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Volumn 1853, Issue 5, 2015, Pages 1130-1144

Cellular iron uptake, trafficking and metabolism: Key molecules and mechanisms and their roles in disease

Author keywords

Iron metabolism; Iron uptake; ISC biogenesis; Mitochondrion; Transferrin

Indexed keywords

CHAPERONE; FRATAXIN; HEAT SHOCK PROTEIN 20; HEAT SHOCK PROTEIN 70; IRON; IRON SULFUR CLUSTER; SULFUR; UNCLASSIFIED DRUG; IRON SULFUR PROTEIN;

EID: 84923547839     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2015.01.021     Document Type: Review
Times cited : (300)

References (149)
  • 1
    • 50949102412 scopus 로고    scopus 로고
    • Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network
    • Muckenthaler M.U., Galy B., Hentze M.W. Systemic iron homeostasis and the iron-responsive element/iron-regulatory protein (IRE/IRP) regulatory network. Annu. Rev. Nutr. 2008, 28:197-213.
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 197-213
    • Muckenthaler, M.U.1    Galy, B.2    Hentze, M.W.3
  • 2
    • 84877741258 scopus 로고    scopus 로고
    • Mammalian iron homeostasis in health and disease: uptake, storage, transport, and molecular mechanisms of action
    • Lawen A., Lane D.J.R. Mammalian iron homeostasis in health and disease: uptake, storage, transport, and molecular mechanisms of action. Antioxid. Redox Signal. 2013, 18:2473-2507.
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 2473-2507
    • Lawen, A.1    Lane, D.J.R.2
  • 4
    • 84881484318 scopus 로고    scopus 로고
    • Out of balance-systemic iron homeostasis in iron-related disorders
    • Steinbicker A.U., Muckenthaler M.U. Out of balance-systemic iron homeostasis in iron-related disorders. Nutrients 2013, 5:3034-3061.
    • (2013) Nutrients , vol.5 , pp. 3034-3061
    • Steinbicker, A.U.1    Muckenthaler, M.U.2
  • 5
    • 77953810574 scopus 로고    scopus 로고
    • Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage
    • Arosio P., Levi S. Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage. Biochim. Biophys. Acta 2010, 1800:783-792.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 783-792
    • Arosio, P.1    Levi, S.2
  • 6
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • Lill R. Function and biogenesis of iron-sulphur proteins. Nature 2009, 460:831-838.
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 7
    • 84858015433 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease
    • Rouault T.A. Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease. Dis. Model. Mech. 2012, 5:155-164.
    • (2012) Dis. Model. Mech. , vol.5 , pp. 155-164
    • Rouault, T.A.1
  • 8
    • 84904741541 scopus 로고    scopus 로고
    • Special delivery: distributing iron in the cytosol of mammalian cells
    • Philpott C.C., Ryu M.S. Special delivery: distributing iron in the cytosol of mammalian cells. Front. Pharmacol. 2014, 5:173.
    • (2014) Front. Pharmacol. , vol.5 , pp. 173
    • Philpott, C.C.1    Ryu, M.S.2
  • 9
    • 84859956110 scopus 로고    scopus 로고
    • Coming into view: eukaryotic iron chaperones and intracellular iron delivery
    • Philpott C.C. Coming into view: eukaryotic iron chaperones and intracellular iron delivery. J. Biol. Chem. 2012, 287:13518-13523.
    • (2012) J. Biol. Chem. , vol.287 , pp. 13518-13523
    • Philpott, C.C.1
  • 10
    • 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., Kuhn L.C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:8175-8182.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 11
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • Richardson D.R., Ponka P. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta 1997, 1331:1-40.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 12
    • 77954249308 scopus 로고    scopus 로고
    • Two to tango: regulation of mammalian iron metabolism
    • Hentze M.W., Muckenthaler M.U., Galy B., Camaschella C. Two to tango: regulation of mammalian iron metabolism. Cell 2010, 142:24-38.
    • (2010) Cell , vol.142 , pp. 24-38
    • Hentze, M.W.1    Muckenthaler, M.U.2    Galy, B.3    Camaschella, C.4
  • 14
    • 84906092681 scopus 로고    scopus 로고
    • The active role of vitamin C in mammalian iron metabolism: much more than just enhanced iron absorption!
    • Lane D.J., Richardson D.R. The active role of vitamin C in mammalian iron metabolism: much more than just enhanced iron absorption!. Free Radic. Biol. Med. 2014, 75C:69-83.
    • (2014) Free Radic. Biol. Med. , vol.75 C , pp. 69-83
    • Lane, D.J.1    Richardson, D.R.2
  • 15
    • 45149113881 scopus 로고    scopus 로고
    • Non-transferrin iron reduction and uptake are regulated by transmembrane ascorbate cycling in K562 cells
    • Lane D.J.R., Lawen A. Non-transferrin iron reduction and uptake are regulated by transmembrane ascorbate cycling in K562 cells. J. Biol. Chem. 2008, 283:12701-12708.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12701-12708
    • Lane, D.J.R.1    Lawen, A.2
  • 16
    • 84874244468 scopus 로고    scopus 로고
    • The glutamate aspartate transporter (GLAST) mediates l-glutamate-stimulated ascorbate-release via swelling-activated anion channels in cultured neonatal rodent astrocytes
    • Lane D.J.R., Lawen A. The glutamate aspartate transporter (GLAST) mediates l-glutamate-stimulated ascorbate-release via swelling-activated anion channels in cultured neonatal rodent astrocytes. Cell Biochem. Biophys. 2012, 65:107-119.
