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Volumn 109, Issue 8, 2007, Pages 3552-3559

RNA silencing of the mitochondrial ABCB7 transporter in HeLa cells causes an iron-deficient phenotype with mitochondrial iron overload

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ACONITATE HYDRATASE; ADENOSINE TRIPHOSPHATE; CITRATE SYNTHASE; FERRITIN; HYDROGEN PEROXIDE; MANGANESE SUPEROXIDE DISMUTASE; PROTEIN ABCB7 TRANSPORTER; PROTOPORPHYRIN; SMALL INTERFERING RNA; SUCCINATE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 34147165135     PISSN: 00064971     EISSN: 00064971     Source Type: Journal    
DOI: 10.1182/blood-2006-08-041632     Document Type: Article
Times cited : (148)

References (58)
  • 1
    • 2042546096 scopus 로고    scopus 로고
    • Balancing acts: Molecular control of mammalian iron metabolism
    • Hentze MW, Muckenthaler MU, Andrews NC. Balancing acts: molecular control of mammalian iron metabolism. Cell. 2004;117:285-297.
    • (2004) Cell , vol.117 , pp. 285-297
    • Hentze, M.W.1    Muckenthaler, M.U.2    Andrews, N.C.3
  • 2
    • 14744294785 scopus 로고    scopus 로고
    • Iron-sulfur-protein biogenesis in eukaryotes
    • Lill R, Muhlenhoff U. Iron-sulfur-protein biogenesis in eukaryotes. Trends Biochem Sci. 2005;30:133-141.
    • (2005) Trends Biochem Sci , vol.30 , pp. 133-141
    • Lill, R.1    Muhlenhoff, U.2
  • 3
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: Novel pathways revealed by disease
    • Napier I, Ponka P, Richardson DR. Iron trafficking in the mitochondrion: novel pathways revealed by disease. Blood. 2005;105:1867-1874.
    • (2005) Blood , vol.105 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 5
    • 0036799489 scopus 로고    scopus 로고
    • The genetics of inherited sideroblastic anemias
    • Fleming MD. The genetics of inherited sideroblastic anemias. Semin Hematol. 2002;39:270-281.
    • (2002) Semin Hematol , vol.39 , pp. 270-281
    • Fleming, M.D.1
  • 6
    • 0032920837 scopus 로고    scopus 로고
    • Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A)
    • Allikmets R, Raskind WH, Hutchinson A, Schueck ND, Dean M, Koeller DM. Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A). Hum Mol Genet. 1999;8:743-749.
    • (1999) Hum Mol Genet , vol.8 , pp. 743-749
    • Allikmets, R.1    Raskind, W.H.2    Hutchinson, A.3    Schueck, N.D.4    Dean, M.5    Koeller, D.M.6
  • 7
    • 0033565665 scopus 로고    scopus 로고
    • The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
    • Kispal G, Csere P, Prohl C, Lill R. The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins. EMBO J. 1999;18:3981-3989.
    • (1999) EMBO J , vol.18 , pp. 3981-3989
    • Kispal, G.1    Csere, P.2    Prohl, C.3    Lill, R.4
  • 8
    • 20044391418 scopus 로고    scopus 로고
    • Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria
    • Kispal G, Sipos K, Lange H, et al. Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria. EMBO J. 2005;24:589-598.
    • (2005) EMBO J , vol.24 , pp. 589-598
    • Kispal, G.1    Sipos, K.2    Lange, H.3
  • 9
    • 14744301484 scopus 로고    scopus 로고
    • Functional link between ribosome formation and biogenesis of iron-sulfur proteins
    • Yarunin A, Panse VG, Petfalski E, Dez C, Tollervey D, Hurt EC. Functional link between ribosome formation and biogenesis of iron-sulfur proteins. EMBO J. 2005;24:580-588.
