메뉴 건너뛰기




Volumn 42, Issue 7, 2012, Pages 635-645

A Rhipicephalus (Boophilus) microplus cathepsin with dual peptidase and antimicrobial activity

Author keywords

Antimicrobial peptide; Cysteine endopeptidase; Tick

Indexed keywords

ACARICIDE; ANTIGEN; CATHEPSIN L; COMPLEMENTARY DNA; CYSTEINE PROTEINASE; PEPTIDASE; POLYCLONAL ANTIBODY; POLYPEPTIDE ANTIBIOTIC AGENT; PROTEINASE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; VACCINE; VITELLIN DEGRADING CYSTEINE ENDOPEPTIDASE;

EID: 84862323892     PISSN: 00207519     EISSN: 18790135     Source Type: Journal    
DOI: 10.1016/j.ijpara.2012.04.013     Document Type: Article
Times cited : (20)

References (85)
  • 3
    • 84355166500 scopus 로고    scopus 로고
    • Control of tick infestations in cattle vaccinated with bacterial membranes containing surface-exposed tick protective antigens
    • Almazán C., Moreno-Cantú O., Moreno-Cid J.A., Galindo R.C., Canales M., Villar M., de la Fuente J. Control of tick infestations in cattle vaccinated with bacterial membranes containing surface-exposed tick protective antigens. Vaccine 2012, 30:265-272.
    • (2012) Vaccine , vol.30 , pp. 265-272
    • Almazán, C.1    Moreno-Cantú, O.2    Moreno-Cid, J.A.3    Galindo, R.C.4    Canales, M.5    Villar, M.6    de la Fuente, J.7
  • 4
    • 33747724096 scopus 로고    scopus 로고
    • Antimicrobial activity in the egg wax of the African cattletick Amblyomma hebraeum (Acari: Ixodidae)
    • Arrieta M.C., Leskiw B.K., Kaufman W.R. Antimicrobial activity in the egg wax of the African cattletick Amblyomma hebraeum (Acari: Ixodidae). Exp. Appl. Acarol. 2006, 39:297-313.
    • (2006) Exp. Appl. Acarol. , vol.39 , pp. 297-313
    • Arrieta, M.C.1    Leskiw, B.K.2    Kaufman, W.R.3
  • 5
    • 0025050764 scopus 로고
    • Identification of the primary antimicrobial domains in human neutrophil cathepsin G
    • Bangalore N., Travis J., Onunka V.C., Pohl J., Shafer W.M. Identification of the primary antimicrobial domains in human neutrophil cathepsin G. J. Biol. Chem. 1990, 265:13584-13588.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13584-13588
    • Bangalore, N.1    Travis, J.2    Onunka, V.C.3    Pohl, J.4    Shafer, W.M.5
  • 7
    • 0038482128 scopus 로고    scopus 로고
    • The intestinal protozoan parasite Entamoeba histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation
    • Bruchhaus I., Loftus B.J., Hall N., Tannich E. The intestinal protozoan parasite Entamoeba histolytica contains 20 cysteine protease genes, of which only a small subset is expressed during in vitro cultivation. Eukaryot. Cell 2003, 2:501-509.
    • (2003) Eukaryot. Cell , vol.2 , pp. 501-509
    • Bruchhaus, I.1    Loftus, B.J.2    Hall, N.3    Tannich, E.4
  • 9
    • 77957772696 scopus 로고    scopus 로고
    • Diagnoses of fipronil resistance in Brazilian cattle ticks (Rhipicephalus (Boophilus) microplus) using in vitro larval bioassays
    • Castro-Janer E., Martins J.R., Mendes M.C., Namindome A., Klafke G.M., Schumaker T.T. Diagnoses of fipronil resistance in Brazilian cattle ticks (Rhipicephalus (Boophilus) microplus) using in vitro larval bioassays. Vet. Parasitol. 2010, 173:300-306.
