메뉴 건너뛰기




Volumn 113, Issue 1, 2007, Pages 30-54

Ferritin and ferritin isoforms I: Structure-function relationships, synthesis, degradation and secretion

Author keywords

Ferritin; H subunit; Haemosiderin; Isoferritins; L subunit

Indexed keywords

FERRITIN; ISOPROTEIN;

EID: 34249686049     PISSN: 13813455     EISSN: 17444160     Source Type: Journal    
DOI: 10.1080/13813450701318583     Document Type: Article
Times cited : (126)

References (138)
  • 1
    • 0026280616 scopus 로고
    • Ferritin receptors and the role of ferritin in iron transport
    • Aisen P. 1991. Ferritin receptors and the role of ferritin in iron transport. Targeted Diag Ther 4:339-4.
    • (1991) Targeted Diag Ther , vol.4 , pp. 339-334
    • Aisen, P.1
  • 2
    • 0035976393 scopus 로고    scopus 로고
    • Release of iron from ferritin by metabolites of benzene and Superoxide radical generating agents
    • Agrawal R, Sharma PK, Rao, GS. 2001. Release of iron from ferritin by metabolites of benzene and Superoxide radical generating agents. Toxicol 168:223-30.
    • (2001) Toxicol , vol.168 , pp. 223-230
    • Agrawal, R.1    Sharma, P.K.2    Rao, G.S.3
  • 3
    • 0024431912 scopus 로고
    • Induction of hypoferremia and modulation of macrophage iron metabolism by tumor necrosis factor
    • Alvarez-Hernández X, Licéaga J, McKay IC, Brock JH. 1989. Induction of hypoferremia and modulation of macrophage iron metabolism by tumor necrosis factor. Lab Invest 61(3): 319-22.
    • (1989) Lab Invest , vol.61 , Issue.3 , pp. 319-322
    • Alvarez-Hernández, X.1    Licéaga, J.2    McKay, I.C.3    Brock, J.H.4
  • 4
    • 0017182231 scopus 로고
    • Structural and immunological relationships of isoferritins in normal and malignant cells
    • Arosio P, Yokota M, Drysdale JW. 1976. Structural and immunological relationships of isoferritins in normal and malignant cells. Cancer Res 36:1735-9.
    • (1976) Cancer Res , vol.36 , pp. 1735-1739
    • Arosio, P.1    Yokota, M.2    Drysdale, J.W.3
  • 5
    • 0017881105 scopus 로고
    • On ferritin heterogeneity; further evidence for heteropolymers
    • Arosio P, Adelman TG, Drysdale JW. 1978. On ferritin heterogeneity; further evidence for heteropolymers. J Biol Chem 253(12):4451-8.
    • (1978) J Biol Chem , vol.253 , Issue.12 , pp. 4451-4458
    • Arosio, P.1    Adelman, T.G.2    Drysdale, J.W.3
  • 8
    • 0026534555 scopus 로고
    • Stimulation of growth of neuroblastoma cells by ferritin in vitro
    • Blatt J, Wharton V. 1992. Stimulation of growth of neuroblastoma cells by ferritin in vitro. J Lab Clin Med 119:139-43.
    • (1992) J Lab Clin Med , vol.119 , pp. 139-143
    • Blatt, J.1    Wharton, V.2
  • 9
    • 0019482785 scopus 로고
    • Adaptive responses of rat tissue isoferritins to iron administration
    • Bomford A, Conlon-Hollingshead C, Munro HN. 1981. Adaptive responses of rat tissue isoferritins to iron administration. J Biol Chem 256(2):948-55.
    • (1981) J Biol Chem , vol.256 , Issue.2 , pp. 948-955
    • Bomford, A.1    Conlon-Hollingshead, C.2    Munro, H.N.3
  • 11
    • 1842583828 scopus 로고    scopus 로고
    • The putative 'nucleation site' in human H-chain ferritin is not required for mineralization of the iron core
    • Bou-Abdallah F, Biasiotto G, Arosio P, Chasteen ND. 2004. The putative 'nucleation site' in human H-chain ferritin is not required for mineralization of the iron core. Biochem 43:4332-7.