    • (2005) EMBO J , vol.24 , pp. 580-588
    • Yarunin, A.1    Panse, V.G.2    Petfalski, E.3    Dez, C.4    Tollervey, D.5    Hurt, E.C.6
  • 10
    • 14744279245 scopus 로고    scopus 로고
    • The eukaryotic P loop NTPase Nbp35: An essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery
    • Hausmann A, Aguilar Netz DJ, Balk J, Pierik AJ, Muhlenhoff U, Lill R. The eukaryotic P loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machinery. Proc Natl Acad Sci U S A. 2005;102:3266-3271.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3266-3271
    • Hausmann, A.1    Aguilar Netz, D.J.2    Balk, J.3    Pierik, A.J.4    Muhlenhoff, U.5    Lill, R.6
  • 11
    • 15444371876 scopus 로고    scopus 로고
    • Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis
    • Rutherford JC, Ojeda L, Balk J, Muhlenhoff U, Lill R, Winge DR. Activation of the iron regulon by the yeast Aft1/Aft2 transcription factors depends on mitochondrial but not cytosolic iron-sulfur protein biogenesis. J Biol Chem. 2005;280:10135-10140.
    • (2005) J Biol Chem , vol.280 , pp. 10135-10140
    • Rutherford, J.C.1    Ojeda, L.2    Balk, J.3    Muhlenhoff, U.4    Lill, R.5    Winge, D.R.6
  • 12
    • 3142667831 scopus 로고    scopus 로고
    • Transcription of the yeast iron regulon does not respond directly to iron but rather to iron-sulfur cluster biosynthesis
    • Chen OS, Crisp RJ, Valachovic M, Bard M, Winge DR, Kaplan J. Transcription of the yeast iron regulon does not respond directly to iron but rather to iron-sulfur cluster biosynthesis. J Biol Chem. 2004;279:29513-29518.
    • (2004) J Biol Chem , vol.279 , pp. 29513-29518
    • Chen, O.S.1    Crisp, R.J.2    Valachovic, M.3    Bard, M.4    Winge, D.R.5    Kaplan, J.6
  • 13
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • Lill R, Kispal G. Maturation of cellular Fe-S proteins: an essential function of mitochondria. Trends Biochem Sci. 2000;25:352-356.
    • (2000) Trends Biochem Sci , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 14
    • 31544445770 scopus 로고    scopus 로고
    • Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
    • Gakh O, Park S, Liu G, et al. Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity. Hum Mol Genet. 2006;15:467-479.
    • (2006) Hum Mol Genet , vol.15 , pp. 467-479
    • Gakh, O.1    Park, S.2    Liu, G.3
  • 15
    • 33744956665 scopus 로고    scopus 로고
    • Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly
    • Li K, Tong WH, Hughes RM, Rouault TA. Roles of the mammalian cytosolic cysteine desulfurase, ISCS, and scaffold protein, ISCU, in iron-sulfur cluster assembly. J Biol Chem. 2006;281:12344-12351.
    • (2006) J Biol Chem , vol.281 , pp. 12344-12351
    • Li, K.1    Tong, W.H.2    Hughes, R.M.3    Rouault, T.A.4
  • 16
    • 0034331239 scopus 로고    scopus 로고
    • Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells
    • Tong WH, Rouault T. Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells. EMBO J. 2000;19:5692-5700.
    • (2000) EMBO J , vol.19 , pp. 5692-5700
    • Tong, W.H.1    Rouault, T.2
  • 17
    • 33644623262 scopus 로고    scopus 로고
    • Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
    • Tong WH, Rouault TA. Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis. Cell Metab. 2006;3:199-210.
    • (2006) Cell Metab , vol.3 , pp. 199-210
    • Tong, W.H.1    Rouault, T.A.2
  • 18
    • 33746509655 scopus 로고    scopus 로고
    • Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation
    • Biederbick A, Stehling O, Rosser R, et al. Role of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulation. Mol Cell Biol. 2006;26:5675-5687.
