메뉴 건너뛰기




Volumn 5 MAY, Issue , 2014, Pages

Neurodegeneration with brain iron accumulation: Update on pathogenic mechanisms

Author keywords

Brain; Iron; NBIA disorders; Neurodegeneration; Oxidative stress; Pathogenesis

Indexed keywords

ADENOSINE TRIPHOSPHATASE (POTASSIUM); BETA PROPELLER PROTEIN; CERULOPLASMIN; FATTY ACID SYNTHASE; GENOMIC DNA; HYDROXYMETHYLGLUTARYL COENZYME A SYNTHASE; MEMBRANE PROTEIN; MITOCHONDRIAL MEMBRANE PROTEIN; PANTOTHENATE KINASE 2; PHOSPHOLIPASE; PHOSPHOLIPASE 2; PHOSPHOLIPASE A2; PROTEIN; UNCLASSIFIED DRUG;

EID: 84904622975     PISSN: None     EISSN: 16639812     Source Type: Journal    
DOI: 10.3389/fphar.2014.00099     Document Type: Review
Times cited : (137)

References (176)
  • 1
    • 80355129916 scopus 로고    scopus 로고
    • A pilot trial of deferiprone for neurodegeneration with brain iron accumulation
    • doi: 10.3324/haematol.2011.043018
    • Abbruzzese, G., Cossu, G., Balocco, M., Marchese, R., Murgia, D., Melis, M., et al. (2011). A pilot trial of deferiprone for neurodegeneration with brain iron accumulation. Haematologica 96, 1708-1711. doi: 10.3324/haematol.2011.043018
    • (2011) Haematologica , vol.96 , pp. 1708-1711
    • Abbruzzese, G.1    Cossu, G.2    Balocco, M.3    Marchese, R.4    Murgia, D.5    Melis, M.6
  • 2
    • 0028175958 scopus 로고
    • Ca(2+)-independent cytosolic phospholipase A2 from macrophage-like P388D1 cells Isolation and characterization.
    • Ackermann, E. J., Kempner, E. S., and Dennis, E. A. (1994). Ca(2+)-independent cytosolic phospholipase A2 from macrophage-like P388D1 cells. Isolation and characterization. J. Biol. Chem. 269, 9227-9233.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9227-9233
    • Ackermann, E.J.1    Kempner, E.S.2    Dennis, E.A.3
  • 3
    • 0035100102 scopus 로고    scopus 로고
    • fumble encodes a pantothenate kinase homolog required for proper mitosis and meiosis in Drosophila melanogaster
    • Afshar, K., Gönczy, P., DiNardo, S., and Wasserman, S. A. (2001). fumble encodes a pantothenate kinase homolog required for proper mitosis and meiosis in Drosophila melanogaster. Genetics 157, 1267-1276.
    • (2001) Genetics , vol.157 , pp. 1267-1276
    • Afshar, K.1    Gönczy, P.2    DiNardo, S.3    Wasserman, S.A.4
  • 4
    • 84869006206 scopus 로고    scopus 로고
    • Compartmentalization of mammalian pantothenate kinases
    • doi: 10.1371/journal.pone.0049509
    • Alfonso-Pecchio, A., Garcia, M., Leonardi, R., and Jackowski, S. (2012). Compartmentalization of mammalian pantothenate kinases. PLoS ONE 7:e49509. doi: 10.1371/journal.pone.0049509
    • (2012) PLoS ONE , vol.7
    • Alfonso-Pecchio, A.1    Garcia, M.2    Leonardi, R.3    Jackowski, S.4
  • 5
    • 84889100159 scopus 로고    scopus 로고
    • Loss of iron triggers PINK1/Parkin-independent mitophagy
    • doi: 10.1038/embor.2013.168
    • Allen, G. F., Toth, R., James, J., and Ganley, I. G. (2013). Loss of iron triggers PINK1/Parkin-independent mitophagy. EMBO Rep. 14, 1127-1135. doi: 10.1038/embor.2013.168
    • (2013) EMBO Rep. , vol.14 , pp. 1127-1135
    • Allen, G.F.1    Toth, R.2    James, J.3    Ganley, I.G.4
  • 6
    • 77953810574 scopus 로고    scopus 로고
    • Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage
    • doi: 10.1016/j.bbagen.2010.02.005
    • Arosio, P., and Levi, S. (2010). Cytosolic and mitochondrial ferritins in the regulation of cellular iron homeostasis and oxidative damage. Biochim. Biophys. Acta 1800, 783-792. doi: 10.1016/j.bbagen.2010.02.005
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 783-792
    • Arosio, P.1    Levi, S.2
  • 7
    • 41549111075 scopus 로고    scopus 로고
    • Calcium-independent phospholipase A2 mediates proliferation of human promonocytic U937 cells
    • doi: 10.1111/j.1742-4658.2008.06350.x
    • Balboa, M. A., Pérez, R., and Balsinde, J. (2008). Calcium-independent phospholipase A2 mediates proliferation of human promonocytic U937 cells. FEBS J. 275, 1915-1924. doi: 10.1111/j.1742-4658.2008.06350.x
    • (2008) FEBS J. , vol.275 , pp. 1915-1924
    • Balboa, M.A.1    Pérez, R.2    Balsinde, J.3
  • 8
    • 0037201952 scopus 로고    scopus 로고
    • Expression and function of phospholipase A(2) in brain
    • doi: 10.1016/S0014-5793(02)03481-6
    • Balboa, M. A., Varela-Nieto, I., Killermann Lucas, K., and Dennis, E. A. (2002). Expression and function of phospholipase A(2) in brain. FEBS Lett. 531, 12-17. doi: 10.1016/S0014-5793(02)03481-6
    • (2002) FEBS Lett. , vol.531 , pp. 12-17
    • Balboa, M.A.1    Varela-Nieto, I.2    Killermann Lucas, K.3    Dennis, E.A.4
  • 9
    • 0031010112 scopus 로고    scopus 로고
    • Function and inhibition of intracellular calcium-independent phospholipase A2
    • doi: 10.1074/jbc.272.26.16069
    • Balsinde, J., and Dennis, E. A. (1997). Function and inhibition of intracellular calcium-independent phospholipase A2. J. Biol. Chem. 272, 16069-16072. doi: 10.1074/jbc.272.26.16069
    • (1997) J. Biol. Chem. , vol.272 , pp. 16069-16072
    • Balsinde, J.1    Dennis, E.A.2
  • 10
    • 4644235280 scopus 로고    scopus 로고
    • Male mice that do not express group VIA phospholipase A2 produce spermatozoa with impaired motility and have greatly reduced fertility
    • doi: 10.1074/jbc.M406489200
    • Bao, S., Miller, D. J., Ma, Z., Wohltmann, M., Eng, G., Ramanadham, S., et al. (2004). Male mice that do not express group VIA phospholipase A2 produce spermatozoa with impaired motility and have greatly reduced fertility. J. Biol. Chem. 279, 38194-38200. doi: 10.1074/jbc.M406489200
    • (2004) J. Biol. Chem. , vol.279 , pp. 38194-38200
    • Bao, S.1    Miller, D.J.2    Ma, Z.3    Wohltmann, M.4    Eng, G.5    Ramanadham, S.6
  • 11
    • 57649133953 scopus 로고    scopus 로고
    • Iron-mediated aggregation and a localized structural change characterize ferritin from a mutant light chain polypeptide that causes neurodegeneration
    • doi: 10.1074/jbc.M805532200
    • Baraibar, M. A., Barbeito, A. G., Muhoberac, B. B., and Vidal, R. (2008). Iron-mediated aggregation and a localized structural change characterize ferritin from a mutant light chain polypeptide that causes neurodegeneration. J. Biol. Chem. 283, 31679-31689. doi: 10.1074/jbc.M805532200
    • (2008) J. Biol. Chem. , vol.283 , pp. 31679-31689
    • Baraibar, M.A.1    Barbeito, A.G.2    Muhoberac, B.B.3    Vidal, R.4
  • 12
    • 84858971462 scopus 로고    scopus 로고
    • A mutant light-chain ferritin that causes neurodegeneration has enhanced propensity toward oxidative damage
    • doi: 10.1016/j.freeradbiomed.2012.02.015
    • Baraibar, M. A., Barbeito, A. G., Muhoberac, B. B., and Vidal, R. (2012). A mutant light-chain ferritin that causes neurodegeneration has enhanced propensity toward oxidative damage. Free Radic. Biol. Med. 52, 1692-1697. doi: 10.1016/j.freeradbiomed.2012.02.015
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 1692-1697
    • Baraibar, M.A.1    Barbeito, A.G.2    Muhoberac, B.B.3    Vidal, R.4
  • 13
    • 76249107256 scopus 로고    scopus 로고
    • Unraveling of the E-helices and disruption of 4-fold pores are associated with iron mishandling in a mutant ferritin causing neurodegeneration
    • doi: 10.1074/jbc.M109.042986
    • Baraibar, M. A., Muhoberac, B. B., Garringer, H. J., Hurley, T. D., and Vidal, R. (2010). Unraveling of the E-helices and disruption of 4-fold pores are associated with iron mishandling in a mutant ferritin causing neurodegeneration. J. Biol. Chem. 285, 1950-1956. doi: 10.1074/jbc.M109.042986
    • (2010) J. Biol. Chem. , vol.285 , pp. 1950-1956
    • Baraibar, M.A.1    Muhoberac, B.B.2    Garringer, H.J.3    Hurley, T.D.4    Vidal, R.5
  • 14
    • 65649154118 scopus 로고    scopus 로고
    • Abnormal iron metabolism and oxidative stress in mice expressing a mutant form of the ferritin light polypeptide gene
    • doi: 10.1111/j.1471-4159.2009.06028.x
    • Barbeito, A. G., Garringer, H. J., Baraibar, M. A., Gao, X., Arredondo, M., Nunez, M. T., et al. (2009). Abnormal iron metabolism and oxidative stress in mice expressing a mutant form of the ferritin light polypeptide gene. J. Neurochem. 109, 1067-1078. doi: 10.1111/j.1471-4159.2009.06028.x
    • (2009) J. Neurochem. , vol.109 , pp. 1067-1078
    • Barbeito, A.G.1    Garringer, H.J.2    Baraibar, M.A.3    Gao, X.4    Arredondo, M.5    Nunez, M.T.6
  • 15
    • 78149277684 scopus 로고    scopus 로고
    • Abnormal iron metabolism in fibroblasts from a patient with the neurodegenerative disease hereditary ferritinopathy
    • doi: 10.1186/1750-1326-5-50
    • Barbeito, A. G., Levade, T., Delisle, M. B., Ghetti, B., and Vidal, R. (2010). Abnormal iron metabolism in fibroblasts from a patient with the neurodegenerative disease hereditary ferritinopathy. Mol. Neurodegener. 5:50. doi: 10.1186/1750-1326-5-50
    • (2010) Mol. Neurodegener. , vol.5 , pp. 50
    • Barbeito, A.G.1    Levade, T.2    Delisle, M.B.3    Ghetti, B.4    Vidal, R.5
  • 16
    • 79961224923 scopus 로고    scopus 로고
    • Neuroaxonal dystrophy in calcium-independent phospholipase A2ß deficiency results from insufficient remodeling and degeneration of mitochondrial and presynaptic membranes
    • doi: 10.1523/JNEUROSCI.0345-11.2011
    • Beck, G., Sugiura, Y., Shinzawa, K., Kato, S., Setou, M., Tsujimoto, Y., et al. (2011). Neuroaxonal dystrophy in calcium-independent phospholipase A2ß deficiency results from insufficient remodeling and degeneration of mitochondrial and presynaptic membranes. J. Neurosci. 31, 11411-11420. doi: 10.1523/JNEUROSCI.0345-11.2011
    • (2011) J. Neurosci. , vol.31 , pp. 11411-11420
    • Beck, G.1    Sugiura, Y.2    Shinzawa, K.3    Kato, S.4    Setou, M.5    Tsujimoto, Y.6
  • 17
    • 77954237882 scopus 로고    scopus 로고
    • Network organization of the human autophagy system
    • doi: 10.1038/nature09204
    • Behrends, C., Sowa, M. E., Gygi, S. P., and Harper, J. W. (2010). Network organization of the human autophagy system. Nature 466, 68-76. doi: 10.1038/nature09204
    • (2010) Nature , vol.466 , pp. 68-76
    • Behrends, C.1    Sowa, M.E.2    Gygi, S.P.3    Harper, J.W.4
  • 18
    • 45749083772 scopus 로고    scopus 로고
    • De novo CoA biosynthesis is required to maintain DNA integrity during development of the Drosophila nervous system
    • doi: 10.1093/hmg/ddn105
    • Bosveld, F., Rana, A., van der Wouden, P. E., Lemstra, W., Ritsema, M., Kampinga, H. H., et al. (2008). De novo CoA biosynthesis is required to maintain DNA integrity during development of the Drosophila nervous system. Hum. Mol. Genet. 17, 2058-2069. doi: 10.1093/hmg/ddn105
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2058-2069
    • Bosveld, F.1    Rana, A.2    van der Wouden, P.E.3    Lemstra, W.4    Ritsema, M.5    Kampinga, H.H.6
  • 19
    • 84861723960 scopus 로고    scopus 로고
    • Mutation of the parkinsonism gene ATP13A2 causes neuronal ceroid-lipofuscinosis
    • doi: 10.1093/hmg/dds089
    • Bras, J., Verloes, A., Schneider, S. A., Mole, S. E., and Guerreiro, R. J. (2012). Mutation of the parkinsonism gene ATP13A2 causes neuronal ceroid-lipofuscinosis. Hum. Mol. Genet. 21, 2646-2650. doi: 10.1093/hmg/dds089
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2646-2650
    • Bras, J.1    Verloes, A.2    Schneider, S.A.3    Mole, S.E.4    Guerreiro, R.J.5
  • 20
    • 84857373097 scopus 로고    scopus 로고
    • Non-transferrin bound iron: a key role in iron overload and iron toxicity
    • doi: 10.1016/j.bbagen.2011.07.014
    • Brissot, P., Ropert, M., Le Lan, C., and Loreal, O. (2012). Non-transferrin bound iron: a key role in iron overload and iron toxicity. Biochim. Biophys. Acta 1820, 403-410. doi: 10.1016/j.bbagen.2011.07.014
    • (2012) Biochim. Biophys. Acta , vol.1820 , pp. 403-410
    • Brissot, P.1    Ropert, M.2    Le Lan, C.3    Loreal, O.4
  • 21
    • 84892734388 scopus 로고    scopus 로고
    • Pantethine treatment is effective in recovering the disease phenotype induced by ketogenic diet in a pantothenate kinase-associated neurodegeneration mouse model
    • doi: 10.1093/brain/awt325
    • Brunetti, D., Dusi, S., Giordano, C., Lamperti, C., Morbin, M., Fugnanesi, V., et al. (2014). Pantethine treatment is effective in recovering the disease phenotype induced by ketogenic diet in a pantothenate kinase-associated neurodegeneration mouse model. Brain 137(Pt 1), 57-68. doi: 10.1093/brain/awt325
    • (2014) Brain , vol.137 , Issue.PART. 1 , pp. 57-68
    • Brunetti, D.1    Dusi, S.2    Giordano, C.3    Lamperti, C.4    Morbin, M.5    Fugnanesi, V.6
  • 22
    • 84870387253 scopus 로고    scopus 로고
    • Pantothenate kinase-associated neurodegeneration: altered mitochondria membrane potential and defective respiration in Pank2 knock-out mouse model
    • doi: 10.1093/hmg/dds380
    • Brunetti, D., Dusi, S., Morbin, M., Uggetti, A., Moda, F., D'Amato, I., et al. (2012). Pantothenate kinase-associated neurodegeneration: altered mitochondria membrane potential and defective respiration in Pank2 knock-out mouse model. Hum. Mol. Genet. 21, 5294-5305. doi: 10.1093/hmg/dds380
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 5294-5305
    • Brunetti, D.1    Dusi, S.2    Morbin, M.3    Uggetti, A.4    Moda, F.5    D'Amato, I.6
  • 23
    • 66349090778 scopus 로고    scopus 로고
    • Phospholipase A2 structure/function, mechanism, and signaling