    • (2012) Cell Biochem. Biophys. , vol.65 , pp. 107-119
    • Lane, D.J.R.1    Lawen, A.2
  • 17
    • 78649734938 scopus 로고    scopus 로고
    • Two routes of iron accumulation in astrocytes: ascorbate-dependent ferrous iron uptake via the divalent metal transporter (DMT1) plus an independent route for ferric iron
    • Lane D.J.R., Robinson S.R., Czerwinska H., Bishop G.M., Lawen A. Two routes of iron accumulation in astrocytes: ascorbate-dependent ferrous iron uptake via the divalent metal transporter (DMT1) plus an independent route for ferric iron. Biochem. J. 2010, 432:123-132.
    • (2010) Biochem. J. , vol.432 , pp. 123-132
    • Lane, D.J.R.1    Robinson, S.R.2    Czerwinska, H.3    Bishop, G.M.4    Lawen, A.5
  • 19
    • 84864923612 scopus 로고    scopus 로고
    • Physiologic implications of metal-ion transport by ZIP14 and ZIP8
    • Jenkitkasemwong S., Wang C.Y., Mackenzie B., Knutson M.D. Physiologic implications of metal-ion transport by ZIP14 and ZIP8. Biometals 2012, 25:643-655.
    • (2012) Biometals , vol.25 , pp. 643-655
    • Jenkitkasemwong, S.1    Wang, C.Y.2    Mackenzie, B.3    Knutson, M.D.4
  • 21
    • 84880031116 scopus 로고    scopus 로고
    • Transferrin iron uptake is stimulated by ascorbate via an intracellular reductive mechanism
    • Lane D.J.R., Chikhani S., Richardson V., Richardson D.R. Transferrin iron uptake is stimulated by ascorbate via an intracellular reductive mechanism. Biochim. Biophys. Acta 2013, 1833:1527-1541.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 1527-1541
    • Lane, D.J.R.1    Chikhani, S.2    Richardson, V.3    Richardson, D.R.4
  • 22
    • 0026623265 scopus 로고
    • Effect of ascorbate in the reduction of transferrin-associated iron in endocytic vesicles
    • Escobar A., Gaete V., Nunez M.T. Effect of ascorbate in the reduction of transferrin-associated iron in endocytic vesicles. J. Bioenerg. Biomembr. 1992, 24:227-233.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 227-233
    • Escobar, A.1    Gaete, V.2    Nunez, M.T.3
  • 23
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1996, 1275:161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 24
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: an efficient means of iron storage
    • Chasteen N.D., Harrison P.M. Mineralization in ferritin: an efficient means of iron storage. J. Struct. Biol. 1999, 126:182-194.
    • (1999) J. Struct. Biol. , vol.126 , pp. 182-194
    • Chasteen, N.D.1    Harrison, P.M.2
  • 25
    • 73349099034 scopus 로고    scopus 로고
    • Specific iron chelators determine the route of ferritin degradation
    • De Domenico I., Ward D.M., Kaplan J. Specific iron chelators determine the route of ferritin degradation. Blood 2009, 114:4546-4551.
    • (2009) Blood , vol.114 , pp. 4546-4551
    • De Domenico, I.1    Ward, D.M.2    Kaplan, J.3
  • 26
    • 84899746695 scopus 로고    scopus 로고
    • Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy
    • Mancias J.D., Wang X., Gygi S.P., Harper J.W., Kimmelman A.C. Quantitative proteomics identifies NCOA4 as the cargo receptor mediating ferritinophagy. Nature 2014, 509:105-109.
    • (2014) Nature , vol.509 , pp. 105-109
    • Mancias, J.D.1    Wang, X.2    Gygi, S.P.3    Harper, J.W.4    Kimmelman, A.C.5
  • 28
    • 84907835250 scopus 로고    scopus 로고
    • Lysosome-related organelles as mediators of metal homeostasis
    • Blaby-Haas C.E., Merchant S.S. Lysosome-related organelles as mediators of metal homeostasis. J. Biol. Chem. 2014, 289:28129-28136.
    • (2014) J. Biol. Chem. , vol.289 , pp. 28129-28136
    • Blaby-Haas, C.E.1    Merchant, S.S.2
  • 29
    • 34347375300 scopus 로고    scopus 로고
    • Direct interorganellar transfer of iron from endosome to mitochondrion
    • Sheftel A.D., Zhang A.S., Brown C., Shirihai O.S., Ponka P. Direct interorganellar transfer of iron from endosome to mitochondrion. Blood 2007, 110:125-132.
