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Volumn 37, Issue 10, 2003, Pages 1113-1121

Aminoacetone induces loss of ferritin ferroxidase and iron uptake activities

Author keywords

Aminoacetone; Apoferritin; Ferritin; Free radical; Iron catalyzed oxidation; Protein oxidative damage

Indexed keywords

ACETONE; ADENOSINE TRIPHOSPHATE; ALCOHOL; AMINE OXIDASE (COPPER CONTAINING); AMINOACETONE; AMMONIA; APOFERRITIN; CATALASE; CERULOPLASMIN; CITRIC ACID; COPPER ION; EDETIC ACID; FERRITIN; GLYCINE; HYDROGEN PEROXIDE; IRON; ISOFERRITIN; MANNITOL; METHYLGLYOXAL; NITROGEN; OXYGEN; PHOSPHATE; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE; THIOL; THREONINE; TRYPTOPHAN; UNCLASSIFIED DRUG;

EID: 0142094013     PISSN: 10715762     EISSN: None     Source Type: Journal    
DOI: 10.1080/10715760310001604116     Document Type: Review
Times cited : (16)

References (62)
  • 1
    • 0021111716 scopus 로고
    • "Formation of methylglyoxal from aminoacetone by amine oxidase from goat plasma"
    • Ray, S. and Ray, M. (1983) "Formation of methylglyoxal from aminoacetone by amine oxidase from goat plasma", J. Biol. Chem. 258, 3461-3462.
    • (1983) J. Biol. Chem. , vol.258 , pp. 3461-3462
    • Ray, S.1    Ray, M.2
  • 2
    • 0029869337 scopus 로고    scopus 로고
    • "Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidase: Biochemical, pharmacological and toxicological aspects"
    • Lyles, G.A. (1996) "Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidase: biochemical, pharmacological and toxicological aspects", Int. J. Biochem. Cell Biol. 28,259-274.
    • (1996) Int. J. Biochem. Cell Biol. , vol.28 , pp. 259-274
    • Lyles, G.A.1
  • 3
    • 0038549049 scopus 로고    scopus 로고
    • "Physiological and pathological implications of semicarbazide-sensitive amine oxidase"
    • 1647
    • Yu, P.H., Wright, S., Fan, E.H., Lun, Z.R. and Gubisne-Harberle, D. (2003) "Physiological and pathological implications of semicarbazide-sensitive amine oxidase", Biochem. Biophys. Acta 1647, 193-199.
    • (2003) Biochem. Biophys. Acta , pp. 193-199
    • Yu, P.H.1    Wright, S.2    Fan, E.H.3    Lun, Z.R.4    Gubisne-Harberle, D.5
  • 4
    • 0003446726 scopus 로고
    • "Aminoacetone: Its isolation and role in metabolism"
    • Elliott, W.H. (1959) "Aminoacetone: its isolation and role in metabolism", Nature 183, 1051.
    • (1959) Nature , vol.183 , pp. 1051
    • Elliott, W.H.1
  • 5
    • 0032703938 scopus 로고    scopus 로고
    • "Methylglyoxal in living organism: Chemistry, biochemistry, toxicology and biological implications"
    • Kalapos, M.P. (1999) "Methylglyoxal in living organism: chemistry, biochemistry, toxicology and biological implications", Toxicol. Lett. 110, 145-175.
    • (1999) Toxicol. Lett. , vol.110 , pp. 145-175
    • Kalapos, M.P.1
  • 6
    • 0021772598 scopus 로고
    • "Formation of glycine and aminoacetone from L-threonine by rat liver mitochondria"
    • Bird, M.I., Nunn, P.B. and Lord, L.A.J. (1984) "Formation of glycine and aminoacetone from L-threonine by rat liver mitochondria" Biochim. Biophys. Acta 802, 229-236.
