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Volumn 14, Issue 22, 2005, Pages 3397-3405

RNAi-mediated suppression of the mitochondrial iron chaperone, frataxin, in Drosophila

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; FERRITIN; FRATAXIN; HEME; IRON; SULFUR;

EID: 27944495710     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddi367     Document Type: Article
Times cited : (119)

References (61)
  • 2
    • 0030813487 scopus 로고    scopus 로고
    • Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin
    • Koutnikova, H., Campuzano, V., Foury, F., Dolle, P., Cazzalini, O. and Koenig, M. (1997) Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat. Genet., 16, 345-351.
    • (1997) Nat. Genet. , vol.16 , pp. 345-351
    • Koutnikova, H.1    Campuzano, V.2    Foury, F.3    Dolle, P.4    Cazzalini, O.5    Koenig, M.6
  • 4
    • 0034969491 scopus 로고    scopus 로고
    • Friedreich ataxia: From GAA triplet-repeat expansion to frataxin deficiency
    • Patel, P.I. and Isaya, G. (2001) Friedreich ataxia: From GAA triplet-repeat expansion to frataxin deficiency. Am. J. Hum. Genet., 69, 15-24.
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 15-24
    • Patel, P.I.1    Isaya, G.2
  • 8
    • 0033582421 scopus 로고    scopus 로고
    • The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle
    • Radisky, D.C., Babcock, M.C. and Kaplan, J. (1999) The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle. J. Biol. Chem., 274, 4497-4499.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4497-4499
    • Radisky, D.C.1    Babcock, M.C.2    Kaplan, J.3
  • 9
    • 0033838364 scopus 로고    scopus 로고
    • Iron-dependent self-assembly of recombinant yeast frataxin: Implications for Friedreich ataxia
    • Adamec, J., Rusnak, F., Owen, W.G., Naylor, S., Benson, L.M., Gacy, A.M. and Isaya, G. (2000) Iron-dependent self-assembly of recombinant yeast frataxin: Implications for Friedreich ataxia. Am. J. Hum. Genet., 67, 549-562.
    • (2000) Am. J. Hum. Genet. , vol.67 , pp. 549-562
    • Adamec, J.1    Rusnak, F.2    Owen, W.G.3    Naylor, S.4    Benson, L.M.5    Gacy, A.M.6    Isaya, G.7
  • 10
    • 0035976840 scopus 로고    scopus 로고
    • YFH1-mediated iron homeostatis is independent of mitochondrial respiration
    • Chen, O.P. and Kaplan, J. (2001) YFH1-mediated iron homeostatis is independent of mitochondrial respiration. FEBS Lett., 509, 131-134.
    • (2001) FEBS Lett. , vol.509 , pp. 131-134
    • Chen, O.P.1    Kaplan, J.2
  • 11
    • 0037188390 scopus 로고    scopus 로고
    • Physical evidence that yeast frataxin is an iron storage protein
    • Gakh, O., Adamec, J., Gacy, A.M., Twesten, R.D., Owen, W.G. and Isaya, G. (2002) Physical evidence that yeast frataxin is an iron storage protein. Biochemistry, 41, 6798-6804.
    • (2002) Biochemistry , vol.41 , pp. 6798-6804
    • Gakh, O.1    Adamec, J.2    Gacy, A.M.3    Twesten, R.D.4    Owen, W.G.5    Isaya, G.6
  • 12
    • 0037064027 scopus 로고    scopus 로고
    • The ferroxidase activity of yeast frataxin
    • Park, S., Gakh, O., Mooney, S.M. and Isaya, G. (2002) The ferroxidase activity of yeast frataxin. J. Biol. Chem., 277, 38589-38595.
    • (2002) J. Biol. Chem. , vol.277 , pp. 38589-38595
    • Park, S.1    Gakh, O.2    Mooney, S.M.3    Isaya, G.4
  • 13
  • 14
    • 0042232045 scopus 로고    scopus 로고
    • Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation
    • Park, S., Gakh, O., O'Neill, H.A., Mangravita, A., Nichol, H., Ferreira, G.C. and Isaya, G. (2003) Yeast frataxin sequentially chaperones and stores iron by coupling protein assembly with iron oxidation. J. Biol. Chem., 278, 31340-31351.
