메뉴 건너뛰기




Volumn 216, Issue 10, 2013, Pages 1905-1915

Multiple ferritins are vital to successful blood feeding and reproduction of the hard tick Haemaphysalis longicornis

Author keywords

Ferritin; Iron; RNA interference; Ticks

Indexed keywords

ANTISERUM; COMPLEMENTARY DNA; FERRITIN; IRON; MESSENGER RNA; RECOMBINANT PROTEIN; VITELLOGENIN;

EID: 84877128087     PISSN: 00220949     EISSN: None     Source Type: Journal    
DOI: 10.1242/jeb.081240     Document Type: Article
Times cited : (57)

References (58)
  • 1
    • 0022831769 scopus 로고
    • Scanning electron microscopy of digest cells in the midgut epithelium of Boophilus microplus
    • Agbede, R. I. S. (1986). Scanning electron microscopy of digest cells in the midgut epithelium of Boophilus microplus. Exp. Appl. Acarol. 2, 329-335.
    • (1986) Exp. Appl. Acarol. , vol.2 , pp. 329-335
    • Agbede, R.I.S.1
  • 2
    • 0022049116 scopus 로고
    • Digestion in the cattle-tick Boophilus microplus: Light microscope study of the gut cells in nymphs and females
    • Agbede, R. I. S. and Kemp, D. H. (1985). Digestion in the cattle-tick Boophilus microplus: light microscope study of the gut cells in nymphs and females. Int. J. Parasitol. 15, 147-157.
    • (1985) Int. J. Parasitol. , vol.15 , pp. 147-157
    • Agbede, R.I.S.1    Kemp, D.H.2
  • 3
    • 0028795658 scopus 로고
    • Studies on the morphological changes in the midguts of two ixodid tick species Boophilus microplus and Rhipicephalus appendiculatus during digestion of the blood meal
    • Agyei, A. D. and Runham, N. W. (1995). Studies on the morphological changes in the midguts of two ixodid tick species Boophilus microplus and Rhipicephalus appendiculatus during digestion of the blood meal. Int. J. Parasitol. 25, 55-62.
    • (1995) Int. J. Parasitol. , vol.25 , pp. 55-62
    • Agyei, A.D.1    Runham, N.W.2
  • 4
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: A family of molecules for iron storage, antioxidation and more
    • Arosio, P., Ingrassia, R. and Cavadini, P. (2009). Ferritins: a family of molecules for iron storage, antioxidation and more. Biochim. Biophys. Acta 1790, 589-599.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 5
    • 19044396103 scopus 로고    scopus 로고
    • Nutritional regulation of vitellogenesis in mosquitoes: Implications for anautogeny
    • Attardo, G. M., Hansen, I. A. and Raikhel, A. S. (2005). Nutritional regulation of vitellogenesis in mosquitoes: implications for anautogeny. Insect Biochem. Mol. Biol. 35, 661-675.
    • (2005) Insect Biochem. Mol. Biol. , vol.35 , pp. 661-675
    • Attardo, G.M.1    Hansen, I.A.2    Raikhel, A.S.3
  • 7
    • 0016938325 scopus 로고
    • Ultrafine structure of the midgut epithelium in nymphal Hyalomma asiaticum (Acarina, Ixodidae) during feeding
    • Balashov, Y. S. and Raikhel, A. S. (1976). Ultrafine structure of the midgut epithelium in nymphal Hyalomma asiaticum (Acarina, Ixodidae) during feeding. Parazitologiya 10, 201-209.
    • (1976) Parazitologiya , vol.10 , pp. 201-209
    • Balashov, Y.S.1    Raikhel, A.S.2
  • 8
    • 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., Xuan, X. and Fujisaki, K. (2006). Molecular cloning and functional characterization of an aspartic protease from the hard tick Haemaphysalis longicornis. Insect Biochem. Mol. Biol. 36, 25-36.
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 25-36
    • Boldbaatar, D.1    Sikalizyo Sikasunge, C.2    Battsetseg, B.3    Xuan, X.4    Fujisaki, K.5
  • 9
    • 75949118911 scopus 로고    scopus 로고
    • GATA transcription, translation and regulation in Haemaphysalis longicornis tick: Analysis of the cDNA and an essential role for vitellogenesis
    • Boldbaatar, D., Battur, B., Umemiya-Shirafuji, R., Liao, M., Tanaka, T. and Fujisaki, K. (2010a). GATA transcription, translation and regulation in Haemaphysalis longicornis tick: analysis of the cDNA and an essential role for vitellogenesis. Insect Biochem. Mol. Biol. 40, 49-57.