    • (1984) Biochim. Biophys. Acta , vol.802 , pp. 229-236
    • Bird, M.I.1    Nunn, P.B.2    Lord, L.A.J.3
  • 7
    • 31744433849 scopus 로고
    • "Biosynthesis of α-amino-ketones and the metabolism of aminoacetone"
    • Urata, G. and Granick, S. (1963) "Biosynthesis of α-amino-ketones and the metabolism of aminoacetone", J. Biol. Chem. 238, 811-820.
    • (1963) J. Biol. Chem. , vol.238 , pp. 811-820
    • Urata, G.1    Granick, S.2
  • 8
    • 0031890977 scopus 로고    scopus 로고
    • "Acute porphyrias: Pathogenesis of neurological manifestations"
    • Meyer, UA., Schuurmans, M.M. and Lindberg, R.L.P. (1998) "Acute porphyrias: pathogenesis of neurological manifestations", Semin. Liver Dis. 18, 43-52.
    • (1998) Semin. Liver Dis. , vol.18 , pp. 43-52
    • Meyer, U.A.1    Schuurmans, M.M.2    Lindberg, R.L.P.3
  • 9
    • 0000637739 scopus 로고
    • "Role of the acidity of the ketone in determining the mechanism of enolization via proton abstraction from ketone, carbinolamine, or imine. Catalysis of the enolization of 2,4-pentanedione and 3-methyl-2,4-pentanedione by oxyanions and by primary, secondary, and tertiary amines"
    • Bruice, P.Y. (1990) "Role of the acidity of the ketone in determining the mechanism of enolization via proton abstraction from ketone, carbinolamine, or imine. Catalysis of the enolization of 2,4-pentanedione and 3-methyl-2,4-pentanedione by oxyanions and by primary, secondary, and tertiary anmines", J. Am. Chem. Soc. 112, 7361-7368.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 7361-7368
    • Bruice, P.Y.1
  • 10
    • 0024597762 scopus 로고
    • "Free radical generation during δ-amino-levulinic acid autoxidation: Induction by hemoglobin and connections with porphyrinpathies"
    • Monteiro, H.P., Abdalla, D.S.P., Augusto, O. and Bechara, E.J.H. (1989) "Free radical generation during δ-amino-levulinic acid autoxidation: induction by hemoglobin and connections with porphyrinpathies", Arch. Biochem. Biophys. 271, 206-216.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 206-216
    • Monteiro, H.P.1    Abdalla, D.S.P.2    Augusto, O.3    Bechara, E.J.H.4
  • 11
    • 0026057381 scopus 로고
    • "Damage to rat liver mitochondria promoted by δ-aminolevulinic acid-generated reactive oxygen species: Connections with acute intermittent porphyria and lead-poisoning"
    • 1056
    • Hermes-Lima, M., Valle, VG.R., Vercesi, A.E. and Bechara, E.J.H. (1991) "Damage to rat liver mitochondria promoted by δ-aminolevulinic acid-generated reactive oxygen species: connections with acute intermittent porphyria and leadpoisoning", Biochim. Biophys. Acta 1056, 57-63.
    • (1991) Biochim. Biophys. Acta , pp. 57-63
    • Hermes-Lima, M.1    Valle, V.G.R.2    Vercesi, A.E.3    Bechara, E.J.H.4
  • 12
    • 0030016990 scopus 로고    scopus 로고
    • "Oxidative stress in acute intermittent porphyria and lead poisoning may be triggered by 5-aminolevulinic acid"
    • Bechara, E.J.H. (1996) "Oxidative stress in acute intermittent porphyria and lead poisoning may be triggered by 5-aminolevulinic acid", Braz. J. Med. Biol. Res. 29,841-851.