    • (2004) Biochem , vol.43 , pp. 4332-4337
    • Bou-Abdallah, F.1    Biasiotto, G.2    Arosio, P.3    Chasteen, N.D.4
  • 12
    • 14744304889 scopus 로고    scopus 로고
    • Unique iron binding and oxidation properties of human mitochondrial ferritin: A comparative analysis with human H-chain ferritin
    • Bou-Abdallah F, Santambrogio P, Levi S, Arosio P, Chasteen ND. 2005. Unique iron binding and oxidation properties of human mitochondrial ferritin: a comparative analysis with human H-chain ferritin. J Mol Biol 347:543-54.
    • (2005) J Mol Biol , vol.347 , pp. 543-554
    • Bou-Abdallah, F.1    Santambrogio, P.2    Levi, S.3    Arosio, P.4    Chasteen, N.D.5
  • 13
    • 0022199982 scopus 로고
    • Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones
    • Boyd D, Vecoli C, Belcher DM, Jain SK, Drysdale JW. 1985. Structural and functional relationships of human ferritin H and L chains deduced from cDNA clones. J Biol Chem 260(21): 11755-61.
    • (1985) J Biol Chem , vol.260 , Issue.21 , pp. 11755-11761
    • Boyd, D.1    Vecoli, C.2    Belcher, D.M.3    Jain, S.K.4    Drysdale, J.W.5
  • 14
    • 0003049873 scopus 로고
    • The red cell cycle
    • Brock JH, Halliday JW, Pippard MJ, Powell LW, editors, London: WB Saunders Company Ltd. pp
    • Brittenham GM. 1994. The red cell cycle. In: Brock JH, Halliday JW, Pippard MJ, Powell LW, editors. Iron metabolism in health and disease. London: WB Saunders Company Ltd. pp 31-62.
    • (1994) Iron metabolism in health and disease , pp. 31-62
    • Brittenham, G.M.1
  • 16
    • 0022861717 scopus 로고
    • The influence of purified recombinant human heavy-subunit and light-subunit ferritins on colony formation in vitro by granulocytemacrophage and erythroid progenitor cells
    • Broxmeyer HE, Lu L, Bicknell DC, Williams DE, Cooper S, Levi S, Salfeld J, Arosio P. 1986. The influence of purified recombinant human heavy-subunit and light-subunit ferritins on colony formation in vitro by granulocytemacrophage and erythroid progenitor cells. Blood 68(6): 1257-63.
    • (1986) Blood , vol.68 , Issue.6 , pp. 1257-1263
    • Broxmeyer, H.E.1    Lu, L.2    Bicknell, D.C.3    Williams, D.E.4    Cooper, S.5    Levi, S.6    Salfeld, J.7    Arosio, P.8
  • 17
    • 0026013466 scopus 로고
    • Mutated recombinant human heavy-chain ferritins and myelosuppression in vitro and in vivo: A link between ferritin ferroxidase activity and biological function
    • Broxmeyer HE, Cooper S, Levi, S, Arosio P. 1991. Mutated recombinant human heavy-chain ferritins and myelosuppression in vitro and in vivo: a link between ferritin ferroxidase activity and biological function. Proc Nad Acad Sci USA 88:770-4.
    • (1991) Proc Nad Acad Sci USA , vol.88 , pp. 770-774
    • Broxmeyer, H.E.1    Cooper, S.2    Levi, S.3    Arosio, P.4
  • 18
    • 0026657421 scopus 로고
    • H-ferritin: A regulatory cytokine that down-modulates cell proliferation
    • Broxmeyer HE. 1992. H-ferritin: A regulatory cytokine that down-modulates cell proliferation. J Lab Clin Med 120(3):367-70.
    • (1992) J Lab Clin Med , vol.120 , Issue.3 , pp. 367-370
    • Broxmeyer, H.E.1
  • 21
    • 0022653878 scopus 로고
    • Red cell ferritin as a diagnostic tool
    • Cazzola M, Ascari A. 1986. Red cell ferritin as a diagnostic tool. Br J Haematol 62(2):209- 13.
    • (1986) Br J Haematol , vol.62 , Issue.2 , pp. 209-213
    • Cazzola, M.1    Ascari, A.2
  • 23
    • 0031605490 scopus 로고    scopus 로고
    • Ferritin. Uptake, storage, and release of iron
    • Chasteen ND. 1998. Ferritin. Uptake, storage, and release of iron. Met Ions Biol Syst 35:479-514.
    • (1998) Met Ions Biol Syst , vol.35 , pp. 479-514
    • Chasteen, N.D.1
  • 24
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: An efficient means of iron storage
    • Chasteen ND, Harrison PM. 1999. Mineralization in ferritin: An efficient means of iron storage. J Struct Biol 126:182-94.
