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Volumn 712, Issue , 2011, Pages 177-191

Cysteine proteases from bloodfeeding arthropod ectoparasites

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CATHEPSIN B; CATHEPSIN L; CYSTEINE PROTEINASE; HEMOGLOBIN; LEGUMAIN;

EID: 80053297181     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-8414-2_11     Document Type: Article
Times cited : (34)

References (58)
  • 1
    • 62549111856 scopus 로고    scopus 로고
    • An overview of systematics and evolution of ticks
    • Nava S, Guglielmone AA, Mangold AJ. An overview of systematics and evolution of ticks. Front Biosci 2009; 14:2857-2877
    • (2009) Front Biosci , vol.14 , pp. 2857-2877
    • Nava, S.1    Guglielmone, A.A.2    Mangold, A.J.3
  • 2
    • 52049116868 scopus 로고    scopus 로고
    • Overview: Ticks as vectors of pathogens that cause disease in humans and animals
    • de la Fuente J, Estrada-Pena A, Venzal JM et al. Overview: Ticks as vectors of pathogens that cause disease in humans and animals. Front Biosci 2008; 13:6938-6946
    • (2008) Front Biosci , vol.13 , pp. 6938-6946
    • De La Fuente, J.1    Estrada-Pena, A.2    Venzal, J.M.3
  • 3
    • 0015886449 scopus 로고
    • Contribution to the study of digestion in ticks: Histology and fine structure of the midgut ephithelium of Ornithodorus moubata, Murray (Ixodoidea, Argasidae)
    • Grandjean O, Aeschlimann A. Contribution to the study of digestion in ticks: histology and fine structure of the midgut ephithelium of Ornithodorus moubata, Murray (Ixodoidea, Argasidae). Acta Trop 1973; 30:193-212
    • (1973) Acta Trop , vol.30 , pp. 193-212
    • Grandjean, O.1    Aeschlimann, A.2
  • 6
    • 0024322082 scopus 로고
    • Ultrastructure ofthe midgut and blood meal digestion in the adult tick Dermacentor variabilis
    • Tarnowski BI, Coons LB. Ultrastructure ofthe midgut and blood meal digestion in the adult tick Dermacentor variabilis. Exp Appl Acarol 1989; 6:263-289
    • (1989) Exp Appl Acarol , vol.6 , pp. 263-289
    • Tarnowski, B.I.1    Coons, L.B.2
  • 8
    • 0024508203 scopus 로고
    • Tick-host interaction: A synthesis of current concepts
    • Kaufman WR. Tick-host interaction: a synthesis of current concepts. Parasitol Today 1989; 5:47-56
    • (1989) Parasitol Today , vol.5 , pp. 47-56
    • Kaufman, W.R.1
  • 10
    • 0017931684 scopus 로고
    • Boophilus microplus: characterization oflarval proteases
    • Reich CI, Zorzopulos J. Boophilus microplus: characterization oflarval proteases. Exp Parasitol 1978; 44:1-6
    • (1978) Exp Parasitol , vol.44 , pp. 1-6
    • Reich, C.I.1    Zorzopulos, J.2
  • 11
    • 0017977316 scopus 로고
    • Boophilus microplus: Characterization of larval phosphomonoesterases and isolation of subcellular fractions with high phosphatase activity
    • Zorzopulos J, Reich CI, Galassi N. Boophilus microplus: characterization of larval phosphomonoesterases and isolation of subcellular fractions with high phosphatase activity. Exp Parasitol 1978; 45:128-138
    • (1978) Exp Parasitol , vol.45 , pp. 128-138
    • Zorzopulos, J.1    Reich, C.I.2    Galassi, N.3
  • 12
    • 0033808652 scopus 로고    scopus 로고
    • Cloning and functional expression of a Boophilus microplus cathepsin L-like enzyme