    • (1996) Braz. J. Med. Biol. Res. , vol.29 , pp. 841-851
    • Bechara, E.J.H.1
  • 13
    • 0029929578 scopus 로고    scopus 로고
    • "The prooxidant effect of 5-aminolevulinic acid in the brain tissue of rats: Implications in neuropsychiatric manifestations in porphyrias"
    • Demasi, M., Penatti, C.A.A., DeLucia, R. and Bechara, E.J.H. (1996) "The prooxidant effect of 5-aminolevulinic acid in the brain tissue of rats: implications in neuropsychiatric manifestations in porphyrias", Free Radic. Biol. Med. 20, 291-299.
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 291-299
    • Demasi, M.1    Penatti, C.A.A.2    DeLucia, R.3    Bechara, E.J.H.4
  • 14
    • 0032557407 scopus 로고    scopus 로고
    • "Hydroxyl radicals are involved in the oxidation of isolated and cellular DNA bases by 5-aminolevulinic acid"
    • Douki, T., Onuki, J., Medeiros, M.H.G., Bechara, E.J.H., Cadet, J. and Di Mascio, P. (1998) "Hydroxyl radicals are involved in the oxidation of isolated and cellular DNA bases by 5-aminolevulinic acid", FEBS Lett. 428, 93-96.
    • (1998) FEBS Lett. , vol.428 , pp. 93-96
    • Douki, T.1    Onuki, J.2    Medeiros, M.H.G.3    Bechara, E.J.H.4    Cadet, J.5    Di Mascio, P.6
  • 15
    • 0025853670 scopus 로고
    • "Protein glycation and oxidative stress in diabetes mellitus and ageing"
    • Wolff, S.P., Jiang, Z.Y. and Hunt, V. (1991) "Protein glycation and oxidative stress in diabetes mellitus and ageing", Free Radic. Biol. Med. 10, 339-352.
    • (1991) Free Radic. Biol. Med. , vol.10 , pp. 339-352
    • Wolff, S.P.1    Jiang, Z.Y.2    Hunt, V.3
  • 16
    • 0034802987 scopus 로고    scopus 로고
    • "Aerobic oxidation of aminoacetone, a threonine catabolite: Iron catalysis and coupled iron release from ferritin"
    • Dutra, F., Knudsen, F.S., Curi, D. and Bechara, E.J.H. (2001) "Aerobic oxidation of aminoacetone, a threonine catabolite: iron catalysis and coupled iron release from ferritin", Chem. Res. Toxicol. 14, 1323-1329.
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 1323-1329
    • Dutra, F.1    Knudsen, F.S.2    Curi, D.3    Bechara, E.J.H.4
  • 19
    • 0034939115 scopus 로고    scopus 로고
    • "The role of oxidative stress in the onset and progression of diabetes and its complications: A summary of a congress series sponsored by UNESCO-MCBN, the American Diabetes Association and the German Diabetes Society"
    • Rösen, P, Nawroth, P.P., King, G., Möller, W., Tritschler, H.J. and Packer, L. (2001) "The role of oxidative stress in the onset and progression of diabetes and its complications: a summary of a congress series sponsored by UNESCO-MCBN, the American Diabetes Association and the German Diabetes Society", Diabetes Metab. Res. Rev. 17, 189-212.
    • (2001) Diabetes Metab. Res. Rev. , vol.17 , pp. 189-212
    • Rösen, P.1    Nawroth, P.P.2    King, G.3    Möller, W.4    Tritschler, H.J.5    Packer, L.6
  • 20
    • 0033146494 scopus 로고    scopus 로고
    • "Diabetes mellitus in hemochromatosis"
    • Niederau, C. (1999) "Diabetes mellitus in hemochromatosis", Z. Gastroenterol. 1(suppl.), 22-32.
    • (1999) Z. Gastroenterol. , vol.1 , Issue.SUPPL. , pp. 22-32
    • Niederau, C.1
  • 21
    • 0029764551 scopus 로고    scopus 로고
    • "Alpha-lipoic acid: Antioxidant potency against lipid peroxidation of neural tissues in vitro and implications for diabetic neuropathy"
    • Nickander, K.K., McPhee, B.R., Low, P.A. and Tritschler, H. (1996) "Alpha-lipoic acid: antioxidant potency against lipid peroxidation of neural tissues in vitro and implications for diabetic neuropathy", Free Radic. Biol. Med. 21, 631-639.