    • (2006) Mol Cell Biol , vol.26 , pp. 5675-5687
    • Biederbick, A.1    Stehling, O.2    Rosser, R.3
  • 19
    • 33748745666 scopus 로고    scopus 로고
    • RNA silencing of mitochondrial m-Nfs1 reduces Fe-S enzyme activity both in mitochondria and cytosol of mammalian cells
    • Fosset C, Chauveau MJ, Guillon B, Canal F, Drapier JC, Bouton C. RNA silencing of mitochondrial m-Nfs1 reduces Fe-S enzyme activity both in mitochondria and cytosol of mammalian cells. J Biol Chem. 2006;281:25398-25406.
    • (2006) J Biol Chem , vol.281 , pp. 25398-25406
    • Fosset, C.1    Chauveau, M.J.2    Guillon, B.3    Canal, F.4    Drapier, J.C.5    Bouton, C.6
  • 20
    • 0032414310 scopus 로고    scopus 로고
    • Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p
    • Csere P, Lill R, Kispal G. Identification of a human mitochondrial ABC transporter, the functional orthologue of yeast Atm1p. FEBS Lett. 1998;441:266-270.
    • (1998) FEBS Lett , vol.441 , pp. 266-270
    • Csere, P.1    Lill, R.2    Kispal, G.3
  • 21
    • 0037944100 scopus 로고    scopus 로고
    • Involvement of ABC7 in the biosynthesis of heme in erythroid cells: Interaction of ABC7 with ferrochelatase
    • Taketani S, Kakimoto K, Ueta H, Masaki R, Furukawa T. Involvement of ABC7 in the biosynthesis of heme in erythroid cells: interaction of ABC7 with ferrochelatase. Blood. 2003;101:3274-3280.
    • (2003) Blood , vol.101 , pp. 3274-3280
    • Taketani, S.1    Kakimoto, K.2    Ueta, H.3    Masaki, R.4    Furukawa, T.5
  • 22
    • 33644772614 scopus 로고    scopus 로고
    • The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron-sulfur cluster biogenesis
    • Pondarre C, Antiochos BB, Campagna DR, et al. The mitochondrial ATP-binding cassette transporter Abcb7 is essential in mice and participates in cytosolic iron-sulfur cluster biogenesis. Hum Mol Genet. 2006;15:953-964.
    • (2006) Hum Mol Genet , vol.15 , pp. 953-964
    • Pondarre, C.1    Antiochos, B.B.2    Campagna, D.R.3
  • 23
    • 0012756249 scopus 로고    scopus 로고
    • RNA interference in mammalian cells using siRNAs synthesized with T7 RNA polymerase
    • Donze O, Picard D. RNA interference in mammalian cells using siRNAs synthesized with T7 RNA polymerase. Nucleic Acids Res. 2002;30:e46.
    • (2002) Nucleic Acids Res , vol.30
    • Donze, O.1    Picard, D.2
  • 24
    • 1542373640 scopus 로고    scopus 로고
    • Analysis of the biologic functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNAs: Evidence for a proliferative role of L-ferritin
    • Cozzi A, Corsi B, Levi S, Santambrogio P, Biasiotto G, Arosio P. Analysis of the biologic functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNAs: evidence for a proliferative role of L-ferritin. Blood. 2004;103:2377-2383.
    • (2004) Blood , vol.103 , pp. 2377-2383
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Biasiotto, G.5    Arosio, P.6
  • 25
    • 0037151089 scopus 로고    scopus 로고
    • Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism
    • Corsi B, Cozzi A, Arosio P, et al. Human mitochondrial ferritin expressed in HeLa cells incorporates iron and affects cellular iron metabolism. J Biol Chem. 2002;277:22430-22437.
    • (2002) J Biol Chem , vol.277 , pp. 22430-22437
    • Corsi, B.1    Cozzi, A.2    Arosio, P.3
  • 26
    • 0034327415 scopus 로고    scopus 로고
    • A novel frameshift mutation of the mtDNA COIII gene leads to impaired assembly of cytochrome c oxidase in a patient affected by Leigh-like syndrome
    • Tiranti V, Corona P, Greco M, et al. A novel frameshift mutation of the mtDNA COIII gene leads to impaired assembly of cytochrome c oxidase in a patient affected by Leigh-like syndrome. Hum Mol Genet. 2000;9:2733-2742.