    • (2010) Vet. Parasitol. , vol.173 , pp. 300-306
    • Castro-Janer, E.1    Martins, J.R.2    Mendes, M.C.3    Namindome, A.4    Klafke, G.M.5    Schumaker, T.T.6
  • 10
    • 0033532165 scopus 로고    scopus 로고
    • Mosquito Cathepsin B-like Protease Involved in Embryonic Degradation of Vitellin Is Produced as a Latent Extraovarian Precursor
    • Cho W.L., Tsao S.M., Hays A.R., Walter R., Chen J.S., Snigirevskaya E.S., Raikhel A.S. Mosquito Cathepsin B-like Protease Involved in Embryonic Degradation of Vitellin Is Produced as a Latent Extraovarian Precursor. J. Biol. Chem. 1999, 274:13311-13321.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13311-13321
    • Cho, W.L.1    Tsao, S.M.2    Hays, A.R.3    Walter, R.4    Chen, J.S.5    Snigirevskaya, E.S.6    Raikhel, A.S.7
  • 11
    • 37549006845 scopus 로고    scopus 로고
    • Cleaved thioredoxin fusion protein enables the crystallization of poorly soluble ERα in complex with synthetic ligands
    • Cura V., Gangloff M., Eiler S., Moras D., Ruff M. Cleaved thioredoxin fusion protein enables the crystallization of poorly soluble ERα in complex with synthetic ligands. Acta Crystallogr. F: Struct. Biol. Cryst. Commun. 2008, 64:54-57.
    • (2008) Acta Crystallogr. F: Struct. Biol. Cryst. Commun. , vol.64 , pp. 54-57
    • Cura, V.1    Gangloff, M.2    Eiler, S.3    Moras, D.4    Ruff, M.5
  • 13
    • 20344393137 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of cDNAs encoding for Boophilus microplus, Haemaphysalis longicornis and Rhipicephalus appendiculatus actins
    • da Silva Vaz I., Imamura S., Nakajima C., de Cardoso F.C., Ferreira C.A., Renard G., Masuda A., Ohashi K., Onuma M. Molecular cloning and sequence analysis of cDNAs encoding for Boophilus microplus, Haemaphysalis longicornis and Rhipicephalus appendiculatus actins. Vet. Parasitol. 2005, 127:147-155.
    • (2005) Vet. Parasitol. , vol.127 , pp. 147-155
    • da Silva Vaz, I.1    Imamura, S.2    Nakajima, C.3    de Cardoso, F.C.4    Ferreira, C.A.5    Renard, G.6    Masuda, A.7    Ohashi, K.8    Onuma, M.9
  • 15
    • 33846424608 scopus 로고    scopus 로고
    • Structure-dependent functional properties of human defensin 5
    • de Leeuw E., Burks S.R., Li X., Kao J.P., Lu W. Structure-dependent functional properties of human defensin 5. FEBS Lett. 2007, 581:515-520.
    • (2007) FEBS Lett. , vol.581 , pp. 515-520
    • de Leeuw, E.1    Burks, S.R.2    Li, X.3    Kao, J.P.4    Lu, W.5
  • 16
    • 0842313260 scopus 로고    scopus 로고
    • Prediction of proprotein convertase cleavage sites
    • Duckert P., Brunak S., Blom N. Prediction of proprotein convertase cleavage sites. Protein Eng. Des. Sel. 2004, 17:107-112.
    • (2004) Protein Eng. Des. Sel. , vol.17 , pp. 107-112
    • Duckert, P.1    Brunak, S.2    Blom, N.3
  • 17
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 18
    • 67349172161 scopus 로고    scopus 로고
    • Antimicrobial activity in the tick Rhipicephalus (Boophilus) microplus eggs: cellular localization and temporal expression of microplusin during oogenesis and embryogenesis
    • Esteves E., Fogaça A.C., Maldonado R., Silva F.D., Manso P.P., Pelajo-Machado M., Valle D., Daffre S. Antimicrobial activity in the tick Rhipicephalus (Boophilus) microplus eggs: cellular localization and temporal expression of microplusin during oogenesis and embryogenesis. Dev. Comp. Immunol. 2009, 33:913-919.
    • (2009) Dev. Comp. Immunol. , vol.33 , pp. 913-919
    • Esteves, E.1    Fogaça, A.C.2    Maldonado, R.3    Silva, F.D.4    Manso, P.P.5    Pelajo-Machado, M.6    Valle, D.7    Daffre, S.8
  • 20
    • 0025529201 scopus 로고
    • Yolk degradation in tick eggs: II. Evidence that cathepsin L-like proteinase is stored as a latent, acid activable proenzyme
    • Fagotto F. Yolk degradation in tick eggs: II. Evidence that cathepsin L-like proteinase is stored as a latent, acid activable proenzyme. Arch. Insect Biochem. Physiol. 1990, 14:237-252.