    • doi: 10.1194/jlr.R800033-JLR200
    • Burke, J. E., and Dennis, E. A. (2009). Phospholipase A2 structure/function, mechanism, and signaling. J. Lipid Res. 50(Suppl.), S237-S242. doi: 10.1194/jlr.R800033-JLR200
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Burke, J.E.1    Dennis, E.A.2
  • 24
    • 84865729644 scopus 로고    scopus 로고
    • Skin fibroblasts from pantothenate kinase-associated neurodegeneration patients show altered cellular oxidative status and have defective iron-handling properties
    • doi: 10.1093/hmg/dds229
    • Campanella, A., Privitera, D., Guaraldo, M., Rovelli, E., Barzaghi, C., Garavaglia, B., et al. (2012). Skin fibroblasts from pantothenate kinase-associated neurodegeneration patients show altered cellular oxidative status and have defective iron-handling properties. Hum. Mol. Genet. 21, 4049-4059. doi: 10.1093/hmg/dds229
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 4049-4059
    • Campanella, A.1    Privitera, D.2    Guaraldo, M.3    Rovelli, E.4    Barzaghi, C.5    Garavaglia, B.6
  • 25
    • 33845899114 scopus 로고    scopus 로고
    • Clinical features and natural history of neuroferritinopathy caused by the FTL1 460InsA mutation
    • doi: 10.1093/brain/awl319
    • Chinnery, P. F., Crompton, D. E., Birchall, D., Jackson, M. J., Coulthard, A., Lombes, A., et al. (2007). Clinical features and natural history of neuroferritinopathy caused by the FTL1 460InsA mutation. Brain 130(Pt 1), 110-119. doi: 10.1093/brain/awl319
    • (2007) Brain , vol.130 , Issue.PT. 1 , pp. 110-119
    • Chinnery, P.F.1    Crompton, D.E.2    Birchall, D.3    Jackson, M.J.4    Coulthard, A.5    Lombes, A.6
  • 27
    • 70449519036 scopus 로고    scopus 로고
    • Oxidative stress and cell death in cells expressing L-ferritin variants causing neuroferritinopathy
    • doi: 10.1016/j.nbd.2009.09.009
    • Cozzi, A., Rovelli, E., Frizzale, G., Campanella, A., Amendola, M., Arosio, P., et al. (2010). Oxidative stress and cell death in cells expressing L-ferritin variants causing neuroferritinopathy. Neurobiol. Dis. 37, 77-85. doi: 10.1016/j.nbd.2009.09.009
    • (2010) Neurobiol. Dis. , vol.37 , pp. 77-85
    • Cozzi, A.1    Rovelli, E.2    Frizzale, G.3    Campanella, A.4    Amendola, M.5    Arosio, P.6
  • 28
    • 33747154110 scopus 로고    scopus 로고
    • Characterization of the L-ferritin variant 460InsA responsible of a hereditary ferritinopathy disorder
    • doi: 10.1016/j.nbd.2006.05.004
    • Cozzi, A., Santambrogio, P., Corsi, B., Campanella, A., Arosio, P., and Levi, S. (2006). Characterization of the L-ferritin variant 460InsA responsible of a hereditary ferritinopathy disorder. Neurobiol. Dis. 23, 644-652. doi: 10.1016/j.nbd.2006.05.004
    • (2006) Neurobiol. Dis. , vol.23 , pp. 644-652
    • Cozzi, A.1    Santambrogio, P.2    Corsi, B.3    Campanella, A.4    Arosio, P.5    Levi, S.6
  • 29
    • 0041952925 scopus 로고    scopus 로고
    • Neuroferritinopathy: a window on the role of iron in neurodegeneration
    • doi: 10.1006/bcmd.2002.0589
    • Crompton, D. E., Chinnery, P. F., Fey, C., Curtis, A. R., Morris, C. M., Kierstan, J., et al. (2002). Neuroferritinopathy: a window on the role of iron in neurodegeneration. Blood Cells Mol. Dis. 29, 522-531. doi: 10.1006/bcmd.2002.0589
    • (2002) Blood Cells Mol. Dis. , vol.29 , pp. 522-531
    • Crompton, D.E.1    Chinnery, P.F.2    Fey, C.3    Curtis, A.R.4    Morris, C.M.5    Kierstan, J.6
  • 30
    • 77952095626 scopus 로고    scopus 로고
    • Multiplex ligation-dependent probe amplification (MLPA) analysis is an effective tool for the detection of novel intragenic PLA2G6 mutations: implications for molecular diagnosis
    • doi: 10.1016/j.ymgme.2010.02.009
    • Crompton, D., Rehal, P. K., MacPherson, L., Foster, K., Lunt, P., Hughes, I., et al. (2010). Multiplex ligation-dependent probe amplification (MLPA) analysis is an effective tool for the detection of novel intragenic PLA2G6 mutations: implications for molecular diagnosis. Mol. Genet. Metab. 100, 207-212. doi: 10.1016/j.ymgme.2010.02.009
    • (2010) Mol. Genet. Metab. , vol.100 , pp. 207-212
    • Crompton, D.1    Rehal, P.K.2    MacPherson, L.3    Foster, K.4    Lunt, P.5    Hughes, I.6
  • 31
    • 69749121597 scopus 로고    scopus 로고
    • Age-dependent expression of hephaestin in the brain of ceruloplasmin-deficient mice
    • doi: 10.1016/j.jtemb.2009.05.004
    • Cui, R., Duan, X. L., Anderson, G. J., Qiao, Y. T., Yu, P., Qian, Z. M., et al. (2009). Age-dependent expression of hephaestin in the brain of ceruloplasmin-deficient mice. J. Trace Elem. Med. Biol. 23, 290-299. doi: 10.1016/j.jtemb.2009.05.004
    • (2009) J. Trace Elem. Med. Biol. , vol.23 , pp. 290-299
    • Cui, R.1    Duan, X.L.2    Anderson, G.J.3    Qiao, Y.T.4    Yu, P.5    Qian, Z.M.6
  • 32
    • 0034941118 scopus 로고    scopus 로고
    • Mutation in the gene encoding ferritin light polypeptide causes dominant adult-onset basal ganglia disease
    • doi: 10.1038/ng571
    • Curtis, A. R., Fey, C., Morris, C. M., Bindoff, L. A., Ince, P. G., Chinnery, P. F., et al. (2001). Mutation in the gene encoding ferritin light polypeptide causes dominant adult-onset basal ganglia disease. Nat. Genet. 28, 350-354. doi: 10.1038/ng571
    • (2001) Nat. Genet. , vol.28 , pp. 350-354
    • Curtis, A.R.1    Fey, C.2    Morris, C.M.3    Bindoff, L.A.4    Ince, P.G.5    Chinnery, P.F.6
  • 33
    • 84862189804 scopus 로고    scopus 로고
    • Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration
    • doi: 10.1073/pnas.1112368109
    • Dehay, B., Ramirez, A., Martinez-Vicente, M., Perier, C., Canron, M. H., Doudnikoff, E., et al. (2012). Loss of P-type ATPase ATP13A2/PARK9 function induces general lysosomal deficiency and leads to Parkinson disease neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 109, 9611-9616. doi: 10.1073/pnas.1112368109
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 9611-9616
    • Dehay, B.1    Ramirez, A.2    Martinez-Vicente, M.3    Perier, C.4    Canron, M.H.5    Doudnikoff, E.6
  • 34
    • 77953713610 scopus 로고    scopus 로고
    • Accumulation of oxidative DNA damage in brain mitochondria in mouse model of hereditary ferritinopathy
    • doi: 10.1016/j.neulet.2010.05.025
    • Deng, X., Vidal, R., and Englander, E. W. (2010). Accumulation of oxidative DNA damage in brain mitochondria in mouse model of hereditary ferritinopathy. Neurosci. Lett. 479, 44-48. doi: 10.1016/j.neulet.2010.05.025
    • (2010) Neurosci. Lett. , vol.479 , pp. 44-48
    • Deng, X.1    Vidal, R.2    Englander, E.W.3
  • 35
    • 84897930725 scopus 로고    scopus 로고
    • Targeting chelatable iron as a therapeutic modality in Parkinson's disease
    • doi: 10.1089/ars.2013.5593 [Epub ahead of print]
    • Devos, D., Moreau, C., Devedjian, J. C., Kluza, J., Petrault, M., Laloux, C., et al. (2014). Targeting chelatable iron as a therapeutic modality in Parkinson's disease. Antioxid. Redox Signal. doi: 10.1089/ars.2013.5593 [Epub ahead of print].
    • (2014) Antioxid. Redox Signal.
    • Devos, D.1    Moreau, C.2    Devedjian, J.C.3    Kluza, J.4    Petrault, M.5    Laloux, C.6
  • 36
    • 67649414590 scopus 로고    scopus 로고
    • Clinical features and natural history of neuroferritinopathy caused by the 458dupA FTL mutation
    • doi: 10.1093/brain/awn274
    • Devos, D., Tchofo, P. J., Vuillaume, I., Destée, A., Batey, S., Burn, J., et al. (2009). Clinical features and natural history of neuroferritinopathy caused by the 458dupA FTL mutation. Brain 132(Pt 6):e109. doi: 10.1093/brain/awn274
    • (2009) Brain , vol.132 , Issue.PT. 6
    • Devos, D.1    Tchofo, P.J.2    Vuillaume, I.3    Destée, A.4    Batey, S.5    Burn, J.6
  • 37
    • 84866459888 scopus 로고    scopus 로고
    • Two forms of iron as an intrinsic contrast agent in the basal ganglia of PKAN patients
    • doi: 10.1002/cmmi.1482
    • Dezortova, M., Herynek, V., Krssak, M., Kronerwetter, C., Trattnig, S., and Hajek, M. (2012). Two forms of iron as an intrinsic contrast agent in the basal ganglia of PKAN patients. Contrast Media Mol. Imaging 7, 509-515. doi: 10.1002/cmmi.1482
    • (2012) Contrast Media Mol. Imaging , vol.7 , pp. 509-515
    • Dezortova, M.1    Herynek, V.2    Krssak, M.3    Kronerwetter, C.4    Trattnig, S.5    Hajek, M.6
  • 38
    • 77950467334 scopus 로고    scopus 로고
    • Mutation of FA2H underlies a complicated form of hereditary spastic paraplegia (SPG35)
    • doi: 10.1002/humu.21205
    • Dick, K. J., Eckhardt, M., Paisán-Ruiz, C., Alshehhi, A. A., Proukakis, C., Sibtain, N. A., et al. (2010). Mutation of FA2H underlies a complicated form of hereditary spastic paraplegia (SPG35). Hum. Mutat. 31, E1251-E1260. doi: 10.1002/humu.21205
    • (2010) Hum. Mutat. , vol.31
    • Dick, K.J.1    Eckhardt, M.2    Paisán-Ruiz, C.3    Alshehhi, A.A.4    Proukakis, C.5    Sibtain, N.A.6
  • 39
    • 63249102412 scopus 로고    scopus 로고
    • Dominant mutants of ceruloplasmin impair the copper loading machinery in aceruloplasminemia
    • doi: 10.1074/jbc.M805688200
    • di Patti, M. C., Maio, N., Rizzo, G., De Francesco, G., Persichini, T., Colasanti, M., et al. (2009). Dominant mutants of ceruloplasmin impair the copper loading machinery in aceruloplasminemia. J. Biol. Chem. 284, 4545-4554. doi: 10.1074/jbc.M805688200
    • (2009) J. Biol. Chem. , vol.284 , pp. 4545-4554
    • di Patti, M.C.1    Maio, N.2    Rizzo, G.3    De Francesco, G.4    Persichini, T.5    Colasanti, M.6
  • 40
    • 84887232075 scopus 로고    scopus 로고
    • Imaging of iron
    • doi: 10.1016/B978-0-12-410502-7.00010-7
    • Dusek, P., Dezortova, M., and Wuerfel, J. (2013). Imaging of iron. Int. Rev. Neurobiol. 110, 195-239. doi: 10.1016/B978-0-12-410502-7.00010-7
    • (2013) Int. Rev. Neurobiol. , vol.110 , pp. 195-239
    • Dusek, P.1    Dezortova, M.2    Wuerfel, J.3
  • 41
    • 84863725376 scopus 로고    scopus 로고
    • Neurodegeneration with brain iron accumulation
    • doi: 10.1097/WCO.0b013e3283550cac
    • Dusek, P., and Schneider, S. A. (2012). Neurodegeneration with brain iron accumulation. Curr. Opin. Neurol. 25, 499-506. doi: 10.1097/WCO.0b013e3283550cac
    • (2012) Curr. Opin. Neurol. , vol.25 , pp. 499-506
    • Dusek, P.1    Schneider, S.A.2
  • 42
    • 84895686324 scopus 로고    scopus 로고
    • Neurodegenerative disorder with brain iron accumulation previously known as SENDA syndrome now genetically determined
    • doi: 10.1002/mds.25424
    • Dusek, P., and Schneider, S. A. (2013). Neurodegenerative disorder with brain iron accumulation previously known as SENDA syndrome now genetically determined. Mov. Disord. 28, 1051-1052. doi: 10.1002/mds.25424
    • (2013) Mov. Disord. , vol.28 , pp. 1051-1052
    • Dusek, P.1    Schneider, S.A.2
  • 43
    • 84891835067 scopus 로고    scopus 로고
    • Exome sequence reveals mutations in CoA synthase as a cause of neurodegeneration with brain iron accumulation
    • doi: 10.1016/j.ajhg.2013.11.008
    • Dusi, S., Valletta, L., Haack, T. B., Tsuchiya, Y., Venco, P., Pasqualato, S., et al. (2014). Exome sequence reveals mutations in CoA synthase as a cause of neurodegeneration with brain iron accumulation. Am. J. Hum. Genet. 94, 11-22. doi: 10.1016/j.ajhg.2013.11.008
    • (2014) Am. J. Hum. Genet. , vol.94 , pp. 11-22
    • Dusi, S.1    Valletta, L.2    Haack, T.B.3    Tsuchiya, Y.4    Venco, P.5    Pasqualato, S.6
  • 44
    • 55049092207 scopus 로고    scopus 로고
    • Mutations in the fatty acid 2-hydroxylase gene are associated with leukodystrophy with spastic paraparesis and dystonia
    • doi: 10.1016/j.ajhg.2008.10.010
    • Edvardson, S., Hama, H., Shaag, A., Gomori, J. M., Berger, I., Soffer, D., et al. (2008). Mutations in the fatty acid 2-hydroxylase gene are associated with leukodystrophy with spastic paraparesis and dystonia. Am. J. Hum. Genet. 83, 643-648. doi: 10.1016/j.ajhg.2008.10.010
    • (2008) Am. J. Hum. Genet. , vol.83 , pp. 643-648
    • Edvardson, S.1    Hama, H.2    Shaag, A.3    Gomori, J.M.4    Berger, I.5    Soffer, D.6
  • 45
    • 77958612571 scopus 로고    scopus 로고
    • Catalytic function of PLA2G6 is impaired by mutations associated with infantile neuroaxonal dystrophy but not dystonia-parkinsonism
    • doi: 10.1371/journal.pone.0012897
    • Engel, L. A., Jing, Z. O'Brien, D. E., Sun, M., and Kotzbauer, P. T. (2010). Catalytic function of PLA2G6 is impaired by mutations associated with infantile neuroaxonal dystrophy but not dystonia-parkinsonism. PLoS ONE 5:e12897. doi: 10.1371/journal.pone.0012897
    • (2010) PLoS ONE , vol.5
    • Engel, L.A.1    Jing Z.O'Brien, D.E.2    Sun, M.3    Kotzbauer, P.T.4
  • 47
    • 78049463804 scopus 로고    scopus 로고
    • Hepatic but not brain iron is rapidly chelated by deferasirox in aceruloplasminemia due to a novel gene mutation
    • doi: 10.1016/j.jhep.2010.04.039
    • Finkenstedt, A., Wolf, E., Hofner, E., Gasser, B. I., Bosch, S., Bakry, R., et al. (2010). Hepatic but not brain iron is rapidly chelated by deferasirox in aceruloplasminemia due to a novel gene mutation. J. Hepatol. 53, 1101-1107. doi: 10.1016/j.jhep.2010.04.039
    • (2010) J. Hepatol. , vol.53 , pp. 1101-1107
    • Finkenstedt, A.1    Wolf, E.2    Hofner, E.3    Gasser, B.I.4    Bosch, S.5    Bakry, R.6
  • 48
    • 78449288141 scopus 로고    scopus 로고
    • Targeting the correct HDAC(s) to treat cognitive disorders
