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Volumn 1012, Issue , 2004, Pages 326-341

Novel chelators for central nervous system disorders that involve alterations in the metabolism of iron and other metal ions

Author keywords

2 pyridylcarboxaldehyde isonicotinoyl hydrazone; Alzheimer's disease; Clioquinol; Friedreich's ataxia; Huntington's disease; Iron; Iron chelators; Iron metabolism; Parkinson's disease; Pyridoxal isonicotinoyl hydrazone

Indexed keywords

2 PYRIDYLCARBOXALDEHYDE ISONICOTINOYLHYDRAZONE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; CHELATING AGENT; CLIOQUINOL; DEFEROXAMINE; HYDRAZONE DERIVATIVE; IRON; IRON CHELATING AGENT; METAL ION; PYRIDOXAL ISONICOTINOYLHYDRAZONE; UNCLASSIFIED DRUG;

EID: 1842608741     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1196/annals.1306.026     Document Type: Review
Times cited : (94)

References (88)
  • 1
    • 0027435899 scopus 로고
    • Iron induced oxidative stress and mitochondrial dysfunction: Relevance to Parkinson's disease
    • HARLEY, A. et al. 1993. Iron induced oxidative stress and mitochondrial dysfunction: relevance to Parkinson's disease. Brain Res. 627: 349-353.
    • (1993) Brain Res. , vol.627 , pp. 349-353
    • Harley, A.1
  • 2
    • 0032975570 scopus 로고    scopus 로고
    • The role of iron in neurodegeneration: Prospects for pharmacotherapy of Parkinson's disease
    • JELLINGER, K.A. 1999. The role of iron in neurodegeneration: prospects for pharmacotherapy of Parkinson's disease. Drugs Aging 14: 115-140.
    • (1999) Drugs Aging , vol.14 , pp. 115-140
    • Jellinger, K.A.1
  • 3
    • 1642555537 scopus 로고    scopus 로고
    • Iron involvement in neural damage and microgliosis in models of neurodegenerative diseases
    • SHOHAM, S. & M.B. YOUDIM. 2000. Iron involvement in neural damage and microgliosis in models of neurodegenerative diseases. Cell. Mol. Biol. 46: 743-760.
    • (2000) Cell. Mol. Biol. , vol.46 , pp. 743-760
    • Shoham, S.1    Youdim, M.B.2
  • 4
    • 0031001278 scopus 로고    scopus 로고
    • Iron chelating therapy and the treatment of thalassemia
    • OLIVIERI, N.F. & G. BRITTENHAM. 1997. Iron chelating therapy and the treatment of thalassemia. Blood 89: 739-761.
    • (1997) Blood , vol.89 , pp. 739-761
    • Olivieri, N.F.1    Brittenham, G.2
  • 5
    • 0037411115 scopus 로고    scopus 로고
    • β-Thalassaemia: Emergence of new and improved chelators for treatment
    • WONG, C. & D.R. RICHARDSON. 2003. β-Thalassaemia: emergence of new and improved chelators for treatment. Int. J. Biochem. Cell Biol. 35: 1144-1149.
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 1144-1149
    • Wong, C.1    Richardson, D.R.2
  • 6
    • 0000723121 scopus 로고    scopus 로고
    • Iron transport in the central nervous system
    • Dekker. New York
    • BURDO, J.R. & J.R. CONNOR. 2002. Iron transport in the central nervous system. In Molecular and Cellular Iron Transport, pp. 487-508. Dekker. New York.
    • (2002) Molecular and Cellular Iron Transport , pp. 487-508
    • Burdo, J.R.1    Connor, J.R.2
  • 7
    • 0031567095 scopus 로고    scopus 로고
    • The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells
    • RICHARDSON, D.R. & P. PONKA. 1997. The molecular mechanisms of the metabolism and transport of iron in normal and neoplastic cells. Biochim. Biophys. Acta 1331: 1-40.
    • (1997) Biochim. Biophys. Acta , vol.1331 , pp. 1-40
    • Richardson, D.R.1    Ponka, P.2
  • 8
    • 0019860059 scopus 로고
    • Transferrin biochemistry, physiology, and clinical significance
    • MORGAN, E. 1981. Transferrin biochemistry, physiology, and clinical significance. Mol. Aspects Med. 4: 1-123.
    • (1981) Mol. Aspects Med. , vol.4 , pp. 1-123
    • Morgan, E.1
  • 9
    • 0030755366 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian proton-coupled metal-ion transporter
    • GUNSHIN, H. et al. 1997. Cloning and characterization of a mammalian proton-coupled metal-ion transporter. Nature 388: 482-488.