    • (2003) J. Biol. Chem. , vol.278 , pp. 31340-31351
    • Park, S.1    Gakh, O.2    O'Neill, H.A.3    Mangravita, A.4    Nichol, H.5    Ferreira, G.C.6    Isaya, G.7
  • 16
    • 0037168598 scopus 로고    scopus 로고
    • Genetic analysis of iron citrate toxicity in yeast: Implications for mammalian iron homeostasis
    • Chen, O.S., Hemenway, S. and Kaplan, J. (2002) Genetic analysis of iron citrate toxicity in yeast: Implications for mammalian iron homeostasis. Proc. Natl Acad. Sci. USA, 99, 16922-16927.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16922-16927
    • Chen, O.S.1    Hemenway, S.2    Kaplan, J.3
  • 17
    • 0032800601 scopus 로고    scopus 로고
    • Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
    • Foury, F. (1999) Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain. FEBS Lett., 456, 281-284.
    • (1999) FEBS Lett. , vol.456 , pp. 281-284
    • Foury, F.1
  • 18
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • Muhlenhoff, U., Richhardt, N., Ristow, M., Kispal, G. and Lill, R. (2002) The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol. Genet., 11, 2025-2036.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2025-2036
    • Muhlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 19
    • 2242453224 scopus 로고    scopus 로고
    • Characterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron
    • Muhlenhoff, U., Richhardt, N., Gerber, J. and Lill, R. (2002) Characterization of iron-sulfur protein assembly in isolated mitochondria. A requirement for ATP, NADH, and reduced iron. J. Biol. Chem., 277, 29810-29816.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29810-29816
    • Muhlenhoff, U.1    Richhardt, N.2    Gerber, J.3    Lill, R.4
  • 20
    • 0141737067 scopus 로고    scopus 로고
    • Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p
    • Muhlenhoff, U., Gerber, J., Richhardt, N. and Lill, R. (2003) Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J., 22, 4815-4825.
    • (2003) EMBO J. , vol.22 , pp. 4815-4825
    • Muhlenhoff, U.1    Gerber, J.2    Richhardt, N.3    Lill, R.4
  • 22
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau, A.L., O'Neill, H.A., Kennedy, M.C., Ikeda-Saito, M., Isaya, G. and Szweda, L.I. (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science, 305, 242-245.
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 23
    • 0030825723 scopus 로고    scopus 로고
    • Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue
    • Wilson, R.B. and Roof, D.M. (1997) Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue. Nat. Genet., 16, 352-357.
    • (1997) Nat. Genet. , vol.16 , pp. 352-357
    • Wilson, R.B.1    Roof, D.M.2
  • 24
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio, H., Simon, D., Cossee, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P. and Koenig, M. (2001) Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet., 27, 181-186.
    • (2001) Nat. Genet. , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossee, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6    Hindelang, C.7    Matyas, R.8    Rustin, P.9    Koenig, M.10
  • 25
    • 0034601719 scopus 로고    scopus 로고
    • dfh is a Drosophila homolog of the Friedreich's ataxia disease gene
    • Canizares, J., Blanca, J.M., Navarro, J.A., Monros, E., Palau, F. and Molto, M.D. (2000) dfh is a Drosophila homolog of the Friedreich's ataxia disease gene. Gene, 256, 35-42.
    • (2000) Gene , vol.256 , pp. 35-42
    • Canizares, J.1    Blanca, J.M.2    Navarro, J.A.3    Monros, E.4    Palau, F.5    Molto, M.D.6
  • 26
    • 0034731447 scopus 로고    scopus 로고
    • Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates
    • Cavadini, P., Adamec, J., Taroni, F., Gakh, O. and Isaya, G. (2000) Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates. J. Biol. Chem., 275, 41469-41475.
    • (2000) J. Biol. Chem. , vol.275 , pp. 41469-41475
    • Cavadini, P.1    Adamec, J.2    Taroni, F.3    Gakh, O.4    Isaya, G.5
  • 27
    • 0035253385 scopus 로고    scopus 로고
    • Distinct roles for two N-terminal cleaved domains in mitochondrial import of the yeast frataxin homolog, Yfh1p
    • Gordon, D.M., Kogan, M., Knight, S.A., Dancis, A., Pain, D., Gordon, B.N. and Kogan, K.L. (2001) Distinct roles for two N-terminal cleaved domains in mitochondrial import of the yeast frataxin homolog, Yfh1p. Hum. Mol. Genet., 10, 259-269.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 259-269
    • Gordon, D.M.1    Kogan, M.2    Knight, S.A.3    Dancis, A.4    Pain, D.5    Gordon, B.N.6    Kogan, K.L.7
  • 29
    • 0029045343 scopus 로고
    • Expression of crumbs confers apical character on plasma membrane domains of ectodermal epithelia of Drosophila
    • Wodarz, A., Hinz, U., Engelbert, M. and Knust, E. (1995) Expression of crumbs confers apical character on plasma membrane domains of ectodermal epithelia of Drosophila. Cell, 82, 67-76.