    • (1990) Arch. Insect Biochem. Physiol. , vol.14 , pp. 237-252
    • Fagotto, F.1
  • 21
    • 0026035346 scopus 로고
    • Yolk degradation in tick eggs: III. Developmentally regulated acidification of the yolk spheres
    • Fagotto F. Yolk degradation in tick eggs: III. Developmentally regulated acidification of the yolk spheres. Develop. Growth Diff. 1991, 35:57-66.
    • (1991) Develop. Growth Diff. , vol.35 , pp. 57-66
    • Fagotto, F.1
  • 22
    • 0041364483 scopus 로고    scopus 로고
    • Oncorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss
    • Fernandes J.M., Saint N., Kemp G.D., Smith V.J. Oncorhyncin III: a potent antimicrobial peptide derived from the non-histone chromosomal protein H6 of rainbow trout, Oncorhynchus mykiss. Biochem. J. 2003, 373:621-628.
    • (2003) Biochem. J. , vol.373 , pp. 621-628
    • Fernandes, J.M.1    Saint, N.2    Kemp, G.D.3    Smith, V.J.4
  • 24
    • 0344983395 scopus 로고    scopus 로고
    • Cysteine-rich antimicrobial peptides of the cattle tick Boophilus microplus: isolation, structural characterization and tissue expression profile
    • Fogaça A.C., Lorenzini D.M., Kaku L.M., Esteves E., Bulet P., Daffre S. Cysteine-rich antimicrobial peptides of the cattle tick Boophilus microplus: isolation, structural characterization and tissue expression profile. Dev. Comp. Immunol. 2004, 28:191-200.
    • (2004) Dev. Comp. Immunol. , vol.28 , pp. 191-200
    • Fogaça, A.C.1    Lorenzini, D.M.2    Kaku, L.M.3    Esteves, E.4    Bulet, P.5    Daffre, S.6
  • 25
    • 0032919921 scopus 로고    scopus 로고
    • Towards a permanent solution for controlling cattle ticks
    • Frisch J.E. Towards a permanent solution for controlling cattle ticks. Int. J. Parasitol. 1999, 29:57-71.
    • (1999) Int. J. Parasitol. , vol.29 , pp. 57-71
    • Frisch, J.E.1
  • 26
    • 34249791781 scopus 로고    scopus 로고
    • Immune upregulation of novel antibacterial proteins from silkmoths (Lepidoptera) that resemble lysozymes but lack muramidase activity
    • Gandhe A.S., Janardhan G., Nagaraju J. Immune upregulation of novel antibacterial proteins from silkmoths (Lepidoptera) that resemble lysozymes but lack muramidase activity. Insect Biochem. Mol. Biol. 2007, 37:655-666.
    • (2007) Insect Biochem. Mol. Biol. , vol.37 , pp. 655-666
    • Gandhe, A.S.1    Janardhan, G.2    Nagaraju, J.3
  • 27
    • 0042905861 scopus 로고    scopus 로고
    • The role of antimicrobial peptides in innate immunity
    • Ganz T. The role of antimicrobial peptides in innate immunity. Integr. Comp. Biol. 2003, 43:300-304.
    • (2003) Integr. Comp. Biol. , vol.43 , pp. 300-304
    • Ganz, T.1
  • 29
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 1983, 166:557-580.
    • (1983) J. Mol. Biol. , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 30
    • 0000193630 scopus 로고
    • Vitellogenin and vitellin in insects
    • Hagedoom H.H., Kunkel J.G. Vitellogenin and vitellin in insects. Ann. Rev. Entomol. 1979, 24:475-505.
    • (1979) Ann. Rev. Entomol. , vol.24 , pp. 475-505
    • Hagedoom, H.H.1    Kunkel, J.G.2
  • 31
    • 80054063343 scopus 로고    scopus 로고
    • Identification and structure-activity relationship of an antimicrobial peptide of the palustrin-2 family isolated from the skin of the endangered frog Odorrana ishikawae
    • Iwakoshi-Ukena, EIwakoshi-Ukena E., Okada G., Okimoto A., Fujii T., Sumida M., Ukena K. Identification and structure-activity relationship of an antimicrobial peptide of the palustrin-2 family isolated from the skin of the endangered frog Odorrana ishikawae. Peptides 2011, 32:2052-2057.