    • Renard G, Garcia JF, Cardoso FC et al. Cloning and functional expression of a Boophilus microplus cathepsin L-like enzyme. Insect Biochem Mol Biol 2000; 30:1017-1026
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 1017-1026
    • Renard, G.1    Garcia, J.F.2    Cardoso, F.C.3
  • 13
    • 0036676666 scopus 로고    scopus 로고
    • Expression and immunolocalization of a Boophilus microplus cathepsin L-like enzyme
    • Renard G, Lara FA, de Cardoso FC et al. Expression and immunolocalization of a Boophilus microplus cathepsin L-like enzyme. Insect Mol Biol 2002; 11:325-328
    • (2002) Insect Mol Biol , vol.11 , pp. 325-328
    • Renard, G.1    Lara, F.A.2    De Cardoso, F.C.3
  • 14
    • 0033073674 scopus 로고    scopus 로고
    • Characterization of proteolytic enzymes expressed in the midgut of Haemaphysalis longicornis
    • Mulenga A, Sugimoto C, Onuma M. Characterization of proteolytic enzymes expressed in the midgut of Haemaphysalis longicornis. Jpn J Vet Res 1999; 46:179-184
    • (1999) Jpn J Vet Res , vol.46 , pp. 179-184
    • Mulenga, A.1    Sugimoto, C.2    Onuma, M.3
  • 15
    • 0033128927 scopus 로고    scopus 로고
    • Molecular cloning of two Haemaphysalis longicornis cathepsin L-like cysteine proteinase genes
    • Mulenga A, Sugimoto C, Ingram G et al. Molecular cloning of two Haemaphysalis longicornis cathepsin L-like cysteine proteinase genes. J Vet Med Sci 1999; 61:497-502
    • (1999) J Vet Med Sci , vol.61 , pp. 497-502
    • Mulenga, A.1    Sugimoto, C.2    Ingram, G.3
  • 16
    • 67650591033 scopus 로고    scopus 로고
    • Hemoglobinase activity of a cysteine protease from the ixodid tick Haemaphysalis longicornis
    • Yamaji K, Tsuji N, Miyoshi T et al. Hemoglobinase activity of a cysteine protease from the ixodid tick Haemaphysalis longicornis. Parasitol Int 2009; 58:232-237
    • (2009) Parasitol Int , vol.58 , pp. 232-237
    • Yamaji, K.1    Tsuji, N.2    Miyoshi, T.3
  • 17
    • 44949197678 scopus 로고    scopus 로고
    • A cysteine protease is critical for Babesia spp. transmission in Haemaphysalis ticks
    • Tsuji N, Miyoshi T, Battsetseg B et al. A cysteine protease is critical for Babesia spp. transmission in Haemaphysalis ticks. PLoS Pathog 2008; 4:e1000062
    • (2008) PLoS Pathog , vol.4
    • Tsuji, N.1    Miyoshi, T.2    Battsetseg, B.3
  • 18
    • 34247593923 scopus 로고    scopus 로고
    • IrAE: An asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus
    • Sojka D, Hajdusek O, Dvorak J et al. IrAE: an asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinus. Int J Parasitol 2007; 37:713-724
    • (2007) Int J Parasitol , vol.37 , pp. 713-724
    • Sojka, D.1    Hajdusek, O.2    Dvorak, J.3
  • 19
    • 42949122012 scopus 로고    scopus 로고
    • Aza-peptidyl Michael acceptors. A new class of potent and selective inhibitors of asparaginyl endopeptidases (legumains) from evolutionarily diverse pathogens
    • Gotz MG, James KE, Hansell E et al. Aza-peptidyl Michael acceptors. A new class of potent and selective inhibitors of asparaginyl endopeptidases (legumains) from evolutionarily diverse pathogens. J Med Chem 2008; 51:2816-2832
    • (2008) J Med Chem , vol.51 , pp. 2816-2832