    • (1997) Nature , vol.388 , pp. 482-488
    • Gunshin, H.1
  • 10
    • 0030763856 scopus 로고    scopus 로고
    • Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene
    • FLEMING, M.D. et al. 1997. Microcytic anaemia mice have a mutation in Nramp2, a candidate iron transporter gene. Nat. Genet. 16: 383-386.
    • (1997) Nat. Genet. , vol.16 , pp. 383-386
    • Fleming, M.D.1
  • 11
    • 0021130764 scopus 로고
    • Transferrin receptor on endothelium of brain capillaries
    • JEFFERIES, W.A. et al. 1984. Transferrin receptor on endothelium of brain capillaries. Nature 312: 162-163.
    • (1984) Nature , vol.312 , pp. 162-163
    • Jefferies, W.A.1
  • 12
    • 0023547088 scopus 로고
    • Receptor-mediated transcytosis of transferrin across the blood brain barrier
    • FISHMAN, J.B. et al. 1987. Receptor-mediated transcytosis of transferrin across the blood brain barrier. J. Neurosci. Res. 18: 299-304.
    • (1987) J. Neurosci. Res. , vol.18 , pp. 299-304
    • Fishman, J.B.1
  • 13
    • 0027535206 scopus 로고
    • Receptor-mediated endocytosis of transferrin at the blood-brain barrier
    • ROBERTS, R.L. et al. 1993. Receptor-mediated endocytosis of transferrin at the blood-brain barrier. J. Cell. Sci. 104: 521-532.
    • (1993) J. Cell. Sci. , vol.104 , pp. 521-532
    • Roberts, R.L.1
  • 14
    • 0025354340 scopus 로고
    • Developmental changes in transferrin and iron uptake by the brain in the rat
    • TAYLOR, E.M. & E.H. MORGAN. 1990. Developmental changes in transferrin and iron uptake by the brain in the rat. Dev. Brain Res. 55: 35-42.
    • (1990) Dev. Brain Res. , vol.55 , pp. 35-42
    • Taylor, E.M.1    Morgan, E.H.2
  • 15
    • 0033597780 scopus 로고    scopus 로고
    • Molecular cloning of transferrin receptor 2: A new member of the transferrin receptor-like family
    • KAWABATA, H. et al. 1999. Molecular cloning of transferrin receptor 2: a new member of the transferrin receptor-like family. J. Biol. Chem. 274: 20826-20832.
    • (1999) J. Biol. Chem. , vol.274 , pp. 20826-20832
    • Kawabata, H.1
  • 16
    • 0034595856 scopus 로고    scopus 로고
    • Transferrin receptor 2-α supports cell growth both in iron-chelated cultured cells and in vivo
    • KAWABATA, H. et al. 2000. Transferrin receptor 2-α supports cell growth both in iron-chelated cultured cells and in vivo. J. Biol. Chem. 275: 16618-16625.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16618-16625
    • Kawabata, H.1
  • 17
    • 0027944830 scopus 로고
    • Two saturable mechanisms of iron uptake from transferrin in human melanoma cells: The effect of transferrin concentration, chelators, and metabolic probes on transferrin and iron uptake
    • RICHARDSON, D.R. & E. BAKER. 1994. Two saturable mechanisms of iron uptake from transferrin in human melanoma cells: the effect of transferrin concentration, chelators, and metabolic probes on transferrin and iron uptake. J. Cell. Physiol. 161: 160-168.
    • (1994) J. Cell. Physiol. , vol.161 , pp. 160-168
    • Richardson, D.R.1    Baker, E.2
  • 18
    • 0029953577 scopus 로고    scopus 로고
    • Transferrin receptor-independent uptake of diferric transferrin by human hepatoma cells with antisense inhibition of receptor expression
    • TRINDER, D. et al. 1996. Transferrin receptor-independent uptake of diferric transferrin by human hepatoma cells with antisense inhibition of receptor expression. Hepatology 23: 1512-1520.
    • (1996) Hepatology , vol.23 , pp. 1512-1520
    • Trinder, D.1
  • 19
    • 0017700831 scopus 로고
    • Low molecular weight intracellular iron transport compounds
    • JACOBS, A. 1977. Low molecular weight intracellular iron transport compounds. Blood 50: 433-439.
    • (1977) Blood , vol.50 , pp. 433-439
    • Jacobs, A.1
  • 20
    • 0032533549 scopus 로고    scopus 로고
    • Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts
    • RADISKY, D.C. & J. KAPLAN. 1998, Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts. Biochem. J. 336: 201-205.
    • (1998) Biochem. J. , vol.336 , pp. 201-205
    • Radisky, D.C.1    Kaplan, J.2
  • 21
    • 0029865751 scopus 로고    scopus 로고
    • Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: Examination of the intermediates involved in iron metabolism
    • RICHARDSON, D.R. et al. 1996. Distribution of iron in reticulocytes after inhibition of heme synthesis with succinylacetone: examination of the intermediates involved in iron metabolism. Blood 87: 3477-3488.
