메뉴 건너뛰기




Volumn 247, Issue 2, 1997, Pages 470-475

Isolation and properties of Drosophila melanogaster ferritin - Molecular cloning of a cDNA that encodes one subunit, and localization of the gene on the third chromosome

Author keywords

Drosophila melanogaster; Ferritin; Iron regulatory element; Molecular evolution; Sequence

Indexed keywords

COMPLEMENTARY DNA; FERRITIN; PROTEIN SUBUNIT;

EID: 0030791329     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00470.x     Document Type: Article
Times cited : (58)

References (26)
  • 3
    • 0029176319 scopus 로고
    • Isolation and characterization of a mosquito ferritin and cloning of a cDNA that encodes one subunit
    • Dunkov, B. C., Zhang, D., Choumarov, K., Winzerling, J. J. & Law, J. H. (1995) Isolation and characterization of a mosquito ferritin and cloning of a cDNA that encodes one subunit, Archs. Insect Biochem. Physiol. 29, 293-307.
    • (1995) Archs. Insect Biochem. Physiol. , vol.29 , pp. 293-307
    • Dunkov, B.C.1    Zhang, D.2    Choumarov, K.3    Winzerling, J.J.4    Law, J.H.5
  • 5
    • 0029899154 scopus 로고    scopus 로고
    • Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements
    • Gray, N. K., Pantopoulos, K., Dandekar, T., Ackrell, B. A. C & Hentze, M. W. (1996) Translational regulation of mammalian and Drosophila citric acid cycle enzymes via iron-responsive elements, Proc. Natl Acad. Sci. USA 93, 4925-4930.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 4925-4930
    • Gray, N.K.1    Pantopoulos, K.2    Dandekar, T.3    Ackrell, B.A.C.4    Hentze, M.W.5
  • 7
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: NRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • Hentze, M. W. & Kühn, L. C (1996) Molecular control of vertebrate iron metabolism: nRNA-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    Kühn, L.C.2
  • 8
    • 0029875555 scopus 로고    scopus 로고
    • Purification and cDNA cloning of ferritin from the freshwater crayfish Pacifastacus leniusculus
    • Huang, T. S., Law, J. H. & Söderhäll, K. (1996) Purification and cDNA cloning of ferritin from the freshwater crayfish Pacifastacus leniusculus, Eur. J. Biochem. 236, 450-456.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 450-456
    • Huang, T.S.1    Law, J.H.2    Söderhäll, K.3
  • 10
    • 0029557688 scopus 로고
    • Suceinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5′-unstranslated region
    • Köhler, S. A., Henderson, B. R. & Kühn, L. C. (1995) Suceinate dehydrogenase b mRNA of Drosophila melanogaster has a functional iron-responsive element in its 5′-unstranslated region. J. Biol. Chem. 270, 30781-30786.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30781-30786
    • Köhler, S.A.1    Henderson, B.R.2    Kühn, L.C.3
  • 12
    • 0026684574 scopus 로고
    • Iron dependent regulation of ferritin and transferrin receptor expression by the iron responsive element binding protein
    • Leibold, E. A. & Guo, B. (1992) Iron dependent regulation of ferritin and transferrin receptor expression by the iron responsive element binding protein, Annu. Rev. Nutr. 12, 345-368.
    • (1992) Annu. Rev. Nutr. , vol.12 , pp. 345-368
    • Leibold, E.A.1    Guo, B.2
  • 13
    • 0001657675 scopus 로고
    • Iron economy in insects: Transport, metabolism, and storage
    • Locke, M. & 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
  • 14
    • 0029130335 scopus 로고
    • Regulation of iron metabolism. Translational effects mediated by iron, heme, and cytokines
    • Mascotti, D. P., Rup, D. & Thach, R. E. (1995) Regulation of iron metabolism. Translational effects mediated by iron, heme, and cytokines, Annu. Rev. Nutr. 15, 239-261.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 239-261
    • Mascotti, D.P.1    Rup, D.2    Thach, R.E.3
  • 15
    • 0029984343 scopus 로고    scopus 로고
    • Translational regulation in vivo of the Drosophila melanogaster mRNA encoding succinate dehydrogenase iron protein via iron responsive elements
