메뉴 건너뛰기




Volumn 13, Issue 4, 2004, Pages 423-433

Stress and transcriptional regulation of tick ferritin HC

Author keywords

Dermacentor andersoni; Dermacentor variabilis; Escherichia coli; Ferritin HC; Stress and immune response

Indexed keywords

COMPLEMENTARY DNA; FERRITIN; MESSENGER RNA; PRIMER DNA;

EID: 3943097414     PISSN: 09621075     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.0962-1075.2004.00502.x     Document Type: Article
Times cited : (22)

References (50)
  • 2
    • 0031861480 scopus 로고    scopus 로고
    • Rickettsial pathogens and their arthropod vectors
    • Azad, A.F. and Beard, C.B. (1998) Rickettsial pathogens and their arthropod vectors. Emerg Infect Dis 4: 179-186.
    • (1998) Emerg Infect Dis , vol.4 , pp. 179-186
    • Azad, A.F.1    Beard, C.B.2
  • 3
    • 0036027763 scopus 로고    scopus 로고
    • Evolutionof the acute phase respons: Iron release by echinoderm (Asterias forbesi) coelomocytes, and cloning of an echinoderm ferritin molecule
    • Beck, G., Ellis, T.W., Habicht, G.S., Schluter, S.F. and Marchalonis, J.J. (2002) Evolutionof the acute phase respons: iron release by echinoderm (Asterias forbesi) coelomocytes, and cloning of an echinoderm ferritin molecule. Devel Comp Immunol 26: 11-26.
    • (2002) Devel Comp Immunol , vol.26 , pp. 11-26
    • Beck, G.1    Ellis, T.W.2    Habicht, G.S.3    Schluter, S.F.4    Marchalonis, J.J.5
  • 4
    • 0142025364 scopus 로고    scopus 로고
    • The relationship between serum ferritin levels and disease activity in systemic lupus erthematosus
    • Beyan, E., Beyan, C., Demirezer, A., Ertugrul, E. and Uzuner, A. (2003) The relationship between serum ferritin levels and disease activity in systemic lupus erthematosus. Scand J Rheumat 32: 225-228.
    • (2003) Scand J Rheumat , vol.32 , pp. 225-228
    • Beyan, E.1    Beyan, C.2    Demirezer, A.3    Ertugrul, E.4    Uzuner, A.5
  • 5
    • 3943075856 scopus 로고
    • Structural and functional relationships of human H and L chains deduced from cDNA clones
    • Boyd, G., Jain, S.K., Crompton, J., Barret, K.J. and Drysdale, J. (1985) Structural and functional relationships of human H and L chains deduced from cDNA clones. Proc Natl Acad Sci USA 81: 4751-4755.
    • (1985) Proc Natl Acad Sci USA , vol.81 , pp. 4751-4755
    • Boyd, G.1    Jain, S.K.2    Crompton, J.3    Barret, K.J.4    Drysdale, J.5
  • 6
    • 0029815291 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: A protective strategy against oxidative injury
    • Cairo, G., Gastrusini, E., Minoti, E. G. and Bernelli-Zazzera, A. (1996) Superoxide and hydrogen peroxide-dependent inhibition of iron regulatory protein activity: a protective strategy against oxidative injury. FASEB J 10: 1326-1335.
    • (1996) FASEB J , vol.10 , pp. 1326-1335
    • Cairo, G.1    Gastrusini, E.2    Minoti, E.G.3    Bernelli-Zazzera, A.4
  • 7
    • 0034038169 scopus 로고    scopus 로고
    • Ferritin acts as the most abundant binding protein for snowdrop lectin in the midgut of rice brown planthoppers (Nilaparvata lugens)
    • Du, J.X. Foissac, A. Carss, A.M.R. Gatehouse and Gatehouse. (2000) Ferritin acts as the most abundant binding protein for snowdrop lectin in the midgut of rice brown planthoppers (Nilaparvata lugens). Insect Biochem Mol Biol 30: 297-305.