    • doi: 10.1016/j.tips.2010.09.003
    • Fischer, A., Sananbenesi, F., Mungenast, A., and Tsai, L. H. (2010). Targeting the correct HDAC(s) to treat cognitive disorders. Trends Pharmacol. Sci. 31, 605-617. doi: 10.1016/j.tips.2010.09.003
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 605-617
    • Fischer, A.1    Sananbenesi, F.2    Mungenast, A.3    Tsai, L.H.4
  • 49
    • 52449091285 scopus 로고    scopus 로고
    • Regression of symptoms after selective iron chelation therapy in a case of neurodegeneration with brain iron accumulation
    • doi: 10.1002/mds.22002
    • Forni, G. L., Balocco, M., Cremonesi, L., Abbruzzese, G., Parodi, R. C., and Marchese, R. (2008). Regression of symptoms after selective iron chelation therapy in a case of neurodegeneration with brain iron accumulation. Mov. Disord. 23, 904-907. doi: 10.1002/mds.22002
    • (2008) Mov. Disord. , vol.23 , pp. 904-907
    • Forni, G.L.1    Balocco, M.2    Cremonesi, L.3    Abbruzzese, G.4    Parodi, R.C.5    Marchese, R.6
  • 50
    • 0033897735 scopus 로고    scopus 로고
    • Neurodegeneration with brain iron accumulation, type 1 is characterized by alpha-, beta-, and gamma-synuclein neuropathology
    • Galvin, J. E., Giasson, B., Hurtig, H. I., Lee, V. M., and Trojanowski, J. Q. (2000). Neurodegeneration with brain iron accumulation, type 1 is characterized by alpha-, beta-, and gamma-synuclein neuropathology. Am. J. Pathol. 157, 361-368.
    • (2000) Am. J. Pathol. , vol.157 , pp. 361-368
    • Galvin, J.E.1    Giasson, B.2    Hurtig, H.I.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 51
    • 84864005176 scopus 로고    scopus 로고
    • Germline deletion of pantothenate kinases 1 and 2 reveals the key roles for CoA in postnatal metabolism
    • doi: 10.1371/journal.pone.0040871
    • Garcia, M., Leonardi, R., Zhang, Y. M., Rehg, J. E., and Jackowski, S. (2012). Germline deletion of pantothenate kinases 1 and 2 reveals the key roles for CoA in postnatal metabolism. PLoS ONE 7:e40871. doi: 10.1371/journal.pone.0040871
    • (2012) PLoS ONE , vol.7
    • Garcia, M.1    Leonardi, R.2    Zhang, Y.M.3    Rehg, J.E.4    Jackowski, S.5
  • 53
    • 46749143765 scopus 로고    scopus 로고
    • The emerging role of group VI calcium-independent phospholipase A2 in releasing docosahexaenoic acid from brain phospholipids
    • doi: 10.1194/jlr.R700017-JLR200
    • Green, J. T., Orr, S. K., and Bazinet, R. P. (2008). The emerging role of group VI calcium-independent phospholipase A2 in releasing docosahexaenoic acid from brain phospholipids. J. Lipid Res. 49, 939-944. doi: 10.1194/jlr.R700017-JLR200
    • (2008) J. Lipid Res. , vol.49 , pp. 939-944
    • Green, J.T.1    Orr, S.K.2    Bazinet, R.P.3
  • 54
    • 79961146091 scopus 로고    scopus 로고
    • Genetics of neurodegeneration with brain iron accumulation
    • doi: 10.1007/s11910-011-0181-3
    • Gregory, A., and Hayflick, S. J. (2011). Genetics of neurodegeneration with brain iron accumulation. Curr. Neurol. Neurosci. Rep. 11, 254-261. doi: 10.1007/s11910-011-0181-3
    • (2011) Curr. Neurol. Neurosci. Rep. , vol.11 , pp. 254-261
    • Gregory, A.1    Hayflick, S.J.2
  • 55
    • 62149099955 scopus 로고    scopus 로고
    • Clinical and genetic delineation of neurodegeneration with brain iron accumulation
    • doi: 10.1136/jmg.2008.061929
    • Gregory, A., Polster, B. J., and Hayflick, S. J. (2009). Clinical and genetic delineation of neurodegeneration with brain iron accumulation. J. Med. Genet. 46, 73-80. doi: 10.1136/jmg.2008.061929
    • (2009) J. Med. Genet. , vol.46 , pp. 73-80
    • Gregory, A.1    Polster, B.J.2    Hayflick, S.J.3
  • 56
    • 58149229973 scopus 로고    scopus 로고
    • Neurodegeneration associated with genetic defects in phospholipase A(2)
    • doi: 10.1212/01.wnl.0000327094.67726.28
    • Gregory, A., Westaway, S. K., Holm, I. E., Kotzbauer, P. T., Hogarth, P., Sonek, S., et al. (2008). Neurodegeneration associated with genetic defects in phospholipase A(2). Neurology 71, 1402-1409. doi: 10.1212/01.wnl.0000327094.67726.28
    • (2008) Neurology , vol.71 , pp. 1402-1409
    • Gregory, A.1    Westaway, S.K.2    Holm, I.E.3    Kotzbauer, P.T.4    Hogarth, P.5    Sonek, S.6
  • 57
    • 84861883543 scopus 로고    scopus 로고
    • ATP13A2 mutations impair mitochondrial function in fibroblasts from patients with Kufor-Rakeb syndrome
    • doi: 10.1016/j.neurobiolaging.2011.12.035
    • Grünewald, A., Arns, B., Seibler, P., Rakovic, A., Münchau, A., Ramirez, A., et al. (2012). ATP13A2 mutations impair mitochondrial function in fibroblasts from patients with Kufor-Rakeb syndrome. Neurobiol. Aging 33, 1843.e1-1843.e7. doi: 10.1016/j.neurobiolaging.2011.12.035
    • (2012) Neurobiol. Aging , vol.33
    • Grünewald, A.1    Arns, B.2    Seibler, P.3    Rakovic, A.4    Münchau, A.5    Ramirez, A.6
  • 58
    • 84870913730 scopus 로고    scopus 로고
    • Exome sequencing reveals de novo WDR45 mutations causing a phenotypically distinct, X-linked dominant form of NBIA
    • doi: 10.1016/j.ajhg.2012.10.019
    • Haack, T. B., Hogarth, P., Kruer, M. C., Gregory, A., Wieland, T., Schwarzmayr, T., et al. (2012). Exome sequencing reveals de novo WDR45 mutations causing a phenotypically distinct, X-linked dominant form of NBIA. Am. J. Hum. Genet. 91, 1144-1149. doi: 10.1016/j.ajhg.2012.10.019
    • (2012) Am. J. Hum. Genet. , vol.91 , pp. 1144-1149
    • Haack, T.B.1    Hogarth, P.2    Kruer, M.C.3    Gregory, A.4    Wieland, T.5    Schwarzmayr, T.6
  • 59
    • 47249131160 scopus 로고    scopus 로고
    • Ceruloplasmin/hephaestin knockout mice model morphologic and molecular features of AMD
    • doi: 10.1167/iovs.07-1472
    • Hadziahmetovic, M., Dentchev, T., Song, Y., Haddad, N., He, X., Hahn, P., et al. (2008). Ceruloplasmin/hephaestin knockout mice model morphologic and molecular features of AMD. Invest. Ophthalmol. Vis. Sci. 49, 2728-2736. doi: 10.1167/iovs.07-1472
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 2728-2736
    • Hadziahmetovic, M.1    Dentchev, T.2    Song, Y.3    Haddad, N.4    He, X.5    Hahn, P.6
  • 60
    • 79953272637 scopus 로고    scopus 로고
    • The oral iron chelator deferiprone protects against iron overload-induced retinal degeneration
    • doi: 10.1167/iovs.10-6207
    • Hadziahmetovic, M., Song, Y., Wolkow, N., Iacovelli, J., Grieco, S., Lee, J., et al. (2011). The oral iron chelator deferiprone protects against iron overload-induced retinal degeneration. Invest. Ophthalmol. Vis. Sci. 52, 959-968. doi: 10.1167/iovs.10-6207
    • (2011) Invest. Ophthalmol. Vis. Sci. , vol.52 , pp. 959-968
    • Hadziahmetovic, M.1    Song, Y.2    Wolkow, N.3    Iacovelli, J.4    Grieco, S.5    Lee, J.6
  • 61
    • 4644293303 scopus 로고    scopus 로고
    • Disruption of ceruloplasmin and hephaestin in mice causes retinal iron overload and retinal degeneration with features of age-related macular degeneration
    • doi: 10.1073/pnas.0405146101
    • Hahn, P., Qian, Y., Dentchev, T., Chen, L., Beard, J., Harris, Z. L., et al. (2004). Disruption of ceruloplasmin and hephaestin in mice causes retinal iron overload and retinal degeneration with features of age-related macular degeneration. Proc. Natl. Acad. Sci. U.S.A. 101, 13850-13855. doi: 10.1073/pnas.0405146101
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13850-13855
    • Hahn, P.1    Qian, Y.2    Dentchev, T.3    Chen, L.4    Beard, J.5    Harris, Z.L.6
  • 62
    • 0032875387 scopus 로고    scopus 로고
    • Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux
    • Harris, Z. L., Durley, A. P., Man, T. K., and Gitlin, J. D. (1999). Targeted gene disruption reveals an essential role for ceruloplasmin in cellular iron efflux. Proc. Natl. Acad. Sci. U.S.A. 96, 10812-10817.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 10812-10817
    • Harris, Z.L.1    Durley, A.P.2    Man, T.K.3    Gitlin, J.D.4
  • 63
    • 32044455822 scopus 로고    scopus 로고
    • Genotypic and phenotypic spectrum of PANK2 mutations in patients with neurodegeneration with brain iron accumulation
    • doi: 10.1002/ana.20771
    • Hartig, M. B., Hörtnagel, K., Garavaglia, B., Zorzi, G., Kmiec, T., Klopstock, T., et al. (2006). Genotypic and phenotypic spectrum of PANK2 mutations in patients with neurodegeneration with brain iron accumulation. Ann. Neurol. 59, 248-256. doi: 10.1002/ana.20771
    • (2006) Ann. Neurol. , vol.59 , pp. 248-256
    • Hartig, M.B.1    Hörtnagel, K.2    Garavaglia, B.3    Zorzi, G.4    Kmiec, T.5    Klopstock, T.6
  • 64
    • 80053916609 scopus 로고    scopus 로고
    • Absence of an orphan mitochondrial protein, c19orf12, causes a distinct clinical subtype of neurodegeneration with brain iron accumulation
    • doi: 10.1016/j.ajhg.2011.09.007
    • Hartig, M. B., Iuso, A., Haack, T., Kmiec, T., Jurkiewicz, E., Heim, K., et al. (2011). Absence of an orphan mitochondrial protein, c19orf12, causes a distinct clinical subtype of neurodegeneration with brain iron accumulation. Am. J. Hum. Genet. 89, 543-550. doi: 10.1016/j.ajhg.2011.09.007
    • (2011) Am. J. Hum. Genet. , vol.89 , pp. 543-550
    • Hartig, M.B.1    Iuso, A.2    Haack, T.3    Kmiec, T.4    Jurkiewicz, E.5    Heim, K.6
  • 65
    • 84878841473 scopus 로고    scopus 로고
    • ß-Propeller protein-associated neurodegeneration: a new X-linked dominant disorder with brain iron accumulation
    • doi: 10.1093/brain/awt095
    • Hayflick, S. J., Kruer, M. C., Gregory, A., Haack, T. B., Kurian, M. A., Houlden, H. H., et al. (2013). ß-Propeller protein-associated neurodegeneration: a new X-linked dominant disorder with brain iron accumulation. Brain 136(Pt 6), 1708-1717. doi: 10.1093/brain/awt095
    • (2013) Brain , vol.136 , Issue.PT. 6 , pp. 1708-1717
    • Hayflick, S.J.1    Kruer, M.C.2    Gregory, A.3    Haack, T.B.4    Kurian, M.A.5    Houlden, H.H.6
  • 66
    • 0037413484 scopus 로고    scopus 로고
    • Genetic, clinical, and radiographic delineation of Hallervorden-Spatz syndrome
    • doi: 10.1056/NEJMoa020817
    • Hayflick, S. J., Westaway, S. K., Levinson, B., Zhou, B., Johnson, M. A., Ching, K. H., et al. (2003). Genetic, clinical, and radiographic delineation of Hallervorden-Spatz syndrome. N. Engl. J. Med. 348, 33-40. doi: 10.1056/NEJMoa020817
    • (2003) N. Engl. J. Med. , vol.348 , pp. 33-40
    • Hayflick, S.J.1    Westaway, S.K.2    Levinson, B.3    Zhou, B.4    Johnson, M.A.5    Ching, K.H.6
  • 67
    • 0037059741 scopus 로고    scopus 로고
    • Biochemical analysis of a missense mutation in aceruloplasminemia
    • doi: 10.1074/jbc.M109123200
    • Hellman, N. E., Kono, S., Miyajima, H., and Gitlin, J. D. (2002). Biochemical analysis of a missense mutation in aceruloplasminemia. J. Biol. Chem. 277, 1375-1380. doi: 10.1074/jbc.M109123200
    • (2002) J. Biol. Chem. , vol.277 , pp. 1375-1380
    • Hellman, N.E.1    Kono, S.2    Miyajima, H.3    Gitlin, J.D.4
  • 68
    • 84873649203 scopus 로고    scopus 로고
    • New NBIA subtype: genetic, clinical, pathologic, and radiographic features of MPAN
    • doi: 10.1212/WNL.0b013e31827e07be
    • Hogarth, P., Gregory, A., Kruer, M. C., Sanford, L., Wagoner, W., Natowicz, M. R., et al. (2013). New NBIA subtype: genetic, clinical, pathologic, and radiographic features of MPAN. Neurology 80, 268-275. doi: 10.1212/WNL.0b013e31827e07be
    • (2013) Neurology , vol.80 , pp. 268-275
    • Hogarth, P.1    Gregory, A.2    Kruer, M.C.3    Sanford, L.4    Wagoner, W.5    Natowicz, M.R.6
  • 69
    • 53649086025 scopus 로고    scopus 로고
    • Role of Ca2+-independent phospholipase A2 in cell growth and signaling
    • doi: 10.1016/j.bcp.2008.07.044
    • Hooks, S. B., and Cummings, B. S. (2008). Role of Ca2+-independent phospholipase A2 in cell growth and signaling. Biochem. Pharmacol. 76, 1059-1067. doi: 10.1016/j.bcp.2008.07.044
    • (2008) Biochem. Pharmacol. , vol.76 , pp. 1059-1067
    • Hooks, S.B.1    Cummings, B.S.2
  • 70
    • 0037322485 scopus 로고    scopus 로고
    • An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria
    • Hörtnagel, K., Prokisch, H., and Meitinger, T. (2003). An isoform of hPANK2, deficient in pantothenate kinase-associated neurodegeneration, localizes to mitochondria. Hum. Mol. Genet. 12, 321-327.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 321-327
    • Hörtnagel, K.1    Prokisch, H.2    Meitinger, T.3
  • 71
    • 80155135813 scopus 로고    scopus 로고
    • Mitochondrial mayhem: the mitochondrion as a modulator of iron metabolism and its role in disease
    • doi: 10.1089/ars.2011.3921
    • Huang, M. L., Lane, D. J., and Richardson. D. R. (2011). Mitochondrial mayhem: the mitochondrion as a modulator of iron metabolism and its role in disease. Antioxid. Redox. Signal. 15, 3003-3019. doi: 10.1089/ars.2011.3921
    • (2011) Antioxid. Redox. Signal. , vol.15 , pp. 3003-3019
    • Huang, M.L.1    Lane, D.J.2    Richardson, D.R.3
  • 72
    • 0027639404 scopus 로고
    • Infantile neuroaxonal dystrophy - immunohistochemical and ultrastructural studies on the central and peripheral nervous systems in infantile neuroaxonal dystrophy
    • Itoh, K., Negishi, H., Obayashi, C., Hayashi, Y., Hanioka, K., Imai, Y., et al. (1993). Infantile neuroaxonal dystrophy - immunohistochemical and ultrastructural studies on the central and peripheral nervous systems in infantile neuroaxonal dystrophy. Kobe J. Med. Sci. 39, 133-146.