    • (2007) Blood , vol.110 , pp. 125-132
    • Sheftel, A.D.1    Zhang, A.S.2    Brown, C.3    Shirihai, O.S.4    Ponka, P.5
  • 30
    • 0032557816 scopus 로고    scopus 로고
    • Iron transport in K562 cells: a kinetic study using native gel electrophoresis and 59Fe autoradiography
    • Vyoral D., Petrak J. Iron transport in K562 cells: a kinetic study using native gel electrophoresis and 59Fe autoradiography. Biochim. Biophys. Acta 1998, 1403:179-188.
    • (1998) Biochim. Biophys. Acta , vol.1403 , pp. 179-188
    • Vyoral, D.1    Petrak, J.2
  • 33
    • 84904693203 scopus 로고    scopus 로고
    • Chaperone protein involved in transmembrane transport of iron
    • Yanatori I., Yasui Y., Tabuchi M., Kishi F. Chaperone protein involved in transmembrane transport of iron. Biochem. J. 2014, 462:25-37.
    • (2014) Biochem. J. , vol.462 , pp. 25-37
    • Yanatori, I.1    Yasui, Y.2    Tabuchi, M.3    Kishi, F.4
  • 35
    • 45849123222 scopus 로고    scopus 로고
    • A cytosolic iron chaperone that delivers iron to ferritin
    • Shi H., Bencze K.Z., Stemmler T.L., Philpott C.C. A cytosolic iron chaperone that delivers iron to ferritin. Science 2008, 320:1207-1210.
    • (2008) Science , vol.320 , pp. 1207-1210
    • Shi, H.1    Bencze, K.Z.2    Stemmler, T.L.3    Philpott, C.C.4
  • 38
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • Rouault T.A. The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol. 2006, 2:406-414.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 406-414
    • Rouault, T.A.1
  • 39
    • 0028982262 scopus 로고
    • Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome
    • Guo B., Phillips J.D., Yu Y., Leibold E.A. Iron regulates the intracellular degradation of iron regulatory protein 2 by the proteasome. J. Biol. Chem. 1995, 270:21645-21651.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21645-21651
    • Guo, B.1    Phillips, J.D.2    Yu, Y.3    Leibold, E.A.4
  • 43
    • 75149190912 scopus 로고    scopus 로고
    • Iron homeostasis and its interaction with prolyl hydroxylases
    • Mole D.R. Iron homeostasis and its interaction with prolyl hydroxylases. Antioxid. Redox Signal. 2010, 12:445-458.
    • (2010) Antioxid. Redox Signal. , vol.12 , pp. 445-458
    • Mole, D.R.1
  • 45
    • 61349203895 scopus 로고    scopus 로고
    • The power plant of the cell is also a smithy: the emerging role of mitochondria in cellular iron homeostasis
    • Sheftel A.D., Lill R. The power plant of the cell is also a smithy: the emerging role of mitochondria in cellular iron homeostasis. Ann. Med. 2009, 41:82-99.
    • (2009) Ann. Med. , vol.41 , pp. 82-99
    • Sheftel, A.D.1    Lill, R.2
  • 47
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases
    • Lill R., Mühlenhoff U. Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem. 2008, 77:669-700.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Mühlenhoff, U.2
  • 48
    • 80155135813 scopus 로고    scopus 로고
    • Mitochondrial mayhem: the mitochondrion as a modulator of iron metabolism and its role in disease
    • Huang M.L., Lane D.J.R., Richardson D.R. Mitochondrial mayhem: the mitochondrion as a modulator of iron metabolism and its role in disease. Antioxid. Redox Signal. 2011, 15:3003-3019.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 3003-3019
    • Huang, M.L.1    Lane, D.J.R.2    Richardson, D.R.3
  • 49
  • 51
    • 0037025331 scopus 로고    scopus 로고
    • Deletion of the mitochondrial carrier genes MRS3 and MRS4 suppresses mitochondrial iron accumulation in a yeast frataxin-deficient strain
    • Foury F., Roganti T. Deletion of the mitochondrial carrier genes MRS3 and MRS4 suppresses mitochondrial iron accumulation in a yeast frataxin-deficient strain. J. Biol. Chem. 2002, 277:24475-24483.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24475-24483
    • Foury, F.1    Roganti, T.2
  • 53
    • 59449083869 scopus 로고    scopus 로고
    • Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2
    • Paradkar P.N., Zumbrennen K.B., Paw B.H., Ward D.M., Kaplan J. Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2. Mol. Cell. Biol. 2009, 29:1007-1016.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1007-1016
    • Paradkar, P.N.1    Zumbrennen, K.B.2    Paw, B.H.3    Ward, D.M.4    Kaplan, J.5
  • 56
    • 77956044833 scopus 로고    scopus 로고
    • Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis
    • Chen W., Dailey H.A., Paw B.H. Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis. Blood 2010, 116:628-630.
    • (2010) Blood , vol.116 , pp. 628-630
    • Chen, W.1    Dailey, H.A.2    Paw, B.H.3
  • 57
    • 0031028178 scopus 로고    scopus 로고
    • Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells
    • Ponka P. Tissue-specific regulation of iron metabolism and heme synthesis: distinct control mechanisms in erythroid cells. Blood 1997, 89:1-25.