    • (1996) Blood , vol.87 , pp. 3477-3488
    • Richardson, D.R.1
  • 22
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function, and cellular regulation
    • HARRISON, P.M. & P. AROSIO. 1996. The ferritins: molecular properties, iron storage function, and cellular regulation. Biochim. Biophys. Acta 1275: 161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 23
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
    • HENTZE, M.W. & L.C. KÜHN. 1996. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci. USA 93: 8175-8182.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kühn, L.C.2
  • 24
    • 0037316787 scopus 로고    scopus 로고
    • Huntingtin in health and disease
    • YOUNG, A.B. 2003. Huntingtin in health and disease. J. Clin. Invest. 111: 299-302.
    • (2003) J. Clin. Invest. , vol.111 , pp. 299-302
    • Young, A.B.1
  • 25
    • 0034703860 scopus 로고    scopus 로고
    • Huntingtin: An iron regulated protein essential for normal nuclear and perinuclear organelles
    • HILDITCH-MAGUIRE, P. et al. 2000. Huntingtin: an iron regulated protein essential for normal nuclear and perinuclear organelles. Hum. Mol. Genet. 9: 2789-2797.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 2789-2797
    • Hilditch-Maguire, P.1
  • 26
    • 0036048876 scopus 로고    scopus 로고
    • Recent developments in the pathology of Parkinson's disease
    • JELLINGER, K.A. 2002. Recent developments in the pathology of Parkinson's disease. J. Neural Transm. Suppl. 62: 347-376.
    • (2002) J. Neural Transm. Suppl. , vol.62 , pp. 347-376
    • Jellinger, K.A.1
  • 27
    • 0036591852 scopus 로고    scopus 로고
    • Formation of hydrogen peroxide and hydroxyl radicals from A(beta) and alpha-synuclein as a possible mechanism of cell death in Alzheimer's disease and Parkinson's disease
    • TABNER, B.J. et al. 2002. Formation of hydrogen peroxide and hydroxyl radicals from A(beta) and alpha-synuclein as a possible mechanism of cell death in Alzheimer's disease and Parkinson's disease. Free Radical Biol. Med. 32: 1076-1083.
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 1076-1083
    • Tabner, B.J.1
  • 28
    • 0036152892 scopus 로고    scopus 로고
    • Iron and Parkinson's disease
    • WOLOZIN, B. & N. GOLTS. 2002. Iron and Parkinson's disease. Neuroscientist 8: 22-32.
    • (2002) Neuroscientist , vol.8 , pp. 22-32
    • Wolozin, B.1    Golts, N.2
  • 29
    • 0036670712 scopus 로고    scopus 로고
    • Aggregation and neurotoxicity of alpha-synuclein and related peptides
    • EL-AGNAF, O.M. & G.B. IRVINE. 2002. Aggregation and neurotoxicity of alpha-synuclein and related peptides. Biochem. Soc. Trans. 30: 559-565.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 559-565
    • El-Agnaf, O.M.1    Irvine, G.B.2
  • 30
    • 0036798434 scopus 로고    scopus 로고
    • Lack of up-regulatjon of ferritin is associated with sustained iron regulatory protein-1 binding activity in the substantia nigra of patients with Parkinson's disease
    • FAUCHEUX, B.A. et al. 2002. Lack of up-regulatjon of ferritin is associated with sustained iron regulatory protein-1 binding activity in the substantia nigra of patients with Parkinson's disease. J. Neurochem. 83: 320-330.
    • (2002) J. Neurochem. , vol.83 , pp. 320-330
    • Faucheux, B.A.1
  • 31
    • 0037216723 scopus 로고    scopus 로고
    • Mouse brains deficient in H-ferritin have normal iron concentration, but a protein profile of iron deficiency and increased evidence of oxidative stress
    • THOMPSON, K. et al. 2003. Mouse brains deficient in H-ferritin have normal iron concentration, but a protein profile of iron deficiency and increased evidence of oxidative stress. J. Neurosci. Res. 71: 46-63.
    • (2003) J. Neurosci. Res. , vol.71 , pp. 46-63
    • Thompson, K.1
  • 32
    • 0035138456 scopus 로고    scopus 로고
    • Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice
    • LAVAUTE, T. et al. 2001. Targeted deletion of the gene encoding iron regulatory protein-2 causes misregulation of iron metabolism and neurodegenerative disease in mice. Nat. Genet. 27: 209-214.
    • (2001) Nat. Genet. , vol.27 , pp. 209-214
    • LaVaute, T.1
  • 33
    • 0036869157 scopus 로고    scopus 로고
    • Polymorphisms in iron-responsive binding protein 2 and lack of association with sporadic Parkinson's disease
    • LEE, P.L. et al. 2002. Polymorphisms in iron-responsive binding protein 2 and lack of association with sporadic Parkinson's disease. Mov. Disord. 17: 1302-1304.