    • (2010) Insect Biochem. Mol. Biol. , vol.40 , pp. 49-57
    • Boldbaatar, D.1    Battur, B.2    Umemiya-Shirafuji, R.3    Liao, M.4    Tanaka, T.5    Fujisaki, K.6
  • 10
    • 77955771029 scopus 로고    scopus 로고
    • Multiple vitellogenins from the Haemaphysalis longicornis tick are crucial for ovarian development
    • Boldbaatar, D., Umemiya-Shirafuji, R., Liao, M., Tanaka, T., Xuan, X. and Fujisaki, K. (2010b). Multiple vitellogenins from the Haemaphysalis longicornis tick are crucial for ovarian development. J. Insect Physiol. 56, 1587-1598.
    • (2010) J. Insect Physiol. , vol.56 , pp. 1587-1598
    • Boldbaatar, D.1    Umemiya-Shirafuji, R.2    Liao, M.3    Tanaka, T.4    Xuan, X.5    Fujisaki, K.6
  • 11
    • 0022853319 scopus 로고
    • The involvement of iron in lipid peroxidation. Importance of ferric to ferrous ratios in initiation
    • Braughler, J. M., Duncan, L. A. and Chase, R. L. (1986). The involvement of iron in lipid peroxidation. Importance of ferric to ferrous ratios in initiation. J. Biol. Chem. 261, 10282-10289.
    • (1986) J. Biol. Chem. , vol.261 , pp. 10282-10289
    • Braughler, J.M.1    Duncan, L.A.2    Chase, R.L.3
  • 12
    • 0033166924 scopus 로고    scopus 로고
    • A missing metabolic pathway in the cattle tick Boophilus microplus
    • Braz, G. R. C., Coelho, H. S. L., Masuda, H. and Oliveira, P. L. (1999). A missing metabolic pathway in the cattle tick Boophilus microplus. Curr. Biol. 9, 703-706.
    • (1999) Curr. Biol. , vol.9 , pp. 703-706
    • Braz, G.R.C.1    Coelho, H.S.L.2    Masuda, H.3    Oliveira, P.L.4
  • 13
    • 20944445785 scopus 로고    scopus 로고
    • RNA interference screening in ticks for identification of protective antigens
    • de la Fuente, J., Almazán, C., Blouin, E. F., Naranjo, V. and Kocan, K. M. (2005). RNA interference screening in ticks for identification of protective antigens. Parasitol. Res. 96, 137-141.
    • (2005) Parasitol. Res. , vol.96 , pp. 137-141
    • De La Fuente, J.1    Almazán, C.2    Blouin, E.F.3    Naranjo, V.4    Kocan, K.M.5
  • 14
    • 34548033965 scopus 로고    scopus 로고
    • RNA interference for the study and genetic manipulation of ticks
    • de la Fuente, J., Kocan, K. M., Almazán, C. and Blouin, E. F. (2007). RNA interference for the study and genetic manipulation of ticks. Trends Parasitol. 23, 427-433.
    • (2007) Trends Parasitol. , vol.23 , pp. 427-433
    • De La Fuente, J.1    Kocan, K.M.2    Almazán, C.3    Blouin, E.F.4
  • 15
    • 34447344092 scopus 로고    scopus 로고
    • Two ferritin subunits from disk abalone (Haliotis discus discus): Cloning, characterization and expression analysis
    • De Zoysa, M. and Lee, J. (2007). Two ferritin subunits from disk abalone (Haliotis discus discus): cloning, characterization and expression analysis. Fish Shellfish Immunol. 23, 624-635.
    • (2007) Fish Shellfish Immunol. , vol.23 , pp. 624-635
    • De Zoysa, M.1    Lee, J.2
  • 17
    • 68349093906 scopus 로고    scopus 로고
    • Salivary gland degeneration and vitellogenesis in the ixodid tick Amblyomma hebraeum: Surpassing a critical weight is the prerequisite and detachment from the host is the trigger
    • Friesen, K. J. and Kaufman, W. R. (2009). Salivary gland degeneration and vitellogenesis in the ixodid tick Amblyomma hebraeum: surpassing a critical weight is the prerequisite and detachment from the host is the trigger. J. Insect Physiol. 55, 936-942.