    • (1993) Kobe J. Med. Sci. , vol.39 , pp. 133-146
    • Itoh, K.1    Negishi, H.2    Obayashi, C.3    Hayashi, Y.4    Hanioka, K.5    Imai, Y.6
  • 73
    • 84896778537 scopus 로고    scopus 로고
    • Impairment of Drosophila orthologs of the human orphan protein C19orf12 induces bang sensitivity and neurodegeneration
    • doi: 10.1371/journal.pone.0089439
    • Iuso, A., Sibon, O. C., Gorza, M., Heim, K., Organisti, C., Meitinger, T., et al. (2014). Impairment of Drosophila orthologs of the human orphan protein C19orf12 induces bang sensitivity and neurodegeneration. PLoS ONE 9:e89439. doi: 10.1371/journal.pone.0089439
    • (2014) PLoS ONE , vol.9
    • Iuso, A.1    Sibon, O.C.2    Gorza, M.3    Heim, K.4    Organisti, C.5    Meitinger, T.6
  • 74
    • 0038711587 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system
    • doi: 10.1074/jbc.M301988200
    • Jeong, S. Y., and David, S. (2003). Glycosylphosphatidylinositol-anchored ceruloplasmin is required for iron efflux from cells in the central nervous system. J. Biol. Chem. 278, 27144-27148. doi: 10.1074/jbc.M301988200
    • (2003) J. Biol. Chem. , vol.278 , pp. 27144-27148
    • Jeong, S.Y.1    David, S.2
  • 75
    • 33748889489 scopus 로고    scopus 로고
    • Age-related changes in iron homeostasis and cell death in the cerebellum of ceruloplasmin-deficient mice
    • doi: 10.1523/JNEUROSCI.2922-06.2006
    • Jeong, S. Y., and David, S. (2006). Age-related changes in iron homeostasis and cell death in the cerebellum of ceruloplasmin-deficient mice. J. Neurosci. 26, 9810-9819. doi: 10.1523/JNEUROSCI.2922-06.2006
    • (2006) J. Neurosci. , vol.26 , pp. 9810-9819
    • Jeong, S.Y.1    David, S.2
  • 76
    • 1842504252 scopus 로고    scopus 로고
    • Mitochondrial localization of human PANK2 and hypotheses of secondary iron accumulation in pantothenate kinase-associated neurodegeneration
    • doi: 10.1196/annals.1306.023
    • Johnson, M. A., Kuo, Y. M., Westaway, S. K., Parker, S. M., Ching, K. H., Gitschier, J., et al. (2004). Mitochondrial localization of human PANK2 and hypotheses of secondary iron accumulation in pantothenate kinase-associated neurodegeneration. Ann. N. Y. Acad. Sci. 1012, 282-298. doi: 10.1196/annals.1306.023
    • (2004) Ann. N. Y. Acad. Sci. , vol.1012 , pp. 282-298
    • Johnson, M.A.1    Kuo, Y.M.2    Westaway, S.K.3    Parker, S.M.4    Ching, K.H.5    Gitschier, J.6
  • 77
    • 84857048845 scopus 로고    scopus 로고
    • Extensive brain pathology in a patient with aceruloplasminemia with a prolonged duration of illness
    • doi: 10.1016/j.humpath.2011.05.016
    • Kaneko, K., Hineno, A., Yoshida, K., Ohara, S., Morita, H., and Ikeda, S. (2012). Extensive brain pathology in a patient with aceruloplasminemia with a prolonged duration of illness. Hum. Pathol. 43, 451-456. doi: 10.1016/j.humpath.2011.05.016
    • (2012) Hum. Pathol. , vol.43 , pp. 451-456
    • Kaneko, K.1    Hineno, A.2    Yoshida, K.3    Ohara, S.4    Morita, H.5    Ikeda, S.6
  • 78
    • 84864564238 scopus 로고    scopus 로고
    • Aceruloplasminemia
    • Kono, S. (2012). Aceruloplasminemia. Curr. Drug Targets 13, 1190-1199.
    • (2012) Curr. Drug Targets , vol.13 , pp. 1190-1199
    • Kono, S.1
  • 79
    • 84887253073 scopus 로고    scopus 로고
    • Aceruloplasminemia: an update
    • doi: 10.1016/B978-0-12-41-0502-7.00007-7
    • Kono, S. (2013). Aceruloplasminemia: an update. Int. Rev. Neurobiol. 110, 125-151. doi: 10.1016/B978-0-12-41-0502-7.00007-7
    • (2013) Int. Rev. Neurobiol. , vol.110 , pp. 125-151
    • Kono, S.1
  • 80
    • 33745870402 scopus 로고    scopus 로고
    • Molecular and pathological basis of aceruloplasminemia
    • doi: 10.4067/S0716-97602006000100003
    • Kono, S., and Miyajima, H. (2006). Molecular and pathological basis of aceruloplasminemia. Biol. Res. 39, 15-23. doi: 10.4067/S0716-97602006000100003
    • (2006) Biol. Res. , vol.39 , pp. 15-23
    • Kono, S.1    Miyajima, H.2
  • 81
    • 33745225581 scopus 로고    scopus 로고
    • Biochemical features of ceruloplasmin gene mutations linked to aceruloplasminemia
    • doi: 10.1385/NMM:8:3:361
    • Kono, S., Suzuki, H., Oda, T., Miyajima, H., Takahashi, Y., Shirakawa, K., et al. (2006). Biochemical features of ceruloplasmin gene mutations linked to aceruloplasminemia. Neuromol. Med. 8, 361-374. doi: 10.1385/NMM:8:3:361
    • (2006) Neuromol. Med. , vol.8 , pp. 361-374
    • Kono, S.1    Suzuki, H.2    Oda, T.3    Miyajima, H.4    Takahashi, Y.5    Shirakawa, K.6
  • 82
    • 35748963527 scopus 로고    scopus 로고
    • Cys-881 is essential for the trafficking and secretion of truncated mutant ceruloplasmin in aceruloplasminemia
    • doi: 10.1016/j.jhep.2007.05.013
    • Kono, S., Suzuki, H., Oda, T., Shirakawa, K., Takahashi, Y., Kitagawa, M., et al. (2007). Cys-881 is essential for the trafficking and secretion of truncated mutant ceruloplasmin in aceruloplasminemia. J. Hepatol. 47, 844-850. doi: 10.1016/j.jhep.2007.05.013
    • (2007) J. Hepatol. , vol.47 , pp. 844-850
    • Kono, S.1    Suzuki, H.2    Oda, T.3    Shirakawa, K.4    Takahashi, Y.5    Kitagawa, M.6
  • 83
    • 77956651790 scopus 로고    scopus 로고
    • Biological effects of mutant ceruloplasmin on hepcidin-mediated internalization of ferroportin
    • doi: 10.1016/j.bbadis.2010.07.011
    • Kono, S., Yoshida, K., Tomosugi, N., Terada, T., Hamaya, Y., Kanaoka, S., et al. (2010). Biological effects of mutant ceruloplasmin on hepcidin-mediated internalization of ferroportin. Biochim. Biophys. Acta 1802, 968-975. doi: 10.1016/j.bbadis.2010.07.011
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 968-975
    • Kono, S.1    Yoshida, K.2    Tomosugi, N.3    Terada, T.4    Hamaya, Y.5    Kanaoka, S.6
  • 84
    • 12744280679 scopus 로고    scopus 로고
    • Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused by abnormal processing, stability, and catalytic activity of mutant pantothenate kinase 2
    • doi: 10.1523/JNEUROSCI.4265-04.2005
    • Kotzbauer, P. T., Truax, A. C., Trojanowski, J. Q., and Lee, V. M. (2005). Altered neuronal mitochondrial coenzyme A synthesis in neurodegeneration with brain iron accumulation caused by abnormal processing, stability, and catalytic activity of mutant pantothenate kinase 2. J. Neurosci. 25, 689-698. doi: 10.1523/JNEUROSCI.4265-04.2005
    • (2005) J. Neurosci. , vol.25 , pp. 689-698
    • Kotzbauer, P.T.1    Truax, A.C.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 85
    • 84862326273 scopus 로고    scopus 로고
    • Neurodegeneration with brain iron accumulation: a diagnostic algorithm
    • doi: 10.1016/j.spen.2012.04.001
    • Kruer, M. C., and Boddaert, N. (2012). Neurodegeneration with brain iron accumulation: a diagnostic algorithm. Semin. Pediatr. Neurol. 19, 67-74. doi: 10.1016/j.spen.2012.04.001
    • (2012) Semin. Pediatr. Neurol. , vol.19 , pp. 67-74
    • Kruer, M.C.1    Boddaert, N.2
  • 86
    • 79953665042 scopus 로고    scopus 로고
    • Novel histopathologic findings in molecularly-confirmed pantothenate kinase-associated neurodegeneration
    • doi: 10.1093/brain/awr042
    • Kruer, M. C., Hiken, M., Gregory, A., Malandrini, A., Clark, D., Hogarth, P., et al. (2011). Novel histopathologic findings in molecularly-confirmed pantothenate kinase-associated neurodegeneration. Brain 134(Pt 4), 947-958. doi: 10.1093/brain/awr042
    • (2011) Brain , vol.134 , Issue.PT. 4 , pp. 947-958
    • Kruer, M.C.1    Hiken, M.2    Gregory, A.3    Malandrini, A.4    Clark, D.5    Hogarth, P.6
  • 87
    • 78249252333 scopus 로고    scopus 로고
    • Defective FA2H leads to a novel form of neurodegeneration with brain iron accumulation (NBIA)
    • doi: 10.1002/ana.22122
    • Kruer, M. C., Paisán-Ruiz, C., Boddaert, N., Yoon, M. Y., Hama, H., Gregory, A., et al. (2010). Defective FA2H leads to a novel form of neurodegeneration with brain iron accumulation (NBIA). Ann. Neurol. 68, 611-618. doi: 10.1002/ana.22122
    • (2010) Ann. Neurol. , vol.68 , pp. 611-618
    • Kruer, M.C.1    Paisán-Ruiz, C.2    Boddaert, N.3    Yoon, M.Y.4    Hama, H.5    Gregory, A.6
  • 88
    • 84893700221 scopus 로고    scopus 로고
    • C19orf12 mutation leads to a pallido-pyramidal syndrome
    • doi: 10.1016/j.gene.2013.11.039
    • Kruer, M. C., Salih, M. A., Mooney, C., Alzahrani, J., Elmalik, S. A., Kabiraj, M. M., et al. (2014). C19orf12 mutation leads to a pallido-pyramidal syndrome. Gene 537, 352-356. doi: 10.1016/j.gene.2013.11.039
    • (2014) Gene , vol.537 , pp. 352-356
    • Kruer, M.C.1    Salih, M.A.2    Mooney, C.3    Alzahrani, J.4    Elmalik, S.A.5    Kabiraj, M.M.6
  • 89
    • 67651103065 scopus 로고    scopus 로고
    • A novel ferritin light chain gene mutation in a Japanese family with neuroferritinopathy: description of clinical features and implications for genotype-phenotype correlations
    • doi: 10.1002/mds.22435
    • Kubota, A., Hida, A., Ichikawa, Y., Momose, Y., Goto, J., Igeta, Y., et al. (2009). A novel ferritin light chain gene mutation in a Japanese family with neuroferritinopathy: description of clinical features and implications for genotype-phenotype correlations. Mov. Disord. 24, 441-445. doi: 10.1002/mds.22435
    • (2009) Mov. Disord. , vol.24 , pp. 441-445
    • Kubota, A.1    Hida, A.2    Ichikawa, Y.3    Momose, Y.4    Goto, J.5    Igeta, Y.6
  • 90
    • 12344334370 scopus 로고    scopus 로고
    • Deficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia
    • doi: 10.1093/hmg/ddi005
    • Kuo, Y. M., Duncan, J. L., Westaway, S. K., Yang, H., Nune, G., Xu, E. Y., et al. (2005). Deficiency of pantothenate kinase 2 (Pank2) in mice leads to retinal degeneration and azoospermia. Hum. Mol. Genet. 14, 49-57. doi: 10.1093/hmg/ddi005
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 49-57
    • Kuo, Y.M.1    Duncan, J.L.2    Westaway, S.K.3    Yang, H.4    Nune, G.5    Xu, E.Y.6
  • 91
    • 84887245377 scopus 로고    scopus 로고
    • Pantothenate kinase-associated neurodegeneration (PKAN) and PLA2G6-associated neurodegeneration (PLAN): review of two major neurodegeneration with brain iron accumulation (NBIA) phenotypes
    • doi: 10.1016/B978-0-12-410502-7.00003-X
    • Kurian, M. A., and Hayflick, S. J. (2013). Pantothenate kinase-associated neurodegeneration (PKAN) and PLA2G6-associated neurodegeneration (PLAN): review of two major neurodegeneration with brain iron accumulation (NBIA) phenotypes. Int. Rev. Neurobiol. 110, 49-71. doi: 10.1016/B978-0-12-410502-7.00003-X
    • (2013) Int. Rev. Neurobiol. , vol.110 , pp. 49-71
    • Kurian, M.A.1    Hayflick, S.J.2
  • 92
    • 42949158281 scopus 로고    scopus 로고
    • Phenotypic spectrum of neurodegeneration associated with mutations in the PLA2G6 gene (PLAN)
    • doi: 10.1212/01.wnl.0000310986.48286.8e
    • Kurian, M. A., Morgan, N. V., MacPherson, L., Foster, K., Peake, D., Gupta, R., et al. (2008). Phenotypic spectrum of neurodegeneration associated with mutations in the PLA2G6 gene (PLAN). Neurology 70, 1623-1629. doi: 10.1212/01.wnl.0000310986.48286.8e