    • (2000) Hum Mol Genet , vol.9 , pp. 2733-2742
    • Tiranti, V.1    Corona, P.2    Greco, M.3
  • 27
    • 0024429683 scopus 로고
    • Development of an immunoassay for all human isoferritins, and its application to serum ferritin evaluation
    • Cozzi A, Levi S, Bazzigaluppi E, Ruggeri G, Arosio P. Development of an immunoassay for all human isoferritins, and its application to serum ferritin evaluation. Clin Chim Acta. 1989;184:197-206.
    • (1989) Clin Chim Acta , vol.184 , pp. 197-206
    • Cozzi, A.1    Levi, S.2    Bazzigaluppi, E.3    Ruggeri, G.4    Arosio, P.5
  • 28
    • 0033529554 scopus 로고    scopus 로고
    • Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase
    • Branda SS, Cavadini P, Adamec J, Kalousek F, Taroni F, Isaya G. Yeast and human frataxin are processed to mature form in two sequential steps by the mitochondrial processing peptidase. J Biol Chem. 1999;274:2763-2769.
    • (1999) J Biol Chem , vol.274 , pp. 2763-2769
    • Branda, S.S.1    Cavadini, P.2    Adamec, J.3    Kalousek, F.4    Taroni, F.5    Isaya, G.6
  • 29
    • 0028075773 scopus 로고
    • Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs
    • Gardner PR, Nguyen DD, White CW. Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs. Proc Natl Acad Sci U S A. 1994;91:12248-12252.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 12248-12252
    • Gardner, P.R.1    Nguyen, D.D.2    White, C.W.3
  • 30
    • 0018337607 scopus 로고
    • Assay of citric acid cycle intermediates and related compounds-update with tissue metabolite levels and intracellular distribution
    • Williamson JR, Corkey BE. Assay of citric acid cycle intermediates and related compounds-update with tissue metabolite levels and intracellular distribution. Methods Enzymol. 1979;55:200-222.
    • (1979) Methods Enzymol , vol.55 , pp. 200-222
    • Williamson, J.R.1    Corkey, B.E.2
  • 31
    • 0027254848 scopus 로고
    • Assay of succinate dehydrogenase activity by a colorimetric-continuous method using iodonitrotetrazolium chloride as electron acceptor
    • Munujos P, Coll-Canti J, Gonzalez-Sastre F, Gella FJ. Assay of succinate dehydrogenase activity by a colorimetric-continuous method using iodonitrotetrazolium chloride as electron acceptor. Anal Biochem. 1993;212:506-509.
    • (1993) Anal Biochem , vol.212 , pp. 506-509
    • Munujos, P.1    Coll-Canti, J.2    Gonzalez-Sastre, F.3    Gella, F.J.4
  • 32
    • 0027359173 scopus 로고
    • Expression of manganese superoxide dismutase is not altered in transgenic mice with elevated level of copper-zinc superoxide dismutase
    • White CW, Nguyen DH, Suzuki K, et al. Expression of manganese superoxide dismutase is not altered in transgenic mice with elevated level of copper-zinc superoxide dismutase. Free Radic Biol Med. 1993;5:629-636.
    • (1993) Free Radic Biol Med , vol.5 , pp. 629-636
    • White, C.W.1    Nguyen, D.H.2    Suzuki, K.3
  • 33
    • 0035839306 scopus 로고    scopus 로고
    • Evaluation of protoporphyrin IX production, phototoxicity and cell death pathway induced by hexylester of 5-aminolevulinic acid in Reh and HPB-ALL cells
    • Luksiene Z, Eggen I, Moan J, Nesland JM, Peng Q. Evaluation of protoporphyrin IX production, phototoxicity and cell death pathway induced by hexylester of 5-aminolevulinic acid in Reh and HPB-ALL cells. Cancer Lett. 2001;169:33-39.