    • (2011) Peptides , vol.32 , pp. 2052-2057
    • Iwakoshi-Ukena1    EIwakoshi-Ukena, E.2    Okada, G.3    Okimoto, A.4    Fujii, T.5    Sumida, M.6    Ukena, K.7
  • 32
    • 0032112286 scopus 로고    scopus 로고
    • Control of bacterial infections in the hard tick Dermacentor variabilis (Acari: Ixodidae): evidence for the existence of antimicrobial proteins in tick haemolymph
    • Johns R., Sonenshine D.E., Hynes W.L. Control of bacterial infections in the hard tick Dermacentor variabilis (Acari: Ixodidae): evidence for the existence of antimicrobial proteins in tick haemolymph. J. Med. Entomol. 1998, 35:458-464.
    • (1998) J. Med. Entomol. , vol.35 , pp. 458-464
    • Johns, R.1    Sonenshine, D.E.2    Hynes, W.L.3
  • 33
    • 0035954687 scopus 로고    scopus 로고
    • Identification of a defensin from the hemolymph of the american dog tick Dermacentor variabilis
    • Johns R., Sonenshine D.E., Hynes W.L. Identification of a defensin from the hemolymph of the american dog tick Dermacentor variabilis. Insect Biochem. Mol. Biol. 2001, 31:857-865.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 857-865
    • Johns, R.1    Sonenshine, D.E.2    Hynes, W.L.3
  • 34
  • 35
    • 33846601728 scopus 로고    scopus 로고
    • Complement inactivating proteins and intraspecies venom variation in Crotalus oreganus helleri
    • Jurado J.D., Rael E.D., Lieb C.S., Nakayasu E., Hayes W.K., Bush S.P., Ross J.A. Complement inactivating proteins and intraspecies venom variation in Crotalus oreganus helleri. Toxicon 2007, 49:339-350.
    • (2007) Toxicon , vol.49 , pp. 339-350
    • Jurado, J.D.1    Rael, E.D.2    Lieb, C.S.3    Nakayasu, E.4    Hayes, W.K.5    Bush, S.P.6    Ross, J.A.7
  • 36
    • 0344069728 scopus 로고    scopus 로고
    • Purification and characterization of the lysozyme from the gut of the soft tick Ornithodoros moubata
    • Kopacek P., Vogt R., Jindrak L., Weise C., Safarik I. Purification and characterization of the lysozyme from the gut of the soft tick Ornithodoros moubata. Insect Biochem. Mol. Biol. 1999, 29:989-997.
    • (1999) Insect Biochem. Mol. Biol. , vol.29 , pp. 989-997
    • Kopacek, P.1    Vogt, R.2    Jindrak, L.3    Weise, C.4    Safarik, I.5
  • 37
    • 0029882031 scopus 로고    scopus 로고
    • Ultrastructural localization of a sialic acid-specific hemolymphlectin in the hemocytes and other tissues of the hard tick Ixodes ricinus (Acari: Chelicerata)
    • Kuhn K.H., Uhlir J., Grubhoffer L. Ultrastructural localization of a sialic acid-specific hemolymphlectin in the hemocytes and other tissues of the hard tick Ixodes ricinus (Acari: Chelicerata). Parasitol. Res. 1996, 82:215-221.
    • (1996) Parasitol. Res. , vol.82 , pp. 215-221
    • Kuhn, K.H.1    Uhlir, J.2    Grubhoffer, L.3
  • 38
    • 0347991711 scopus 로고    scopus 로고
    • Antimicrobial and cytolytic peptides of venomous arthropods
    • Kuhn-Nentwig L. Antimicrobial and cytolytic peptides of venomous arthropods. Cell Mol. Life Sci. 2003, 60:2651-2668.
    • (2003) Cell Mol. Life Sci. , vol.60 , pp. 2651-2668
    • Kuhn-Nentwig, L.1
  • 39
    • 9444251086 scopus 로고    scopus 로고
    • A new type of antimicrobial protein with multiple histidines from the hard tick, Amblyomma hebraeum
    • Lai R., Takeuchi H., Lomas L.O., Jonczy J., Rigden D.J., Rees H.H., Turner P.C. A new type of antimicrobial protein with multiple histidines from the hard tick, Amblyomma hebraeum. FASEB J. 2004, 18:1447-1449.