    • (2002) Mov. Disord. , vol.17 , pp. 1302-1304
    • Lee, P.L.1
  • 34
    • 0036306510 scopus 로고    scopus 로고
    • Association study between iron-related genes polymorphisms and Parkinson's disease
    • BORIE, C. et al. 2002. Association study between iron-related genes polymorphisms and Parkinson's disease. J. Neurol. 249: 801-804.
    • (2002) J. Neurol. , vol.249 , pp. 801-804
    • Borie, C.1
  • 35
    • 0035941201 scopus 로고    scopus 로고
    • Metal triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein: A possible molecular NK between Parkinson's disease and heavy metal exposure
    • UVERSKY, V.N. et al. 2001. Metal triggered structural transformations, aggregation, and fibrillation of human alpha-synuclein: a possible molecular NK between Parkinson's disease and heavy metal exposure. J. Biol. Chem. 276: 44284-44296.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1
  • 36
    • 0035241245 scopus 로고    scopus 로고
    • Neuroimaging in basal ganglia disorders: Perspectives for transcranial ultrasound
    • BECKER, G. & D. BERG. 2001. Neuroimaging in basal ganglia disorders: perspectives for transcranial ultrasound. Mov. Disord. 16: 23-32.
    • (2001) Mov. Disord. , vol.16 , pp. 23-32
    • Becker, G.1    Berg, D.2
  • 37
    • 0035227581 scopus 로고    scopus 로고
    • Do alterations in glutathione and iron levels contribute to pathology associated with Parkinson's disease?
    • ANDERSEN, J.K. 2001. Do alterations in glutathione and iron levels contribute to pathology associated with Parkinson's disease? Novartis Found. Symp. 235: 11-20.
    • (2001) Novartis Found. Symp. , vol.235 , pp. 11-20
    • Andersen, J.K.1
  • 38
    • 0037188472 scopus 로고    scopus 로고
    • The galvanization of β-amyloid in Alzheimer's disease
    • BUSH, A.I. & R.E. TANZI. 2002. The galvanization of β-amyloid in Alzheimer's disease. Proc. Natl. Acad. Sci. USA 99: 7317-7319.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7317-7319
    • Bush, A.I.1    Tanzi, R.E.2
  • 39
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of purification and characterization of a novel cerebrovascular protein
    • GLENNER, G.G. & C.W. WONG. 1984. Alzheimer's disease: initial report of purification and characterization of a novel cerebrovascular protein. Biochem. Biophys. Res. Commun. 120: 885-890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 40
    • 0029063033 scopus 로고
    • Amyloid beta-binding protein in vitro and in normal human cerebrospinal fluid
    • GOLABECK, A. et al. 1995. Amyloid beta-binding protein in vitro and in normal human cerebrospinal fluid. Neurosci. Lett. 191: 79-82.
    • (1995) Neurosci. Lett. , vol.191 , pp. 79-82
    • Golabeck, A.1
  • 41
    • 0033986037 scopus 로고    scopus 로고
    • Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains
    • SU, S.W. et al. 2000. Histochemically-reactive zinc in amyloid plaques, angiopathy, and degenerating neurons of Alzheimer's diseased brains. Brain Res. 852: 274-278.
    • (2000) Brain Res. , vol.852 , pp. 274-278
    • Su, S.W.1
  • 42
    • 0033855331 scopus 로고    scopus 로고
    • Chelation and intercalation: Complementary properties in a compound for the treatment of Alzheimer's disease
    • CHERNY, R.A. et al. 2000. Chelation and intercalation: complementary properties in a compound for the treatment of Alzheimer's disease. J. Struct. Biol. 130: 209-216.
    • (2000) J. Struct. Biol. , vol.130 , pp. 209-216
    • Cherny, R.A.1
  • 43
    • 0034964390 scopus 로고    scopus 로고
    • Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice
    • CHERNY, R.A. et al. 2002. Treatment with a copper-zinc chelator markedly and rapidly inhibits beta-amyloid accumulation in Alzheimer's disease transgenic mice. Neuron 30: 665-676.
    • (2002) Neuron , vol.30 , pp. 665-676
    • Cherny, R.A.1
  • 44
    • 0032557425 scopus 로고    scopus 로고
    • Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis
    • ATWODD, C.S. et al. 1998. Dramatic aggregation of Alzheimer Aβ by Cu(II) is induced by conditions representing physiological acidosis. J. Biol. Chem. 273: 12817-12826.