    • Gotz, M.G.1    James, K.E.2    Hansell, E.3
  • 20
    • 70949088531 scopus 로고    scopus 로고
    • Aza-peptidyl Michael acceptor and epoxide inhibitors-potent and selective inhibitors of Schistosoma mansoni and Ixodes ricinus legumains (asparaginyl endopeptidases)
    • Ovat A, Muindi F, Fagan C et al. Aza-peptidyl Michael acceptor and epoxide inhibitors-potent and selective inhibitors of Schistosoma mansoni and Ixodes ricinus legumains (asparaginyl endopeptidases). J Med Chem 2009; 52:7192-7210
    • (2009) J Med Chem , vol.52 , pp. 7192-7210
    • Ovat, A.1    Muindi, F.2    Fagan, C.3
  • 21
    • 34547532754 scopus 로고    scopus 로고
    • Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis
    • Abdul Alim M, Tsuji N, Miyoshi T et al. Characterization of asparaginyl endopeptidase, legumain induced by blood feeding in the ixodid tick Haemaphysalis longicornis. Insect Biochem Mol Bio 2007; 37:911-922
    • (2007) Insect Biochem Mol Bio , vol.37 , pp. 911-922
    • Abdul Alim, M.1    Tsuji, N.2    Miyoshi, T.3
  • 22
    • 40849104745 scopus 로고    scopus 로고
    • HlLgm2, a member of asparaginyl endopeptidases/legumains in the midgut of the ixodid tick Haemaphysalis longicornis, is involved in blood-meal digestion
    • Alim MA, Tsuji N, Miyoshi T et al. HlLgm2, a member of asparaginyl endopeptidases/legumains in the midgut of the ixodid tick Haemaphysalis longicornis, is involved in blood-meal digestion. J Insect Physiol 2008; 54:573-585
    • (2008) J Insect Physiol , vol.54 , pp. 573-585
    • Alim, M.A.1    Tsuji, N.2    Miyoshi, T.3
  • 23
    • 62149090267 scopus 로고    scopus 로고
    • Developmental stage- and organ-specific expression profiles of asparaginyl endopeptidases/legumains in the ixodid tick Haemaphysalis longicornis
    • Alim MA, Tsuji N, Miyoshi T et al. Developmental stage- and organ-specific expression profiles of asparaginyl endopeptidases/legumains in the ixodid tick Haemaphysalis longicornis. J Vet Med Sci 2008; 70:1363-1366
    • (2008) J Vet Med Sci , vol.70 , pp. 1363-1366
    • Alim, M.A.1    Tsuji, N.2    Miyoshi, T.3
  • 24
    • 57549087068 scopus 로고    scopus 로고
    • Legumains from the hard tick Haemaphysalis longicornis play modulatory roles in blood feeding and gut cellular remodelling and impact on embryogenesis
    • Alim MA, Tsuji N, Miyoshi T et al. Legumains from the hard tick Haemaphysalis longicornis play modulatory roles in blood feeding and gut cellular remodelling and impact on embryogenesis. Int J Parasitol 2009; 39:97-107
    • (2009) Int J Parasitol , vol.39 , pp. 97-107
    • Alim, M.A.1    Tsuji, N.2    Miyoshi, T.3
  • 25
    • 29144503154 scopus 로고    scopus 로고
    • Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis
    • Boldbaatar D, Sikalizyo Sikasunge C, Battsetseg B et al. Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis. Insect Biochem Mol Biol 2006; 36:25-36
    • (2006) Insect Biochem Mol Biol , vol.36 , pp. 25-36
    • Boldbaatar, D.1    Sikalizyo Sikasunge, C.2    Battsetseg, B.3
  • 26
    • 57549115852 scopus 로고    scopus 로고
    • Profiling of proteolytic enzymes in the gut ofthe tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases
    • Sojka D, Franta Z, Horn M et al. Profiling of proteolytic enzymes in the gut ofthe tick Ixodes ricinus reveals an evolutionarily conserved network of aspartic and cysteine peptidases. Parasit Vectors 2008; 1:7
    • (2008) Parasit Vectors , vol.1 , pp. 7
    • Sojka, D.1    Franta, Z.2    Horn, M.3
  • 27
    • 33747120925 scopus 로고    scopus 로고
    • Identification and characterisation of a leucine aminopeptidase from the hard tick Haemaphysalis longicornis
    • Hatta T, Kazama K, Miyoshi T et al. Identification and characterisation of a leucine aminopeptidase from the hard tick Haemaphysalis longicornis. Int J Parasitol 2006; 36:1123-1132
    • (2006) Int J Parasitol , vol.36 , pp. 1123-1132
    • Hatta, T.1    Kazama, K.2    Miyoshi, T.3
  • 28
    • 1942519435 scopus 로고    scopus 로고
    • Blood 'n' guts: An update on schistosome digestive peptidases
    • Caffrey CR, McKerrow JH, Salter JP et al. Blood 'n' guts: an update on schistosome digestive peptidases. Trends Parasitol 2004; 20:241-248
    • (2004) Trends Parasitol , vol.20 , pp. 241-248
    • Caffrey, C.R.1    McKerrow, J.H.2    Salter, J.P.3
  • 29
    • 33845968082 scopus 로고    scopus 로고
    • A multienzyme network functions in intestinal protein digestion by a platyhelminth parasite
    • Delcroix M, Sajid M, Caffrey CR et al. A multienzyme network functions in intestinal protein digestion by a platyhelminth parasite. J Biol Chem 2006; 281:39316-39329
    • (2006) J Biol Chem , vol.281 , pp. 39316-39329
    • Delcroix, M.1    Sajid, M.2    Caffrey, C.R.3
  • 31
    • 60849099047 scopus 로고    scopus 로고
    • Exploring the mialome of ticks: An annotated catalogue of midgut transcripts from the hard tick, Dermacentor variabilis (Acari: Ixodidae)
    • Anderson JM, Sonenshine DE, Valenzuela JG. Exploring the mialome of ticks: an annotated catalogue of midgut transcripts from the hard tick, Dermacentor variabilis (Acari: Ixodidae). BMC Genomics 2008; 9:552
    • (2008) BMC Genomics , vol.9 , pp. 552
    • Anderson, J.M.1    Sonenshine, D.E.2    Valenzuela, J.G.3
  • 32
    • 71449096345 scopus 로고    scopus 로고
    • Hemoglobin digestion in blood-feeding ticks: Mapping a multipeptidase pathway by functional proteomics
    • Horn M, Nussbaumerova M, Sanda M et al. Hemoglobin digestion in blood-feeding ticks: mapping a multipeptidase pathway by functional proteomics. Chem Biol 2009; 16:1053-1063
    • (2009) Chem Biol , vol.16 , pp. 1053-1063
    • Horn, M.1    Nussbaumerova, M.2    Sanda, M.3
  • 33
    • 33751538306 scopus 로고    scopus 로고
    • Two secreted cystatins of the soft tick Ornithodoros moubata: Differential expression pattern and inhibitory specificity
    • Grunclova L, Horn M, Vancova M et al. Two secreted cystatins of the soft tick Ornithodoros moubata: differential expression pattern and inhibitory specificity. Biol Chem 2006; 387:1635-1644
    • (2006) Biol Chem , vol.387 , pp. 1635-1644
    • Grunclova, L.1    Horn, M.2    Vancova, M.3
  • 34
    • 0025527484 scopus 로고
    • Yolk degradation in tick eggs. I. Occurrence of a cathepsin L-like acid proteinase in yolk spheres
    • Fagotto F. Yolk degradation in tick eggs: I. Occurrence of a cathepsin L-like acid proteinase in yolk spheres. Arch Insect Biochem Physiol 1990; 14:217-235
