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Volumn 44, Issue 3, 2011, Pages 165-169

Oxidative modification of ferritin induced by hydrogen peroxide

Author keywords

Ferritin; H2O2; Hydroxyl radical; Oxidative stress

Indexed keywords

FERRITIN; FREE RADICAL; HYDROGEN PEROXIDE; IRON; OXIDIZING AGENT; REACTIVE OXYGEN METABOLITE; SCAVENGER;

EID: 79953220506     PISSN: 19766696     EISSN: 1976670X     Source Type: Journal    
DOI: 10.5483/BMBRep.2011.44.3.165     Document Type: Article
Times cited : (18)

References (26)
  • 3
    • 67650720510 scopus 로고    scopus 로고
    • Immune and inflammatory mechanisms of atherosclerosis
    • Galkina, E. and Ley, K. (2009) Immune and inflammatory mechanisms of atherosclerosis. Annu. Rev. Immunol. 27, 165-197.
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 165-197
    • Galkina, E.1    Ley, K.2
  • 4
    • 58949084649 scopus 로고    scopus 로고
    • Base excision repair of oxidative DNA damage and association with cancer and aging
    • Maynarol, S., Schurman, S. H., Harboe, C., de Souta-Pinto, N. C. and Bohr, V. A. (2009) Base excision repair of oxidative DNA damage and association with cancer and aging. Carcinogenesis 30, 2-10.
    • (2009) Carcinogenesis , vol.30 , pp. 2-10
    • Maynarol, S.1    Schurman, S.H.2    Harboe, C.3    de Souta-Pinto, N.C.4    Bohr, V.A.5
  • 5
    • 66849091772 scopus 로고    scopus 로고
    • Role of oxidative stress in contrast-induced acute kidney injury in diabetes mellitus
    • Pflueger, A., Avramowitt, D. and Calvin, A. D. (2009) Role of oxidative stress in contrast-induced acute kidney injury in diabetes mellitus. Med. Sci. Monit. 15, 125-136.
    • (2009) Med. Sci. Monit. , vol.15 , pp. 125-136
    • Pflueger, A.1    Avramowitt, D.2    Calvin, A.D.3
  • 6
    • 39749110624 scopus 로고    scopus 로고
    • Oxidative stress and iron homeostasis: mechanistic and health aspects
    • Galaris, D. and Pantopoulos, K. (2008) Oxidative stress and iron homeostasis: mechanistic and health aspects. Crit. Rev. Clin. Lab. Sci. 45, 1-23.
    • (2008) Crit. Rev. Clin. Lab. Sci. , vol.45 , pp. 1-23
    • Galaris, D.1    Pantopoulos, K.2
  • 7
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti, F. M. and Torti, S. V. (2002) Regulation of ferritin genes and protein. Blood 99, 3505-3516.
    • (2002) Blood , vol.99 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 8
    • 4043144143 scopus 로고    scopus 로고
    • Neurodegenerative disease and iron storage in the brain
    • Thomas, M. and Jankovic, J. (2004) Neurodegenerative disease and iron storage in the brain. Curr. Opin. Neurol. 17, 437-442.
    • (2004) Curr. Opin. Neurol. , vol.17 , pp. 437-442
    • Thomas, M.1    Jankovic, J.2
  • 12
    • 0021368004 scopus 로고
    • Oxygen effect in the radiolysis of proteins. Part 2. Bovine serum albumin
    • Schuessler, H. and Schilling, K. (1984) Oxygen effect in the radiolysis of proteins. Part 2. Bovine serum albumin. Int. J. Radiat. Biol. 45, 267-281.
    • (1984) Int. J. Radiat. Biol. , vol.45 , pp. 267-281
    • Schuessler, H.1    Schilling, K.2
  • 13
    • 0024325699 scopus 로고
    • Free radical-mediated degradation of proteins: the protective and deleterious effects of membranes
    • Hunt, J. V. and Dean, R. T. (1989) Free radical-mediated degradation of proteins: the protective and deleterious effects of membranes. Biochem. Biophys. Res. Commun. 162, 1076-1084.
    • (1989) Biochem. Biophys. Res. Commun. , vol.162 , pp. 1076-1084
    • Hunt, J.V.1    Dean, R.T.2
  • 14
    • 0031010333 scopus 로고    scopus 로고
    • Reactive oxygen-mediated protein oxidation in aging and disease
    • Stadtman, E. R. and Berlett, B. S. (1997) Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10, 485-494.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 485-494
    • Stadtman, E.R.1    Berlett, B.S.2
