory hormone
    • Rossi E (2005) Hepcidin- the iron regulatory hormone. Clin Biochem Rev 26:47-49
    • (2005) Clin Biochem Rev , vol.26 , pp. 47-49
    • Rossi, E.1
  • 43
    • 23944502314 scopus 로고    scopus 로고
    • Time course analysis of hepcidin, serum iron and plasma cytokine levels in human injected with LPS
    • Kemna E, Pickkers P, Nemeth E, van der Hoeven H, Swinkels D (2005) Time course analysis of hepcidin, serum iron and plasma cytokine levels in human injected with LPS. Blood 106:1864-1866
    • (2005) Blood , vol.106 , pp. 1864-1866
    • Kemna, E.1    Pickkers, P.2    Nemeth, E.3    Van Der Hoeven, H.4    Swinkels, D.5
  • 44
    • 33645295541 scopus 로고    scopus 로고
    • Hepcidin: An important new regulator of iron homeostasis
    • Hugman A (2006) Hepcidin: an important new regulator of iron homeostasis. Clin Lab Haematol 28:75-83
    • (2006) Clin Lab Haematol , vol.28 , pp. 75-83
    • Hugman, A.1
  • 46
    • 77957283326 scopus 로고    scopus 로고
    • Tilapia hepcidin 2-3 peptide modulates lipopolysaccharide-induced cytokines and inhibits tumor necrosis factor-alpha through cyclooxygenase-2 and phosphodiesterase 4D
    • Rajanbabu V, Pan CY, Lee SC, Lin CC, Li CL (2010) Tilapia hepcidin 2-3 peptide modulates lipopolysaccharide-induced cytokines and inhibits tumor necrosis factor-alpha through cyclooxygenase-2 and phosphodiesterase 4D. J Biol Chem 285: 30577-30586
    • (2010) J Biol Chem , vol.285 , pp. 30577-30586
    • Rajanbabu, V.1    Pan, C.Y.2    Lee, S.C.3    Lin, C.C.4    Li, C.L.5
  • 47
    • 79960931688 scopus 로고    scopus 로고
    • Host-defense peptides: From biology to therapeutic strategies
    • Mangoni ML (2011) Host-defense peptides: from biology to therapeutic strategies. Cell Mol Life Sci 68:2157-2159
    • (2011) Cell Mol Life Sci , vol.68 , pp. 2157-2159
    • Mangoni, M.L.1
  • 48
    • 79960936612 scopus 로고    scopus 로고
    • Multifunctional cationic host defence peptides and their clinical applications
    • Yeung ATY, Gellatly SL, Hancock REW (2011) Multifunctional cationic host defence peptides and their clinical applications. Cell Mol Life Sci 68:2161-2176
    • (2011) Cell Mol Life Sci , vol.68 , pp. 2161-2176
    • Yeung, A.T.Y.1    Gellatly, S.L.2    Hancock, R.E.W.3
  • 49
    • 67349192783 scopus 로고    scopus 로고
    • Application of antimicrobial peptides in agriculture and food industry
    • Keymanesh K, Soltani S, Soroush S (2009) Application of antimicrobial peptides in agriculture and food industry. World J Microbiol Biotechnol 25:933-944
    • (2009) World J Microbiol Biotechnol , vol.25 , pp. 933-944
    • Keymanesh, K.1    Soltani, S.2    Soroush, S.3
  • 50
    • 17844393073 scopus 로고    scopus 로고
    • Effects of clove oil anaesthesia on rainbow trout (Oncorhynchus mykiss)
    • Veliek J, Svobodova Z, Piakova V (2005) Effects of clove oil anaesthesia on rainbow trout (Oncorhynchus mykiss). Acta Vet Brno 74:139-146
    • (2005) Acta Vet Brno , vol.74 , pp. 139-146
    • Veliek, J.1    Svobodova, Z.2    Piakova, V.3
  • 54
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DJ, Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acid Res 22:4673-4680
    • (1994) Nucleic Acid Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.J.2    Gibson, T.J.3
  • 55
    • 84898600646 scopus 로고    scopus 로고
    • MODELLER: A program for protein structure modeling release 9.10, r8346
    • Sali A (2011) MODELLER: a program for protein structure modeling release 9.10, r8346. Modeller. http://salilab.org/modeller/
    • (2011) Modeller
    • Sali, A.1
  • 56
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA-A self parameterizing force field