    • (2008) Neurology , vol.70 , pp. 1623-1629
    • Kurian, M.A.1    Morgan, N.V.2    MacPherson, L.3    Foster, K.4    Peake, D.5    Gupta, R.6
  • 93
    • 84655167560 scopus 로고    scopus 로고
    • Long-term improvement under deferiprone in a case of neurodegeneration with brain iron accumulation
    • doi: 10.1016/j.parkreldis.2011.06.024
    • Kwiatkowski, A., Ryckewaert, G., Jissendi Tchofo, P., Moreau, C., Vuillaume, I., Chinnery, P. F., et al. (2012). Long-term improvement under deferiprone in a case of neurodegeneration with brain iron accumulation. Parkinsonism Relat. Disord. 18, 110-112. doi: 10.1016/j.parkreldis.2011.06.024
    • (2012) Parkinsonism Relat. Disord. , vol.18 , pp. 110-112
    • Kwiatkowski, A.1    Ryckewaert, G.2    Jissendi Tchofo, P.3    Moreau, C.4    Vuillaume, I.5    Chinnery, P.F.6
  • 94
    • 84884535149 scopus 로고    scopus 로고
    • Hereditary spastic paraplegia type 43 (SPG43) is caused by mutation in C19orf12
    • doi: 10.1002/humu.22378
    • Landouré, G., Zhu, P. P., Lourenço, C. M., Johnson, J. O., Toro, C., Bricceno, K. V., et al. (2013). Hereditary spastic paraplegia type 43 (SPG43) is caused by mutation in C19orf12. Hum. Mutat. 34, 1357-1360. doi: 10.1002/humu.22378
    • (2013) Hum. Mutat. , vol.34 , pp. 1357-1360
    • Landouré, G.1    Zhu, P.P.2    Lourenço, C.M.3    Johnson, J.O.4    Toro, C.5    Bricceno, K.V.6
  • 95
    • 0031983455 scopus 로고    scopus 로고
    • Multiple splice variants of the human calcium-independent phospholipase A2 and their effect on enzyme activity
    • doi: 10.1074/jbc.273.1.207
    • Larsson, P. K., Claesson, H. E., and Kennedy, B. P. (1998). Multiple splice variants of the human calcium-independent phospholipase A2 and their effect on enzyme activity. J. Biol. Chem. 273, 207-214. doi: 10.1074/jbc.273.1.207
    • (1998) J. Biol. Chem. , vol.273 , pp. 207-214
    • Larsson, P.K.1    Claesson, H.E.2    Kennedy, B.P.3
  • 96
    • 0026059720 scopus 로고
    • Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts
    • doi: 10.1038/349541a0
    • Lawson, D. M., Artymiuk, P. J., Yewdall, S. J., Smith, J. M., Livingstone, J. C., Treffry, A., et al. (1991). Solving the structure of human H ferritin by genetically engineering intermolecular crystal contacts. Nature 349, 541-544. doi: 10.1038/349541a0
    • (1991) Nature , vol.349 , pp. 541-544
    • Lawson, D.M.1    Artymiuk, P.J.2    Yewdall, S.J.3    Smith, J.M.4    Livingstone, J.C.5    Treffry, A.6
  • 98
    • 33846818915 scopus 로고    scopus 로고
    • Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine
    • doi: 10.1073/pnas.0607621104
    • Leonardi, R., Rock, C. O., Jackowski, S., and Zhang, Y. M. (2007a). Activation of human mitochondrial pantothenate kinase 2 by palmitoylcarnitine. Proc. Natl. Acad. Sci. U.S.A. 104, 1494-1499. doi: 10.1073/pnas.0607621104
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 1494-1499
    • Leonardi, R.1    Rock, C.O.2    Jackowski, S.3    Zhang, Y.M.4
  • 99
    • 34548665512 scopus 로고    scopus 로고
    • Localization and regulation of mouse pantothenate kinase 2
    • doi: 10.1016/j.febslet.2007.08.056
    • Leonardi, R., Zhang, Y. M., Lykidis, A., Rock, C. O., and Jackowski, S. (2007b). Localization and regulation of mouse pantothenate kinase 2. FEBS Lett. 581, 4639-4644. doi: 10.1016/j.febslet.2007.08.056
    • (2007) FEBS Lett. , vol.581 , pp. 4639-4644
    • Leonardi, R.1    Zhang, Y.M.2    Lykidis, A.3    Rock, C.O.4    Jackowski, S.5
  • 100
    • 19544372226 scopus 로고    scopus 로고
    • Coenzyme A: back in action
    • doi: 10.1016/j.plipres.2005.04.001
    • Leonardi, R., Zhang, Y. M., Rock, C. O., and Jackowski, S. (2005). Coenzyme A: back in action. Prog. Lipid Res. 44, 125-153. doi: 10.1016/j.plipres.2005.04.001
    • (2005) Prog. Lipid Res. , vol.44 , pp. 125-153
    • Leonardi, R.1    Zhang, Y.M.2    Rock, C.O.3    Jackowski, S.4
  • 102
    • 80051474094 scopus 로고    scopus 로고
    • The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of omegasomes to autophagosomes
    • doi: 10.1016/j.devcel.2011.06.024
    • Lu, Q., Yang, P., Huang, X., Hu, W., Guo, B., Wu, F., et al. (2011). The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of omegasomes to autophagosomes. Dev. Cell 21, 343-357. doi: 10.1016/j.devcel.2011.06.024
    • (2011) Dev. Cell , vol.21 , pp. 343-357
    • Lu, Q.1    Yang, P.2    Huang, X.3    Hu, W.4    Guo, B.5    Wu, F.6
  • 103
    • 77951249355 scopus 로고    scopus 로고
    • Mutant ferritin L-chains that cause neurodegeneration act in a dominant-negative manner to reduce ferritin iron incorporation
    • doi: 10.1074/jbc.M109.096404
    • Luscieti, S., Santambrogio, P., Langlois d'Estaintot, B., Granier, T., Cozzi, A., Poli, M., et al. (2010). Mutant ferritin L-chains that cause neurodegeneration act in a dominant-negative manner to reduce ferritin iron incorporation. J. Biol. Chem. 285, 11948-11957. doi: 10.1074/jbc.M109.096404
    • (2010) J. Biol. Chem. , vol.285 , pp. 11948-11957
    • Luscieti, S.1    Santambrogio, P.2    Langlois d'Estaintot, B.3    Granier, T.4    Cozzi, A.5    Poli, M.6
  • 104
    • 23844553465 scopus 로고    scopus 로고
    • Neuroferritinopathy: missense mutation in FTL causing early-onset bilateral pallidal involvement
    • doi: 10.1212/01.wnl.0000178224.81169.c2
    • Maciel, P., Cruz, V. T., Constante, M., Iniesta, I., Costa, M. C., Gallati, S., et al. (2005). Neuroferritinopathy: missense mutation in FTL causing early-onset bilateral pallidal involvement. Neurology 65, 603-605. doi: 10.1212/01.wnl.0000178224.81169.c2
    • (2005) Neurology , vol.65 , pp. 603-605
    • Maciel, P.1    Cruz, V.T.2    Constante, M.3    Iniesta, I.4    Costa, M.C.5    Gallati, S.6
  • 105
    • 39549085125 scopus 로고    scopus 로고
    • Disrupted membrane homeostasis and accumulation of ubiquitinated proteins in a mouse model of infantile neuroaxonal dystrophy caused by PLA2G6 mutations
    • doi: 10.2353/ajpath.2008.070823
    • Malik, I., Turk, J., Mancuso, D. J., Montier, L., Wohltmann, M., Wozniak, D. F., et al. (2008). Disrupted membrane homeostasis and accumulation of ubiquitinated proteins in a mouse model of infantile neuroaxonal dystrophy caused by PLA2G6 mutations. Am. J. Pathol. 172, 406-416. doi: 10.2353/ajpath.2008.070823
    • (2008) Am. J. Pathol. , vol.172 , pp. 406-416
    • Malik, I.1    Turk, J.2    Mancuso, D.J.3    Montier, L.4    Wohltmann, M.5    Wozniak, D.F.6
  • 107
    • 2342434172 scopus 로고    scopus 로고
    • Iron chelation therapy in aceruloplasminaemia: study of a patient with a novel missense mutation
    • doi: 10.1136/gut.2003.030429
    • Mariani, R., Arosio, C., Pelucchi, S., Grisoli, M., Piga, A., Trombini, P., et al. (2004). Iron chelation therapy in aceruloplasminaemia: study of a patient with a novel missense mutation. Gut 53, 756-758. doi: 10.1136/gut.2003.030429
    • (2004) Gut , vol.53 , pp. 756-758
    • Mariani, R.1    Arosio, C.2    Pelucchi, S.3    Grisoli, M.4    Piga, A.5    Trombini, P.6
  • 108
    • 42949158787 scopus 로고    scopus 로고
    • T2* and FSE MRI distinguishes four subtypes of neurodegeneration with brain iron accumulation
    • doi: 10.1212/01.wnl.0000310985.40011.d6
    • McNeill, A., Birchall, D., Hayflick, S. J., Gregory, A., Schenk, J. F., Zimmerman, E. A., et al. (2008). T2* and FSE MRI distinguishes four subtypes of neurodegeneration with brain iron accumulation. Neurology 70, 1614-1619. doi: 10.1212/01.wnl.0000310985.40011.d6
    • (2008) Neurology , vol.70 , pp. 1614-1619
    • McNeill, A.1    Birchall, D.2    Hayflick, S.J.3    Gregory, A.4    Schenk, J.F.5    Zimmerman, E.A.6
  • 109
    • 0346847502 scopus 로고    scopus 로고
    • Aceruloplasminemia, an iron metabolic disorder
    • doi: 10.1046/j.1440-1789.2003.00521.x
    • Miyajima, H. (2003). Aceruloplasminemia, an iron metabolic disorder. Neuropathology 23, 345-350. doi: 10.1046/j.1440-1789.2003.00521.x
    • (2003) Neuropathology , vol.23 , pp. 345-350
    • Miyajima, H.1
  • 110
    • 0023240051 scopus 로고
    • Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration
    • doi: 10.1212/WNL.37.5.761
    • Miyajima, H., Nishimura, Y., Mizoguchi, K., Sakamoto, M., Shimizu, T., and Honda, N. (1987). Familial apoceruloplasmin deficiency associated with blepharospasm and retinal degeneration. Neurology 37, 761-767. doi: 10.1212/WNL.37.5.761
    • (1987) Neurology , vol.37 , pp. 761-767
    • Miyajima, H.1    Nishimura, Y.2    Mizoguchi, K.3    Sakamoto, M.4    Shimizu, T.5    Honda, N.6
  • 111
    • 33745553895 scopus 로고    scopus 로고
    • PLA2G6, encoding a phospholipase A2, is mutated in neurodegenerative disorders with high brain iron
    • doi: 10.1038/ng1826
    • Morgan, N. V., Westaway, S. K., Morton, J. E., Gregory, A., Gissen, P., Sonek, S., et al. (2006). PLA2G6, encoding a phospholipase A2, is mutated in neurodegenerative disorders with high brain iron. Nat. Genet. 38, 752-754. doi: 10.1038/ng1826
    • (2006) Nat. Genet. , vol.38 , pp. 752-754
    • Morgan, N.V.1    Westaway, S.K.2    Morton, J.E.3    Gregory, A.4    Gissen, P.5    Sonek, S.6
  • 112
    • 0029007765 scopus 로고
    • Hereditary ceruloplasmin deficiency with hemosiderosis: a clinicopathological study of a Japanese family
    • doi: 10.1002/ana.410370515
    • Morita, H., Ikeda, S., Yamamoto, K., Morita, S., Yoshida, K., Nomoto, S., et al. (1995). Hereditary ceruloplasmin deficiency with hemosiderosis: a clinicopathological study of a Japanese family. Ann. Neurol. 37, 646-656. doi: 10.1002/ana.410370515
    • (1995) Ann. Neurol. , vol.37 , pp. 646-656
    • Morita, H.1    Ikeda, S.2    Yamamoto, K.3    Morita, S.4    Yoshida, K.5    Nomoto, S.6
  • 113
    • 79951671438 scopus 로고    scopus 로고
    • Iron loading-induced aggregation and reduction of iron incorporation in heteropolymeric ferritin containing a mutant light chain that causes neurodegeneration
    • doi: 10.1016/j.bbadis.2010.10.010
    • Muhoberac, B. B., Baraibar, M. A., and Vidal, R. (2011). Iron loading-induced aggregation and reduction of iron incorporation in heteropolymeric ferritin containing a mutant light chain that causes neurodegeneration. Biochim. Biophys. Acta 1812, 544-548. doi: 10.1016/j.bbadis.2010.10.010
    • (2011) Biochim. Biophys. Acta , vol.1812 , pp. 544-548
    • Muhoberac, B.B.1    Baraibar, M.A.2    Vidal, R.3
  • 114
    • 0033817296 scopus 로고    scopus 로고
    • Alpha-synuclein accumulation in a case of neurodegeneration with brain iron accumulation type 1 (NBIA-1, formerly Hallervorden-Spatz syndrome) with widespread cortical and brainstem-type Lewy bodies
    • Neumann, M., Adler, S., Schlüter, O., Kremmer, E., Benecke, R., and Kretzschmar, H. A. (2000). Alpha-synuclein accumulation in a case of neurodegeneration with brain iron accumulation type 1 (NBIA-1, formerly Hallervorden-Spatz syndrome) with widespread cortical and brainstem-type Lewy bodies. Acta Neuropathol. 100, 568-574.