    • (1999) J Struct Biol , vol.126 , pp. 182-194
    • Chasteen, N.D.1    Harrison, P.M.2
  • 25
    • 0032511729 scopus 로고    scopus 로고
    • Cellular distribution of ferritin subunits in postnatal rat brain
    • Cheepsunthorn P, Palmer C, Connor JR. 1998. Cellular distribution of ferritin subunits in postnatal rat brain. J Comp Neurol 400:73-86.
    • (1998) J Comp Neurol , vol.400 , pp. 73-86
    • Cheepsunthorn, P.1    Palmer, C.2    Connor, J.R.3
  • 26
    • 34249713878 scopus 로고    scopus 로고
    • Chiancone E, Stefanini S. 1984. Heterogeneity of ferritin. I. Structural and functional aspects. In: Albertini A, Arosio P, Chiancone E, Drysdale J, editors. Ferritins and isoferritins as biochemical markers. Amsterdam: Elsevier Science Publishers. pp 23-32.
    • Chiancone E, Stefanini S. 1984. Heterogeneity of ferritin. I. Structural and functional aspects. In: Albertini A, Arosio P, Chiancone E, Drysdale J, editors. Ferritins and isoferritins as biochemical markers. Amsterdam: Elsevier Science Publishers. pp 23-32.
  • 27
    • 0023666802 scopus 로고
    • Measurement of ferritin-bearing lymphocytes in man. Preliminary studies on the use of monoclonal antibodies specific for the L and H subunits of ferritin
    • Ciriello MM, Cazzola, M, Dezza L, Levi S, Arosio P. 1987. Measurement of ferritin-bearing lymphocytes in man. Preliminary studies on the use of monoclonal antibodies specific for the L and H subunits of ferritin. Tumori 73: 37-41.
    • (1987) Tumori , vol.73 , pp. 37-41
    • Ciriello, M.M.1    Cazzola, M.2    Dezza, L.3    Levi, S.4    Arosio, P.5
  • 28
    • 0026766571 scopus 로고
    • Modulation of ferritin H-chain expression in Friend erythroleukemia cells: Transcriptional and translational regulation by hemin
    • Coccia EM, Profita V, Fiorucci G, Romeo G, Affrabi SE, Testa U, Hentze MW, Battistini A. 1992. Modulation of ferritin H-chain expression in Friend erythroleukemia cells: transcriptional and translational regulation by hemin. Mol Cell Biol 12(7):3015-22.
    • (1992) Mol Cell Biol , vol.12 , Issue.7 , pp. 3015-3022
    • Coccia, E.M.1    Profita, V.2    Fiorucci, G.3    Romeo, G.4    Affrabi, S.E.5    Testa, U.6    Hentze, M.W.7    Battistini, A.8
  • 29
    • 0028350924 scopus 로고
    • Isoforms of ferritin have a specific cellular distribution in the brain
    • Connor JR, Boeshore KL, Benkovic SA, Menzies SL. 1994. Isoforms of ferritin have a specific cellular distribution in the brain. J Neurosci Res 37(4):461 -5.
    • (1994) J Neurosci Res , vol.37 , Issue.4 , pp. 461-465
    • Connor, J.R.1    Boeshore, K.L.2    Benkovic, S.A.3    Menzies, S.L.4
  • 31
    • 34249656476 scopus 로고
    • Isoferritins in plasma
    • Albertini A, Arosio P, Chiancone E, Drysdale J, editors, Amsterdam: Elsevier Science Publishers, pp
    • Covell AM, Worwood M. 1984. Isoferritins in plasma. In: Albertini A, Arosio P, Chiancone E, Drysdale J, editors. Ferritins and isoferritins as biochemical markers. Amsterdam: Elsevier Science Publishers, pp 49-65.
    • (1984) Ferritins and isoferritins as biochemical markers , pp. 49-65
    • Covell, A.M.1    Worwood, M.2
  • 32
    • 0034682761 scopus 로고    scopus 로고
    • Overexpression of wild type and mutated human ferritin H-chain in HeLa cells
    • Cozzi A, Corsi B, Levi S, Santambrogio P, Albertini A, Arosioj P. 2000. Overexpression of wild type and mutated human ferritin H-chain in HeLa cells. J Biochem 275(33): 25122-9.