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 297-305
    • Du, J.X.1    Foissac, A.2    Carss, A.M.R.3    Gatehouse4    Gatehouse5
  • 8
    • 0035192367 scopus 로고    scopus 로고
    • Reorganization of genera in the families Rickettsiaceae and Anaplasmataceae in the order Rickettsiales: Unification of some species of Ehrlichia with Anaplasma, Cowdria and Ehrlichia with Neorickettsia, descriptions of six new species combinations and designation of Ehrlichia equi HE agent as subjective synonyms of Ehrlichia Phagocytophila
    • Dumler, J.S., Barbet, A.F., Bekker, C.P.J., Dasch, G.A., Palmer, G.H., Rikihisa, S.C. and Rurangirwa, F.R. (2001) Reorganization of genera in the families Rickettsiaceae and Anaplasmataceae in the order Rickettsiales: unification of some species of Ehrlichia with Anaplasma, Cowdria and Ehrlichia with Neorickettsia, descriptions of six new species combinations and designation of Ehrlichia equi HE agent as subjective synonyms of Ehrlichia Phagocytophila Int J Syst Bacteriol 51: 2145-2165.
    • (2001) Int J Syst Bacteriol , vol.51 , pp. 2145-2165
    • Dumler, J.S.1    Barbet, A.F.2    Bekker, C.P.J.3    Dasch, G.A.4    Palmer, G.H.5    Rikihisa, S.C.6    Rurangirwa, F.R.7
  • 9
    • 0029176319 scopus 로고
    • Isolation and characterization of mosquito ferritin and cloning of a cDNA that encodes one subunit
    • Dunkov, B.C., Zang, D., Choumarov, K., Winzerling, J.J. and Law, J.H. (1995) Isolation and characterization of mosquito ferritin and cloning of a cDNA that encodes one subunit. Arch Insect Biochem Physiol 29: 293-307.
    • (1995) Arch Insect Biochem Physiol , vol.29 , pp. 293-307
    • Dunkov, B.C.1    Zang, D.2    Choumarov, K.3    Winzerling, J.J.4    Law, J.H.5
  • 11
    • 0141447418 scopus 로고    scopus 로고
    • Aedes aegypti ferritin. A cytotoxic protector against iron and oxidative challenge
    • Geiser, D.L., Chavez, C.A., Flores-Mungia, R., Winzerling, J.J. and Pham, D.Q. (2003) Aedes aegypti ferritin. A cytotoxic protector against iron and oxidative challenge. Eur J Biochem 18: 3667-3670.
    • (2003) Eur J Biochem , vol.18 , pp. 3667-3670
    • Geiser, D.L.1    Chavez, C.A.2    Flores-Mungia, R.3    Winzerling, J.J.4    Pham, D.Q.5
  • 12
    • 0033019925 scopus 로고    scopus 로고
    • Iron availability dramatically alters the distribution of ferritin subunit messages in Drosophila melanogaster
    • Georgieva, T., Dunkov, C.B., Harizanova, N., Ralchev, K. and Law, H.L. (1999) Iron availability dramatically alters the distribution of ferritin subunit messages in Drosophila melanogaster. Proc Natl Acad Sci USA 96: 2716-2721.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2716-2721
    • Georgieva, T.1    Dunkov, C.B.2    Harizanova, N.3    Ralchev, K.4    Law, H.L.5
  • 14
    • 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 Biophy Acta 1275: 161-203.
    • (1996) Biochim Biophy Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 15
    • 0038007043 scopus 로고    scopus 로고
    • Profiles of the acute-phase reactants C-reactive protein and ferritin related to the disease course of patients with systemic lupus erythromatosus
    • Hasselink, D.A., Aarden, L.A. and Swak, A.J. (2003) Profiles of the acute-phase reactants C-reactive protein and ferritin related to the disease course of patients with systemic lupus erythromatosus. Scand J Rheumatol 32: 151-155.
    • (2003) Scand J Rheumatol , vol.32 , pp. 151-155
    • Hasselink, D.A.1    Aarden, L.A.2    Swak, A.J.3
  • 16
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress
    • Hentze, M.W. and Kuhn, L.C. (1996) Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress. Proc Natl Acad Sci USA 93: 8175-8182.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 17
    • 0029875555 scopus 로고    scopus 로고
    • Purification and cDNA cloning of ferritin from hepatopancreas of the freshwater crayfish Pacifastacus leniusculus
    • Huang, T.S., Law, J.H. and Soderhall, K. (1996) Purification and cDNA cloning of ferritin from hepatopancreas of the freshwater crayfish Pacifastacus leniusculus. Eur J Biochem 236: 50-456.