    • (1997) Blood , vol.89 , pp. 1-25
    • Ponka, P.1
  • 58
    • 84865298912 scopus 로고    scopus 로고
    • Mitochondrial ABC transporters function: the role of ABCB10 (ABC-me) as a novel player in cellular handling of reactive oxygen species
    • Liesa M., Qiu W., Shirihai O.S. Mitochondrial ABC transporters function: the role of ABCB10 (ABC-me) as a novel player in cellular handling of reactive oxygen species. Biochim. Biophys. Acta 2012, 1823:1945-1957.
    • (2012) Biochim. Biophys. Acta , vol.1823 , pp. 1945-1957
    • Liesa, M.1    Qiu, W.2    Shirihai, O.S.3
  • 60
    • 56149121299 scopus 로고    scopus 로고
    • Translocation of iron from lysosomes into mitochondria is a key event during oxidative stress-induced hepatocellular injury
    • Uchiyama A., Kim J.S., Kon K., Jaeschke H., Ikejima K., Watanabe S., Lemasters J.J. Translocation of iron from lysosomes into mitochondria is a key event during oxidative stress-induced hepatocellular injury. Hepatology 2008, 48:1644-1654.
    • (2008) Hepatology , vol.48 , pp. 1644-1654
    • Uchiyama, A.1    Kim, J.S.2    Kon, K.3    Jaeschke, H.4    Ikejima, K.5    Watanabe, S.6    Lemasters, J.J.7
  • 61
    • 84872069315 scopus 로고    scopus 로고
    • Mitoferrin-2-dependent mitochondrial iron uptake sensitizes human head and neck squamous carcinoma cells to photodynamic therapy
    • Hung H.I., Schwartz J.M., Maldonado E.N., Lemasters J.J., Nieminen A.L. Mitoferrin-2-dependent mitochondrial iron uptake sensitizes human head and neck squamous carcinoma cells to photodynamic therapy. J. Biol. Chem. 2013, 288:677-686.
    • (2013) J. Biol. Chem. , vol.288 , pp. 677-686
    • Hung, H.I.1    Schwartz, J.M.2    Maldonado, E.N.3    Lemasters, J.J.4    Nieminen, A.L.5
  • 67
    • 84939946161 scopus 로고    scopus 로고
    • Assembly of Fe/S proteins in bacterial systems: Biochemistry of the bacterial ISC system
    • Blanc B., Gerez C., Ollagnier de Choudens S. Assembly of Fe/S proteins in bacterial systems: Biochemistry of the bacterial ISC system 2014, Biochim. Biophys, Acta. 10.1016/j.bbamcr.2014.12.009.
    • (2014) Biochim. Biophys, Acta
    • Blanc, B.1    Gerez, C.2    Ollagnier de Choudens, S.3
  • 68
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson D.C., Dean D.R., Smith A.D., Johnson M.K. Structure, function, and formation of biological iron-sulfur clusters. Annu. Rev. Biochem. 2005, 74:247-281.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 69
    • 47249142777 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis and human disease
    • Rouault T.A., Tong W.H. Iron-sulfur cluster biogenesis and human disease. Trends Genet. 2008, 24:398-407.
    • (2008) Trends Genet. , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.H.2
  • 70
    • 78651451160 scopus 로고    scopus 로고
    • Key players and their role during mitochondrial iron-sulfur cluster biosynthesis
    • Rawat S., Stemmler T.L. Key players and their role during mitochondrial iron-sulfur cluster biosynthesis. Chemistry 2011, 17:746-753.
    • (2011) Chemistry , vol.17 , pp. 746-753
    • Rawat, S.1    Stemmler, T.L.2
  • 71
    • 77953669993 scopus 로고    scopus 로고
    • Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease
    • Ye H., Rouault T.A. Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease. Biochemistry 2010, 49:4945-4956.
    • (2010) Biochemistry , vol.49 , pp. 4945-4956
    • Ye, H.1    Rouault, T.A.2
  • 72
    • 30444433568 scopus 로고    scopus 로고
    • The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria
    • Adam A.C., Bornhovd C., Prokisch H., Neupert W., Hell K. The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria. EMBO J. 2006, 25:174-183.
    • (2006) EMBO J. , vol.25 , pp. 174-183
    • Adam, A.C.1    Bornhovd, C.2    Prokisch, H.3    Neupert, W.4    Hell, K.5
  • 73
    • 84869029429 scopus 로고    scopus 로고
    • Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis
    • Pandey A., Golla R., Yoon H., Dancis A., Pain D. Persulfide formation on mitochondrial cysteine desulfurase: enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis. Biochem. J. 2012, 448:171-187.
    • (2012) Biochem. J. , vol.448 , pp. 171-187
    • Pandey, A.1    Golla, R.2    Yoon, H.3    Dancis, A.4    Pain, D.5
  • 75
    • 33644623262 scopus 로고    scopus 로고
    • Functions of mitochondrial ISCU and cytosolic ISCU in mammalian iron-sulfur cluster biogenesis and iron homeostasis
    • Tong W.H., Rouault T.A. 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
  • 76
    • 84855766784 scopus 로고    scopus 로고
    • Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis
    • Shi Y., Ghosh M., Kovtunovych G., Crooks D.R., Rouault T.A. Both human ferredoxins 1 and 2 and ferredoxin reductase are important for iron-sulfur cluster biogenesis. Biochim. Biophys. Acta. 2012, 1823:484-492.