    • (2000) J Biochem , vol.275 , Issue.33 , pp. 25122-25129
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Albertini, A.5    Arosioj, P.6
  • 33
    • 0034682761 scopus 로고    scopus 로고
    • Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: In vivo role of ferroxidase activity
    • Cozzi A, Corsi B, Levi S, Santambrogio P, Albertini A, Arosio, P. 2002. Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferroxidase activity. J Biol Chem 275:25122-9.
    • (2002) J Biol Chem , vol.275 , pp. 25122-25129
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Albertini, A.5    Arosio, P.6
  • 35
    • 1542373640 scopus 로고    scopus 로고
    • Analysis of the biological functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNA: Evidence for a proliferative role of ferritin
    • Cozzi A, Corsi, B, Levi S, Santambrogio P, Biasiotto G, Arosio P. 2004. Analysis of the biological functions of H- and L-ferritins in HeLa cells by transfection with siRNAs and cDNA: Evidence for a proliferative role of ferritin. Blood 103(6): 2377-83.
    • (2004) Blood , vol.103 , Issue.6 , pp. 2377-2383
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Biasiotto, G.5    Arosio, P.6
  • 36
    • 0019835872 scopus 로고
    • Detection of a glycosylated subunit in human serum ferritin
    • Cragg SJ, Wagstaff M, Worwood M. 1981. Detection of a glycosylated subunit in human serum ferritin. Biochem J 199:565-71.
    • (1981) Biochem J , vol.199 , pp. 565-571
    • Cragg, S.J.1    Wagstaff, M.2    Worwood, M.3
  • 37
    • 0020740239 scopus 로고
    • Iron metabolism in reticuloendothelial cells
    • Deiss A. 1983. Iron metabolism in reticuloendothelial cells. Semin Hematol 20(2):81-90.
    • (1983) Semin Hematol , vol.20 , Issue.2 , pp. 81-90
    • Deiss, A.1
  • 39
    • 0027358656 scopus 로고
    • Modulation of iron metabolism in monocyte cell line U937 by inflammatory cytokines: Changes in transferrin uptake, iron handling and ferritin mRNA
    • Fahmy M, Young SP. 1993. Modulation of iron metabolism in monocyte cell line U937 by inflammatory cytokines: changes in transferrin uptake, iron handling and ferritin mRNA. Biochem J 296:175-81.
    • (1993) Biochem J , vol.296 , pp. 175-181
    • Fahmy, M.1    Young, S.P.2
  • 41
    • 0034711295 scopus 로고    scopus 로고
    • Overexpression of H ferritin and up-regulation of iron regulatory protein genes during differentiation of 3T3-L1 preadipocytes
    • Festa M, Ricciardelli G, Mele G, Pietropaolo C, Ruffo A, Colonna A. 2000. Overexpression of H ferritin and up-regulation of iron regulatory protein genes during differentiation of 3T3-L1 preadipocytes. J Biol Chem 275(47):36708-12.
    • (2000) J Biol Chem , vol.275 , Issue.47 , pp. 36708-36712
    • Festa, M.1    Ricciardelli, G.2    Mele, G.3    Pietropaolo, C.4    Ruffo, A.5    Colonna, A.6
  • 45
    • 17444413051 scopus 로고    scopus 로고
    • Release of iron from ferritin by aceto- and benzohy-droxamic acids
    • Gálvez N, Ruiz B, Cuesta R, Colacio E, Dominguez-Vera JM. 2005. Release of iron from ferritin by aceto- and benzohy-droxamic acids. Inorg Chem 44(8):2706-9.
    • (2005) Inorg Chem , vol.44 , Issue.8 , pp. 2706-2709
    • Gálvez, N.1    Ruiz, B.2    Cuesta, R.3    Colacio, E.4    Dominguez-Vera, J.M.5
  • 46
    • 0029919416 scopus 로고    scopus 로고
    • Ferritin uptake by human erythroid precursors is a regulated iron uptake pathway
    • Gelvan D, Fibach E, Meyron-Holtz EG, Konijn AM. 1996. Ferritin uptake by human erythroid precursors is a regulated iron uptake pathway. Blood 88(8):3200-7.
    • (1996) Blood , vol.88 , Issue.8 , pp. 3200-3207
    • Gelvan, D.1    Fibach, E.2    Meyron-Holtz, E.G.3    Konijn, A.M.4
  • 47
    • 0018746110 scopus 로고
    • The kinetics of serum and tissue ferritins: Relation to carbohydrate content
    • Halliday JW, Mack U, Powell LW. 1979. The kinetics of serum and tissue ferritins: relation to carbohydrate content. Br J of Haematol 42:535-46.