    • (2000) Acta Neuropathol. , vol.100 , pp. 568-574
    • Neumann, M.1    Adler, S.2    Schlüter, O.3    Kremmer, E.4    Benecke, R.5    Kretzschmar, H.A.6
  • 115
    • 79960065060 scopus 로고    scopus 로고
    • Criteria for early identification of aceruloplasminemia
    • doi: 10.2169/internalmedicine.50.5108
    • Ogimoto, M., Anzai, K., Takenoshita, H., Kogawa, K., Akehi, Y., Yoshida, R., et al. (2011). Criteria for early identification of aceruloplasminemia. Intern. Med. 50, 1415-1418. doi: 10.2169/internalmedicine.50.5108
    • (2011) Intern. Med. , vol.50 , pp. 1415-1418
    • Ogimoto, M.1    Anzai, K.2    Takenoshita, H.3    Kogawa, K.4    Akehi, Y.5    Yoshida, R.6
  • 116
    • 84865601614 scopus 로고    scopus 로고
    • MRI findings in neuroferritinopathy
    • doi: 10.1155/2012/197438
    • Ohta, E., and Takiyama, Y. (2012). MRI findings in neuroferritinopathy. Neurol. Res. Int. 2012, 197438. doi: 10.1155/2012/197438
    • (2012) Neurol. Res. Int. , vol.2012 , pp. 197438
    • Ohta, E.1    Takiyama, Y.2
  • 117
    • 42049109697 scopus 로고    scopus 로고
    • Neuroferritinopathy in a Japanese family with a duplication in the ferritin light chain gene
    • doi: 10.1212/01.wnl.0000310428.74624.95
    • Ohta, E., Nagasaka, T., Shindo, K., Toma, S., Nagasaka, K., Ohta, K., et al. (2008). Neuroferritinopathy in a Japanese family with a duplication in the ferritin light chain gene. Neurology 70(16 Pt 2), 1493-1494. doi: 10.1212/01.wnl.0000310428.74624.95
    • (2008) Neurology , vol.70 , Issue.16 PT. 2 , pp. 1493-1494
    • Ohta, E.1    Nagasaka, T.2    Shindo, K.3    Toma, S.4    Nagasaka, K.5    Ohta, K.6
  • 118
    • 84856964851 scopus 로고    scopus 로고
    • Widespread Lewy body and tau accumulation in childhood and adult onset dystonia-parkinsonism cases with PLA2G6 mutations
    • doi: 10.1016/j.neurobiolaging.2010.05.009
    • Paisán-Ruiz, C., Li, A., Schneider, S. A., Holton, J. L., Johnson, R., Kidd, D., et al. (2012). Widespread Lewy body and tau accumulation in childhood and adult onset dystonia-parkinsonism cases with PLA2G6 mutations. Neurobiol. Aging 33, 814-823. doi: 10.1016/j.neurobiolaging.2010.05.009
    • (2012) Neurobiol. Aging , vol.33 , pp. 814-823
    • Paisán-Ruiz, C.1    Li, A.2    Schneider, S.A.3    Holton, J.L.4    Johnson, R.5    Kidd, D.6
  • 119
    • 84885117281 scopus 로고    scopus 로고
    • A new in vivo model of pantothenate kinase-associated neurodegeneration reveals a surprising role for transcriptional regulation in pathogenesis
    • doi: 10.3389/fncel.2013.00146
    • Pandey, V., Varun, P., Turm, H., Hagit, T., Bekenstein, U., Uriya, B., et al. (2013). A new in vivo model of pantothenate kinase-associated neurodegeneration reveals a surprising role for transcriptional regulation in pathogenesis. Front. Cell. Neurosci. 7:146. doi: 10.3389/fncel.2013.00146
    • (2013) Front. Cell. Neurosci. , vol.7 , pp. 146
    • Pandey, V.1    Varun, P.2    Turm, H.3    Hagit, T.4    Bekenstein, U.5    Uriya, B.6
  • 120
    • 84862311702 scopus 로고    scopus 로고
    • C19orf12 and FA2H mutations are rare in Italian patients with neurodegeneration with brain iron accumulation
    • doi: 10.1016/j.spen.2012.03.006
    • Panteghini, C., Zorzi, G., Venco, P., Dusi, S., Reale, C., Brunetti, D., et al. (2012). C19orf12 and FA2H mutations are rare in Italian patients with neurodegeneration with brain iron accumulation. Semin. Pediatr. Neurol. 19, 75-81. doi: 10.1016/j.spen.2012.03.006
    • (2012) Semin. Pediatr. Neurol. , vol.19 , pp. 75-81
    • Panteghini, C.1    Zorzi, G.2    Venco, P.3    Dusi, S.4    Reale, C.5    Brunetti, D.6
  • 121
    • 84899903061 scopus 로고    scopus 로고
    • Parkinson's disease-associated human ATP13A2 (PARK9) deficiency causes zinc dyshomeostasis and mitochondrial dysfunction
    • doi: 10.1093/hmg/ddt623 [Epub ahead of print]
    • Park, J. S., Koentjoro, B., Veivers, D., Mackay-Sim, A., and Sue, C. M. (2014). Parkinson's disease-associated human ATP13A2 (PARK9) deficiency causes zinc dyshomeostasis and mitochondrial dysfunction. Hum. Mol. Genet. doi: 10.1093/hmg/ddt623 [Epub ahead of print].
    • (2014) Hum. Mol. Genet.
    • Park, J.S.1    Koentjoro, B.2    Veivers, D.3    Mackay-Sim, A.4    Sue, C.M.5
  • 122
    • 0034635402 scopus 로고    scopus 로고
    • Alternative RNA splicing generates a glycosylphosphatidylinositol-anchored form of ceruloplasmin in mammalian brain
    • doi: 10.1074/jbc.275.6.4305
    • Patel, B. N., Dunn, R. J., and David, S. (2000). Alternative RNA splicing generates a glycosylphosphatidylinositol-anchored form of ceruloplasmin in mammalian brain. J. Biol. Chem. 275, 4305-4310. doi: 10.1074/jbc.275.6.4305
    • (2000) J. Biol. Chem. , vol.275 , pp. 4305-4310
    • Patel, B.N.1    Dunn, R.J.2    David, S.3
  • 123
    • 0036703490 scopus 로고    scopus 로고
    • Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury
    • Patel, B. N., Dunn, R. J., Jeong, S. Y., Zhu, Q., Julien, J. P., and David, S. (2002). Ceruloplasmin regulates iron levels in the CNS and prevents free radical injury. J. Neurosci. 22, 6578-6586.
    • (2002) J. Neurosci. , vol.22 , pp. 6578-6586
    • Patel, B.N.1    Dunn, R.J.2    Jeong, S.Y.3    Zhu, Q.4    Julien, J.P.5    David, S.6
  • 124
    • 84872713118 scopus 로고    scopus 로고
    • Loss of cardiolipin leads to perturbation of mitochondrial and cellular iron homeostasis
    • doi: 10.1074/jbc.M112.428938
    • Patil, V. A., Fox, J. L., Gohil, V. M., Winge, D. R., and Greenberg, M. L. (2013). Loss of cardiolipin leads to perturbation of mitochondrial and cellular iron homeostasis. J. Biol. Chem. 288, 1696-1705. doi: 10.1074/jbc.M112.428938
    • (2013) J. Biol. Chem. , vol.288 , pp. 1696-1705
    • Patil, V.A.1    Fox, J.L.2    Gohil, V.M.3    Winge, D.R.4    Greenberg, M.L.5
  • 125
    • 32044462285 scopus 로고    scopus 로고
    • Involvement of group VIA calcium-independent phospholipase A2 in macrophage engulfment of hydrogen peroxide-treated U937 cells
    • doi: 10.4049/jimmunol.176.4.2555
    • Pérez, R., Balboa, M. A., and Balsinde, J. (2006). Involvement of group VIA calcium-independent phospholipase A2 in macrophage engulfment of hydrogen peroxide-treated U937 cells. J. Immunol. 176, 2555-2561. doi: 10.4049/jimmunol.176.4.2555
    • (2006) J. Immunol. , vol.176 , pp. 2555-2561
    • Pérez, R.1    Balboa, M.A.2    Balsinde, J.3
  • 126
    • 0022381482 scopus 로고
    • Hallervorden-Spatz disease: cysteine accumulation and cysteine dioxygenase deficiency in the globus pallidus
    • doi: 10.1002/ana.410180411
    • Perry, T. L., Norman, M. G., Yong, V. W., Whiting, S., Crichton, J. U., Hansen, S., et al. (1985). Hallervorden-Spatz disease: cysteine accumulation and cysteine dioxygenase deficiency in the globus pallidus. Ann. Neurol. 18, 482-489. doi: 10.1002/ana.410180411
    • (1985) Ann. Neurol. , vol.18 , pp. 482-489
    • Perry, T.L.1    Norman, M.G.2    Yong, V.W.3    Whiting, S.4    Crichton, J.U.5    Hansen, S.6
  • 127
    • 77953703758 scopus 로고    scopus 로고
    • Pantothenate kinase-2 (Pank2) silencing causes cell growth reduction, cell-specific ferroportin upregulation and iron deregulation
    • doi: 10.1016/j.nbd.2010.04.009
    • Poli, M., Derosas, M., Luscieti, S., Cavadini, P., Campanella, A., Verardi, R., et al. (2010). Pantothenate kinase-2 (Pank2) silencing causes cell growth reduction, cell-specific ferroportin upregulation and iron deregulation. Neurobiol. Dis. 39, 204-210. doi: 10.1016/j.nbd.2010.04.009
    • (2010) Neurobiol. Dis. , vol.39 , pp. 204-210
    • Poli, M.1    Derosas, M.2    Luscieti, S.3    Cavadini, P.4    Campanella, A.5    Verardi, R.6
  • 128
    • 77955587648 scopus 로고    scopus 로고
    • Characterization of the human PANK2 promoter
    • doi: 10.1016/j.gene.2010.06.011
    • Polster, B. J., Yoon, M. Y., and Hayflick, S. J. (2010). Characterization of the human PANK2 promoter. Gene 465, 53-60. doi: 10.1016/j.gene.2010.06.011
    • (2010) Gene , vol.465 , pp. 53-60
    • Polster, B.J.1    Yoon, M.Y.2    Hayflick, S.J.3
  • 129
    • 79955860321 scopus 로고    scopus 로고
    • Central nervous system dysfunction in a mouse model of FA2H deficiency
    • doi: 10.1002/glia.21172
    • Potter, K. A., Kern, M. J., Fullbright, G., Bielawski, J., Scherer, S. S., Yum, S. W., et al. (2011). Central nervous system dysfunction in a mouse model of FA2H deficiency. Glia 59, 1009-1021. doi: 10.1002/glia.21172
    • (2011) Glia , vol.59 , pp. 1009-1021
    • Potter, K.A.1    Kern, M.J.2    Fullbright, G.3    Bielawski, J.4    Scherer, S.S.5    Yum, S.W.6
  • 130
    • 84859246513 scopus 로고    scopus 로고
    • PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity
    • doi: 10.1093/hmg/ddr606
    • Ramonet, D., Podhajska, A., Stafa, K., Sonnay, S., Trancikova, A., Tsika, E., et al. (2012). PARK9-associated ATP13A2 localizes to intracellular acidic vesicles and regulates cation homeostasis and neuronal integrity. Hum. Mol. Genet. 21, 1725-1743. doi: 10.1093/hmg/ddr606
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1725-1743
    • Ramonet, D.1    Podhajska, A.2    Stafa, K.3    Sonnay, S.4    Trancikova, A.5    Tsika, E.6
  • 131
    • 77951055908 scopus 로고    scopus 로고
    • Pantethine rescues a Drosophila model for pantothenate kinase-associated neurodegeneration
    • doi: 10.1073/pnas.0912105107
    • Rana, A., Seinen, E., Siudeja, K., Muntendam, R., Srinivasan, B., van der Want, J. J., et al. (2010). Pantethine rescues a Drosophila model for pantothenate kinase-associated neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 107, 6988-6993. doi: 10.1073/pnas.0912105107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 6988-6993
    • Rana, A.1    Seinen, E.2    Siudeja, K.3    Muntendam, R.4    Srinivasan, B.5    van der Want, J.J.6
  • 132
    • 82855180184 scopus 로고    scopus 로고
    • Aceruloplasminemia: a rare disease - diagnosis and treatment of two cases
    • doi: 10.5581/1516-8484.20110104
    • Roberti Mdo, R., Borges Filho, H. M., Goncalves, C. H., and Lima, F. L. (2011). Aceruloplasminemia: a rare disease - diagnosis and treatment of two cases. Rev. Bras. Hematol. Hemoter. 33, 389-392. doi: 10.5581/1516-8484.20110104
    • (2011) Rev. Bras. Hematol. Hemoter. , vol.33 , pp. 389-392
    • Roberti Mdo, R.1    Borges Filho, H.M.2    Goncalves, C.H.3    Lima, F.L.4
  • 133
    • 84858015433 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease
    • doi: 10.1242/dmm.009019
    • Rouault, T. A. (2012). Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease. Dis. Model. Mech. 5, 155-164. doi: 10.1242/dmm.009019
    • (2012) Dis. Model. Mech. , vol.5 , pp. 155-164
    • Rouault, T.A.1
  • 134
    • 84880805523 scopus 로고    scopus 로고
    • Iron metabolism in the CNS: implications for neurodegenerative diseases
    • doi: 10.1038/nrn3453
    • Rouault, T. A. (2013). Iron metabolism in the CNS: implications for neurodegenerative diseases. Nat. Rev. Neurosci. 14, 551-564. doi: 10.1038/nrn3453
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 551-564
    • Rouault, T.A.1
  • 135
    • 84875757691 scopus 로고    scopus 로고
    • De novo mutations in the autophagy gene WDR45 cause static encephalopathy of childhood with neurodegeneration in adulthood
    • 449e1, doi: 10.1038/ng.2562
    • Saitsu, H., Nishimura, T., Muramatsu, K., Kodera, H., Kumada, S., Sugai, K., et al. (2013). De novo mutations in the autophagy gene WDR45 cause static encephalopathy of childhood with neurodegeneration in adulthood. Nat. Genet. 45, 445-449, 449e1. doi: 10.1038/ng.2562
    • (2013) Nat. Genet. , vol.45 , pp. 445-449
    • Saitsu, H.1    Nishimura, T.2    Muramatsu, K.3    Kodera, H.4    Kumada, S.5    Sugai, K.6
  • 136
    • 0027198736 scopus 로고
    • Production and characterization of recombinant heteropolymers of human ferritin H and L chains
    • Santambrogio, P., Levi, S., Cozzi, A., Rovida, E., Albertini, A., and Arosio, P. (1993). Production and characterization of recombinant heteropolymers of human ferritin H and L chains. J. Biol. Chem. 268, 12744-12748.