    • (1990) Arch Insect Biochem Physiol , vol.14 , pp. 217-235
    • Fagotto, F.1
  • 35
    • 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
  • 36
    • 0037295006 scopus 로고    scopus 로고
    • A Boophilus microplus vitellin-degrading cysteine endopeptidase
    • Seixas A, Dos Santos PC, Velloso FF et al. A Boophilus microplus vitellin-degrading cysteine endopeptidase. Parasitology 2003; 126(Pt 2):155-163
    • (2003) Parasitology , vol.126 , Issue.PART 2 , pp. 155-163
    • Seixas, A.1    Dos Santos, P.C.2    Velloso, F.F.3
  • 38
    • 35648963593 scopus 로고    scopus 로고
    • A cysteine endopeptidase from tick Rhipicephalus (Boophilus) microplus) larvae with vitellin digestion activity
    • Estrela A, Seixas A, Termignoni C. A cysteine endopeptidase from tick Rhipicephalus (Boophilus) microplus) larvae with vitellin digestion activity. Comp Biochem Physiol B Biochem Mol Biol 2007; 148:410-416
    • (2007) Comp Biochem Physiol B Biochem Mol Biol , vol.148 , pp. 410-416
    • Estrela, A.1    Seixas, A.2    Termignoni, C.3
  • 39
    • 0033532165 scopus 로고    scopus 로고
    • Mosquito cathepsin B-like protease involved in embryonic degradation of vitellin is produced as a latent extraovarian precursor
    • Cho WL, Tsao SM, Hays AR et al. 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
  • 40
    • 13544264646 scopus 로고    scopus 로고
    • The accumulation of specific mRNAs following multiple blood meals in Anopheles gambiae
    • Nirmala X, Marinotti O, James AA. The accumulation of specific mRNAs following multiple blood meals in Anopheles gambiae. Insect Mol Biol 2005; 14:95-103
    • (2005) Insect Mol Biol , vol.14 , pp. 95-103
    • Nirmala, X.1    Marinotti, O.2    James, A.A.3
  • 41
    • 0035449501 scopus 로고    scopus 로고
    • Preoviposition activation of cathepsin-like proteinases in degenerating ovarian follicles of the mosquito Culex pipiens pallens
    • Uchida K, Ohmori D, Ueno T et al. Preoviposition activation of cathepsin-like proteinases in degenerating ovarian follicles of the mosquito Culex pipiens pallens. Dev Biol 2001; 237:68-78
    • (2001) Dev Biol , vol.237 , pp. 68-78
    • Uchida, K.1    Ohmori, D.2    Ueno, T.3
  • 43
    • 34248597362 scopus 로고    scopus 로고
    • Characterization of Aedes Dredd: A novel initiator caspase from the yellow fever mosquito, Aedes aegypti
    • Cooper DM, Pio F, Thi EP et al. Characterization of Aedes Dredd: a novel initiator caspase from the yellow fever mosquito, Aedes aegypti. Insect Biochem Mol Biol 2007; 37:559-569
    • (2007) Insect Biochem Mol Biol , vol.37 , pp. 559-569
    • Cooper, D.M.1    Pio, F.2    Thi, E.P.3
  • 44
    • 34748823570 scopus 로고    scopus 로고
    • Aedes Dronc: A novel ecdysone-inducible caspase in the yellow fever mosquito, Aedes aegypti
    • Cooper DM, Thi EP, Chamberlain CM et al. Aedes Dronc: a novel ecdysone-inducible caspase in the yellow fever mosquito, Aedes aegypti. Insect Mol Biol 2007; 16:563-572
    • (2007) Insect Mol Biol , vol.16 , pp. 563-572
    • Cooper, D.M.1    Thi, E.P.2    Chamberlain, C.M.3
  • 45
    • 59849129347 scopus 로고    scopus 로고
    • Aedes FADD a novel death domain-containing protein required for antibacterial immunity in the yellow fever mosquito, Aedes aegypti