    • (2012) Biochim. Biophys. Acta. , vol.1823 , pp. 484-492
    • Shi, Y.1    Ghosh, M.2    Kovtunovych, G.3    Crooks, D.R.4    Rouault, T.A.5
  • 78
    • 77956248535 scopus 로고    scopus 로고
    • Frataxin and mitochondrial FeS cluster biogenesis
    • Stemmler T.L., Lesuisse E., Pain D., Dancis A. Frataxin and mitochondrial FeS cluster biogenesis. J. Biol. Chem. 2010, 285:26737-26743.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26737-26743
    • Stemmler, T.L.1    Lesuisse, E.2    Pain, D.3    Dancis, A.4
  • 79
    • 33947272031 scopus 로고    scopus 로고
    • Acidic residues of yeast frataxin have an essential role in Fe-S cluster assembly
    • Foury F., Pastore A., Trincal M. Acidic residues of yeast frataxin have an essential role in Fe-S cluster assembly. EMBO Rep. 2007, 8:194-199.
    • (2007) EMBO Rep. , vol.8 , pp. 194-199
    • Foury, F.1    Pastore, A.2    Trincal, M.3
  • 80
    • 84880346984 scopus 로고    scopus 로고
    • Frataxin: a protein in search for a function
    • Pastore A., Puccio H. Frataxin: a protein in search for a function. J. Neurochem. 2013, 126:43-52.
    • (2013) J. Neurochem. , vol.126 , pp. 43-52
    • Pastore, A.1    Puccio, H.2
  • 81
    • 84891379841 scopus 로고    scopus 로고
    • Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly
    • Pandey A., Gordon D.M., Pain J., Stemmler T.L., Dancis A., Pain D. Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly. J. Biol. Chem. 2013, 288:36773-36786.
    • (2013) J. Biol. Chem. , vol.288 , pp. 36773-36786
    • Pandey, A.1    Gordon, D.M.2    Pain, J.3    Stemmler, T.L.4    Dancis, A.5    Pain, D.6
  • 82
    • 80051779168 scopus 로고    scopus 로고
    • Structure-function analysis of Friedreich's ataxia mutants reveals determinants of frataxin binding and activation of the Fe-S assembly complex
    • Bridwell-Rabb J., Winn A.M., Barondeau D.P. Structure-function analysis of Friedreich's ataxia mutants reveals determinants of frataxin binding and activation of the Fe-S assembly complex. Biochemistry 2011, 50:7265-7274.
    • (2011) Biochemistry , vol.50 , pp. 7265-7274
    • Bridwell-Rabb, J.1    Winn, A.M.2    Barondeau, D.P.3
  • 83
    • 79954430645 scopus 로고    scopus 로고
    • Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange
    • Qi W., Cowan J.A. Mechanism of glutaredoxin-ISU [2Fe-2S] cluster exchange. Chem. Commun. (Camb.) 2011, 47:4989-4991.
    • (2011) Chem. Commun. (Camb.) , vol.47 , pp. 4989-4991
    • Qi, W.1    Cowan, J.A.2
  • 85
    • 77956235790 scopus 로고    scopus 로고
    • Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation
    • Sharma A.K., Pallesen L.J., Spang R.J., Walden W.E. Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation. J. Biol. Chem. 2010, 285:26745-26751.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26745-26751
    • Sharma, A.K.1    Pallesen, L.J.2    Spang, R.J.3    Walden, W.E.4
  • 86
    • 21244445718 scopus 로고    scopus 로고
    • A disulfide relay system in the intermembrane space of mitochondria that mediates protein import
    • Mesecke N., Terziyska N., Kozany C., Baumann F., Neupert W., Hell K., Herrmann J.M. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell 2005, 121:1059-1069.
    • (2005) Cell , vol.121 , pp. 1059-1069
    • Mesecke, N.1    Terziyska, N.2    Kozany, C.3    Baumann, F.4    Neupert, W.5    Hell, K.6    Herrmann, J.M.7
  • 87
    • 84896278245 scopus 로고    scopus 로고
    • A structural model for glutathione-complexed iron-sulfur cluster as a substrate for ABCB7-type transporters
    • Qi W., Li J., Cowan J.A. A structural model for glutathione-complexed iron-sulfur cluster as a substrate for ABCB7-type transporters. Chem. Commun. (Camb) 2014, 50:3795-3798.
    • (2014) Chem. Commun. (Camb) , vol.50 , pp. 3795-3798
    • Qi, W.1    Li, J.2    Cowan, J.A.3
  • 90
    • 84930051032 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis in mammalian cells: new insights into the molecular mechanisms of cluster delivery
    • Maio N., Rouault T.A. Iron-sulfur cluster biogenesis in mammalian cells: new insights into the molecular mechanisms of cluster delivery. Biochim. Biophys. Acta 2014, 10.1016/j.bbamcr.2014.09.009.