    • (1998) J. Biol. Chem. , vol.273 , pp. 12817-12826
    • Atwodd, C.S.1
  • 45
    • 0033844944 scopus 로고    scopus 로고
    • Characterization of copper interactions with Alzheimer amyloid beta peptides: Identification of an attomolar-affinity copper binding site on amyloid beta 1-42
    • ATWODD, C.S. et al. 2000. Characterization of copper interactions with Alzheimer amyloid beta peptides: identification of an attomolar-affinity copper binding site on amyloid beta 1-42. J. Neurochem. 75: 1219-1233.
    • (2000) J. Neurochem. , vol.75 , pp. 1219-1233
    • Atwodd, C.S.1
  • 46
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • CURTAIN, C.C. et al. 2001. Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 276: 20466-20473.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20466-20473
    • Curtain, C.C.1
  • 47
    • 0037174856 scopus 로고    scopus 로고
    • Metalloenzyme-like activity of Alzheimer's disease beta-amyloid: Cu-dependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H(2)O(2)
    • OPAZO, C. et al. 2002. Metalloenzyme-like activity of Alzheimer's disease beta-amyloid: Cu-dependent catalytic conversion of dopamine, cholesterol, and biological reducing agents to neurotoxic H(2)O(2). J. Biol. Chem. 277: 40302-40308.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40302-40308
    • Opazo, C.1
  • 48
    • 0027980901 scopus 로고
    • Rapid induction of Alzheimer A beta amyloid formation by zinc
    • BUSH, A.I. et al. 1994. Rapid induction of Alzheimer A beta amyloid formation by zinc. Science 265: 1464-1467.
    • (1994) Science , vol.265 , pp. 1464-1467
    • Bush, A.I.1
  • 49
    • 0033587478 scopus 로고    scopus 로고
    • Histidine-13 is a critical residue in the zinc-ion induced aggregation of the A beta peptide in Alzheimer's disease
    • LIU, S.T. et al. 1999. Histidine-13 is a critical residue in the zinc-ion induced aggregation of the A beta peptide in Alzheimer's disease. Biochemistry 38: 9373-9378.
    • (1999) Biochemistry , vol.38 , pp. 9373-9378
    • Liu, S.T.1
  • 50
    • 0037188530 scopus 로고    scopus 로고
    • Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice
    • LEE, J-Y. et al. 2002. Contribution by synaptic zinc to the gender-disparate plaque formation in human Swedish mutant APP transgenic mice. Proc. Natl. Acad. Sci. USA 99: 7705-7710.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 7705-7710
    • Lee, J.-Y.1
  • 51
    • 0036860349 scopus 로고    scopus 로고
    • Metal completing agents as therapies for Alzheimer's disease
    • BUSH, A.I. 2002. Metal completing agents as therapies for Alzheimer's disease. Neurobiol. Aging 23: 1031-1038.
    • (2002) Neurobiol. Aging , vol.23 , pp. 1031-1038
    • Bush, A.I.1
  • 52
    • 0035865905 scopus 로고    scopus 로고
    • Redox-active iron mediated beta-amyloid toxicity
    • ROTTKAMP, C.A. et al. 2001. Redox-active iron mediated beta-amyloid toxicity. Free Radical Biol. Med. 30: 447-450.
    • (2001) Free Radical Biol. Med. , vol.30 , pp. 447-450
    • Rottkamp, C.A.1
  • 53
    • 0347928847 scopus 로고    scopus 로고
    • An iron-responsive element type II in the 5′-untranslated region of the Alzheimer's amyloid precursor protein transcript
    • ROGERS, J.T. et al. 2002. An iron-responsive element type II in the 5′-untranslated region of the Alzheimer's amyloid precursor protein transcript. J. Biol. Chem. 277: 45518-45528.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45518-45528
    • Rogers, J.T.1
  • 54
    • 0036975682 scopus 로고    scopus 로고
    • Beta-amyloid production, aggregation, and clearance as targets for therapy in Alzheimer's disease
    • DE FELICE, F.G. & ST. FERREIRA. 2002. Beta-amyloid production, aggregation, and clearance as targets for therapy in Alzheimer's disease. Cell. Mol. Neurobiol. 22: 545-563.
    • (2002) Cell. Mol. Neurobiol. , vol.22 , pp. 545-563
    • De Felice, F.G.1    Ferreira, S.T.2
  • 55
    • 18444399243 scopus 로고    scopus 로고
    • Treatment of Alzheimer's disease with clioquinol
    • REGLAND, B. et al. 2001 Treatment of Alzheimer's disease with clioquinol. Dement. Geriatr. Cogn. Disord. 12: 408-414.
    • (2001) Dement. Geriatr. Cogn. Disord. , vol.12 , pp. 408-414
    • Regland, B.1
  • 57
    • 0016726066 scopus 로고
    • The neuropathology of subacute myelo-optico-neuropathy (SMONS) in the humans: With special reference to the quinoform intoxication
    • SHIRAKI, H. 1975. The neuropathology of subacute myelo-optico-neuropathy (SMONS) in the humans: with special reference to the quinoform intoxication. Jpn. J. Med. Sci. Biol. 28: 101-164.