    • (2004) FASEB J. , vol.18 , pp. 1447-1449
    • Lai, R.1    Takeuchi, H.2    Lomas, L.O.3    Jonczy, J.4    Rigden, D.J.5    Rees, H.H.6    Turner, P.C.7
  • 42
    • 0029973555 scopus 로고    scopus 로고
    • Cloning of a cysteine protease required for the molting of Onchocerca volvulus third stage larvae
    • Lustigman S., McKerrow J.H., Shah K., Lui J., Huima T., Hough M., Brotman B. Cloning of a cysteine protease required for the molting of Onchocerca volvulus third stage larvae. J Biol Chem. 1996, 271:30181-30189.
    • (1996) J Biol Chem. , vol.271 , pp. 30181-30189
    • Lustigman, S.1    McKerrow, J.H.2    Shah, K.3    Lui, J.4    Huima, T.5    Hough, M.6    Brotman, B.7
  • 43
    • 0035859592 scopus 로고    scopus 로고
    • Avermectin resistance of the cattle tick Boophilus microplus in Brazil
    • Martins J.R., Furlong J. Avermectin resistance of the cattle tick Boophilus microplus in Brazil. Vet. Rec. 2001, 149:64.
    • (2001) Vet. Rec. , vol.149 , pp. 64
    • Martins, J.R.1    Furlong, J.2
  • 44
    • 79951810123 scopus 로고    scopus 로고
    • Control of Rhipicephalus (Boophilus) microplus infestations by the combination of subolesin vaccination and tick autocidal control after subolesin gene knockdown in ticks fed on cattle
    • Merino O., Almazán C., Canales M., Villar M., Moreno-Cid J.A., Estrada-Peña A., Kocan K.M., de la Fuente J. Control of Rhipicephalus (Boophilus) microplus infestations by the combination of subolesin vaccination and tick autocidal control after subolesin gene knockdown in ticks fed on cattle. Vaccine 2011, 29:2248-2254.
    • (2011) Vaccine , vol.29 , pp. 2248-2254
    • Merino, O.1    Almazán, C.2    Canales, M.3    Villar, M.4    Moreno-Cid, J.A.5    Estrada-Peña, A.6    Kocan, K.M.7    de la Fuente, J.8
  • 45
    • 0033781718 scopus 로고    scopus 로고
    • Issues in tick vaccine development: identification and characterization of potential candidate vaccine antigens
    • Mulenga A., Sugimoto C., Onuma M. Issues in tick vaccine development: identification and characterization of potential candidate vaccine antigens. Microbes Infect. 2000, 2:1353-1361.
    • (2000) Microbes Infect. , vol.2 , pp. 1353-1361
    • Mulenga, A.1    Sugimoto, C.2    Onuma, M.3
  • 46
    • 22544441350 scopus 로고    scopus 로고
    • Iron salts perturb biofilm formation and disrupt existing biofilms of Pseudomonas aeruginosa
    • Musk D.J., Banko D.A., Hergenrother P.J. Iron salts perturb biofilm formation and disrupt existing biofilms of Pseudomonas aeruginosa. Chem. Biol. 2005, 12:789-796.
    • (2005) Chem. Biol. , vol.12 , pp. 789-796
    • Musk, D.J.1    Banko, D.A.2    Hergenrother, P.J.3
  • 47
    • 33646347372 scopus 로고    scopus 로고
    • Critical roles for excretory-secretory cysteine proteases during tissue invasion of Paragonimus westermani newly excysted metacercariae
    • Na B.K., Kim S.H., Lee E.G., Kim T.S., Bae Y.A., Kang I., Yu J.R., Sohn W.M., Cho S.Y., Kong Y. Critical roles for excretory-secretory cysteine proteases during tissue invasion of Paragonimus westermani newly excysted metacercariae. Cell Microbiol. 2006, 8:1034-1046.
    • (2006) Cell Microbiol. , vol.8 , pp. 1034-1046
    • Na, B.K.1    Kim, S.H.2    Lee, E.G.3    Kim, T.S.4    Bae, Y.A.5    Kang, I.6    Yu, J.R.7    Sohn, W.M.8    Cho, S.Y.9    Kong, Y.10
  • 48
    • 0035933371 scopus 로고    scopus 로고
    • Two isoforms of a member of the arthropod defensin family from the soft tick, Ornithodoros moubata (Acari: Argasidae)
    • Nakajima Y., van der Goes van Naters-Yasui A., Taylor D., Yamakawa M. Two isoforms of a member of the arthropod defensin family from the soft tick, Ornithodoros moubata (Acari: Argasidae). Insect Biochem. Mol. Biol. 2001, 31:747-751.