    • (1995) Cell , vol.82 , pp. 67-76
    • Wodarz, A.1    Hinz, U.2    Engelbert, M.3    Knust, E.4
  • 30
    • 0035208075 scopus 로고    scopus 로고
    • The Drosophila daughterless gene autoregulates and is controlled by both positive and negative cis regulation
    • Smith, J.E. and Cronmiller, C. (2001) The Drosophila daughterless gene autoregulates and is controlled by both positive and negative cis regulation. Development, 128, 4705-4714.
    • (2001) Development , vol.128 , pp. 4705-4714
    • Smith, J.E.1    Cronmiller, C.2
  • 31
    • 0026045587 scopus 로고
    • Superoxide sensitivity of the Escherichia coli Aconitase
    • Gardner, P.R. and Fridovich, I. (1991) Superoxide sensitivity of the Escherichia coli Aconitase. J. Biol. Chem., 266, 19 328-19 333.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19328-19333
    • Gardner, P.R.1    Fridovich, I.2
  • 32
    • 0346220295 scopus 로고    scopus 로고
    • Compartment-specific protection of iron-sulfur proteins by superoxide dismutase
    • Missirlis, F., Hu, J., Kirby, K., Hilliker, A.J., Rouault, T.A. and Phillips, J.P. (2003) Compartment-specific protection of iron-sulfur proteins by superoxide dismutase. J. Biol. Chem., 278, 47 365-47 369.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47365-47369
    • Missirlis, F.1    Hu, J.2    Kirby, K.3    Hilliker, A.J.4    Rouault, T.A.5    Phillips, J.P.6
  • 33
    • 0037059057 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of Sod2 in Drosophila leads to early adult-onset mortality and elevated endogenous oxidative stress
    • Kirby, K., Hu, J., Hilliker, A.J. and Phillips, J.P. (2002) RNA interference-mediated silencing of Sod2 in Drosophila leads to early adult-onset mortality and elevated endogenous oxidative stress. Proc. Natl Acad. Sci. USA., 99, 16162-16167.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16162-16167
    • Kirby, K.1    Hu, J.2    Hilliker, A.J.3    Phillips, J.P.4
  • 34
    • 0038332156 scopus 로고    scopus 로고
    • Novel roles for iron regulatory proteins in the adaptive response to iron deficiency
    • Eisenstein, R.S. and Ross, K.L. (2003) Novel roles for iron regulatory proteins in the adaptive response to iron deficiency. J. Nutr., 133, 1510S-1516S.
    • (2003) J. Nutr. , vol.133
    • Eisenstein, R.S.1    Ross, K.L.2
  • 35
    • 0030087911 scopus 로고    scopus 로고
    • Distinct expression patterns detected within individual tissues by the GAL4 enhancer trap technique
    • Gustafson, K. and Boulianne, G.L. (1996) Distinct expression patterns detected within individual tissues by the GAL4 enhancer trap technique. Genome, 39, 174-182.
    • (1996) Genome , vol.39 , pp. 174-182
    • Gustafson, K.1    Boulianne, G.L.2
  • 38
    • 0346100684 scopus 로고    scopus 로고
    • A Sod2 null mutation confers severely reduced adult lifespan in Drosophila
    • Duttaroy, A., Paul A., Kundu, M., and Belton, A. (2003) A Sod2 null mutation confers severely reduced adult lifespan in Drosophila. Genetics, 165, 2295-2299.
    • (2003) Genetics , vol.165 , pp. 2295-2299
    • Duttaroy, A.1    Paul, A.2    Kundu, M.3    Belton, A.4
  • 39
    • 0032728444 scopus 로고    scopus 로고
    • The tamas gene, identified as a mutation that disrupts larval behavior in Drosophila melanogaster, codes for the mitochondrial DNA polymerase catalytic subunit (DNApol-gamma125)
    • Iyengar, B., Roote, J. and Campos, A.R. (1999) The tamas gene, identified as a mutation that disrupts larval behavior in Drosophila melanogaster, codes for the mitochondrial DNA polymerase catalytic subunit (DNApol-gamma125). Genetics, 153, 1809-1824.