    • (1975) Jpn. J. Med. Sci. Biol. , vol.28 , pp. 101-164
    • Shiraki, H.1
  • 58
    • 0031761894 scopus 로고    scopus 로고
    • Clioquinol-zinc chelate: A candidate causative agent of subacute myelo-optic neuropathy
    • ARBISER, J.L. et al. 1998. Clioquinol-zinc chelate: a candidate causative agent of subacute myelo-optic neuropathy. Mol. Med. 4: 665-670.
    • (1998) Mol. Med. , vol.4 , pp. 665-670
    • Arbiser, J.L.1
  • 59
    • 0342700237 scopus 로고    scopus 로고
    • Recent advances in the molecular pathogenesis of Friedreich ataxia
    • PUCCIO, H. & M. KOENIG. 2000. Recent advances in the molecular pathogenesis of Friedreich ataxia. Hum. Mol. Genet. 9: 887-892.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 887-892
    • Puccio, H.1    Koenig, M.2
  • 60
    • 0035122450 scopus 로고    scopus 로고
    • Frataxin: Its role in iron metabolism and the pathogenesis of Friedreich's ataxia
    • BECKER, E. & D.R. RICHARDSON. 2001. Frataxin: its role in iron metabolism and the pathogenesis of Friedreich's ataxia. Int. J. Biochem. Cell Biol. 33: 1-10.
    • (2001) Int. J. Biochem. Cell Biol. , vol.33 , pp. 1-10
    • Becker, E.1    Richardson, D.R.2
  • 61
    • 0033582421 scopus 로고    scopus 로고
    • The yeast frataxin homologue mediates mitochondrial iron efflux: Evidence for a mitochondrial iron cycle
    • RADISKY, D.C. et al. 1999. The yeast frataxin homologue mediates mitochondrial iron efflux: evidence for a mitochondrial iron cycle. J. Biol. Chem. 274: 4497-4499.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4497-4499
    • Radisky, D.C.1
  • 62
    • 0037093206 scopus 로고    scopus 로고
    • Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: Characterisation of frataxin expression compared to molecules involved in iron metabolism and hemoglobinisation
    • BECKER, E. et al. 2002. Erythroid differentiation and protoporphyrin IX down-regulate frataxin expression in Friend cells: characterisation of frataxin expression compared to molecules involved in iron metabolism and hemoglobinisation. Blood 99: 3813-3822.
    • (2002) Blood , vol.99 , pp. 3813-3822
    • Becker, E.1
  • 63
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • MÜIILENHOFF, U. et al. 2002. The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol. Genet. 11: 2025-2036.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2025-2036
    • Müiilenhoff, U.1
  • 64
    • 0037447390 scopus 로고    scopus 로고
    • Iron use for haem synthesis is under the control of the yeast frataxin homologue (Yfh1)
    • LESUISSE, E. et al. 2003. Iron use for haem synthesis is under the control of the yeast frataxin homologue (Yfh1). Hum. Mol. Genet. 12: 879-889.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 879-889
    • Lesuisse, E.1
  • 65
    • 0036569986 scopus 로고    scopus 로고
    • Molecular basis of cellular iron toxicity
    • EATON, J.W. & M. QIAN. 2002. Molecular basis of cellular iron toxicity. Free Radical Biol. Med. 32: 833-840.
    • (2002) Free Radical Biol. Med. , vol.32 , pp. 833-840
    • Eaton, J.W.1    Qian, M.2
  • 66
    • 0030846021 scopus 로고    scopus 로고
    • Regulation of mitochondrial iron accumulation by Yfh1p, a putative homologue of frataxin
    • BABCOCK, M. et al. 1997. Regulation of mitochondrial iron accumulation by Yfh1p, a putative homologue of frataxin. Science 276: 1709-1712.
    • (1997) Science , vol.276 , pp. 1709-1712
    • Babcock, M.1
  • 67
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect, and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • PUCCIO, H. et al. 2001. Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect, and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat Genet. 27: 181-186.
    • (2001) Nat Genet. , vol.27 , pp. 181-186
    • Puccio, H.1
  • 68
    • 0031253821 scopus 로고    scopus 로고
    • Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia
    • ROTIG, A. et al. 1997. Aconitase and mitochondrial iron-sulphur protein deficiency in Friedreich ataxia. Nat. Genet. 17: 215-217.
    • (1997) Nat. Genet. , vol.17 , pp. 215-217
    • Rotig, A.1
  • 69
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • WONG, A. et al. 1999. The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet. 8: 425-430.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 425-430
    • Wong, A.1
  • 70
    • 0033533071 scopus 로고    scopus 로고
    • Effect of idebenone on cardiomyopathy in Friedreich's ataxia: A preliminary study
    • RUSTIN, P. et al. 1999. Effect of idebenone on cardiomyopathy in Friedreich's ataxia: a preliminary study. Lancet 354: 477-479.