    • (2001) Cancer Lett , vol.169 , pp. 33-39
    • Luksiene, Z.1    Eggen, I.2    Moan, J.3    Nesland, J.M.4    Peng, Q.5
  • 34
    • 0001853405 scopus 로고    scopus 로고
    • The role of the mitochondrion in cellular iron homeostasis
    • Schueck ND, Woontner M, Koeller DM. The role of the mitochondrion in cellular iron homeostasis. Mitochondrion. 2001;1:51-60.
    • (2001) Mitochondrion , vol.1 , pp. 51-60
    • Schueck, N.D.1    Woontner, M.2    Koeller, D.M.3
  • 35
    • 0035816608 scopus 로고    scopus 로고
    • A human mitochondrial ferritin encoded by an intronless gene
    • Levi S, Corsi B, Bosisio M, et al. A human mitochondrial ferritin encoded by an intronless gene. J Biol Chem. 2001;276:24437-24440.
    • (2001) J Biol Chem , vol.276 , pp. 24437-24440
    • Levi, S.1    Corsi, B.2    Bosisio, M.3
  • 36
    • 14944358625 scopus 로고    scopus 로고
    • Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis
    • Nie G, Sheftel AD, Kim SF, Ponka P. Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis. Blood. 2005;105:2161-2167.
    • (2005) Blood , vol.105 , pp. 2161-2167
    • Nie, G.1    Sheftel, A.D.2    Kim, S.F.3    Ponka, P.4
  • 37
    • 33646155960 scopus 로고    scopus 로고
    • The effects of mitochondrial iron homeostasis on cofactor specificity of superoxide dismutase 2
    • Yang M, Cobine PA, Molik S, et al. The effects of mitochondrial iron homeostasis on cofactor specificity of superoxide dismutase 2. EMBO J. 2006;25:1775-1783.
    • (2006) EMBO J , vol.25 , pp. 1775-1783
    • Yang, M.1    Cobine, P.A.2    Molik, S.3
  • 38
    • 0034329310 scopus 로고    scopus 로고
    • Human ABC7 transporter: Gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation
    • Bekri S, Kispal G, Lange H, et al. Human ABC7 transporter: gene structure and mutation causing X-linked sideroblastic anemia with ataxia with disruption of cytosolic iron-sulfur protein maturation. Blood. 2000;96:3256-3264.
    • (2000) Blood , vol.96 , pp. 3256-3264
    • Bekri, S.1    Kispal, G.2    Lange, H.3
  • 39
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: Evidence for a function of frataxin
    • Stehling O, Elsasser HP, Bruckel B, Muhlenhoff U, Lill R. Iron-sulfur protein maturation in human cells: evidence for a function of frataxin. Hum Mol Genet. 2004;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
  • 40
    • 0028855545 scopus 로고
    • An ABC transporter in the mitochondrial inner membrane is required for normal growth of yeast
    • Leighton J, Schatz G. An ABC transporter in the mitochondrial inner membrane is required for normal growth of yeast. EMBO J. 1995;14:188-195.
    • (1995) EMBO J , vol.14 , pp. 188-195
    • Leighton, J.1    Schatz, G.2
  • 41
    • 33749530252 scopus 로고    scopus 로고
    • Identification of a mammalian mitochondrial porphyrin transporter
    • Krishnamurthy PC, Du G, Fukuda Y, et al. Identification of a mammalian mitochondrial porphyrin transporter. Nature. 2006;443:586-589.
    • (2006) Nature , vol.443 , pp. 586-589
    • Krishnamurthy, P.C.1    Du, G.2    Fukuda, Y.3
  • 43
    • 0021926630 scopus 로고
    • Hereditary sideroblastic anaemia and ataxia: An X linked recessive disorder
    • Pagon RA, Bird TD, Detter JC, Pierce I. Hereditary sideroblastic anaemia and ataxia: an X linked recessive disorder. J Med Genet. 1985;22:267-273.