    • Melefors, O. (1996) Translational regulation in vivo of the Drosophila melanogaster mRNA encoding succinate dehydrogenase iron protein via iron responsive elements, Biochem. Biophys. Res. Commun. 221, 437-441.
    • (1996) Biochem. Biophys. Res. Commun. , vol.221 , pp. 437-441
    • Melefors, O.1
  • 16
    • 1842414557 scopus 로고
    • Ferritin gene structure and expression
    • (Ponka, P., Schulman, H. M. & Woodworth, R. C., eds) CRC Press, Boca Raton
    • Monro, H. N., Leibold, E. A., Aziz, N., Murray, M. T. White, K. & Rogers, J. (1990) Ferritin gene structure and expression .in Iron transport and storage (Ponka, P., Schulman, H. M. & Woodworth, R. C., eds) pp. 133-149, CRC Press, Boca Raton.
    • (1990) Iron Transport and Storage , pp. 133-149
    • Monro, H.N.1    Leibold, E.A.2    Aziz, N.3    Murray, M.T.4    White, K.5    Rogers, J.6
  • 17
    • 38249026419 scopus 로고
    • The characterization of ferritin in an insect
    • Nichol, H. & Locke, M. (1989) The characterization of ferritin in an insect, Insect Biochem. 19, 587-602.
    • (1989) Insect Biochem. , vol.19 , pp. 587-602
    • Nichol, H.1    Locke, M.2
  • 18
    • 0029856377 scopus 로고    scopus 로고
    • High intrinsic rate of DNA loss in Drosophila
    • Petrov, D. M., Lozovskaya, E. R. & Hartl, D. L. (1996) High intrinsic rate of DNA loss in Drosophila, Nature 384, 346-349.
    • (1996) Nature , vol.384 , pp. 346-349
    • Petrov, D.M.1    Lozovskaya, E.R.2    Hartl, D.L.3
  • 19
    • 0029951578 scopus 로고    scopus 로고
    • Manduca sexta hemolymph ferritin : cDNA sequence and mRNA expression
    • Pham, D. Q.-D., Zhang, D., Hufnagel, D. H. & Winzerling, J. J. (1996) Manduca sexta hemolymph ferritin : cDNA sequence and mRNA expression, Gene (Amst.) 172, 255-259.
    • (1996) Gene (Amst.) , vol.172 , pp. 255-259
    • Pham, D.Q.-D.1    Zhang, D.2    Hufnagel, D.H.3    Winzerling, J.J.4
  • 20
    • 0025186372 scopus 로고
    • Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean
    • Ragland, M., Briat, J. F., Gagnon, J., Laulhere, J. P., Massenet, O. & Theil, E. C. (1990) Evidence for conservation of ferritin sequences among plants and animals and for a transit peptide in soybean, J. Biol. Chem. 265, 18 339-18 344.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18339-18344
    • Ragland, M.1    Briat, J.F.2    Gagnon, J.3    Laulhere, J.P.4    Massenet, O.5    Theil, E.C.6
  • 22
    • 0025112529 scopus 로고
    • The ferritin family of iron storage proteins
    • Theil, E. C. (1990) The ferritin family of iron storage proteins, Adv. Enzymol. Mol. Biol. 63, 421-429.
    • (1990) Adv. Enzymol. Mol. Biol. , vol.63 , pp. 421-429
    • Theil, E.C.1
  • 23
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., Higgins, D. G. & Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice, Nucleic Acids Res. 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 24
    • 0020770479 scopus 로고
    • Patterns of amino acid near signal-sequence cleavage sites
    • von Heijne, G. (1983) Patterns of amino acid near signal-sequence cleavage sites, Eur. J. Biochem. 133, 17-21.
    • (1983) Eur. J. Biochem. , vol.133 , pp. 17-21
    • Von Heijne, G.1
  • 25
    • 0027398912 scopus 로고
    • Formation of an Fe(III)-tyrosinate complex during biomineralization of the H-subunit ferritin
    • Waldo, G. S., Ling, J., Sanders-Loehr, J. & Theil, E. C. (1993) Formation of an Fe(III)-tyrosinate complex during biomineralization of the H-subunit ferritin, Science 259, 796-798.
    • (1993) Science , vol.259 , pp. 796-798
    • Waldo, G.S.1    Ling, J.2    Sanders-Loehr, J.3    Theil, E.C.4
  • 26
    • 0029240487 scopus 로고
    • Rapid and efficient isolation of transferrin and ferritin from Manduca sexta
    • Winzerling, J. J., Nez, P., Porath, J. & Law, J. H. (1995) Rapid and efficient isolation of transferrin and ferritin from Manduca sexta. Insect Biochem. Mol. Biol. 25, 217-224.
    • (1995) Insect Biochem. Mol. Biol. , vol.25 , pp. 217-224
    • Winzerling, J.J.1    Nez, P.2    Porath, J.3    Law, J.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.