  • 15
    • 67349169054 scopus 로고    scopus 로고
    • Labile iron pool and ferritin content in developing rat brain gamma-irradiated in utero
    • Robello, E., Galatro, A. and Puntarulo, S. (2009) Labile iron pool and ferritin content in developing rat brain gamma-irradiated in utero. Neurotoxicology 30, 430-435.
    • (2009) Neurotoxicology , vol.30 , pp. 430-435
    • Robello, E.1    Galatro, A.2    Puntarulo, S.3
  • 16
    • 0037087150 scopus 로고    scopus 로고
    • Aggregation of α-synuclein induced by the Cu,Zn-superoxide dismutase and hydrogen peroxide system
    • Kim, K. S., Choi, S. Y., Kwon, H. Y., Won, M. H., Kang, T. C. and Kang, J. H. (2002) Aggregation of α-synuclein induced by the Cu,Zn-superoxide dismutase and hydrogen peroxide system. Free Radic. Biol. Med. 32, 544-550.
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 544-550
    • Kim, K.S.1    Choi, S.Y.2    Kwon, H.Y.3    Won, M.H.4    Kang, T.C.5    Kang, J.H.6
  • 17
    • 67349164279 scopus 로고    scopus 로고
    • Ferritin enhances salsolinol-mediated DNA strand braekage: protection by carnosine and related compounds
    • Kang, J. H. (2009) Ferritin enhances salsolinol-mediated DNA strand braekage: protection by carnosine and related compounds. Toxicol. Lett. 188, 20-25.
    • (2009) Toxicol. Lett. , vol.188 , pp. 20-25
    • Kang, J.H.1
  • 18
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals. II. Modification of amino acids
    • Davies, K. J., Delsignore, M. E. and Lin, S. W. (1987) Protein damage and degradation by oxygen radicals. II. Modification of amino acids. J. Biol. Chem. 262, 9902-9907.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9902-9907
    • Davies, K.J.1    Delsignore, M.E.2    Lin, S.W.3
  • 19
    • 0035824113 scopus 로고    scopus 로고
    • Oxidative modification of human ceruloplasmin by peroxyl radicals
    • Kang, J. H, Kim, K. S, Choi, S. Y., Kwon, H. Y. and Won, M. H. (2001) Oxidative modification of human ceruloplasmin by peroxyl radicals. Biochem. Biophys. Acta 1568, 30-36.
    • (2001) Biochem. Biophys. Acta , vol.1568 , pp. 30-36
    • Kang, J.H.1    Kim, K.S.2    Choi, S.Y.3    Kwon, H.Y.4    Won, M.H.5
  • 22
    • 0024821055 scopus 로고
    • Measurement and characterization of postischemic free radical generation in the isolated perfused heart
    • Zweier, J. L., Kuppusamy, P., Williams, R., Rayburn, B. K., Smith, D., Weisfeldt, M. L. and Flaherty, J. T. (1989) Measurement and characterization of postischemic free radical generation in the isolated perfused heart. J. Biol. Chem. 264, 18890-18895.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18890-18895
    • Zweier, J.L.1    Kuppusamy, P.2    Williams, R.3    Rayburn, B.K.4    Smith, D.5    Weisfeldt, M.L.6    Flaherty, J.T.7
  • 25
    • 0034777015 scopus 로고    scopus 로고
    • Comparison of bathophenanthroline sulfonate and ferene as chromogens in colorimetric measurement of low hepatic iron concentration
    • Pieroni, L., Khalil, L., Charlotte, F., Poynard, T., Piton, A., Hainque, B. and Imbert-Bismut, F. (2001) Comparison of bathophenanthroline sulfonate and ferene as chromogens in colorimetric measurement of low hepatic iron concentration. Clin. Chem. 47, 2059-2061.
    • (2001) Clin. Chem. , vol.47 , pp. 2059-2061
    • Pieroni, L.1    Khalil, L.2    Charlotte, F.3    Poynard, T.4    Piton, A.5    Hainque, B.6    Imbert-Bismut, F.7
  • 26
    • 0015500932 scopus 로고
    • Determination of the tryptophan content of proteins by ion exchange chromatography of alkaline hydrolysates
    • Hugli, T, E. and Moore, S. (1972) Determination of the tryptophan content of proteins by ion exchange chromatography of alkaline hydrolysates. J. Biol. Chem. 247, 2828-2834
    • (1972) J. Biol. Chem. , vol.247 , pp. 2828-2834
    • Hugli, T.E.1    Moore, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.