    • Cooper DM, Chamberlain CM, Lowenberger C. Aedes FADD: a novel death domain-containing protein required for antibacterial immunity in the yellow fever mosquito, Aedes aegypti. Insect Biochem Mol Biol 2009; 39:47-54
    • (2009) Insect Biochem Mol Biol , vol.39 , pp. 47-54
    • Cooper, D.M.1    Chamberlain, C.M.2    Lowenberger, C.3
  • 46
    • 0034633664 scopus 로고    scopus 로고
    • Invasion in vitro of mosquito midgut cells by the malaria parasite proceeds by a conserved mechanism and results in death of the invaded midgut cells
    • Zieler H, Dvorak JA. Invasion in vitro of mosquito midgut cells by the malaria parasite proceeds by a conserved mechanism and results in death of the invaded midgut cells. Proc Natl Acad Sci USA 2000; 97:11516-11521
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 11516-11521
    • Zieler, H.1    Dvorak, J.A.2
  • 47
    • 1242317019 scopus 로고    scopus 로고
    • Analysis of the Plasmodium and Anopheles transcriptional repertoire during ookinete development and midgut invasion
    • Abraham EG, Islam S, Srinivasan P et al. Analysis of the Plasmodium and Anopheles transcriptional repertoire during ookinete development and midgut invasion. J Biol Chem 2004; 279:5573-5580
    • (2004) J Biol Chem , vol.279 , pp. 5573-5580
    • Abraham, E.G.1    Islam, S.2    Srinivasan, P.3
  • 48
    • 32244435584 scopus 로고    scopus 로고
    • Immune stimulation and malaria infection impose reproductive costs in Anopheles gambiae via follicular apoptosis
    • Ahmed AM, Hurd H. Immune stimulation and malaria infection impose reproductive costs in Anopheles gambiae via follicular apoptosis. Microbes Infect 2006; 8:308-315
    • (2006) Microbes Infect , vol.8 , pp. 308-315
    • Ahmed, A.M.1    Hurd, H.2
  • 49
    • 0036008501 scopus 로고    scopus 로고
    • Molecular characterization of three gut genes from Glossina morsitans morsitans: Cathepsin B, zinc-metalloprotease and zinc-carboxypeptidase
    • Yan J, Cheng Q, Li CB et al. Molecular characterization of three gut genes from Glossina morsitans morsitans: cathepsin B, zinc-metalloprotease and zinc-carboxypeptidase. Insect Mol Biol 2002; 11:57-65
    • (2002) Insect Mol Biol , vol.11 , pp. 57-65
    • Yan, J.1    Cheng, Q.2    Li, C.B.3
  • 50
    • 11044235318 scopus 로고    scopus 로고
    • Activity and sequence characterization of two cysteine proteases in the digestive tract of the reduviid bug Triatoma infestans
    • Kollien AH, Waniek PJ, Nisbet AJ et al. Activity and sequence characterization of two cysteine proteases in the digestive tract of the reduviid bug Triatoma infestans. Insect Mol Biol 2004; 13:569-579
    • (2004) Insect Mol Biol , vol.13 , pp. 569-579
    • Kollien, A.H.1    Waniek, P.J.2    Nisbet, A.J.3
  • 51
    • 0001471673 scopus 로고
    • Activity cycles and the control of four digestive proteinases in the posterior midgut of Rhodnius prolixus Stal (Hemiptera: Reduviidae)
    • Houseman JG, Downe AER. Activity cycles and the control of four digestive proteinases in the posterior midgut of Rhodnius prolixus Stal (Hemiptera: Reduviidae). J Insect Physiol 1983; 29:141-148
    • (1983) J Insect Physiol , vol.29 , pp. 141-148