    • (2009) J. Insect Physiol. , vol.55 , pp. 936-942
    • Friesen, K.J.1    Kaufman, W.R.2
  • 18
    • 0028001652 scopus 로고
    • Iron induces lipid peroxidation in cultured macrophages, increases their ability to oxidatively modify LDL, and affects their secretory properties
    • Fuhrman, B., Oiknine, J. and Aviram, M. (1994). Iron induces lipid peroxidation in cultured macrophages, increases their ability to oxidatively modify LDL, and affects their secretory properties. Atherosclerosis 111, 65-78.
    • (1994) Atherosclerosis , vol.111 , pp. 65-78
    • Fuhrman, B.1    Oiknine, J.2    Aviram, M.3
  • 19
    • 0017943792 scopus 로고
    • Development of acquired resistance precipitating antibody in rabbits experimentally infested with females of Haemaphysalis longicornis (Ixodoidea: Ixodidae)
    • Fujisaki, K. (1978). Development of acquired resistance precipitating antibody in rabbits experimentally infested with females of Haemaphysalis longicornis (Ixodoidea: Ixodidae). Natl. Inst. Anim. Health Q. 18, 27-38.
    • (1978) Natl. Inst. Anim. Health Q , vol.18 , pp. 27-38
    • Fujisaki, K.1
  • 20
    • 0041824774 scopus 로고
    • Hemocyte types and their primary cultures in the argasid tick, Ornithodoros moubata Murray (Ixodoidea)
    • Fujisaki, K., Kitaoka, S. and Morii, T. (1975). Hemocyte types and their primary cultures in the argasid tick, Ornithodoros moubata Murray (Ixodoidea). Appl. Entomol. Zool. 10, 30-39.
    • (1975) Appl. Entomol. Zool. , vol.10 , pp. 30-39
    • Fujisaki, K.1    Kitaoka, S.2    Morii, T.3
  • 21
    • 0028366341 scopus 로고
    • The taxonomy of the bovine Theileria spp
    • Fujisaki, K., Kawazu, S. and Kamio, T. (1994). The taxonomy of the bovine Theileria spp. Parasitol. Today 10, 31-33.
    • (1994) Parasitol. Today , vol.10 , pp. 31-33
    • Fujisaki, K.1    Kawazu, S.2    Kamio, T.3
  • 23
    • 33644551295 scopus 로고    scopus 로고
    • Secreted ferritin: Mosquito defense against iron overload?
    • Geiser, D. L., Zhang, D. and Winzerling, J. J. (2006). Secreted ferritin: mosquito defense against iron overload? Insect Biochem. Mol. Biol. 36, 177-187.
    • (2006) Insect Biochem. Mol. Biol. , vol.36 , pp. 177-187
    • Geiser, D.L.1    Zhang, D.2    Winzerling, J.J.3
  • 26
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison, P. M. and Arosio, P. (1996). The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275, 161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 27
    • 16844371922 scopus 로고    scopus 로고
    • The global importance of ticks
    • Jongejan, F. and Uilenberg, G. (2004). The global importance of ticks. Parasitology 129 Suppl., S3-S14.
    • (2004) Parasitology , vol.129 , Issue.SUPPL.
    • Jongejan, F.1    Uilenberg, G.2
  • 28
    • 18244362050 scopus 로고    scopus 로고
    • Vector-capping: A simple method for preparing a high-quality full-length cDNA library
    • Kato, S., Ohtoko, K., Ohtake, H. and Kimura, T. (2005). Vector-capping: a simple method for preparing a high-quality full-length cDNA library. DNA Res. 12, 53-62.
    • (2005) DNA Res. , vol.12 , pp. 53-62
    • Kato, S.1    Ohtoko, K.2    Ohtake, H.3    Kimura, T.4
  • 29
    • 0037211912 scopus 로고    scopus 로고
    • Molecular cloning, expression and isolation of ferritins from two tick species - Ornithodoros moubata and Ixodes ricinus
    • Kopáček, P., Zdychová, J., Yoshiga, T., Weise, C., Rudenko, N. and Law, J. H. (2003). Molecular cloning, expression and isolation of ferritins from two tick species - Ornithodoros moubata and Ixodes ricinus. Insect Biochem. Mol. Biol. 33, 103-113.