    • (2001) Insect Biochem. Mol. Biol. , vol.31 , pp. 747-751
    • Nakajima, Y.1    van der Goes van Naters-Yasui, A.2    Taylor, D.3    Yamakawa, M.4
  • 49
    • 0037264318 scopus 로고    scopus 로고
    • Antibacterial hemoglobin fragments from the midgut of the soft tick, Ornithodoros moubata (Acari: Argasidae)
    • Nakajima Y., Ogihara K., Taylor D., Yamakawa M.J. Antibacterial hemoglobin fragments from the midgut of the soft tick, Ornithodoros moubata (Acari: Argasidae). Med. Entomol. 2003, 40:78-81.
    • (2003) Med. Entomol. , vol.40 , pp. 78-81
    • Nakajima, Y.1    Ogihara, K.2    Taylor, D.3    Yamakawa, M.J.4
  • 50
    • 0002511466 scopus 로고    scopus 로고
    • GeneDoc: analysis and visualization of genetic variation
    • Nicholas K.B., Nicholas H.B., Deerfield D.W. GeneDoc: analysis and visualization of genetic variation. EMBnet News 1997, 4:1-4.
    • (1997) EMBnet News , vol.4 , pp. 1-4
    • Nicholas, K.B.1    Nicholas, H.B.2    Deerfield, D.W.3
  • 54
    • 0242307126 scopus 로고    scopus 로고
    • Transcriptome identification of putative genes involved in protein catabolism andinnate immune response in human body louse (Pediculicidae: Pediculus humanus)
    • Pedra J.H., Brandt A., Li H.M., Westerman R., Romero-Severson J., Pollack R.J., Murdock L.L., Pittendrigh B.R. Transcriptome identification of putative genes involved in protein catabolism andinnate immune response in human body louse (Pediculicidae: Pediculus humanus). Insect Biochem. Mol. Biol. 2003, 33:1135-1143.
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 1135-1143
    • Pedra, J.H.1    Brandt, A.2    Li, H.M.3    Westerman, R.4    Romero-Severson, J.5    Pollack, R.J.6    Murdock, L.L.7    Pittendrigh, B.R.8
  • 55
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins D.N., Pappin D.J., Creasy D.M., Cottrell J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999, 20:3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 64
  • 67
    • 77957915509 scopus 로고    scopus 로고
    • Localization and function of Rhipicephalus (Boophilus) microplus vitellin-degrading cysteine endopeptidase
    • Seixas A., Estrela A.B., Ceolato J.C., Pontes E.G., Lara F., Gondim K.C., Termignoni C. Localization and function of Rhipicephalus (Boophilus) microplus vitellin-degrading cysteine endopeptidase. Parasitology 2010, 137:1819-1831.
    • (2010) Parasitology , vol.137 , pp. 1819-1831
    • Seixas, A.1    Estrela, A.B.2    Ceolato, J.C.3    Pontes, E.G.4    Lara, F.5    Gondim, K.C.6    Termignoni, C.7
  • 74
    • 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. MEGA5: Molecular Evolutionary Genetics Analysis using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony Methods. Mol. Biol. Evol. 2011, 28:2731-2739.
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 75
    • 57349131989 scopus 로고    scopus 로고
    • Innate immunity in ticks: a review
    • Taylor D. Innate immunity in ticks: a review. J. Acarol. Soc. Jpn. 2006, 15:109-127.
    • (2006) J. Acarol. Soc. Jpn. , vol.15 , pp. 109-127
    • Taylor, D.1
  • 76
    • 33748652487 scopus 로고    scopus 로고
    • Induction of cysteine proteinase in the encapsulation of Hymenolepis diminutaeggs in the American cockroach, Periplaneta americana
    • Tua W.C., Lai S.C. Induction of cysteine proteinase in the encapsulation of Hymenolepis diminutaeggs in the American cockroach, Periplaneta americana. J. Invertebr. Pathol. 2006, 92:73-78.