    • Houseman, J.G.1    Aer, D.2
  • 52
    • 38249031505 scopus 로고
    • Ultrastructural localisation of cathepsin B in the midgut of Rhodnius prolixus Stal (Hemiptera: Reduviidae) during blood digestion
    • Billingsley PF, Downe AER. Ultrastructural localisation of cathepsin B in the midgut of Rhodnius prolixus Stal (Hemiptera: Reduviidae) during blood digestion. Int J Insect Morph Embryol 1988; 17:295-302
    • (1988) Int J Insect Morph Embryol , vol.17 , pp. 295-302
    • Billingsley, P.F.1    Aer, D.2
  • 53
    • 0001624454 scopus 로고
    • Origin, distribution, properties and functions of the major Rhodnius prolixus midgut hydrolases
    • Terra WR, Ferreira C, Garcia ES. Origin, distribution, properties and functions of the major Rhodnius prolixus midgut hydrolases. Insect Biochem 1988; 18:423-434
    • (1988) Insect Biochem , vol.18 , pp. 423-434
    • Terra, W.R.1    Ferreira, C.2    Garcia, E.S.3
  • 54
    • 0001594651 scopus 로고
    • Characterization of an acidic proteinase from the posterior midgut of Rhodnius prolixus Stal (Hemiptera: Reduviidae)
    • Houseman JG, Downe AER. Characterization of an acidic proteinase from the posterior midgut of Rhodnius prolixus Stal (Hemiptera: Reduviidae). Insect Biochem 1982; 12:651-655
    • (1982) Insect Biochem , vol.12 , pp. 651-655
    • Houseman, J.G.1    Aer, D.2
  • 55
    • 0034782251 scopus 로고    scopus 로고
    • Characterization of a cDNA encoding a cathepsin L-like protein of Rhodnius prolixus
    • Lopez-Ordonez T, Rodriguez MH, Hernandez-Hernandez FD. Characterization of a cDNA encoding a cathepsin L-like protein of Rhodnius prolixus. Insect Mol Biol 2001; 10:505-511
    • (2001) Insect Mol Biol , vol.10 , pp. 505-511
    • Lopez-Ordonez, T.1    Rodriguez, M.H.2    Hernandez-Hernandez, F.D.3
  • 56
    • 0034242674 scopus 로고    scopus 로고
    • Proteolytic activation of canatoxin, a plant toxic protein, by insect cathepsin-like enzymes
    • Ferreira-DaSilva CT, Gombarovits ME, Masuda H et al. Proteolytic activation of canatoxin, a plant toxic protein, by insect cathepsin-like enzymes. Arch Insect Biochem Physiol 2000; 44:162-171
    • (2000) Arch Insect Biochem Physiol , vol.44 , pp. 162-171
    • Ferreira-Dasilva, C.T.1    Gombarovits, M.E.2    Masuda, H.3
  • 57
    • 0031111489 scopus 로고    scopus 로고
    • Biological effects of canatoxin in different insect models: Evidence for a proteolytic activation ofthe toxin by insect cathepsinlike enzymes
    • Carlini CR, Oliveira AE, Azambuja P et al. Biological effects of canatoxin in different insect models: evidence for a proteolytic activation ofthe toxin by insect cathepsinlike enzymes. J Econ Entomol 1997; 90:340-348
    • (1997) J Econ Entomol , vol.90 , pp. 340-348
    • Carlini, C.R.1    Oliveira, A.E.2    Azambuja, P.3
  • 58
    • 0030944555 scopus 로고    scopus 로고
    • Proteolytic enzymes in the blood-feeding parasitic copepod, Phrixocephalus cincinnatus
    • Perkins PS, Haley D, Rosenblatt R. Proteolytic enzymes in the blood-feeding parasitic copepod, Phrixocephalus cincinnatus. J Parasitol 1997; 83:6-12
    • (1997) J Parasitol , vol.83 , pp. 6-12
    • Perkins, P.S.1    Haley, D.2    Rosenblatt, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.