    • (2003) Insect Biochem. Mol. Biol. , vol.33 , pp. 103-113
    • Kopáček, P.1    Zdychová, J.2    Yoshiga, T.3    Weise, C.4    Rudenko, N.5    Law, J.H.6
  • 31
    • 0037506077 scopus 로고    scopus 로고
    • A new intracellular pathway of haem detoxification in the midgut of the cattle tick Boophilus microplus: Aggregation inside a specialized organelle, the hemosome
    • Lara, F. A., Lins, U., Paiva-Silva, G., Almeida, I. C., Braga, C. M., Miguens, F. C., Oliveira, P. L. and Dansa-Petretski, M. (2003). A new intracellular pathway of haem detoxification in the midgut of the cattle tick Boophilus microplus: aggregation inside a specialized organelle, the hemosome. J. Exp. Biol. 206, 1707-1715.
    • (2003) J. Exp. Biol. , vol.206 , pp. 1707-1715
    • Lara, F.A.1    Lins, U.2    Paiva-Silva, G.3    Almeida, I.C.4    Braga, C.M.5    Miguens, F.C.6    Oliveira, P.L.7    Dansa-Petretski, M.8
  • 32
    • 38749126197 scopus 로고    scopus 로고
    • Functional analysis of protein disulfide isomerases in blood feeding, viability and oocyte development in Haemaphysalis longicornis ticks
    • Liao, M., Boldbaatar, D., Gong, H., Huang, P., Umemiya, R., Harnnoi, T., Zhou, J., Tanaka, T., Suzuki, H., Xuan, X. et al. (2008). Functional analysis of protein disulfide isomerases in blood feeding, viability and oocyte development in Haemaphysalis longicornis ticks. Insect Biochem. Mol. Biol. 38, 285-295.
    • (2008) Insect Biochem. Mol. Biol. , vol.38 , pp. 285-295
    • Liao, M.1    Boldbaatar, D.2    Gong, H.3    Huang, P.4    Umemiya, R.5    Harnnoi, T.6    Zhou, J.7    Tanaka, T.8    Suzuki, H.9    Xuan, X.10
  • 33
    • 0038686225 scopus 로고    scopus 로고
    • Morphological studies on the extracellular structure of the midgut of a tick, Haemaphysalis longicornis (Acari: Ixodidae)
    • Matsuo, T., Sato, M., Inoue, N., Yokoyama, N., Taylor, D. and Fujisaki, K. (2003). Morphological studies on the extracellular structure of the midgut of a tick, Haemaphysalis longicornis (Acari: Ixodidae). Parasitol. Res. 90, 243-248.
    • (2003) Parasitol. Res. , vol.90 , pp. 243-248
    • Matsuo, T.1    Sato, M.2    Inoue, N.3    Yokoyama, N.4    Taylor, D.5    Fujisaki, K.6
  • 35
    • 80051662320 scopus 로고    scopus 로고
    • A possible role for secreted ferritin in tissue iron distribution
    • Meyron-Holtz, E. G., Moshe-Belizowski, S. and Cohen, L. A. (2011). A possible role for secreted ferritin in tissue iron distribution. J. Neural Transm. 118, 337-347.
    • (2011) J. Neural Transm. , vol.118 , pp. 337-347
    • Meyron-Holtz, E.G.1    Moshe-Belizowski, S.2    Cohen, L.A.3
  • 36
    • 0025637618 scopus 로고
    • The localization of ferritin in insects
    • Nichol, H. and Locke, M. (1990). The localization of ferritin in insects. Tissue Cell 22, 767-777.
    • (1990) Tissue Cell , vol.22 , pp. 767-777
    • Nichol, H.1    Locke, M.2
  • 38
    • 54449085184 scopus 로고    scopus 로고
    • Molecular, physiological and clinical aspects of the iron storage protein ferritin
    • Orino, K. and Watanabe, K. (2008). Molecular, physiological and clinical aspects of the iron storage protein ferritin. Vet. J. 178, 191-201.
    • (2008) Vet. J. , vol.178 , pp. 191-201
    • Orino, K.1    Watanabe, K.2
  • 41
    • 77953749140 scopus 로고    scopus 로고
    • Insect ferritins: Typical or atypical?
    • Pham, D. Q. D. and Winzerling, J. J. (2010). Insect ferritins: typical or atypical? Biochim. Biophys. Acta 1800, 824-833.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 824-833
    • Pham, D.Q.D.1    Winzerling, J.J.2
  • 42
    • 39049183601 scopus 로고    scopus 로고
    • Importance of ticks and their chemical and immunological control in livestock
    • Rajput, Z. H., Hu, S., Chen, W., Arijo, A. and Xiao, C. (2006). Importance of ticks and their chemical and immunological control in livestock. J. Zhejiang Univ. Sci. B 7, 912-921.