    • (1979) Br J of Haematol , vol.42 , pp. 535-546
    • Halliday, J.W.1    Mack, U.2    Powell, L.W.3
  • 48
    • 0018623583 scopus 로고
    • Serum ferritin and isoferritins in clinical medicine
    • Halliday JW, Powell LW. 1979. Serum ferritin and isoferritins in clinical medicine. Progr Hematol 11:229-66.
    • (1979) Progr Hematol , vol.11 , pp. 229-266
    • Halliday, J.W.1    Powell, L.W.2
  • 50
    • 0001439691 scopus 로고
    • The control of cellular iron homeostasis
    • Brock JH, Halliday JW, Pippard MJ, Powell LW, editors, W.B. Saunders Company Ltd. London, pp
    • Harford JB, Rouault TA, Klausner RD. 1994. The control of cellular iron homeostasis. In: Brock JH, Halliday JW, Pippard MJ, Powell LW, editors. Iron metabolism in health and disease. W.B. Saunders Company Ltd. London, pp 123-49.
    • (1994) Iron metabolism in health and disease , pp. 123-149
    • Harford, J.B.1    Rouault, T.A.2    Klausner, R.D.3
  • 51
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison PM, Arosio P. 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
  • 52
    • 13444266052 scopus 로고    scopus 로고
    • Hasan MR, Morishima D, Tomita K, Katsuki M, Kotani S. 2005. Identification of a 250 kDa putative microtubule-associated protein as a bovine ferritin; evidence for a ferritin-microtubule interaction. FEES J 272:822-31.
    • Hasan MR, Morishima D, Tomita K, Katsuki M, Kotani S. 2005. Identification of a 250 kDa putative microtubule-associated protein as a bovine ferritin; evidence for a ferritin-microtubule interaction. FEES J 272:822-31.
  • 53
    • 34249707009 scopus 로고
    • Serum ferritin in hematologic disorders
    • Albertini A, Arosio P, Chiancone E, Drysdale J, editors, Amsterdam: Elsevier Science Publishers, pp
    • Hershko C, Konijn AM. 1984. Serum ferritin in hematologic disorders. In: Albertini A, Arosio P, Chiancone E, Drysdale J, editors. Ferritins and isoferritins as biochemical markers. Amsterdam: Elsevier Science Publishers, pp 143-58.
    • (1984) Ferritins and isoferritins as biochemical markers , pp. 143-158
    • Hershko, C.1    Konijn, A.M.2
  • 54
    • 34249651516 scopus 로고
    • Isoferritins and prognosis of neuroblastoma: The immunological role of acidic isoferritins
    • Albertini A, Arosio P, Chiancone E, Drysdale J, editors, Amsterdam: Elsevier Science Publishers, pp
    • Hie-won L, Stahlhut MW, & Evans AE. 1984. Isoferritins and prognosis of neuroblastoma: the immunological role of acidic isoferritins. In: Albertini A, Arosio P, Chiancone E, Drysdale J, editors. Ferritins and isoferritins as biochemical markers. Amsterdam: Elsevier Science Publishers, pp 171-80.
    • (1984) Ferritins and isoferritins as biochemical markers , pp. 171-180
    • Hie-won, L.1    Stahlhut, M.W.2    Evans, A.E.3
  • 55
    • 0022655868 scopus 로고
    • The ferritin content of normoblasts and megaloblasts from human bone marrow
    • Hodgetts J, Peters SW, Hoy TG, Jacobs A. 1986. The ferritin content of normoblasts and megaloblasts from human bone marrow. Clin cSi 70:47-51.
    • (1986) Clin cSi , vol.70 , pp. 47-51
    • Hodgetts, J.1    Peters, S.W.2    Hoy, T.G.3    Jacobs, A.4
  • 56
    • 0034235751 scopus 로고    scopus 로고
    • Oligodendrocyte progenitor cells internalize ferritin via clathrindependent receptor mediated endocytosis
    • Hulet SW, Heyliger SO, Powers S, Connor JR. 2000. Oligodendrocyte progenitor cells internalize ferritin via clathrindependent receptor mediated endocytosis. J Neurosci Res 61:52-60.