    • (1999) Lancet , vol.354 , pp. 477-479
    • Rustin, P.1
  • 71
    • 0035020940 scopus 로고    scopus 로고
    • Antioxidant treatment improves in vivo cardiac and skeletal muscle bioenergetics in patients with Friedreich's ataxia
    • LODI, R. et al. 2001. Antioxidant treatment improves in vivo cardiac and skeletal muscle bioenergetics in patients with Friedreich's ataxia. Ann. Neurol. 49: 590-596.
    • (2001) Ann. Neurol. , vol.49 , pp. 590-596
    • Lodi, R.1
  • 72
    • 0036221156 scopus 로고    scopus 로고
    • Idebenone and reduced cardiac hypertrophy in Friedreich's ataxia
    • HAUSSE, A.O. et al. 2002. Idebenone and reduced cardiac hypertrophy in Friedreich's ataxia. Heart 87: 346-349.
    • (2002) Heart , vol.87 , pp. 346-349
    • Hausse, A.O.1
  • 73
    • 0028158768 scopus 로고
    • The effect of the iron(III) chelator, desferrioxamine, on iron and transferrin uptake by the human malignant melanoma cell
    • RICHARDSON, D.R. et al. 1994. The effect of the iron(III) chelator, desferrioxamine, on iron and transferrin uptake by the human malignant melanoma cell. Cancer Res. 54: 685-689.
    • (1994) Cancer Res. , vol.54 , pp. 685-689
    • Richardson, D.R.1
  • 74
    • 0018394556 scopus 로고
    • Mobilization of iron from reticulocytes: Identification of pyridoxal isonicotinoyl hydrazone as a new iron chelating agent
    • PONKA, P. et al. 1979. Mobilization of iron from reticulocytes: identification of pyridoxal isonicotinoyl hydrazone as a new iron chelating agent. FEBS Lett. 97: 317-321.
    • (1979) FEBS Lett. , vol.97 , pp. 317-321
    • Ponka, P.1
  • 75
    • 0035978474 scopus 로고    scopus 로고
    • Development of potential iron chelators for the treatment of Friedreich's ataxia: Ligands that mobilize mitochondrial iron
    • RICHARDSON, D.R. et al. 2001. Development of potential iron chelators for the treatment of Friedreich's ataxia: ligands that mobilize mitochondrial iron. Biochim. Biophys. Acta 1536: 133-140.
    • (2001) Biochim. Biophys. Acta , vol.1536 , pp. 133-140
    • Richardson, D.R.1
  • 76
    • 0037317490 scopus 로고    scopus 로고
    • Friedreich's ataxia: Iron chelators that target the mitochondrion as a therapeutic strategy
    • RICHARDSON, D.R. 2003. Friedreich's ataxia: iron chelators that target the mitochondrion as a therapeutic strategy. Exp. Opin. Invest. Drugs 12: 235-245.
    • (2003) Exp. Opin. Invest. Drugs , vol.12 , pp. 235-245
    • Richardson, D.R.1
  • 77
    • 0018567483 scopus 로고
    • Effective iron chelation following oral administration of an isoniazid pyridoxal hydrazone
    • HOY, T. et al. 1979. Effective iron chelation following oral administration of an isoniazid pyridoxal hydrazone. Br. J. Haematol. 43: 443-449.
    • (1979) Br. J. Haematol. , vol.43 , pp. 443-449
    • Hoy, T.1
  • 78
    • 0025194404 scopus 로고
    • Pyridoxal isonicotinoyl hydrazone: An effective chelator after oral administration
    • BRITTENHAM, G.M. 1990. Pyridoxal isonicotinoyl hydrazone: an effective chelator after oral administration. Semin. Hematol. 27: 112-116.
    • (1990) Semin. Hematol. , vol.27 , pp. 112-116
    • Brittenham, G.M.1
  • 79
    • 0024920255 scopus 로고
    • Iron chelators of the pyridoxal isonicotinoyl hydrazone class. III. Formation constants with calcium(II), magnesium(II), and zinc(II)
    • RICHARDSON, D.R. et al. 1989. Iron chelators of the pyridoxal isonicotinoyl hydrazone class. III. Formation constants with calcium(II), magnesium(II), and zinc(II). Biol. Metals 2: 161-167.
    • (1989) Biol. Metals , vol.2 , pp. 161-167
    • Richardson, D.R.1
  • 80
    • 0000424901 scopus 로고
    • Iron chelators of the pyridoxal isonicotinoyl hydrazone class. Part 2, Formation constants with iron(III) and iron(II)
    • VITOLO, L.M.W. et al. 1990. Iron chelators of the pyridoxal isonicotinoyl hydrazone class. Part 2, Formation constants with iron(III) and iron(II). Inorg. Chim. Acta 170: 171-176.