    • (1996) Eur J Biochem , vol.236 , pp. 50-456
    • Huang, T.S.1    Law, J.H.2    Soderhall, K.3
  • 18
    • 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 hemolymph
    • Johns, R., Sonenshine, D.E. and Hynes, W.L. (1998) Control of bacterial infections in the hard tick Dermacentor variabilis (Acari: Ixodidae): Evidence for the existence of antimicrobial proteins in tick hemolymph. J Med Entomol 35: 458-464.
    • (1998) J Med Entomol , vol.35 , pp. 458-464
    • Johns, R.1    Sonenshine, D.E.2    Hynes, W.L.3
  • 19
    • 0032583768 scopus 로고    scopus 로고
    • Experimantal transmission of Ehrlichia canis (Rickettsiales: Ehrlichieae) by Dermacentor variabilis (Acari: Ixodidae)
    • Johnson, E.M., Ewing, S.A., Barker, R.W., Fox, J.C., Crow, D.W. and Kocan, K.M. (1998) Experimantal transmission of Ehrlichia canis (Rickettsiales: Ehrlichieae) by Dermacentor variabilis (Acari: Ixodidae). Vet Parasitol 74: 277-288.
    • (1998) Vet Parasitol , vol.74 , pp. 277-288
    • Johnson, E.M.1    Ewing, S.A.2    Barker, R.W.3    Fox, J.C.4    Crow, D.W.5    Kocan, K.M.6
  • 20
    • 0034783889 scopus 로고    scopus 로고
    • Heme utilization in Bordettela avium is regulated by Rhul, a heme-responsive extracytoplasmic function sigma factor
    • Kirby, A.E., Metzger, D.J., Murphy, E.R. and Connel, T.D. (2001) Heme utilization in Bordettela avium is regulated by Rhul, a heme-responsive extracytoplasmic function sigma factor. Infect Immun 69: 6951-6961.
    • (2001) Infect Immun , vol.69 , pp. 6951-6961
    • Kirby, A.E.1    Metzger, D.J.2    Murphy, E.R.3    Connel, T.D.4
  • 21
    • 0347262495 scopus 로고    scopus 로고
    • Characterization of an alpha-2 macroglobulin-like glycoprotein isolated from the plasma of the soft tick Ornithodoros moubata
    • Kopacek, P., Weise, C., Saravanan, T., Vitova, K. and Grubhoffer, L. (2000) Characterization of an alpha-2 macroglobulin-like glycoprotein isolated from the plasma of the soft tick Ornithodoros moubata. Eur J Biochem 267: 465-475.
    • (2000) Eur J Biochem , vol.267 , pp. 465-475
    • Kopacek, P.1    Weise, C.2    Saravanan, T.3    Vitova, K.4    Grubhoffer, L.5
  • 22
    • 0037211912 scopus 로고    scopus 로고
    • Molecular cloning, expression and isolation of ferritins from two tick species, Ornithodorous moubata and Ixodes ricinus
    • Kopacek, P., Zdychova, J., Yoshiga, T., Weise, C., Rudenko, N. and Law, J.H. (2003) Molecular cloning, expression and isolation of ferritins from two tick species, Ornithodorous moubata and Ixodes ricinus. Insect Biochem Mol Biol 33: 103-113.
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 103-113
    • Kopacek, P.1    Zdychova, J.2    Yoshiga, T.3    Weise, C.4    Rudenko, N.5    Law, J.H.6
  • 23
    • 0343049158 scopus 로고    scopus 로고
    • Isolation and characterization of Dorin M, a lectin from plasma of the soft tick Ornithodoros moubata
    • Kovar, V., Kopacek, P. and Grubhoffer, L. (2000) Isolation and characterization of Dorin M, a lectin from plasma of the soft tick Ornithodoros moubata. Insect Biochem Mol Biol 30: 195-205.