    • (2014) Biochim. Biophys. Acta
    • Maio, N.1    Rouault, T.A.2
  • 92
    • 84897388919 scopus 로고    scopus 로고
    • Fixing frataxin: "ironing out" the metabolic defect in Friedreich's ataxia
    • Anzovino A., Lane D.J., Huang M.L., Richardson D.R. Fixing frataxin: "ironing out" the metabolic defect in Friedreich's ataxia. Br. J. Pharmacol. 2013, 171:2174-2190.
    • (2013) Br. J. Pharmacol. , vol.171 , pp. 2174-2190
    • Anzovino, A.1    Lane, D.J.2    Huang, M.L.3    Richardson, D.R.4
  • 95
    • 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., Koenig M. Studies of human, mouse and yeast homologues indicate a mitochondrial function for frataxin. Nat. Genet. 1997, 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
  • 97
    • 84880077900 scopus 로고    scopus 로고
    • Biochemistry of cardiomyopathy in the mitochondrial disease Friedreich's ataxia
    • Lane D.J.R., Huang M.L., Ting S., Sivagurunathan S., Richardson D.R. Biochemistry of cardiomyopathy in the mitochondrial disease Friedreich's ataxia. Biochem. J. 2013, 453:321-336.
    • (2013) Biochem. J. , vol.453 , pp. 321-336
    • Lane, D.J.R.1    Huang, M.L.2    Ting, S.3    Sivagurunathan, S.4    Richardson, D.R.5
  • 98
    • 62549093116 scopus 로고    scopus 로고
    • The pathogenesis of Friedreich ataxia and the structure and function of frataxin
    • Pandolfo M., Pastore A. The pathogenesis of Friedreich ataxia and the structure and function of frataxin. J. Neurol. 2009, 256(Suppl. 1):9-17.
    • (2009) J. Neurol. , vol.256 , pp. 9-17
    • Pandolfo, M.1    Pastore, A.2
  • 99
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • Yoon T., Cowan J.A. Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J. Am. Chem. Soc. 2003, 125:6078-6084.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 100
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • Yoon T., Cowan J.A. Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. J. Biol. Chem. 2004, 279:25943-25946.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 101
    • 45549107531 scopus 로고    scopus 로고
    • Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu
    • Wang T., Craig E.A. Binding of yeast frataxin to the scaffold for Fe-S cluster biogenesis, Isu. J. Biol. Chem. 2008, 283:12674-12679.
    • (2008) J. Biol. Chem. , vol.283 , pp. 12674-12679
    • Wang, T.1    Craig, E.A.2
  • 106
    • 78649644673 scopus 로고    scopus 로고
    • Normal and Friedreich ataxia cells express different isoforms of frataxin with complementary roles in iron-sulfur cluster assembly
    • Gakh O., Bedekovics T., Duncan S.F., Smith D.Y.T., Berkholz D.S., Isaya G. Normal and Friedreich ataxia cells express different isoforms of frataxin with complementary roles in iron-sulfur cluster assembly. J. Biol. Chem. 2010, 285:38486-38501.
    • (2010) J. Biol. Chem. , vol.285 , pp. 38486-38501
    • Gakh, O.1    Bedekovics, T.2    Duncan, S.F.3    Smith, D.Y.T.4    Berkholz, D.S.5    Isaya, G.6
  • 107
    • 78049305276 scopus 로고    scopus 로고
    • Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
    • Tsai C.L., Barondeau D.P. Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex. Biochemistry 2010, 49:9132-9139.
    • (2010) Biochemistry , vol.49 , pp. 9132-9139
    • Tsai, C.L.1    Barondeau, D.P.2
  • 108
    • 84905674436 scopus 로고    scopus 로고
    • Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry
    • Bridwell-Rabb J., Fox N.G., Tsai C.L., Winn A.M., Barondeau D.P. Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry. Biochemistry 2014, 53:4904-4913.
    • (2014) Biochemistry , vol.53 , pp. 4904-4913
    • Bridwell-Rabb, J.1    Fox, N.G.2    Tsai, C.L.3    Winn, A.M.4    Barondeau, D.P.5
  • 110
    • 84859178535 scopus 로고    scopus 로고
    • Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis
    • Bridwell-Rabb J., Iannuzzi C., Pastore A., Barondeau D.P. Effector role reversal during evolution: the case of frataxin in Fe-S cluster biosynthesis. Biochemistry 2012, 51:2506-2514.
    • (2012) Biochemistry , vol.51 , pp. 2506-2514
    • Bridwell-Rabb, J.1    Iannuzzi, C.2    Pastore, A.3    Barondeau, D.P.4
  • 111
    • 0037093206 scopus 로고    scopus 로고
    • Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization
    • Becker E.M., Greer J.M., Ponka P., Richardson D.R. Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterization of frataxin expression compared to molecules involved in iron metabolism and hemoglobinization. Blood 2002, 99:3813-3822.
    • (2002) Blood , vol.99 , pp. 3813-3822
    • Becker, E.M.1    Greer, J.M.2    Ponka, P.3    Richardson, D.R.4
  • 113
    • 34247124148 scopus 로고    scopus 로고
    • Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation
    • Vickery L.E., Cupp-Vickery J.R. Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Crit. Rev. Biochem. Mol. Biol. 2007, 42:95-111.