    • (1996) Free Radic. Biol. Med. , vol.21 , pp. 631-639
    • Nickander, K.K.1    McPhee, B.R.2    Low, P.A.3    Tritschler, H.4
  • 22
    • 0028934334 scopus 로고
    • "The effects of desferrioxamine and ascorbate on oxidative stress in the streptozotocin diabetic rat"
    • Young, I.S., Tate, S., Lightbody, J.H., McMaster, D. and Trimble, E.R. (1995) "The effects of desferrioxamine and ascorbate on oxidative stress in the streptozotocin diabetic rat", Free Radic. Biol. Med. 18, 833-840.
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 833-840
    • Young, I.S.1    Tate, S.2    Lightbody, J.H.3    McMaster, D.4    Trimble, E.R.5
  • 23
    • 0033025053 scopus 로고    scopus 로고
    • "Iron-induced oxidative stress in erythrocyte membranes of non-insulin-dependent diabetic Nigerians"
    • Okunade, G.W., Odunuga, O.O. and Olorunsogo, O.O. (1999) "Iron-induced oxidative stress in erythrocyte membranes of non-insulin-dependent diabetic Nigerians", Biosci. Rep. 19,1-9.
    • (1999) Biosci. Rep. , vol.19 , pp. 1-9
    • Okunade, G.W.1    Odunuga, O.O.2    Olorunsogo, O.O.3
  • 24
    • 0035128199 scopus 로고    scopus 로고
    • "Iron deficiency and iron overload: Effects of diet and genes"
    • Burke, W., Imperatore, G. and Reyes, M. (2001) "Iron deficiency and iron overload: effects of diet and genes" Proc. Nutr. Soc. 60, 73-80.
    • (2001) Proc. Nutr. Soc. , vol.60 , pp. 73-80
    • Burke, W.1    Imperatore, G.2    Reyes, M.3
  • 25
    • 0033364044 scopus 로고    scopus 로고
    • "Diabetes and serum ferritin concentration among U.S. adults"
    • Ford, E.S. and Cogswell, M.E. (1999) "Diabetes and serum ferritin concentration among U.S. adults", Diabetes Care 22, 1978-1983.
    • (1999) Diabetes Care , vol.22 , pp. 1978-1983
    • Ford, E.S.1    Cogswell, M.E.2
  • 27
    • 0003323122 scopus 로고
    • "Aminoacetone semicarbazone hydrochloride"
    • Hepworth, J.D. (1976) "Aminoacetone semicarbazone hydrochloride" Org. Synth. 45,1-3.
    • (1976) Org. Synth. , vol.45 , pp. 1-3
    • Hepworth, J.D.1
  • 29
    • 0024245282 scopus 로고
    • "Mechanism of ferritin iron uptake: Activity of the H-chain and deletion mapping of the ferro-oxidase site"
    • Levi, S., Luzzago, A., Cesareni, G., Cozzi, A., Franceschinelli, F., Albertini, A. and Arosio, P. (1988) "Mechanism of ferritin iron uptake: Activity of the H-chain and deletion mapping of the ferro-oxidase site", J. Biol. Chem. 263, 18086-18092.
    • (1988) J. Biol. Chem. , vol.263 , pp. 18086-18092
    • Levi, S.1    Luzzago, A.2    Cesareni, G.3    Cozzi, A.4    Franceschinelli, F.5    Albertini, A.6    Arosio, P.7
  • 30
    • 0026799310 scopus 로고
    • "Redox reactions of apo mammalian ferritin"
    • Watt, R.K., Frankel, R.B. and Watt, G.D. (1992) "Redox reactions of apo mammalian ferritin", Biochemistry 31, 9673-9679.