    • (2000) Insect Biochem Mol Biol , vol.30 , pp. 195-205
    • Kovar, V.1    Kopacek, P.2    Grubhoffer, L.3
  • 24
    • 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
  • 25
    • 0037155836 scopus 로고    scopus 로고
    • Characterization of a novel salivay immuno suppressive protein from Ixodes ricinus ticks
    • Leboule, G., Crippa, M., Decrem, Y., Meijri, N., Brossard, M., Bollen, A. and Godfroid, E. (2002b) Characterization of a novel salivay immuno suppressive protein from Ixodes ricinus ticks. J Biol Chem 277: 10083-10089.
    • (2002) J Biol Chem , vol.277 , pp. 10083-10089
    • Leboule, G.1    Crippa, M.2    Decrem, Y.3    Meijri, N.4    Brossard, M.5    Bollen, A.6    Godfroid, E.7
  • 26
    • 0036311291 scopus 로고    scopus 로고
    • Iolation of Ixodes ricinus salivary gland mRNAs encoding factors induced during the blood feeding
    • Leboule, G., Rochez, C., Louahed, J., Rutti, B., Brossard, M., Bollen, A. and Godfroid, E. (2002a) Iolation of Ixodes ricinus salivary gland mRNAs encoding factors induced during the blood feeding. Am J Top Med Hyg 66: 225-233.
    • (2002) Am J Top Med Hyg , vol.66 , pp. 225-233
    • Leboule, G.1    Rochez, C.2    Louahed, J.3    Rutti, B.4    Brossard, M.5    Bollen, A.6    Godfroid, E.7
  • 27
    • 0001657675 scopus 로고
    • Iron economy in insects: Transport, metabolism and storage
    • Locke, M. and Nichol, H. (1992) Iron economy in insects: transport, metabolism and storage. Annu Rev Entomol 37: 195-215.
    • (1992) Annu Rev Entomol , vol.37 , pp. 195-215
    • Locke, M.1    Nichol, H.2
  • 28
    • 0242349667 scopus 로고    scopus 로고
    • Differential expression of genes in uninfected and Rickettsia-infected Dermacentor variabilis as assessed by differential display PCR
    • Macaluso, K.R., Mulenga, A., Simser, J.A. and Azad, A.F. (2003) Differential expression of genes in uninfected and Rickettsia-infected Dermacentor variabilis as assessed by differential display PCR. Infect Immun 71: 6165-6570.
    • (2003) Infect Immun , vol.71 , pp. 6165-6570
    • Macaluso, K.R.1    Mulenga, A.2    Simser, J.A.3    Azad, A.F.4
  • 29
    • 0037384330 scopus 로고    scopus 로고
    • Dynamics of Rickettsia-tick interactions: Identification and characterization of differentially expressed mRNAs in uninfected and infected Dermacentor variabilis
    • Mulenga, A., Macaluso, K.R., Simser, J.A. and Azad, A.F. (2003a) Dynamics of Rickettsia-tick interactions: identification and characterization of differentially expressed mRNAs in uninfected and infected Dermacentor variabilis. Insect Mol Biol 12: 185-193.
    • (2003) Insect Mol Biol , vol.12 , pp. 185-193
    • Mulenga, A.1    Macaluso, K.R.2    Simser, J.A.3    Azad, A.F.4
  • 30
    • 0043241696 scopus 로고    scopus 로고
    • The American dog tick, Dermacentor variabilis, encodes a functional histamine release factor homolog
    • Mulenga, A., Macaluso, K.R., Simser, J.A. and Azad, A.F. (2003b) The American dog tick, Dermacentor variabilis, encodes a functional histamine release factor homolog. Insect Biochem Mol Biol 33: 911-919.
    • (2003) Insect Biochem Mol Biol , vol.33 , pp. 911-919
    • Mulenga, A.1    Macaluso, K.R.2    Simser, J.A.3    Azad, A.F.4
  • 31
    • 0035933451 scopus 로고    scopus 로고
    • Characterization of two cDNAs encoding serine proteinases from the hard tick Haemaphysalis longicornis
    • Mulenga, A., Sugimoto, C., Ingram, G., Ohashi, K. and Onuma, M. (2001) Characterization of two cDNAs encoding serine proteinases from the hard tick Haemaphysalis longicornis. Insect Biochem Mol Biol 31: 817-825.