    • (2006) J. Zhejiang Univ. Sci. B , vol.7 , pp. 912-921
    • Rajput, Z.H.1    Hu, S.2    Chen, W.3    Arijo, A.4    Xiao, C.5
  • 43
    • 3242657100 scopus 로고    scopus 로고
    • Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells
    • Riemer, J., Hoepken, H. H., Czerwinska, H., Robinson, S. R. and Dringen, R. (2004). Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells. Anal. Biochem. 331, 370-375.
    • (2004) Anal. Biochem. , vol.331 , pp. 370-375
    • Riemer, J.1    Hoepken, H.H.2    Czerwinska, H.3    Robinson, S.R.4    Dringen, R.5
  • 44
    • 0024382331 scopus 로고
    • Relationship between feeding, mating, vitellogenin production and vitellogenesis in the tick Dermacentor variabilis
    • Rosell-Davis, R. and Coons, L. B. (1989). Relationship between feeding, mating, vitellogenin production and vitellogenesis in the tick Dermacentor variabilis. Exp. Appl. Acarol. 7, 95-105.
    • (1989) Exp. Appl. Acarol. , vol.7 , pp. 95-105
    • Rosell-Davis, R.1    Coons, L.B.2
  • 45
    • 0029803246 scopus 로고    scopus 로고
    • Ferritin mRNAs in Schistosoma mansoni do not have iron-responsive elements for post-transcriptional regulation
    • Schüssler, P., Pötters, E., Winnen, R., Michel, A., Bottke, W. and Kunz, W. (1996). Ferritin mRNAs in Schistosoma mansoni do not have iron-responsive elements for post-transcriptional regulation. Eur. J. Biochem. 241, 64-69.
    • (1996) Eur. J. Biochem. , vol.241 , pp. 64-69
    • Schüssler, P.1    Pötters, E.2    Winnen, R.3    Michel, A.4    Bottke, W.5    Kunz, W.6
  • 46
    • 0024322082 scopus 로고
    • Ultrastructure of the midgut and blood meal digestion in the adult tick Dermacentor variabilis
    • Tarnowski, B. I. and Coons, L. B. (1989). Ultrastructure of the midgut and blood meal digestion in the adult tick Dermacentor variabilis. Exp. Appl. Acarol. 6, 263-289.
    • (1989) Exp. Appl. Acarol. , vol.6 , pp. 263-289
    • Tarnowski, B.I.1    Coons, L.B.2
  • 47
    • 0032878232 scopus 로고    scopus 로고
    • Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation
    • Thomson, A. M., Rogers, J. T. and Leedman, P. J. (1999). Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation. Int. J. Biochem. Cell Biol. 31, 1139-1152.
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 1139-1152
    • Thomson, A.M.1    Rogers, J.T.2    Leedman, P.J.3
  • 48
    • 0033853838 scopus 로고    scopus 로고
    • Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress
    • Tsuji, Y., Ayaki, H., Whitman, S. P., Morrow, C. S., Torti, S. V. and Torti, F. M. (2000). Coordinate transcriptional and translational regulation of ferritin in response to oxidative stress. Mol. Cell. Biol. 20, 5818-5827.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5818-5827
    • Tsuji, Y.1    Ayaki, H.2    Whitman, S.P.3    Morrow, C.S.4    Torti, S.V.5    Torti, F.M.6
  • 49
    • 34547551741 scopus 로고    scopus 로고
    • Cloning and characterization of an autophagy-related gene, ATG12, from the three-host tick Haemaphysalis longicornis
    • Umemiya, R., Matsuo, T., Hatta, T., Sakakibara, S., Boldbaatar, D. and Fujisaki, K. (2007). Cloning and characterization of an autophagy-related gene, ATG12, from the three-host tick Haemaphysalis longicornis. Insect Biochem. Mol. Biol. 37, 975-984.
    • (2007) Insect Biochem. Mol. Biol. , vol.37 , pp. 975-984
    • Umemiya, R.1    Matsuo, T.2    Hatta, T.3    Sakakibara, S.4    Boldbaatar, D.5    Fujisaki, K.6
  • 50
    • 84856228772 scopus 로고    scopus 로고
    • Akt is an essential player in regulating cell/organ growth at the adult stage in the hard tick Haemaphysalis longicornis
    • Umemiya-Shirafuji, R., Tanaka, T., Boldbaatar, D., Tanaka, T. and Fujisaki, K. (2012). Akt is an essential player in regulating cell/organ growth at the adult stage in the hard tick Haemaphysalis longicornis. Insect Biochem. Mol. Biol. 42, 164-173.