    • (1992) Biochemistry , vol.31 , pp. 9673-9679
    • Watt, R.K.1    Frankel, R.B.2    Watt, G.D.3
  • 31
    • 0019482785 scopus 로고
    • "Adaptative responses of rat tissue isoferritins to iron administration"
    • Bomford, A., Conlon-Hollingshead, C. and Munro, H.N. (1981) "Adaptative responses of rat tissue isoferritins to iron administration" J. Biol. Chem. 256, 948-955.
    • (1981) J. Biol. Chem. , vol.256 , pp. 948-955
    • Bomford, A.1    Conlon-Hollingshead, C.2    Munro, H.N.3
  • 33
    • 0026504976 scopus 로고
    • "Effect of acidosis and anoxia on iron delocalization from brain homogenates"
    • Bralet, J., Schreiber, L. and Bouvier, C. (1992) "Effect of acidosis and anoxia on iron delocalization from brain homogenates", Biochem. Pharmacol. 43, 979-983.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 979-983
    • Bralet, J.1    Schreiber, L.2    Bouvier, C.3
  • 34
    • 0017184389 scopus 로고
    • "A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding"
    • Bradford, M.M. (1976) "A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein-dye binding", Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 35
  • 36
    • 0035887746 scopus 로고    scopus 로고
    • "The consequences of hydroxyl radical formation on the stoichiometry and kinetics of ferrous iron oxidation by human apoferritin"
    • Van Eden, M.E. and Aust, S.D. (2001) "The consequences of hydroxyl radical formation on the stoichiometry and kinetics of ferrous iron oxidation by human apoferritin", Free Radic. Biol. Med. 31,1007-1017.
    • (2001) Free Radic. Biol. Med. , vol.31 , pp. 1007-1017
    • Van Eden, M.E.1    Aust, S.D.2
  • 37
    • 0025095542 scopus 로고
    • "Transition metals as catalysts of autoxidation reactions"
    • Miller, D.M., Buettner, G.R. and Aust, S.D. (1990) "Transition metals as catalysts of autoxidation reactions", Free Radic. Biol. Med. 8,95-108.
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 95-108
    • Miller, D.M.1    Buettner, G.R.2    Aust, S.D.3
  • 38
    • 0030608152 scopus 로고    scopus 로고
    • "The ferritins: Molecular properties, iron storage function and cellular regulation"
    • 1275
    • Harrison, P.M. and Arosio, P. (1996) "The ferritins: molecular properties, iron storage function and cellular regulation", Biochim. Biophys. Acta 1275,161-203.
    • (1996) Biochim. Biophys. Acta , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 42
    • 0029588565 scopus 로고
    • "Ferritin as a source of iron and protection from iron-induced toxicities"
    • Aust, S.D. (1995) "Ferritin as a source of iron and protection from iron-induced toxicities" Toxicol. Lett. 82-83, 941-944.
    • (1995) Toxicol. Lett. , vol.82-83 , pp. 941-944
    • Aust, S.D.1
  • 43
    • 0028067470 scopus 로고
    • "Iron incorporation into ferritins - Evidence for the transfer of monomeric Fe(III) between ferritin molecules and for the formation of an unusual mineral in the ferritin of Escherichia-coli"
    • Bauminger, E.R., Treffry, A., Hudson, A.J., Hechel, D., Hodson, N.W., Andrews, S.C., Levi, S., Nowik, I., Arosio, P, Guest, JR. and Harrison, PM. (1994) "Iron incorporation into ferritins-Evidence for the transfer of monomeric Fe(III) between ferritin molecules and for the formation of an unusual mineral in the ferritin of Escherichia-coli", Biochem. J. 302, 813-820.