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 817-825
    • Mulenga, A.1    Sugimoto, C.2    Ingram, G.3    Ohashi, K.4    Onuma, M.5
  • 32
    • 0031740909 scopus 로고    scopus 로고
    • Molecular and serologic survey of Ehrlichia canis, E. chaffeensis, and E. ewingii in dogs and ticks from Oklahoma
    • Murphy, G.L., Ewing, S.A., Whitworth, L.C., Fox, J.C. and Kocan, A.A. (1998) Molecular and serologic survey of Ehrlichia canis, E. chaffeensis, and E. ewingii in dogs and ticks from Oklahoma. Vet Parasitol 79: 325-339.
    • (1998) Vet Parasitol , vol.79 , pp. 325-339
    • Murphy, G.L.1    Ewing, S.A.2    Whitworth, L.C.3    Fox, J.C.4    Kocan, A.A.5
  • 33
    • 0036785652 scopus 로고    scopus 로고
    • BhuR, a virulence-associated outer membrane protein of Bordetella avium, is required for the acquisition of iron from heme and hemoproteins
    • Murphy, E.R., Sacco, R.E., Dickenson, A., Metzger, D.J., Hu, Y., Ondorf, P.E. and Connel, T.D. (2002) BhuR, a virulence-associated outer membrane protein of Bordetella avium, is required for the acquisition of iron from heme and hemoproteins. Infect Immun 70: 5390-5403.
    • (2002) Infect Immun , vol.70 , pp. 5390-5403
    • Murphy, E.R.1    Sacco, R.E.2    Dickenson, A.3    Metzger, D.J.4    Hu, Y.5    Ondorf, P.E.6    Connel, T.D.7
  • 34
    • 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., Naters-Yasui, A.G., Taylor, D. and Yamakawa, M. (2001) Two isoforms of a member of the arthropod defensin family from the soft tick, Ornithodoros moubata (Acari: Argasidae). Insect Biochem Mol Biol 31: 747-751.
    • (2001) Insect Biochem Mol Biol , vol.31 , pp. 747-751
    • Nakajima, Y.1    Naters-Yasui, A.G.2    Taylor, D.3    Yamakawa, M.4
  • 35
    • 0025637618 scopus 로고
    • The localization of ferritin in insects
    • Nichol, H.K. 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.K.1    Locke, M.2
  • 36
    • 0033230271 scopus 로고    scopus 로고
    • Secreted ferritin subunits of two kinds in insects: Molecular cloning of cDNAs encoding two major subunits of secreted ferritin from Calpodes ethlius
    • Nichol, H. and Locke, M. (1999) Secreted ferritin subunits of two kinds in insects: molecular cloning of cDNAs encoding two major subunits of secreted ferritin from Calpodes ethlius. Insect Biochem Mol Biol 29: 999-1013.
    • (1999) Insect Biochem Mol Biol , vol.29 , pp. 999-1013
    • Nichol, H.1    Locke, M.2
  • 37
    • 0042885835 scopus 로고    scopus 로고
    • Serum ferritin increases in hemorrhaged rats that develop acute lung injury: Effect of an iron-defficient diet
    • Park, Y.Y., Hybertson, B.M., Wright, R.M. and Repine, J.E. (2003) Serum ferritin increases in hemorrhaged rats that develop acute lung injury: effect of an iron-defficient diet. Inflammation 27: 257-263.
    • (2003) Inflammation , vol.27 , pp. 257-263
    • Park, Y.Y.1    Hybertson, B.M.2    Wright, R.M.3    Repine, J.E.4
  • 38
    • 0036133186 scopus 로고    scopus 로고
    • Molecular insect modeling of ferritins
    • Pham, D.Q.-D. (2002) Molecular insect modeling of ferritins. In Silico Biol 2: S31-S44.
    • (2002) In Silico Biol , vol.2
    • Pham, D.Q.-D.1
  • 39
    • 0033571744 scopus 로고    scopus 로고
    • Transcriptional control is relevant in the modulation of mosquito ferritin synthesis by iron
    • Pham, D.Q.-D., Winzerling, J.J., Dodson, M.S. and Law, J.H. (1999) Transcriptional control is relevant in the modulation of mosquito ferritin synthesis by iron. Eur J Biochem 266: 236-240.