    • (2000) J Neurosci Res , vol.61 , pp. 52-60
    • Hulet, S.W.1    Heyliger, S.O.2    Powers, S.3    Connor, J.R.4
  • 57
    • 0034614666 scopus 로고    scopus 로고
    • A short Fe-Fe distance in peroxodiferric ferritin: Control of Fe substrate versus cofactor decay?
    • Hwang J, Krebs C, Huynh BH, Edmondson DE, Theil EC, Penner-Hahn JE. 2000. A short Fe-Fe distance in peroxodiferric ferritin: control of Fe substrate versus cofactor decay? Science 287(5450):122-5.
    • (2000) Science , vol.287 , Issue.5450 , pp. 122-125
    • Hwang, J.1    Krebs, C.2    Huynh, B.H.3    Edmondson, D.E.4    Theil, E.C.5    Penner-Hahn, J.E.6
  • 58
    • 0037150273 scopus 로고    scopus 로고
    • Investigation of the release of iron from ferritin by naturally occurring antioxidants
    • Hynes MJ, Coinceanainn MO. 2002. Investigation of the release of iron from ferritin by naturally occurring antioxidants. J Inorg Biochem 90:18-21.
    • (2002) J Inorg Biochem , vol.90 , pp. 18-21
    • Hynes, M.J.1    Coinceanainn, M.O.2
  • 59
  • 60
    • 0026455697 scopus 로고
    • Ferritin and hemosiderin in pathological tissues
    • lancu TC. 1992. Ferritin and hemosiderin in pathological tissues. Electron Microsc Rev 5:209-29.
    • (1992) Electron Microsc Rev , vol.5 , pp. 209-229
    • lancu, T.C.1
  • 61
    • 0024999971 scopus 로고
    • Immunocytochemical detection of ferritin in human bone marrow and peripheral blood cells using monoclonal antibodies specific for the H and L subunit
    • Invernizzi R, Caccola M, De Fazio P, Rosti V, Ruggeri G, Arosio P. 1990. Immunocytochemical detection of ferritin in human bone marrow and peripheral blood cells using monoclonal antibodies specific for the H and L subunit. Br J Haematol 76:427-32.
    • (1990) Br J Haematol , vol.76 , pp. 427-432
    • Invernizzi, R.1    Caccola, M.2    De Fazio, P.3    Rosti, V.4    Ruggeri, G.5    Arosio, P.6
  • 62
    • 0016499945 scopus 로고
    • Ferritin in serum; clinical and biochemical implications
    • Jacobs A, Worwood M. 1975. Ferritin in serum; clinical and biochemical implications. New Engl J Med 292(18):951 -6.
    • (1975) New Engl J Med , vol.292 , Issue.18 , pp. 951-956
    • Jacobs, A.1    Worwood, M.2
  • 63
    • 0017700831 scopus 로고
    • Low molecular weight intracellular iron transport compounds
    • Jacobs A. 1977. Low molecular weight intracellular iron transport compounds. Blood 50(3):433-9.
    • (1977) Blood , vol.50 , Issue.3 , pp. 433-439
    • Jacobs, A.1
  • 64
    • 0011095583 scopus 로고
    • Functional aspects of isoferritins
    • Albertini A, Arosio P, Chiancone E, Drysdale J, editors, Amsterdam: Elsevier Science Publishers, pp
    • Jacobs A, Hodgetts J, Hoy TG. 1984. Functional aspects of isoferritins. In: Albertini A, Arosio P, Chiancone E, Drysdale J, editors. Ferritins and isoferritins as biochemical markers. Amsterdam: Elsevier Science Publishers, pp 113-27.
    • (1984) Ferritins and isoferritins as biochemical markers , pp. 113-127
    • Jacobs, A.1    Hodgetts, J.2    Hoy, T.G.3
  • 65
    • 4644285245 scopus 로고    scopus 로고
    • New insights into iron release from ferritin: Direct observation of the neurotoxin 6-hydroxydopamine entering ferritin and reaching redox equilibrium with the iron core
    • Jameson GNL, Jameson RF, Linert W. 2004. New insights into iron release from ferritin: direct observation of the neurotoxin 6-hydroxydopamine entering ferritin and reaching redox equilibrium with the iron core. Org Biomol Chem 2:2346-51.