    • (1990) Inorg. Chim. Acta , vol.170 , pp. 171-176
    • Vitolo, L.M.W.1
  • 81
    • 0000166947 scopus 로고
    • Iron chelators of the pyridoxal isonicotinoyl hydrazone class. Part 1. Ionisation characteristics of the ligands and their relevance to biological properties
    • RICHARDSON, D.R. et al. 1990. Iron chelators of the pyridoxal isonicotinoyl hydrazone class. Part 1. Ionisation characteristics of the ligands and their relevance to biological properties. Inorg. Chim. Acta 170: 165-170.
    • (1990) Inorg. Chim. Acta , vol.170 , pp. 165-170
    • Richardson, D.R.1
  • 82
    • 0026081935 scopus 로고
    • The release of iron and transferrin by the human malignant melanoma cell
    • RICHARDSON, D.R. & E. BAKER. 1991. The release of iron and transferrin by the human malignant melanoma cell. Biochim. Biophys. Acta 1091: 294-302.
    • (1991) Biochim. Biophys. Acta , vol.1091 , pp. 294-302
    • Richardson, D.R.1    Baker, E.2
  • 83
    • 0028535112 scopus 로고
    • The iron metabolism of the human neuroblastoma cell: Lack of relationship between the efficacy of iron chelation and the inhibition of DNA synthesis
    • RICHARDSON, D.R. & P. PONKA. 1994. The iron metabolism of the human neuroblastoma cell: lack of relationship between the efficacy of iron chelation and the inhibition of DNA synthesis. J. Lab. Clin. Med. 124: 660-671.
    • (1994) J. Lab. Clin. Med. , vol.124 , pp. 660-671
    • Richardson, D.R.1    Ponka, P.2
  • 84
    • 0028891974 scopus 로고
    • The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferarive agents
    • RICHARDSON, D.R. et al. 1995. The potential of iron chelators of the pyridoxal isonicotinoyl hydrazone class as effective antiproliferarive agents. Blood 86: 4295-4306.
    • (1995) Blood , vol.86 , pp. 4295-4306
    • Richardson, D.R.1
  • 85
    • 0033230124 scopus 로고    scopus 로고
    • Development of novel aroylhydrazone ligands for iron chelation therapy: The 2-pyridylcarboxaldehyde isonicotinoyl hydrazone (PCIH) analogues
    • BECKER, E. & D.R. RICHARDSON. 1999. Development of novel aroylhydrazone ligands for iron chelation therapy: the 2-pyridylcarboxaldehyde isonicotinoyl hydrazone (PCIH) analogues. J. Lab. Clin. Med. 134: 510-521.
    • (1999) J. Lab. Clin. Med. , vol.134 , pp. 510-521
    • Becker, E.1    Richardson, D.R.2
  • 86
    • 0032055861 scopus 로고    scopus 로고
    • Pyridoxal isonicotinoyl hydrazone and its analogues: Potential orally effective iron-chelating agents for the treatment of iron overload disease
    • RICHARDSON, D.R. & P. PONKA. 1998. Pyridoxal isonicotinoyl hydrazone and its analogues: potential orally effective iron-chelating agents for the treatment of iron overload disease. J. Lab. Clin. Med. 131: 306-315.
    • (1998) J. Lab. Clin. Med. , vol.131 , pp. 306-315
    • Richardson, D.R.1    Ponka, P.2
  • 87
    • 0037356211 scopus 로고    scopus 로고
    • Structural variations and formation constants of first-row transition metal complexes of biologically active aroylhydrazones
    • ARMSTRONG, C.M. et al. 2003. Structural variations and formation constants of first-row transition metal complexes of biologically active aroylhydrazones. Eur. J. Inorg. Chem. 2003(6): 1145-1156.
    • (2003) Eur. J. Inorg. Chem. , vol.2003 , Issue.6 , pp. 1145-1156
    • Armstrong, C.M.1
  • 88
    • 0035161372 scopus 로고    scopus 로고
    • Unprecedented oxidation of a biologically active aroylhydrazone chelator catalysed by iron(III): Serendipitous identification of diacylhydrazine ligands with high iron chelation efficacy
    • BERNHARDT, P.V. et al. 2001. Unprecedented oxidation of a biologically active aroylhydrazone chelator catalysed by iron(III): serendipitous identification of diacylhydrazine ligands with high iron chelation efficacy. J. Biol. Inorg. Chem. 6: 801-809.
    • (2001) J. Biol. Inorg. Chem. , vol.6 , pp. 801-809
    • Bernhardt, P.V.1


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