    • (1999) Genetics , vol.153 , pp. 1809-1824
    • Iyengar, B.1    Roote, J.2    Campos, A.R.3
  • 40
    • 0035172433 scopus 로고    scopus 로고
    • Mitochondrial single-stranded DNA-binding protein is required for mitochondrial DNA replication and development in Drosophila melanogaster
    • Maier, D., Farr, C.L., Poeck, B., Alahari, A., Vogel, M., Fischer, S., Kaguni, L.S. and Schneuwly, S. (2001) Mitochondrial single-stranded DNA-binding protein is required for mitochondrial DNA replication and development in Drosophila melanogaster. Mol. Biol. Cell, 12, 821-830.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 821-830
    • Maier, D.1    Farr, C.L.2    Poeck, B.3    Alahari, A.4    Vogel, M.5    Fischer, S.6    Kaguni, L.S.7    Schneuwly, S.8
  • 41
    • 0037007114 scopus 로고    scopus 로고
    • The accessory subunit of DNA polymerase gamma is essential for mitochondrial DNA maintenance and development in Drosophila melanogaster
    • Iyengar, B., Luo, N., Farr, C.L., Kaguni, L.S. and Campos, A.R. (2002) The accessory subunit of DNA polymerase gamma is essential for mitochondrial DNA maintenance and development in Drosophila melanogaster. Proc. Natl Acad. Sci. USA, 99, 4483-4488.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 4483-4488
    • Iyengar, B.1    Luo, N.2    Farr, C.L.3    Kaguni, L.S.4    Campos, A.R.5
  • 42
    • 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. and 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
  • 43
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfar protein maturation in human cells: Evidence for a function of frataxin
    • Stehling, O., Elsasser, H.P., Bruckel, B., Muhlenhoff, U. and Lill, R. (2004) Iron-sulfar protein maturation in human cells: Evidence for a function of frataxin. Hum. Mol. Genet., 13, 3007-3015.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 3007-3015
    • Stehling, O.1    Elsasser, H.P.2    Bruckel, B.3    Muhlenhoff, U.4    Lill, R.5
  • 44
    • 0033019925 scopus 로고    scopus 로고
    • Iron availability dramatically alters the distribution of ferritin subunit messages in Drosophila melanogaster
    • Georgieva, T., Dunkov, B.C., Harizanova, N., Ralchev, K. and Law, J.H. (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, B.C.2    Harizanova, N.3    Ralchev, K.4    Law, J.H.5
  • 45
    • 0022483582 scopus 로고
    • Hypotrophic and dying-back nerve fibers in Friedreich's ataxia
    • Said, G., Marion, M.H., Selva, J. and Jamet, C. (1986) Hypotrophic and dying-back nerve fibers in Friedreich's ataxia. Neurology, 36, 1292-1299.
    • (1986) Neurology , vol.36 , pp. 1292-1299
    • Said, G.1    Marion, M.H.2    Selva, J.3    Jamet, C.4
  • 46
    • 0342700237 scopus 로고    scopus 로고
    • Recent advances in the molecular pathogenesis of Friedreich ataxia
    • Puccio, H. and Koenig, M. (2000) Recent advances in the molecular pathogenesis of Friedreich ataxia. Hum. Mol. Genet., 9, 887-892.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 887-892
    • Puccio, H.1    Koenig, M.2
  • 47
    • 0032193137 scopus 로고    scopus 로고
    • Transgenic analysis of the cSOD-null phenotypic syndrome in Drosophila
    • Parkes, T.L., Kirby, K., Phillips, J.P. and Hilliker, A.J. (1998) Transgenic analysis of the cSOD-null phenotypic syndrome in Drosophila. Genome, 41, 642-651.
    • (1998) Genome , vol.41 , pp. 642-651
    • Parkes, T.L.1    Kirby, K.2    Phillips, J.P.3    Hilliker, A.J.4
  • 48
    • 0035989388 scopus 로고    scopus 로고
    • Induced overexpression of mitochondrial Mn-superoxide dismutase extends the life span of adult Drosophila melanogaster
    • Sun, J., Folk, D., Bradley, T.J. and Tower, J. (2002) Induced overexpression of mitochondrial Mn-superoxide dismutase extends the life span of adult Drosophila melanogaster. Genetics, 161, 661-672.
    • (2002) Genetics , vol.161 , pp. 661-672
    • Sun, J.1    Folk, D.2    Bradley, T.J.3    Tower, J.4
  • 49
    • 0026783733 scopus 로고
    • The effects of Catalase gene overexpression on life span and resistance to oxidative stress in transgenic Drosophila melanogaster
    • Orr, W.C. and Sohal, R.S. (1992) The effects of Catalase gene overexpression on life span and resistance to oxidative stress in transgenic Drosophila melanogaster. Arch. Biochem. Biophys., 297, 35-41.