    • (2004) Org Biomol Chem , vol.2 , pp. 2346-2351
    • Jameson, G.N.L.1    Jameson, R.F.2    Linert, W.3
  • 66
    • 0035954391 scopus 로고    scopus 로고
    • Opening' the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites
    • Jin W, Hidnori T, Pancorbo B, Theil EC. 2001. 'Opening' the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites. Biochem 40:7525-32.
    • (2001) Biochem , vol.40 , pp. 7525-7532
    • Jin, W.1    Hidnori, T.2    Pancorbo, B.3    Theil, E.C.4
  • 67
    • 0020627311 scopus 로고
    • Isoferritins in normal leucocytes
    • Jones BM, Worwood M, Jacobs A. 1983. Isoferritins in normal leucocytes. Br J Haematol 55(1):73-81.
    • (1983) Br J Haematol , vol.55 , Issue.1 , pp. 73-81
    • Jones, B.M.1    Worwood, M.2    Jacobs, A.3
  • 68
    • 0023775222 scopus 로고
    • Ferritin: An iron storage protein with diverse functions
    • Joshi JG, Clauberg M. 1988. Ferritin: an iron storage protein with diverse functions. Biofactors 1(3):207-12.
    • (1988) Biofactors , vol.1 , Issue.3 , pp. 207-212
    • Joshi, J.G.1    Clauberg, M.2
  • 69
    • 0035366598 scopus 로고    scopus 로고
    • Repression of the heavy chain increases the labile iron pool of human K562 cells
    • Kakhlon O, Gruenbaum, Y, Cabantchik ZI. 2001a. Repression of the heavy chain increases the labile iron pool of human K562 cells. Biochem J356(2):311-16.
    • (2001) Biochem , vol.J356 , Issue.2 , pp. 311-316
    • Kakhlon, O.1    Gruenbaum, Y.2    Cabantchik, Z.I.3
  • 70
    • 0035353194 scopus 로고    scopus 로고
    • Repression of ferritin expression increases the labile iron pool, oxidative stress, and short-term growth of human erythroleukemia cells
    • Kakhlon O, Gruenbaum Y, Cabantchik ZI. 2001b. Repression of ferritin expression increases the labile iron pool, oxidative stress, and short-term growth of human erythroleukemia cells. Blood 97:2863-71.
    • (2001) Blood , vol.97 , pp. 2863-2871
    • Kakhlon, O.1    Gruenbaum, Y.2    Cabantchik, Z.I.3
  • 71
    • 0036565766 scopus 로고    scopus 로고
    • Ferritin expression modulates cell cycle dynamics and cell responsiveness to H-ras-induced growth via expansion of the labile iron pool
    • Kakhlon O, Gruenbaum Y, Cabantchik ZI. 2002. Ferritin expression modulates cell cycle dynamics and cell responsiveness to H-ras-induced growth via expansion of the labile iron pool. Biochem J 363(3):431-6.
    • (2002) Biochem J , vol.363 , Issue.3 , pp. 431-436
    • Kakhlon, O.1    Gruenbaum, Y.2    Cabantchik, Z.I.3
  • 73
    • 0028009264 scopus 로고
    • Purification and characterization of a cell growth factor from a human leukaemia cell line: Immunological identity with ferritin
    • Kikyo N, Suda M, Kikyo N, Hagiwara K, Yasukawa K, Fujisawa M, Yazaki Y, Okabe T. 1994. Purification and characterization of a cell growth factor from a human leukaemia cell line: immunological identity with ferritin. Cancer Res 54:268 -71.
    • (1994) Cancer Res , vol.54 , pp. 268-271
    • Kikyo, N.1    Suda, M.2    Kikyo, N.3    Hagiwara, K.4    Yasukawa, K.5    Fujisawa, M.6    Yazaki, Y.7    Okabe, T.8
  • 74
    • 0035941124 scopus 로고    scopus 로고
    • Thermal stability of human ferritin: Concentration dependence and enhanced stability of an N-terminal fusion mutant
    • Kim S-W, Kim Y-H, Lee J. 2001. Thermal stability of human ferritin: concentration dependence and enhanced stability of an N-terminal fusion mutant. Biochem Biophys Res Commun 289:125-9.
    • (2001) Biochem Biophys Res Commun , vol.289 , pp. 125-129
    • Kim, S.-W.1    Kim, Y.-H.2    Lee, J.3
  • 75
    • 0028000035 scopus 로고
    • Cellular ferritin uptake: A highly regulated pathway for iron assimilation in human erythroid precursor cells
    • Konijn AM, Meyron-Holtz EG, Fibach E, Gelvan, D. 1994. Cellular ferritin uptake: a highly regulated pathway for iron assimilation in human erythroid precursor cells. Adv Exp Med Biol 356:189-97.