    • (1993) J. Biol. Chem. , vol.268 , pp. 12744-12748
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Rovida, E.4    Albertini, A.5    Arosio, P.6
  • 137
    • 77953338445 scopus 로고    scopus 로고
    • ATP13A2 mutations (PARK9) cause neurodegeneration with brain iron accumulation
    • doi: 10.1002/mds.22947
    • Schneider, S. A., Paisan-Ruiz, C., Quinn, N. P., Lees, A. J., Houlden, H., Hardy, J., et al. (2010). ATP13A2 mutations (PARK9) cause neurodegeneration with brain iron accumulation. Mov. Disord. 25, 979-984. doi: 10.1002/mds.22947
    • (2010) Mov. Disord. , vol.25 , pp. 979-984
    • Schneider, S.A.1    Paisan-Ruiz, C.2    Quinn, N.P.3    Lees, A.J.4    Houlden, H.5    Hardy, J.6
  • 138
    • 84885187866 scopus 로고    scopus 로고
    • Pathophysiology and treatment of neurodegeneration with brain iron accumulation in the pediatric population
    • doi: 10.1007/s11940-013-0254-5
    • Schneider, S. A., Zorzi, G., and Nardocci, N. (2013). Pathophysiology and treatment of neurodegeneration with brain iron accumulation in the pediatric population. Curr. Treat. Options Neurol. 15, 652-667. doi: 10.1007/s11940-013-0254-5
    • (2013) Curr. Treat. Options Neurol. , vol.15 , pp. 652-667
    • Schneider, S.A.1    Zorzi, G.2    Nardocci, N.3
  • 139
    • 84877010484 scopus 로고    scopus 로고
    • Atp13a2-deficient mice exhibit neuronal ceroid lipofuscinosis, limited a-synuclein accumulation and age-dependent sensorimotor deficits
    • doi: 10.1093/hmg/ddt057
    • Schultheis, P. J., Fleming, S. M., Clippinger, A. K., Lewis, J., Tsunemi, T., Giasson, B., et al. (2013). Atp13a2-deficient mice exhibit neuronal ceroid lipofuscinosis, limited a-synuclein accumulation and age-dependent sensorimotor deficits. Hum. Mol. Genet. 22, 2067-2082. doi: 10.1093/hmg/ddt057
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 2067-2082
    • Schultheis, P.J.1    Fleming, S.M.2    Clippinger, A.K.3    Lewis, J.4    Tsunemi, T.5    Giasson, B.6
  • 140
    • 80052923220 scopus 로고    scopus 로고
    • Iron efflux from oligodendrocytes is differentially regulated in gray and white matter
    • doi: 10.1523/JNEUROSCI.2838-11.2011
    • Schulz, K., Vulpe, C. D., Harris, L. Z., and David, S. (2011). Iron efflux from oligodendrocytes is differentially regulated in gray and white matter. J. Neurosci. 31, 13301-13311. doi: 10.1523/JNEUROSCI.2838-11.2011
    • (2011) J. Neurosci. , vol.31 , pp. 13301-13311
    • Schulz, K.1    Vulpe, C.D.2    Harris, L.Z.3    David, S.4
  • 141
    • 33746836946 scopus 로고    scopus 로고
    • Calcium-independent phospholipase A2 localizes in and protects mitochondria during apoptotic induction by staurosporine
    • doi: 10.1074/jbc.M604330200
    • Seleznev, K., Zhao, C., Zhang, X. H., Song, K., and Ma, Z. A. (2006). Calcium-independent phospholipase A2 localizes in and protects mitochondria during apoptotic induction by staurosporine. J. Biol. Chem. 281, 22275-22288. doi: 10.1074/jbc.M604330200
    • (2006) J. Biol. Chem. , vol.281 , pp. 22275-22288
    • Seleznev, K.1    Zhao, C.2    Zhang, X.H.3    Song, K.4    Ma, Z.A.5
  • 142
    • 0023780837 scopus 로고
    • Hallervorden-Spatz syndrome: clinical and magnetic resonance imaging correlations
    • doi: 10.1002/ana.410240519
    • Sethi, K. D., Adams, R. J., Loring, D. W., and el Gammal, T. (1988). Hallervorden-Spatz syndrome: clinical and magnetic resonance imaging correlations. Ann. Neurol. 24, 692-694. doi: 10.1002/ana.410240519
    • (1988) Ann. Neurol. , vol.24 , pp. 692-694
    • Sethi, K.D.1    Adams, R.J.2    Loring, D.W.3    el Gammal, T.4
  • 143
    • 39849101072 scopus 로고    scopus 로고
    • Neuroaxonal dystrophy caused by group VIA phospholipase A2 deficiency in mice: a model of human neurodegenerative disease
    • doi: 10.1523/JNEUROSCI.4354-07.2008
    • Shinzawa, K., Sumi, H., Ikawa, M., Matsuoka, Y., Okabe, M., Sakoda, S., et al. (2008). Neuroaxonal dystrophy caused by group VIA phospholipase A2 deficiency in mice: a model of human neurodegenerative disease. J. Neurosci. 28, 2212-2220. doi: 10.1523/JNEUROSCI.4354-07.2008
    • (2008) J. Neurosci. , vol.28 , pp. 2212-2220
    • Shinzawa, K.1    Sumi, H.2    Ikawa, M.3    Matsuoka, Y.4    Okabe, M.5    Sakoda, S.6
  • 144
    • 0347363475 scopus 로고    scopus 로고
    • PLA2 activity is required for nuclear shrinkage in caspase-independent cell death
    • doi: 10.1083/jcb.200306159
    • Shinzawa, K., and Tsujimoto, Y. (2003). PLA2 activity is required for nuclear shrinkage in caspase-independent cell death. J. Cell Biol. 163, 1219-1230. doi: 10.1083/jcb.200306159
    • (2003) J. Cell Biol. , vol.163 , pp. 1219-1230
    • Shinzawa, K.1    Tsujimoto, Y.2
  • 145
    • 84865066443 scopus 로고    scopus 로고
    • Cofilin/twinstar phosphorylation levels increase in response to impaired coenzyme a metabolism
    • doi: 10.1371/journal.pone.0043145
    • Siudeja, K., Grzeschik, N. A., Rana, A., de Jong, J., and Sibon, O. C. (2012). Cofilin/twinstar phosphorylation levels increase in response to impaired coenzyme a metabolism. PLoS ONE 7:e43145. doi: 10.1371/journal.pone.0043145
    • (2012) PLoS ONE , vol.7
    • Siudeja, K.1    Grzeschik, N.A.2    Rana, A.3    de Jong, J.4    Sibon, O.C.5
  • 146
    • 82955214822 scopus 로고    scopus 로고
    • Impaired coenzyme A metabolism affects histone and tubulin acetylation in Drosophila and human cell models of pantothenate kinase associated neurodegeneration
    • doi: 10.1002/emmm.201100180
    • Siudeja, K., Srinivasan, B., Xu, L., Rana, A., de Jong, J., Nollen, E. A., et al. (2011). Impaired coenzyme A metabolism affects histone and tubulin acetylation in Drosophila and human cell models of pantothenate kinase associated neurodegeneration. EMBO Mol. Med. 3, 755-766. doi: 10.1002/emmm.201100180
    • (2011) EMBO Mol. Med. , vol.3 , pp. 755-766
    • Siudeja, K.1    Srinivasan, B.2    Xu, L.3    Rana, A.4    de Jong, J.5    Nollen, E.A.6
  • 147
    • 41149150199 scopus 로고    scopus 로고
    • Aceruloplasminaemia with progressive atrophy without brain iron overload: treatment with oral chelation
    • doi: 10.1136/jnnp.2007.120568
    • Skidmore, F. M., Drago, V., Foster, P., Schmalfuss, I. M., Heilman, K. M., and Streiff, R. R. (2008). Aceruloplasminaemia with progressive atrophy without brain iron overload: treatment with oral chelation. J. Neurol. Neurosurg. Psychiatry 79, 467-470. doi: 10.1136/jnnp.2007.120568
    • (2008) J. Neurol. Neurosurg. Psychiatry , vol.79 , pp. 467-470
    • Skidmore, F.M.1    Drago, V.2    Foster, P.3    Schmalfuss, I.M.4    Heilman, K.M.5    Streiff, R.R.6
  • 148
  • 149
    • 84874207879 scopus 로고    scopus 로고
    • De novo FTL mutation: a clinical, neuroimaging, and molecular study
    • doi: 10.1002/mds.25275
    • Storti, E., Cortese, F., Di Fabio, R., Fiorillo, C., Pierallini, A., Tessa, A., et al. (2013). De novo FTL mutation: a clinical, neuroimaging, and molecular study. Mov. Disord. 28, 252-253. doi: 10.1002/mds.25275
    • (2013) Mov. Disord. , vol.28 , pp. 252-253
    • Storti, E.1    Cortese, F.2    Di Fabio, R.3    Fiorillo, C.4    Pierallini, A.5    Tessa, A.6
  • 150
    • 84861737424 scopus 로고    scopus 로고
    • Severe disturbance in the Ca2+ signaling in astrocytes from mouse models of human infantile neuroaxonal dystrophy with mutated Pla2g6
    • doi: 10.1093/hmg/dds108
    • Strokin, M., Seburn, K. L., Cox, G. A., Martens, K. A., and Reiser, G. (2012). Severe disturbance in the Ca2+ signaling in astrocytes from mouse models of human infantile neuroaxonal dystrophy with mutated Pla2g6. Hum. Mol. Genet. 21, 2807-2814. doi: 10.1093/hmg/dds108
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 2807-2814
    • Strokin, M.1    Seburn, K.L.2    Cox, G.A.3    Martens, K.A.4    Reiser, G.5
  • 151
    • 0023503525 scopus 로고
    • Mitochondrial synthesis of coenzyme A is on the external surface
    • doi: 10.1016/S0022-2828(87)80526-6
    • Tahiliani, A. G., and Neely, J. R. (1987). Mitochondrial synthesis of coenzyme A is on the external surface. J. Mol. Cell. Cardiol. 19, 1161-1167. doi: 10.1016/S0022-2828(87)80526-6
    • (1987) J. Mol. Cell. Cardiol. , vol.19 , pp. 1161-1167
    • Tahiliani, A.G.1    Neely, J.R.2
  • 152
    • 80051949129 scopus 로고    scopus 로고
    • Regulation of intracellular manganese homeostasis by Kufor-Rakeb syndrome-associated ATP13A2 protein
    • doi: 10.1074/jbc.M111.233874
    • Tan, J., Zhang, T., Jiang, L., Chi, J., Hu, D., Pan, Q., et al. (2011). Regulation of intracellular manganese homeostasis by Kufor-Rakeb syndrome-associated ATP13A2 protein. J. Biol. Chem. 286, 29654-29662. doi: 10.1074/jbc.M111.233874
    • (2011) J. Biol. Chem. , vol.286 , pp. 29654-29662
    • Tan, J.1    Zhang, T.2    Jiang, L.3    Chi, J.4    Hu, D.5    Pan, Q.6
  • 153
    • 0030964780 scopus 로고    scopus 로고
    • A novel cytosolic calcium-independent phospholipase A2 contains eight ankyrin motifs
    • doi: 10.1074/jbc.272.13.8567
    • Tang, J., Kriz, R. W., Wolfman, N., Shaffer, M., Seehra, J., and Jones, S. S. (1997). A novel cytosolic calcium-independent phospholipase A2 contains eight ankyrin motifs. J. Biol. Chem. 272, 8567-8575. doi: 10.1074/jbc.272.13.8567
    • (1997) J. Biol. Chem. , vol.272 , pp. 8567-8575
    • Tang, J.1    Kriz, R.W.2    Wolfman, N.3    Shaffer, M.4    Seehra, J.5    Jones, S.S.6
  • 154
    • 83855165109 scopus 로고    scopus 로고
    • Ceruloplasmin deficiency results in an anxiety phenotype involving deficits in hippocampal iron, serotonin, and BDNF
    • doi: 10.1111/j.1471-4159.2011.07554.x
    • Texel, S. J., Camandola, S., Ladenheim, B., Rothman, S. M., Mughal, M. R., Unger, E. L., et al. (2012). Ceruloplasmin deficiency results in an anxiety phenotype involving deficits in hippocampal iron, serotonin, and BDNF. J. Neurochem. 120, 125-134. doi: 10.1111/j.1471-4159.2011.07554.x
    • (2012) J. Neurochem. , vol.120 , pp. 125-134
    • Texel, S.J.1    Camandola, S.2    Ladenheim, B.3    Rothman, S.M.4    Mughal, M.R.5    Unger, E.L.6
  • 155
    • 84899971096 scopus 로고    scopus 로고
    • Zn2+ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation
    • doi: 10.1093/hmg/ddt572 [Epub ahead of print]
    • Tsunemi, T., and Krainc, D. (2013). Zn2+ dyshomeostasis caused by loss of ATP13A2/PARK9 leads to lysosomal dysfunction and alpha-synuclein accumulation. Hum Mol. Genet. doi: 10.1093/hmg/ddt572 [Epub ahead of print].
    • (2013) Hum Mol. Genet.