    • (1992) Arch. Biochem. Biophys. , vol.297 , pp. 35-41
    • Orr, W.C.1    Sohal, R.S.2
  • 50
    • 0003455528 scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Ashburner, M. (1989) Drosophila A Laboratory Handbook. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) Drosophila A Laboratory Handbook
    • Ashburner, M.1
  • 51
    • 0027160708 scopus 로고
    • Targeted gene expression as a means of altering cell fates and generating dominant phenotypes
    • Brand, A.H. and Perrimon, N. (1993) Targeted gene expression as a means of altering cell fates and generating dominant phenotypes. Development, 118, 401-415.
    • (1993) Development , vol.118 , pp. 401-415
    • Brand, A.H.1    Perrimon, N.2
  • 52
    • 0019945644 scopus 로고
    • Genetic transformation of Drosophila with transposable element vectors
    • Rubin, G.M. and Spradling, A.C. (1981) Genetic transformation of Drosophila with transposable element vectors. Science, 218, 348-352.
    • (1981) Science , vol.218 , pp. 348-352
    • Rubin, G.M.1    Spradling, A.C.2
  • 54
    • 0017139230 scopus 로고
    • A sensitive assay for superoxide dismutase based on the autoxidation of 6-hydroxydopamine
    • Heikkila, R.E. and Cabbat, F. (1976) A sensitive assay for superoxide dismutase based on the autoxidation of 6-hydroxydopamine. Anal. Biochem., 75, 356-362.
    • (1976) Anal. Biochem. , vol.75 , pp. 356-362
    • Heikkila, R.E.1    Cabbat, F.2
  • 55
    • 0030915736 scopus 로고    scopus 로고
    • The manganese superoxide dismutase gene of Drosophila: Structure, expression, and evidence for regulation by MAP kinase
    • Duttaroy, A., Parkes, T., Emtage, P., Kirby, K., Boulianne, G.L., Wang, X., Hilliker, A.J. and Phillips, J.P. (1997) The manganese superoxide dismutase gene of Drosophila: Structure, expression, and evidence for regulation by MAP kinase. DNA Cell Biol., 16, 391-399.
    • (1997) DNA Cell Biol. , vol.16 , pp. 391-399
    • Duttaroy, A.1    Parkes, T.2    Emtage, P.3    Kirby, K.4    Boulianne, G.L.5    Wang, X.6    Hilliker, A.J.7    Phillips, J.P.8
  • 56
    • 0027284743 scopus 로고
    • Molecular characterization and rescue of acatalasemic mutants of Drosophila melanogaster
    • Griswold, C.M., Matthews, A.L., Bewley, K.E. and Mahaffey, J.W. (1993) Molecular characterization and rescue of acatalasemic mutants of Drosophila melanogaster. Genetics, 134, 781-788.
    • (1993) Genetics , vol.134 , pp. 781-788
    • Griswold, C.M.1    Matthews, A.L.2    Bewley, K.E.3    Mahaffey, J.W.4
  • 57
    • 0000008655 scopus 로고
    • Preparation of insect mitochondria
    • Van den Bergh, S.G. (1967) Preparation of insect mitochondria. Methods Enzymol., 10, 117-122.
    • (1967) Methods Enzymol. , vol.10 , pp. 117-122
    • Van den Bergh, S.G.1
  • 58
    • 0014198972 scopus 로고
    • Purification and kinetic studies of beef liver cytoplasmic aconitase
    • Henson, C.P. and Cleland, W.W. (1967) Purification and kinetic studies of beef liver cytoplasmic aconitase. J. Biol. Chem., 242, 3833-3838.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3833-3838
    • Henson, C.P.1    Cleland, W.W.2
  • 59
    • 0029964226 scopus 로고    scopus 로고
    • Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines
    • Trounce, I.A., Kim, Y.L., Jun, A.S. and Wallace, D.C. (1996) Assessment of mitochondrial oxidative phosphorylation in patient muscle biopsies, lymphoblasts, and transmitochondrial cell lines. Methods Enzymol., 264, 484-509.
    • (1996) Methods Enzymol. , vol.264 , pp. 484-509
    • Trounce, I.A.1    Kim, Y.L.2    Jun, A.S.3    Wallace, D.C.4
  • 61
    • 0034682706 scopus 로고    scopus 로고
    • A-to-I pre-mRNA editing in Drosophila is primarily involved in adult nervous system function and integrity
    • Palladino, M.J., Keegan, L.P., O'Connell, M.A. and Reenan, R.A. (2000) A-to-I pre-mRNA editing in Drosophila is primarily involved in adult nervous system function and integrity. Cell, 102, 437-449.
    • (2000) Cell , vol.102 , pp. 437-449
    • Palladino, M.J.1    Keegan, L.P.2    O'Connell, M.A.3    Reenan, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.