    • (1999) Eur J Biochem , vol.266 , pp. 236-240
    • Pham, D.Q.-D.1    Winzerling, J.J.2    Dodson, M.S.3    Law, J.H.4
  • 40
    • 0034595617 scopus 로고    scopus 로고
    • Lack of a role for iron in the lyme disease pathogen
    • Posey, J.E. and Gherardini, F.C. (2000) Lack of a role for iron in the lyme disease pathogen. Science 288: 1651-1653.
    • (2000) Science , vol.288 , pp. 1651-1653
    • Posey, J.E.1    Gherardini, F.C.2
  • 41
    • 0036199104 scopus 로고    scopus 로고
    • Vector interactions and molecular adaptations of Lyme disease and relapsing fever spirochetes associated with transmission by ticks
    • Schwan, T.G. and Piesman, J. (2002) Vector interactions and molecular adaptations of Lyme disease and relapsing fever spirochetes associated with transmission by ticks. Emerg Infect Dis 8: 115-121.
    • (2002) Emerg Infect Dis , vol.8 , pp. 115-121
    • Schwan, T.G.1    Piesman, J.2
  • 42
    • 1342310723 scopus 로고    scopus 로고
    • An immune responsive factor D-like serine proteinase homolog identified from the American dog tick, Dermacentor variabilis
    • Simser, J.A., Mulenga, A., Macaluso, K.R. and Azad, A.F. (2004) An immune responsive factor D-like serine proteinase homolog identified from the American dog tick, Dermacentor variabilis. Insect Mol Biol 13: 25-36.
    • (2004) Insect Mol Biol , vol.13 , pp. 25-36
    • Simser, J.A.1    Mulenga, A.2    Macaluso, K.R.3    Azad, A.F.4
  • 44
    • 0036635732 scopus 로고    scopus 로고
    • Dermacentor variabilis and Boophilus microplus (Acari: Ixididae): Experimental vectors of Babesia equi to Equitis
    • Stiller, D., Goff, W.L., Johnson, L.W. and Knowles, D.P. (2002) Dermacentor variabilis and Boophilus microplus (Acari: Ixididae): Experimental vectors of Babesia equi to Equitis. J Med Entomol 39: 667-670.
    • (2002) J Med Entomol , vol.39 , pp. 667-670
    • Stiller, D.1    Goff, W.L.2    Johnson, L.W.3    Knowles, D.P.4
  • 45
    • 0038656684 scopus 로고    scopus 로고
    • Inflammation, reactive oxygen species and cytocrome P450
    • Symons, A.M. and King, L.J. (2003) Inflammation, reactive oxygen species and cytocrome P450. Inflammopharmacology 11: 75-86.
    • (2003) Inflammopharmacology , vol.11 , pp. 75-86
    • Symons, A.M.1    King, L.J.2
  • 46
    • 1942503204 scopus 로고    scopus 로고
    • Proinflammatory cytokines increase iron uptake into human moncytes and synovial fibroblasts from patients with rheumatoid arthritis
    • Telfer, J.F. and Brock, J.H. (2004) Proinflammatory cytokines increase iron uptake into human moncytes and synovial fibroblasts from patients with rheumatoid arthritis. Medical Sci Monit 10: BR91-BR95.
    • (2004) Medical Sci Monit , vol.10
    • Telfer, J.F.1    Brock, J.H.2
  • 47
    • 0028114730 scopus 로고
    • Iron regulatory elements (IREs): A family of mRNA non-coding sequences
    • Theil, E.C. (1994) Iron regulatory elements (IREs): a family of mRNA non-coding sequences. Biochem J 304: 1-11.
    • (1994) Biochem J , vol.304 , pp. 1-11
    • Theil, E.C.1
  • 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
    • 0030817280 scopus 로고    scopus 로고
    • Mosquito transferin, an acute-phase protein that is up-regulated upon infection
    • Yoshiga, T., Hernandez, V.P., Fallon, M.A. and Law, J.H. (1997) Mosquito transferin, an acute-phase protein that is up-regulated upon infection. Proc Natl Acad Sci USA 94: 12337-12342.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12337-12342
    • Yoshiga, T.1    Hernandez, V.P.2    Fallon, M.A.3    Law, J.H.4
  • 50


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.