    • (1994) Biochem. J. , vol.302 , pp. 813-820
    • Bauminger, E.R.1    Treffry, A.2    Hudson, A.J.3    Hechel, D.4    Hodson, N.W.5    Andrews, S.C.6    Levi, S.7    Nowik, I.8    Arosio, P.9    Guest, J.R.10    Harrison, P.M.11
  • 44
    • 0027732697 scopus 로고
    • "Defining the roles of the threefold channels in iron uptake, iron oxidation and iron-core formation in ferritin - A study aided by site-directed mutagenesis"
    • Treffry, A., Bauminger, E.R., Hechel, D., Hodson, N.W., Nowik, I., Yendall, S.J. and Harrison, P.M. (1993) "Defining the roles of the threefold channels in iron uptake, iron oxidation and iron-core formation in ferritin-A study aided by site-directed mutagenesis", Biochem. J. 296, 721-728.
    • (1993) Biochem. J. , vol.296 , pp. 721-728
    • Treffry, A.1    Bauminger, E.R.2    Hechel, D.3    Hodson, N.W.4    Nowik, I.5    Yendall, S.J.6    Harrison, P.M.7
  • 45
  • 46
    • 0024384482 scopus 로고
    • "Expression and structural and functional-properties of human ferritin L-chain from Escherichia coli"
    • Levi, S., Salfeld, J., Franceschinelli, F, Cozzi, A., Dorner, M.H. and Arosio, P. (1989) "Expression and structural and functional-properties of human ferritin L-chain from Escherichia coli", Biochemistry 28, 5179-5184.
    • (1989) Biochemistry , vol.28 , pp. 5179-5184
    • Levi, S.1    Salfeld, J.2    Franceschinelli, F.3    Cozzi, A.4    Dorner, M.H.5    Arosio, P.6
  • 47
    • 0023323197 scopus 로고
    • "Release of iron from ferritin by xanthine-oxidase - Role of the superoxide radical"
    • Bolann, B.J. and Ulvik, R.J. (1987) "Release of iron from ferritin by xanthine-oxidase - Role of the superoxide radical" Biochem. J. 243, 55-59.
    • (1987) Biochem. J. , vol.243 , pp. 55-59
    • Bolann, B.J.1    Ulvik, R.J.2
  • 48
    • 0016173575 scopus 로고
    • "Release of iron from horse spleen ferritin by reduced flavins"
    • Sirivech, S., Frieden, E. and Osaki, S. (1974) "Release of iron from horse spleen ferritin by reduced flavins" Biochem. J. 143, 311-315.
    • (1974) Biochem. J. , vol.143 , pp. 311-315
    • Sirivech, S.1    Frieden, E.2    Osaki, S.3
  • 49
    • 0024272271 scopus 로고
    • "The superoxide-dependent transfer of iron from ferritin to transferrin and lactoferrin"
    • Monteiro, H.R and Winterbourn, C.C. (1988) "The superoxide-dependent transfer of iron from ferritin to transferrin and lactoferrin" Biochem. J. 256, 923-928.
    • (1988) Biochem. J. , vol.256 , pp. 923-928
    • Monteiro, H.P.1    Winterbourn, C.C.2
  • 50
    • 0034672594 scopus 로고    scopus 로고
    • "Roles of phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid"
    • Rocha, M.E.M., Ferreira, A.M.D.C. and Bechara, E.J.H. (2000) "Roles of phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid" Free Radic. Biol. Med. 29, 1272-1279.
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 1272-1279
    • Rocha, M.E.M.1    Ferreira, A.M.D.C.2    Bechara, E.J.H.3
  • 53
    • 0025139929 scopus 로고
    • "Iron environment in ferritin with large amounts of phosphate, from Azotobacter vinelandii and horse spleen, analysed using extended X-ray absorption fine structure (EXAFS)"
    • Rohrer, J.S., Islam, Q.T., Watt, G.D., Sayers, D.E. and Theil, E.C. (1990) "Iron environment in ferritin with large amounts of phosphate, from Azotobacter vinelandii and horse spleen, analysed using extended X-ray absorption fine structure (EXAFS)", Biochemistry 29, 259-264.