    • (2006) J. Invertebr. Pathol. , vol.92 , pp. 73-78
    • Tua, W.C.1    Lai, S.C.2
  • 78
    • 0001861317 scopus 로고    scopus 로고
    • Purification and partial amino acid sequence of antibacterial peptides from the haemolymph of the soft tick, Ornithodoros moubata (Acari: Argasidae)
    • Institute of Zoology, Slovak Academy of Sciences, Bratislava, Slovakia, M. Kazinfrova, M. Labuda, P.A. Nuttall (Eds.)
    • Van der Goes van Naters-Yasui A., Taylor D., Shono T., Yamakawa M. Purification and partial amino acid sequence of antibacterial peptides from the haemolymph of the soft tick, Ornithodoros moubata (Acari: Argasidae). Proceedings of the Third International Conference on Ticks and Tick-borne Pathogens: into the 21st Century 2000, 189-194. Institute of Zoology, Slovak Academy of Sciences, Bratislava, Slovakia. M. Kazinfrova, M. Labuda, P.A. Nuttall (Eds.).
    • (2000) Proceedings of the Third International Conference on Ticks and Tick-borne Pathogens: into the 21st Century , pp. 189-194
    • Van der Goes van Naters-Yasui, A.1    Taylor, D.2    Shono, T.3    Yamakawa, M.4
  • 79
    • 36849038025 scopus 로고    scopus 로고
    • Global comparative analysis of ESTs from the southern cattle tick, Rhipicephalus (Boophilus) microplus
    • Wang M., Guerrero F.D., Pertea G., Nene V.M. Global comparative analysis of ESTs from the southern cattle tick, Rhipicephalus (Boophilus) microplus. BMC Genomics 2007, 8:368.
    • (2007) BMC Genomics , vol.8 , pp. 368
    • Wang, M.1    Guerrero, F.D.2    Pertea, G.3    Nene, V.M.4
  • 80
    • 0027479701 scopus 로고
    • "Concealed" antigens: expanding the range of immunological targets
    • Willadsen P., Eisemann C.H., Tellam R.L. "Concealed" antigens: expanding the range of immunological targets. Parasitol. Today 1993, 9:132-135.
    • (1993) Parasitol. Today , vol.9 , pp. 132-135
    • Willadsen, P.1    Eisemann, C.H.2    Tellam, R.L.3
  • 81
    • 33846840838 scopus 로고    scopus 로고
    • Vaccination against ectoparasites
    • Willadsen P. Vaccination against ectoparasites. Parasitology 2006, 133:S9-S25.
    • (2006) Parasitology , vol.133
    • Willadsen, P.1
  • 82
    • 0027218436 scopus 로고
    • Cysteine proteinase from Bombyx eggs: role in programmed degradation of yolk proteins during embryogenesis
    • Yamamoto Y., Takahashi S.Y. Cysteine proteinase from Bombyx eggs: role in programmed degradation of yolk proteins during embryogenesis. Comp. Biochem. Physiol. B. 1993, 106:35-45.
    • (1993) Comp. Biochem. Physiol. B. , vol.106 , pp. 35-45
    • Yamamoto, Y.1    Takahashi, S.Y.2
  • 83
    • 30344463824 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from salivary glands of the hard tick, Ixodes sinensis
    • Yu D., Sheng Z., Xu X., Li J., Yang H., Liu Z., Rees H.H., Lai R. A novel antimicrobial peptide from salivary glands of the hard tick, Ixodes sinensis. Peptides 2006, 27:31-35.
    • (2006) Peptides , vol.27 , pp. 31-35
    • Yu, D.1    Sheng, Z.2    Xu, X.3    Li, J.4    Yang, H.5    Liu, Z.6    Rees, H.H.7    Lai, R.8
  • 84
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • Zasloff M. Antimicrobial peptides of multicellular organisms. Nature. 2002, 415:389-396.
    • (2002) Nature. , vol.415 , pp. 389-396
    • Zasloff, M.1
  • 85
    • 79951517277 scopus 로고    scopus 로고
    • Identification of a cysteine-rich antimicrobial peptide from salivary glands of the tick Rhipicephalus haemaphysaloides
    • Zhang H., Zhang W., Wang X., Zhou Y., Wang N., Zhou J. Identification of a cysteine-rich antimicrobial peptide from salivary glands of the tick Rhipicephalus haemaphysaloides. Peptides 2011, 32:441-446.
    • (2011) Peptides , vol.32 , pp. 441-446
    • Zhang, H.1    Zhang, W.2    Wang, X.3    Zhou, Y.4    Wang, N.5    Zhou, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.