    • (2012) Insect Biochem. Mol. Biol. , vol.42 , pp. 164-173
    • Umemiya-Shirafuji, R.1    Tanaka, T.2    Boldbaatar, D.3    Tanaka, T.4    Fujisaki, K.5
  • 51
    • 0028357845 scopus 로고
    • CDNA cloning and deduced amino acid sequence of two ferritins: Soma ferritin and yolk ferritin, from the snail Lymnaea stagnalis L
    • von Darl, M., Harrison, P. M. and Bottke, W. (1994). cDNA cloning and deduced amino acid sequence of two ferritins: soma ferritin and yolk ferritin, from the snail Lymnaea stagnalis L. Eur. J. Biochem. 222, 353-366.
    • (1994) Eur. J. Biochem. , vol.222 , pp. 353-366
    • Von Darl, M.1    Harrison, P.M.2    Bottke, W.3
  • 52
    • 79952162002 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism
    • Wang, J. and Pantopoulos, K. (2011). Regulation of cellular iron metabolism. Biochem. J. 434, 365-381.
    • (2011) Biochem. J. , vol.434 , pp. 365-381
    • Wang, J.1    Pantopoulos, K.2
  • 53
    • 56949101447 scopus 로고    scopus 로고
    • Molecular characterization of iron binding proteins, transferrin and ferritin heavy chain subunit, from the bumblebee Bombus ignitus
    • Wang, D., Kim, B. Y., Lee, K. S., Yoon, H. J., Cui, Z., Lu, W., Jia, J. M., Kim, D. H., Sohn, H. D. and Jin, B. R. (2009). Molecular characterization of iron binding proteins, transferrin and ferritin heavy chain subunit, from the bumblebee Bombus ignitus. Comp. Biochem. Physiol. 152B, 20-27.
    • (2009) Comp. Biochem. Physiol. , vol.152 B , pp. 20-27
    • Wang, D.1    Kim, B.Y.2    Lee, K.S.3    Yoon, H.J.4    Cui, Z.5    Lu, W.6    Jia, J.M.7    Kim, D.H.8    Sohn, H.D.9    Jin, B.R.10
  • 54
    • 0034766035 scopus 로고    scopus 로고
    • The relationship between 'critical weight' and 20-hydroxyecdysone in the female ixodid tick, Amblyomma hebraeum
    • Weiss, B. L. and Kaufman, W. R. (2001). The relationship between 'critical weight' and 20-hydroxyecdysone in the female ixodid tick, Amblyomma hebraeum. J. Insect Physiol. 47, 1261-1267.
    • (2001) J. Insect Physiol. , vol.47 , pp. 1261-1267
    • Weiss, B.L.1    Kaufman, W.R.2
  • 55
    • 33646367410 scopus 로고    scopus 로고
    • Tick control: Thoughts on a research agenda
    • Willadsen, P. (2006). Tick control: thoughts on a research agenda. Vet. Parasitol. 138, 161-168.
    • (2006) Vet. Parasitol. , vol.138 , pp. 161-168
    • Willadsen, P.1
  • 56
    • 3242779512 scopus 로고    scopus 로고
    • Ferritin gene coding sequences are conserved among eight hard tick species (Ixodida: Ixodidae)
    • Xu, G., Fang, Q. Q., Keirans, J. E. and Durden, L. A. (2004). Ferritin gene coding sequences are conserved among eight hard tick species (Ixodida: Ixodidae). Ann. Entomol. Soc. Am. 97, 567-573.
    • (2004) Ann. Entomol. Soc. Am. , vol.97 , pp. 567-573
    • Xu, G.1    Fang, Q.Q.2    Keirans, J.E.3    Durden, L.A.4
  • 57
    • 77953124293 scopus 로고    scopus 로고
    • Identification and analysis of a Scophthalmus maximus ferritin that is regulated at transcription level by oxidative stress and bacterial infection
    • Zheng, W. J., Hu, Y. H. and Sun, L. (2010). Identification and analysis of a Scophthalmus maximus ferritin that is regulated at transcription level by oxidative stress and bacterial infection. Comp. Biochem. Physiol. 156B, 222-228.
    • (2010) Comp. Biochem. Physiol. , vol.156 B , pp. 222-228
    • Zheng, W.J.1    Hu, Y.H.2    Sun, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.