    • (1990) Biochemistry , vol.29 , pp. 259-264
    • Rohrer, J.S.1    Islam, Q.T.2    Watt, G.D.3    Sayers, D.E.4    Theil, E.C.5
  • 55
    • 0015997959 scopus 로고
    • "Aromatic contributions to circular dichroism spectra of proteins"
    • Strickland, E.H. (1974) "Aromatic contributions to circular dichroism spectra of proteins", CRC Crit. Rev. Biochem. 2, 113-175.
    • (1974) CRC Crit. Rev. Biochem. , vol.2 , pp. 113-175
    • Strickland, E.H.1
  • 56
    • 0019305467 scopus 로고
    • "Differential turnover of rat liver isoferritins"
    • Kohgo, Y., Yokota, M. and Drysdale, JW. (1980) "Differential turnover of rat liver isoferritins", J. Biol. Chem. 255, 5195-5200.
    • (1980) J. Biol. Chem. , vol.255 , pp. 5195-5200
    • Kohgo, Y.1    Yokota, M.2    Drysdale, J.W.3
  • 57
    • 0018079568 scopus 로고
    • "Properties of human tissue isoferritins"
    • Wagstaff, M., Worwood, M. and Jacobs, A. (1978) "Properties of human tissue isoferritins" Biochem. J. 173, 969-977.
    • (1978) Biochem. J. , vol.173 , pp. 969-977
    • Wagstaff, M.1    Worwood, M.2    Jacobs, A.3
  • 58
    • 0018123699 scopus 로고
    • "Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues"
    • Jones, T., Spencer, R. and Walsh, C. (1978) "Mechanism and kinetics of iron release from ferritin by dihydroflavins and dihydroflavin analogues", Biochemistry 17, 4011-4017.
    • (1978) Biochemistry , vol.17 , pp. 4011-4017
    • Jones, T.1    Spencer, R.2    Walsh, C.3
  • 59
    • 0033616738 scopus 로고    scopus 로고
    • "Redox reactivity of animal apoferritins and apoheteropolymers assembled from recombinant heavy and light human chain ferritins"
    • Johnson, J.L., Norcross, D.C., Arioso, P., Frankel, R.B. and Watt, G.D. (1999) "Redox reactivity of animal apoferritins and apoheteropolymers assembled from recombinant heavy and light human chain ferritins", Biochemistry 38, 4089-4096.
    • (1999) Biochemistry , vol.38 , pp. 4089-4096
    • Johnson, J.L.1    Norcross, D.C.2    Arioso, P.3    Frankel, R.B.4    Watt, G.D.5
  • 60
    • 0028234539 scopus 로고
    • "Tryptophan radicals formed by iron/oxygen reaction with Escherichia coli ribonucleotide reductase protein R2 mutant Y122F"
    • Sahlin, M., Lassmann, G., Pötsch, S., Slaby, A., Sjöberg, B.M. and Gräslund, A. (1994) "Tryptophan radicals formed by iron/oxygen reaction with Escherichia coli ribonucleotide reductase protein R2 mutant Y12217", J. Biol. Chem. 269, 11699-11702.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11699-11702
    • Sahlin, M.1    Lassmann, G.2    Pötsch, S.3    Slaby, A.4    Sjöberg, B.M.5    Gräslund, A.6
  • 61
    • 0036667556 scopus 로고    scopus 로고
    • "The role of cysteine residues in the oxidation of ferritin"
    • Welch, K.D., Reilly, C.A. and Aust, S.D. (2002) "The role of cysteine residues in the oxidation of ferritin", Free Radic. Biol. Med. 33, 399-408.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 399-408
    • Welch, K.D.1    Reilly, C.A.2    Aust, S.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.