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 95-111
    • Vickery, L.E.1    Cupp-Vickery, J.R.2
  • 115
    • 84858212583 scopus 로고    scopus 로고
    • HSC20 interacts with frataxin and is involved in iron-sulfur cluster biogenesis and iron homeostasis
    • Shan Y., Cortopassi G. HSC20 interacts with frataxin and is involved in iron-sulfur cluster biogenesis and iron homeostasis. Hum. Mol. Genet. 2012, 21:1457-1469.
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1457-1469
    • Shan, Y.1    Cortopassi, G.2
  • 116
    • 84895735383 scopus 로고    scopus 로고
    • Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery
    • Maio N., Singh A., Uhrigshardt H., Saxena N., Tong W.H., Rouault T.A. Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery. Cell Metab. 2014, 19:445-457.
    • (2014) Cell Metab. , vol.19 , pp. 445-457
    • Maio, N.1    Singh, A.2    Uhrigshardt, H.3    Saxena, N.4    Tong, W.H.5    Rouault, T.A.6
  • 117
    • 84893202765 scopus 로고    scopus 로고
    • Mortalin - a multipotent chaperone regulating cellular processes ranging from viral infection to neurodegeneration
    • Flachbartova Z., Kovacech B. Mortalin - a multipotent chaperone regulating cellular processes ranging from viral infection to neurodegeneration. Acta Virol. 2013, 57:3-15.
    • (2013) Acta Virol. , vol.57 , pp. 3-15
    • Flachbartova, Z.1    Kovacech, B.2
  • 118
    • 0141533145 scopus 로고    scopus 로고
    • Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-chaperone
    • Sun G., Gargus J.J., Ta D.T., Vickery L.E. Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-chaperone. J. Hum. Genet. 2003, 48:415-419.
    • (2003) J. Hum. Genet. , vol.48 , pp. 415-419
    • Sun, G.1    Gargus, J.J.2    Ta, D.T.3    Vickery, L.E.4
  • 119
    • 77956513437 scopus 로고    scopus 로고
    • Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis
    • Uhrigshardt H., Singh A., Kovtunovych G., Ghosh M., Rouault T.A. Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis. Hum. Mol. Genet. 2010, 19:3816-3834.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 3816-3834
    • Uhrigshardt, H.1    Singh, A.2    Kovtunovych, G.3    Ghosh, M.4    Rouault, T.A.5
  • 121
    • 84884600998 scopus 로고    scopus 로고
    • The superfamily of mitochondrial Complex1_LYR motif-containing (LYRM) proteins
    • Angerer H. The superfamily of mitochondrial Complex1_LYR motif-containing (LYRM) proteins. Biochem. Soc. Trans. 2013, 41:1335-1341.
    • (2013) Biochem. Soc. Trans. , vol.41 , pp. 1335-1341
    • Angerer, H.1
  • 122
    • 68049086933 scopus 로고    scopus 로고
    • Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
    • Shi Y., Ghosh M.C., Tong W.H., Rouault T.A. Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis. Hum. Mol. Genet. 2009, 18:3014-3025.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3014-3025
    • Shi, Y.1    Ghosh, M.C.2    Tong, W.H.3    Rouault, T.A.4
  • 123
    • 84905860097 scopus 로고    scopus 로고
    • The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase
    • Na U., Yu W., Cox J., Bricker D.K., Brockmann K., Rutter J., Thummel C.S., Winge D.R. The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase. Cell Metab. 2014, 20:253-266.
    • (2014) Cell Metab. , vol.20 , pp. 253-266
    • Na, U.1    Yu, W.2    Cox, J.3    Bricker, D.K.4    Brockmann, K.5    Rutter, J.6    Thummel, C.S.7    Winge, D.R.8
  • 124
    • 80053601731 scopus 로고    scopus 로고
    • The LYR protein Mzm1 functions in the insertion of the Rieske Fe/S protein in yeast mitochondria
    • Atkinson A., Smith P., Fox J.L., Cui T.Z., Khalimonchuk O., Winge D.R. The LYR protein Mzm1 functions in the insertion of the Rieske Fe/S protein in yeast mitochondria. Mol. Cell. Biol. 2011, 31:3988-3996.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 3988-3996
    • Atkinson, A.1    Smith, P.2    Fox, J.L.3    Cui, T.Z.4    Khalimonchuk, O.5    Winge, D.R.6
  • 125
  • 127
    • 84861850380 scopus 로고    scopus 로고
    • Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis
    • Li H., Outten C.E. Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis. Biochemistry 2012, 51:4377-4389.
    • (2012) Biochemistry , vol.51 , pp. 4377-4389
    • Li, H.1    Outten, C.E.2
  • 130
    • 79952814526 scopus 로고    scopus 로고
    • Friedreich's ataxia: pathology, pathogenesis, and molecular genetics
    • Koeppen A.H. Friedreich's ataxia: pathology, pathogenesis, and molecular genetics. J. Neurol. Sci. 2011, 303:1-12.