    • Tsunemi, T.1    Krainc, D.2
  • 156
    • 84858403126 scopus 로고    scopus 로고
    • Deficiency of ATP13A2 leads to lysosomal dysfunction, a-synuclein accumulation, and neurotoxicity
    • doi: 10.1523/JNEUROSCI.5575-11.2012
    • Usenovic, M., Tresse, E., Mazzulli, J. R., Taylor, J. P., and Krainc, D. (2012). Deficiency of ATP13A2 leads to lysosomal dysfunction, a-synuclein accumulation, and neurotoxicity. J. Neurosci. 32, 4240-4246. doi: 10.1523/JNEUROSCI.5575-11.2012
    • (2012) J. Neurosci. , vol.32 , pp. 4240-4246
    • Usenovic, M.1    Tresse, E.2    Mazzulli, J.R.3    Taylor, J.P.4    Krainc, D.5
  • 157
    • 12144288949 scopus 로고    scopus 로고
    • Intracellular ferritin accumulation in neural and extraneural tissue characterizes a neurodegenerative disease associated with a mutation in the ferritin light polypeptide gene
    • Vidal, R., Ghetti, B., Takao, M., Brefel-Courbon, C., Uro-Coste, E., Glazier, B. S., et al. (2004). Intracellular ferritin accumulation in neural and extraneural tissue characterizes a neurodegenerative disease associated with a mutation in the ferritin light polypeptide gene. J. Neuropathol. Exp. Neurol. 63, 363-380.
    • (2004) J. Neuropathol. Exp. Neurol. , vol.63 , pp. 363-380
    • Vidal, R.1    Ghetti, B.2    Takao, M.3    Brefel-Courbon, C.4    Uro-Coste, E.5    Glazier, B.S.6
  • 158
    • 38149140232 scopus 로고    scopus 로고
    • Expression of a mutant form of the ferritin light chain gene induces neurodegeneration and iron overload in transgenic mice
    • doi: 10.1523/JNEUROSCI.3962-07.2008
    • Vidal, R., Miravalle, L., Gao, X., Barbeito, A. G., Baraibar, M. A., Hekmatyar, S. K., et al. (2008). Expression of a mutant form of the ferritin light chain gene induces neurodegeneration and iron overload in transgenic mice. J. Neurosci. 28, 60-67. doi: 10.1523/JNEUROSCI.3962-07.2008
    • (2008) J. Neurosci. , vol.28 , pp. 60-67
    • Vidal, R.1    Miravalle, L.2    Gao, X.3    Barbeito, A.G.4    Baraibar, M.A.5    Hekmatyar, S.K.6
  • 159
    • 73549116096 scopus 로고    scopus 로고
    • Establishment of an improved mouse model for infantile neuroaxonal dystrophy that shows early disease onset and bears a point mutation in Pla2g6
    • doi: 10.2353/ajpath.2009.090343
    • Wada, H., Yasuda, T., Miura, I., Watabe, K., Sawa, C., Kamijuku, H., et al. (2009). Establishment of an improved mouse model for infantile neuroaxonal dystrophy that shows early disease onset and bears a point mutation in Pla2g6. Am. J. Pathol. 175, 2257-2263. doi: 10.2353/ajpath.2009.090343
    • (2009) Am. J. Pathol. , vol.175 , pp. 2257-2263
    • Wada, H.1    Yasuda, T.2    Miura, I.3    Watabe, K.4    Sawa, C.5    Kamijuku, H.6
  • 160
    • 0033953962 scopus 로고    scopus 로고
    • Juvenile-onset generalized neuroaxonal dystrophy (Hallervorden-Spatz disease) with diffuse neurofibrillary and Lewy body pathology
    • doi: 10.1007/s004010050049
    • Wakabayashi, K., Fukushima, T., Koide, R., Horikawa, Y., Hasegawa, M., Watanabe, Y., et al. (2000). Juvenile-onset generalized neuroaxonal dystrophy (Hallervorden-Spatz disease) with diffuse neurofibrillary and Lewy body pathology. Acta Neuropathol. 99, 331-336. doi: 10.1007/s004010050049
    • (2000) Acta Neuropathol. , vol.99 , pp. 331-336
    • Wakabayashi, K.1    Fukushima, T.2    Koide, R.3    Horikawa, Y.4    Hasegawa, M.5    Watanabe, Y.6
  • 161
    • 34250014148 scopus 로고    scopus 로고
    • Ferroportin1 and hephaestin are involved in the nigral iron accumulation of 6-OHDA-lesioned rats
    • doi: 10.1111/j.1460-9568.2007.05515.x
    • Wang, J., Jiang, H., and Xie, J. X. (2007). Ferroportin1 and hephaestin are involved in the nigral iron accumulation of 6-OHDA-lesioned rats. Eur. J. Neurosci. 25, 2766-2772. doi: 10.1111/j.1460-9568.2007.05515.x
    • (2007) Eur. J. Neurosci. , vol.25 , pp. 2766-2772
    • Wang, J.1    Jiang, H.2    Xie, J.X.3
  • 162
    • 0037083892 scopus 로고    scopus 로고
    • Inhibition of mitochondrial calcium-independent phospholipase A2 (iPLA2) attenuates mitochondrial phospholipid loss and is cardioprotective
    • doi: 10.1042/0264-6021:3620023
    • Williams, S. D., and Gottlieb, R. A. (2002). Inhibition of mitochondrial calcium-independent phospholipase A2 (iPLA2) attenuates mitochondrial phospholipid loss and is cardioprotective. Biochem. J. 362(Pt 1), 23-32. doi: 10.1042/0264-6021:3620023
    • (2002) Biochem. J. , vol.362 , Issue.PT. 1 , pp. 23-32
    • Williams, S.D.1    Gottlieb, R.A.2
  • 163
    • 0036298867 scopus 로고    scopus 로고
    • Palatal tremor and cognitive decline in neuroferritinopathy
    • doi: 10.1136/jnnp.73.1.91
    • Wills, A. J., Sawle, G. V., Guilbert, P. R., and Curtis, A. R. (2002). Palatal tremor and cognitive decline in neuroferritinopathy. J. Neurol. Neurosurg. Psychiatry 73, 91-92. doi: 10.1136/jnnp.73.1.91
    • (2002) J. Neurol. Neurosurg. Psychiatry , vol.73 , pp. 91-92
    • Wills, A.J.1    Sawle, G.V.2    Guilbert, P.R.3    Curtis, A.R.4
  • 164
    • 0034739445 scopus 로고    scopus 로고
    • Calcium-independent phospholipase A(2): structure and function
    • doi: 10.1016/S1388-1981(00)00107-4
    • Winstead, M. V., Balsinde, J., and Dennis, E. A. (2000). Calcium-independent phospholipase A(2): structure and function. Biochim. Biophys. Acta 1488, 28-39. doi: 10.1016/S1388-1981(00)00107-4
    • (2000) Biochim. Biophys. Acta , vol.1488 , pp. 28-39
    • Winstead, M.V.1    Balsinde, J.2    Dennis, E.A.3
  • 165
    • 84859085424 scopus 로고    scopus 로고
    • Ferroxidase hephaestin's cell-autonomous role in the retinal pigment epithelium
    • doi: 10.1016/j.ajpath.2011.12.041
    • Wolkow, N., Song, D., Song, Y., Chu, S., Hadziahmetovic, M., Lee, J. C., et al. (2012). Ferroxidase hephaestin's cell-autonomous role in the retinal pigment epithelium. Am. J. Pathol. 180, 1614-1624. doi: 10.1016/j.ajpath.2011.12.041
    • (2012) Am. J. Pathol. , vol.180 , pp. 1614-1624
    • Wolkow, N.1    Song, D.2    Song, Y.3    Chu, S.4    Hadziahmetovic, M.5    Lee, J.C.6
  • 166
    • 58349116105 scopus 로고    scopus 로고
    • Clinical study and PLA2G6 mutation screening analysis in Chinese patients with infantile neuroaxonal dystrophy
    • doi: 10.1111/j.1468-1331.2008.02397.x
    • Wu, Y., Jiang, Y., Gao, Z., Wang, J., Yuan, Y., Xiong, H., et al. (2009a). Clinical study and PLA2G6 mutation screening analysis in Chinese patients with infantile neuroaxonal dystrophy. Eur. J. Neurol. 16, 240-245. doi: 10.1111/j.1468-1331.2008.02397.x
    • (2009) Eur. J. Neurol. , vol.16 , pp. 240-245
    • Wu, Y.1    Jiang, Y.2    Gao, Z.3    Wang, J.4    Yuan, Y.5    Xiong, H.6
  • 167
    • 70350774174 scopus 로고    scopus 로고
    • Pantothenate kinase-associated neurodegeneration: insights from a Drosophila model
    • doi: 10.1093/hmg/ddp314
    • Wu, Z., Li, C., Lv, S., and Zhou, B. (2009b). Pantothenate kinase-associated neurodegeneration: insights from a Drosophila model. Hum. Mol. Genet. 18, 3659-3672. doi: 10.1093/hmg/ddp314
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 3659-3672
    • Wu, Z.1    Li, C.2    Lv, S.3    Zhou, B.4
  • 168
    • 0037069742 scopus 로고    scopus 로고
    • Quantitative evaluation of expression of iron-metabolism genes in ceruloplasmin-deficient mice
    • doi: 10.1016/S0925-4439(02)00165-5
    • Yamamoto, K., Yoshida, K., Miyagoe, Y., Ishikawa, A., Hanaoka, K., Nomoto, S., et al. (2002). Quantitative evaluation of expression of iron-metabolism genes in ceruloplasmin-deficient mice. Biochim. Biophys. Acta 1588, 195-202. doi: 10.1016/S0925-4439(02)00165-5
    • (2002) Biochim. Biophys. Acta , vol.1588 , pp. 195-202
    • Yamamoto, K.1    Yoshida, K.2    Miyagoe, Y.3    Ishikawa, A.4    Hanaoka, K.5    Nomoto, S.6
  • 169
    • 0344848566 scopus 로고    scopus 로고
    • Group-specific assays that distinguish between the four major types of mammalian phospholipase A2
    • doi: 10.1006/abio.1999.4053
    • Yang, H. C., Mosior, M., Johnson, C. A., Chen, Y., and Dennis, E. A. (1999). Group-specific assays that distinguish between the four major types of mammalian phospholipase A2. Anal. Biochem. 269, 278-288. doi: 10.1006/abio.1999.4053
    • (1999) Anal. Biochem. , vol.269 , pp. 278-288
    • Yang, H.C.1    Mosior, M.2    Johnson, C.A.3    Chen, Y.4    Dennis, E.A.5
  • 170
    • 0028895749 scopus 로고
    • A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans
    • doi: 10.1038/ng0395-267
    • Yoshida, K., Furihata, K., Takeda, S., Nakamura, A., Yamamoto, K., Morita, H., et al. (1995). A mutation in the ceruloplasmin gene is associated with systemic hemosiderosis in humans. Nat. Genet. 9, 267-272. doi: 10.1038/ng0395-267
    • (1995) Nat. Genet. , vol.9 , pp. 267-272
    • Yoshida, K.1    Furihata, K.2    Takeda, S.3    Nakamura, A.4    Yamamoto, K.5    Morita, H.6
  • 171
    • 33645742041 scopus 로고    scopus 로고
    • Disruption of G1-phase phospholipid turnover by inhibition of Ca2+-independent phospholipase A2 induces a p53-dependent cell-cycle arrest in G1 phase
    • doi: 10.1242/jcs.02821
    • Zhang, X. H., Zhao, C., Seleznev, K., Song, K., Manfredi, J. J., and Ma, Z. A. (2006a). Disruption of G1-phase phospholipid turnover by inhibition of Ca2+-independent phospholipase A2 induces a p53-dependent cell-cycle arrest in G1 phase. J. Cell Sci. 119(Pt 6), 1005-1015. doi: 10.1242/jcs.02821
    • (2006) J. Cell Sci. , vol.119 , Issue.PT. 6 , pp. 1005-1015
    • Zhang, X.H.1    Zhao, C.2    Seleznev, K.3    Song, K.4    Manfredi, J.J.5    Ma, Z.A.6
  • 172
    • 33644864274 scopus 로고    scopus 로고
    • Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration
    • doi: 10.1074/jbc.M508825200
    • Zhang, Y. M., Rock, C. O., and Jackowski, S. (2006b). Biochemical properties of human pantothenate kinase 2 isoforms and mutations linked to pantothenate kinase-associated neurodegeneration. J. Biol. Chem. 281, 107-114. doi: 10.1074/jbc.M508825200
    • (2006) J. Biol. Chem. , vol.281 , pp. 107-114
    • Zhang, Y.M.1    Rock, C.O.2    Jackowski, S.3
  • 173
    • 0034935036 scopus 로고    scopus 로고
    • A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome
    • doi: 10.1038/ng572
    • Zhou, B., Westaway, S. K., Levinson, B., Johnson, M. A., Gitschier, J., and Hayflick, S. J. (2001). A novel pantothenate kinase gene (PANK2) is defective in Hallervorden-Spatz syndrome. Nat. Genet. 28, 345-349. doi: 10.1038/ng572
    • (2001) Nat. Genet. , vol.28 , pp. 345-349
    • Zhou, B.1    Westaway, S.K.2    Levinson, B.3    Johnson, M.A.4    Gitschier, J.5    Hayflick, S.J.6
  • 175
    • 55749103552 scopus 로고    scopus 로고
    • Absence of 2-hydroxylated sphingolipids is compatible with normal neural development but causes late-onset axon and myelin sheath degeneration
    • doi: 10.1523/JNEUROSCI.0458-08.2008
    • Zöller, I., Meixner, M., Hartmann, D., Büssow, H., Meyer, R., Gieselmann, V., et al. (2008). Absence of 2-hydroxylated sphingolipids is compatible with normal neural development but causes late-onset axon and myelin sheath degeneration. J. Neurosci. 28, 9741-9754. doi: 10.1523/JNEUROSCI.0458-08.2008
    • (2008) J. Neurosci. , vol.28 , pp. 9741-9754
    • Zöller, I.1    Meixner, M.2    Hartmann, D.3    Büssow, H.4    Meyer, R.5    Gieselmann, V.6
  • 176
    • 79961210514 scopus 로고    scopus 로고
    • Iron-related MRI images in patients with pantothenate kinase-associated neurodegeneration (PKAN) treated with deferiprone: results of a phase II pilot trial
    • doi: 10.1002/mds.23751
    • Zorzi, G., Zibordi, F., Chiapparini, L., Bertini, E., Russo, L., Piga, A., et al. (2011). Iron-related MRI images in patients with pantothenate kinase-associated neurodegeneration (PKAN) treated with deferiprone: results of a phase II pilot trial. Mov. Disord. 26, 1756-1759. doi: 10.1002/mds.23751
    • (2011) Mov. Disord. , vol.26 , pp. 1756-1759
    • Zorzi, G.1    Zibordi, F.2    Chiapparini, L.3    Bertini, E.4    Russo, L.5    Piga, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.