    • (1985) J Med Genet , vol.22 , pp. 267-273
    • Pagon, R.A.1    Bird, T.D.2    Detter, J.C.3    Pierce, I.4
  • 45
    • 0035672913 scopus 로고    scopus 로고
    • X-linked cerebellar ataxia and sideroblastic anaemia associated with a missense mutation in the ABC7 gene predicting V411L
    • Maguire A, Hellier K, Hammans S, May A. X-linked cerebellar ataxia and sideroblastic anaemia associated with a missense mutation in the ABC7 gene predicting V411L. Br J Haematol. 2001;115:910-917.
    • (2001) Br J Haematol , vol.115 , pp. 910-917
    • Maguire, A.1    Hellier, K.2    Hammans, S.3    May, A.4
  • 46
    • 0032489060 scopus 로고    scopus 로고
    • Formation of zinc protoporphyrin in cultured hepatocytes: Effects of ferrochelatase inhibition, iron chelation or lead
    • Jacobs JM, Sinclair PR, Sinclair JF, et al. Formation of zinc protoporphyrin in cultured hepatocytes: effects of ferrochelatase inhibition, iron chelation or lead. Toxicology. 1998;125:95-105.
    • (1998) Toxicology , vol.125 , pp. 95-105
    • Jacobs, J.M.1    Sinclair, P.R.2    Sinclair, J.F.3
  • 47
    • 23944500052 scopus 로고    scopus 로고
    • Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis
    • Wingert RA, Galloway JL, Barut B, et al. Deficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis. Nature. 2005;436:1035-1039.
    • (2005) Nature , vol.436 , pp. 1035-1039
    • Wingert, R.A.1    Galloway, J.L.2    Barut, B.3
  • 48
    • 23044503950 scopus 로고    scopus 로고
    • Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2
    • Cooperman SS, Meyron-Holtz EG, Olivierre-Wilson H, Ghosh MC, McConnell JP, Rouault TA. Microcytic anemia, erythropoietic protoporphyria, and neurodegeneration in mice with targeted deletion of iron-regulatory protein 2. Blood. 2005;106:1084-1091.
    • (2005) Blood , vol.106 , pp. 1084-1091
    • Cooperman, S.S.1    Meyron-Holtz, E.G.2    Olivierre-Wilson, H.3    Ghosh, M.C.4    McConnell, J.P.5    Rouault, T.A.6
  • 49
    • 0037372442 scopus 로고    scopus 로고
    • Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia
    • Cazzola M, Invernizzi R, Bergamaschi G, et al. Mitochondrial ferritin expression in erythroid cells from patients with sideroblastic anemia. Blood. 2003;101:1996-2000.
    • (2003) Blood , vol.101 , pp. 1996-2000
    • Cazzola, M.1    Invernizzi, R.2    Bergamaschi, G.3
  • 50
    • 22044434111 scopus 로고    scopus 로고
    • Aberrant mitochondrial iron distribution and maturation arrest characterize early erythroid precursors in low-risk myelodysplastic syndromes
    • Tehranchi R, Invernizzi R, Grandine A, et al. Aberrant mitochondrial iron distribution and maturation arrest characterize early erythroid precursors in low-risk myelodysplastic syndromes. Blood. 2005;106:247-253.
    • (2005) Blood , vol.106 , pp. 247-253
    • Tehranchi, R.1    Invernizzi, R.2    Grandine, A.3
  • 51
    • 33646480514 scopus 로고    scopus 로고
    • Flow cytometry evaluation of erythroid dysplasia in patients with myelodysplastic syndrome
    • Della Porta MG, Malcovati L, Invernizzi R, et al. Flow cytometry evaluation of erythroid dysplasia in patients with myelodysplastic syndrome. Leukemia. 2006;20:549-555.