    • Krieger E, Koralmann G, Vriend G (2002) Increasing the precision of comparative models with YASARA NOVA-a self parameterizing force field. Proteins 47:393-402
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koralmann, G.2    Vriend, G.3
  • 57
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb viewer: An environment for comparative modelling
    • Guex N, Peltsch MC (1997) SWISS-MODEL and the Swiss-Pdb viewer: an environment for comparative modelling. Electrophoresis 18:2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peltsch, M.C.2
  • 58
    • 0027180507 scopus 로고
    • Verification protein structures: Patterns of non bonded atomic interactions
    • Colovos C, Yeates TO (1993) Verification protein structures: patterns of non bonded atomic interactions. Protein Sci 2: 1511-1519
    • (1993) Protein Sci , vol.2 , pp. 1511-1519
    • Colovos, C.1    Yeates, T.O.2
  • 61
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, Kumar S (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28(10):2731-2739
    • (2011) Mol Biol Evol , vol.28 , Issue.10 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 62
    • 0036139211 scopus 로고    scopus 로고
    • MEGA2: Molecular evolutionary genetics analysis software
    • Kumar S, Tamura K, Jakobsen IB, Nei M (2001) MEGA2: molecular evolutionary genetics analysis software. Bioinformatics 17:1244-1245
    • (2001) Bioinformatics , vol.17 , pp. 1244-1245
    • Kumar, S.1    Tamura, K.2    Jakobsen, I.B.3    Nei, M.4
  • 63
    • 0030614959 scopus 로고    scopus 로고
    • Identification of procariotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen H, Engelbrecht J, Brunak S, von Heijne G (1997) Identification of procariotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng 10:1-6
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Von Heijne, G.4
  • 64
    • 0032693640 scopus 로고    scopus 로고
    • Interaction of antimicrobial peptides with biological and model membranes: Structural and charge requirements for activity
    • Sitaram N, Nagaraj R (1999) Interaction of antimicrobial peptides with biological and model membranes: structural and charge requirements for activity. Biochim Biophys Acta 1462:29-54
    • (1999) Biochim Biophys Acta , vol.1462 , pp. 29-54
    • Sitaram, N.1    Nagaraj, R.2
  • 65
    • 10144229398 scopus 로고    scopus 로고
    • Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes
    • Dathe M, Schumann M, Wieprecht T, Winkler A, Beyermann M, Krause E, Matsuzaki K, Murase O, Bienert M (1996) Peptide helicity and membrane surface charge modulate the balance of electrostatic and hydrophobic interactions with lipid bilayers and biological membranes. Biochemistry 35:12612-12622
    • (1996) Biochemistry , vol.35 , pp. 12612-12622
    • Dathe, M.1    Schumann, M.2    Wieprecht, T.3    Winkler, A.4    Beyermann, M.5    Krause, E.6    Matsuzaki, K.7    Murase, O.8    Bienert, M.9
  • 66
    • 0037050278 scopus 로고    scopus 로고
    • Role of membranes in the activities of antimicrobial cationic peptides
    • Hancock REW, Rozek A (2002) Role of membranes in the activities of antimicrobial cationic peptides. FEMS Microbiol Lett 206:143-149
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 143-149
    • Hancock, R.E.W.1    Rozek, A.2
  • 68
    • 0035812694 scopus 로고    scopus 로고
    • Protein structure prediction and structural genomics
    • Baker D, Sali A (2001) Protein structure prediction and structural genomics. Science 294(5540):93-96
    • (2001) Science , vol.294 , Issue.5540 , pp. 93-96
    • Baker, D.1    Sali, A.2


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