    • (2011) J. Neurol. Sci. , vol.303 , pp. 1-12
    • Koeppen, A.H.1
  • 131
    • 47749130452 scopus 로고    scopus 로고
    • The MCK mouse heart model of Friedreich's ataxia: alterations in iron-regulated proteins and cardiac hypertrophy are limited by iron chelation
    • Whitnall M., Rahmanto Y.S., Sutak R., Xu X., Becker E.M., Mikhael M.R., Ponka P., Richardson D.R. The MCK mouse heart model of Friedreich's ataxia: alterations in iron-regulated proteins and cardiac hypertrophy are limited by iron chelation. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:9757-9762.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 9757-9762
    • Whitnall, M.1    Rahmanto, Y.S.2    Sutak, R.3    Xu, X.4    Becker, E.M.5    Mikhael, M.R.6    Ponka, P.7    Richardson, D.R.8
  • 132
    • 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., Koenig M. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet. 2001, 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
  • 133
    • 64249161639 scopus 로고    scopus 로고
    • Impaired nuclear Nrf2 translocation undermines the oxidative stress response in Friedreich ataxia
    • Paupe V., Dassa E.P., Goncalves S., Auchere F., Lonn M., Holmgren A., Rustin P. Impaired nuclear Nrf2 translocation undermines the oxidative stress response in Friedreich ataxia. PLoS One 2009, 4:e4253.
    • (2009) PLoS One , vol.4 , pp. e4253
    • Paupe, V.1    Dassa, E.P.2    Goncalves, S.3    Auchere, F.4    Lonn, M.5    Holmgren, A.6    Rustin, P.7
  • 136
    • 20444381360 scopus 로고    scopus 로고
    • Role of Nrf2 signaling in regulation of antioxidants and phase 2 enzymes in cardiac fibroblasts: protection against reactive oxygen and nitrogen species-induced cell injury
    • Zhu H., Itoh K., Yamamoto M., Zweier J.L., Li Y. Role of Nrf2 signaling in regulation of antioxidants and phase 2 enzymes in cardiac fibroblasts: protection against reactive oxygen and nitrogen species-induced cell injury. FEBS Lett. 2005, 579:3029-3036.
    • (2005) FEBS Lett. , vol.579 , pp. 3029-3036
    • Zhu, H.1    Itoh, K.2    Yamamoto, M.3    Zweier, J.L.4    Li, Y.5
  • 137
    • 84874111758 scopus 로고    scopus 로고
    • The Nrf2 cell defence pathway: Keap1-dependent and -independent mechanisms of regulation
    • Bryan H.K., Olayanju A., Goldring C.E., Park B.K. The Nrf2 cell defence pathway: Keap1-dependent and -independent mechanisms of regulation. Biochem. Pharmacol. 2013, 85:705-717.
    • (2013) Biochem. Pharmacol. , vol.85 , pp. 705-717
    • Bryan, H.K.1    Olayanju, A.2    Goldring, C.E.3    Park, B.K.4
  • 138
    • 21944452087 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-kappaB and AP-1
    • Yang H., Magilnick N., Lee C., Kalmaz D., Ou X., Chan J.Y., Lu S.C. Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via NF-kappaB and AP-1. Mol. Cell. Biol. 2005, 25:5933-5946.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5933-5946
    • Yang, H.1    Magilnick, N.2    Lee, C.3    Kalmaz, D.4    Ou, X.5    Chan, J.Y.6    Lu, S.C.7
  • 139
    • 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
  • 140
    • 34147158934 scopus 로고    scopus 로고
    • Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis
    • Pondarre C., Campagna D.R., Antiochos B., Sikorski L., Mulhern H., Fleming M.D. Abcb7, the gene responsible for X-linked sideroblastic anemia with ataxia, is essential for hematopoiesis. Blood 2007, 109:3567-3569.
    • (2007) Blood , vol.109 , pp. 3567-3569
    • Pondarre, C.1    Campagna, D.R.2    Antiochos, B.3    Sikorski, L.4    Mulhern, H.5    Fleming, M.D.6
  • 141
    • 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
  • 142
    • 77956044833 scopus 로고    scopus 로고
    • Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis
    • (blood -2009-2012-259614)
    • Chen W., Dailey H.A., Paw B.H. Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis. Blood 2010, (blood -2009-2012-259614).
    • (2010) Blood
    • Chen, W.1    Dailey, H.A.2    Paw, B.H.3
  • 144
  • 147
    • 77952480112 scopus 로고    scopus 로고
    • Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin
    • Condo I., Malisan F., Guccini I., Serio D., Rufini A., Testi R. Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin. Hum. Mol. Genet. 2010, 19:1221-1229.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 1221-1229
    • Condo, I.1    Malisan, F.2    Guccini, I.3    Serio, D.4    Rufini, A.5    Testi, R.6
  • 148
    • 84895748764 scopus 로고    scopus 로고
    • The lure of a LYR: the logistics of iron sulfur cluster delivery
    • Lane D.J., Merlot A.M., Richardson D.R. The lure of a LYR: the logistics of iron sulfur cluster delivery. Cell Metab. 2014, 19:348-350.
    • (2014) Cell Metab. , vol.19 , pp. 348-350
    • Lane, D.J.1    Merlot, A.M.2    Richardson, D.R.3


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