    • (2006) Leukemia , vol.20 , pp. 549-555
    • Della Porta, M.G.1    Malcovati, L.2    Invernizzi, R.3
  • 52
    • 33646754660 scopus 로고    scopus 로고
    • Transgenic rescue of erythroid 5-aminolevulinate synthase-deficient mice results in the formation of ring sideroblasts and siderocytes
    • Nakajima O, Okano S, Harada H, et al. Transgenic rescue of erythroid 5-aminolevulinate synthase-deficient mice results in the formation of ring sideroblasts and siderocytes. Genes Cells. 2006;11:685-700.
    • (2006) Genes Cells , vol.11 , pp. 685-700
    • Nakajima, O.1    Okano, S.2    Harada, H.3
  • 53
    • 0028109484 scopus 로고
    • Multiple deletions of mtDNA in two brothers with sideroblastic anemia and mitochondrial myopathy and in their asymptomatic mother
    • Casademont J, Barrientos A, Cardellach F, et al. Multiple deletions of mtDNA in two brothers with sideroblastic anemia and mitochondrial myopathy and in their asymptomatic mother. Hum Mol Genet. 1994;3:1945-1949.
    • (1994) Hum Mol Genet , vol.3 , pp. 1945-1949
    • Casademont, J.1    Barrientos, A.2    Cardellach, F.3
  • 54
    • 1442308549 scopus 로고    scopus 로고
    • Mitochondrial myopathy and sideroblastic anemia
    • Casas KA, Fischel-Ghodsian N. Mitochondrial myopathy and sideroblastic anemia. Am J Med Genet A. 2004;125:201-204.
    • (2004) Am J Med Genet A , vol.125 , pp. 201-204
    • Casas, K.A.1    Fischel-Ghodsian, N.2
  • 55
    • 0035868772 scopus 로고    scopus 로고
    • A mutation in a mitochondrial transmembrane protein is responsible for the pleiotropic hematological and skeletal phenotype of flexed-tail (f/f) mice
    • Fleming MD, Campagna DR, Haslett JN, Trenor CC III, Andrews NC. A mutation in a mitochondrial transmembrane protein is responsible for the pleiotropic hematological and skeletal phenotype of flexed-tail (f/f) mice. Genes Dev. 2001;15:652-657.
    • (2001) Genes Dev , vol.15 , pp. 652-657
    • Fleming, M.D.1    Campagna, D.R.2    Haslett, J.N.3    Trenor III, C.C.4    Andrews, N.C.5
  • 56
    • 4944225788 scopus 로고    scopus 로고
    • SOD2-deficiency anemia: Protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness
    • Friedman JS, Lopez MF, Fleming MD, et al. SOD2-deficiency anemia: protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness. Blood. 2004;104:2565-2573.
    • (2004) Blood , vol.104 , pp. 2565-2573
    • Friedman, J.S.1    Lopez, M.F.2    Fleming, M.D.3
  • 57
    • 34147171967 scopus 로고    scopus 로고
    • Steensma DP, Hecksel KA, Porcher JC, Lasho TL. Candidate gene mutation analysis in idiopathic acquired sideroblastic anemia (refractory anemia with ringed sideroblasts). Leuk Res. Prepublished on July 24, 2006, as DOI 10.1016/j.leukres.2006.06.005.
    • Steensma DP, Hecksel KA, Porcher JC, Lasho TL. Candidate gene mutation analysis in idiopathic acquired sideroblastic anemia (refractory anemia with ringed sideroblasts). Leuk Res. Prepublished on July 24, 2006, as DOI 10.1016/j.leukres.2006.06.005.
  • 58
    • 0344393012 scopus 로고    scopus 로고
    • Unraveling the Hallervorden-Spatz syndrome: Pantothenate kinase-associated neurodegeneration is the name
    • Hayflick SJ. Unraveling the Hallervorden-Spatz syndrome: pantothenate kinase-associated neurodegeneration is the name. Curr Opin Pediatr. 2003;15:572-577.
    • (2003) Curr Opin Pediatr , vol.15 , pp. 572-577
    • Hayflick, S.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.