    • (1994) Adv Exp Med Biol , vol.356 , pp. 189-197
    • Konijn, A.M.1    Meyron-Holtz, E.G.2    Fibach, E.3    Gelvan, D.4
  • 78
    • 0029126185 scopus 로고
    • Lactoferrin: A general review
    • Levay PF, Viljoen M. 1995. Lactoferrin: a general review. Haematologica 80(3):252-67.
    • (1995) Haematologica , vol.80 , Issue.3 , pp. 252-267
    • Levay, P.F.1    Viljoen, M.2
  • 82
    • 0030035534 scopus 로고    scopus 로고
    • Evidence that residues exposed on the three-fold channels have active roles in the mechanism of ferritin iron incorporation
    • Levi S, Santambrogio P, Corsi B, Cozzi A, Arosio P. 1996. Evidence that residues exposed on the three-fold channels have active roles in the mechanism of ferritin iron incorporation. Biochem J 317(2):467-73.
    • (1996) Biochem J , vol.317 , Issue.2 , pp. 467-473
    • Levi, S.1    Santambrogio, P.2    Corsi, B.3    Cozzi, A.4    Arosio, P.5
  • 85
    • 0037386550 scopus 로고    scopus 로고
    • Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral
    • Liu X, Jin W, Theil EC. 2003. Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral. PNAS 100(7):3653-8.
    • (2003) PNAS , vol.100 , Issue.7 , pp. 3653-3658
    • Liu, X.1    Jin, W.2    Theil, E.C.3
  • 86
    • 2942558543 scopus 로고    scopus 로고
    • Ferritin reactions: Direct identification of the site for the diferric peroxide reaction intermediate
    • Liu X, Theil EC. 2004. Ferritin reactions: direct identification of the site for the diferric peroxide reaction intermediate. PNAS 101(23):8557-62.
    • (2004) PNAS , vol.101 , Issue.23 , pp. 8557-8562
    • Liu, X.1    Theil, E.C.2
  • 87
    • 0031841278 scopus 로고    scopus 로고
    • Distinct stability of recombinant L and H subunits of human ferritin; calorimetric and ANS binding studies
    • Martsev SP, Vlasov AP, Arosio P. 1998. Distinct stability of recombinant L and H subunits of human ferritin; calorimetric and ANS binding studies. Protein Eng 11(5):377-81.
    • (1998) Protein Eng , vol.11 , Issue.5 , pp. 377-381
    • Martsev, S.P.1    Vlasov, A.P.2    Arosio, P.3
  • 88
    • 10644232372 scopus 로고    scopus 로고
    • Oxidation-induced ferritin turnover in microglial cells: Role of proteasome
    • Mehlhase J, Sandig G, Pantopoulos K, Grune T. 2005. Oxidation-induced ferritin turnover in microglial cells: role of proteasome. Free Rad Biol Med 38:276-85.
    • (2005) Free Rad Biol Med , vol.38 , pp. 276-285
    • Mehlhase, J.1    Sandig, G.2    Pantopoulos, K.3    Grune, T.4
  • 89
    • 0028341609 scopus 로고
    • Binding and uptake of exogenous isoferritins by cultured human erythroid precursor cells
    • Meyron-Holtz EG, Fibach E, Gelvan D, Konijn AM. 1994. Binding and uptake of exogenous isoferritins by cultured human erythroid precursor cells. Br J Haematol 86: 635-41.
    • (1994) Br J Haematol , vol.86 , pp. 635-641
    • Meyron-Holtz, E.G.1    Fibach, E.2    Gelvan, D.3    Konijn, A.M.4
  • 90
    • 0033229699 scopus 로고    scopus 로고
    • Regulation of intracellular iron metabolism in human erythroid precursors by internalized extracellular ferritin
    • Meyron-Holtz EG, Vaisman B, Cabantchik ZI, Fibach E, Rovault TA, Hershko C, Konijn AM. 1999. Regulation of intracellular iron metabolism in human erythroid precursors by internalized extracellular ferritin. Blood 94(9):3205-11.
    • (1999) Blood , vol.94 , Issue.9 , pp. 3205-3211
    • Meyron-Holtz, E.G.1    Vaisman, B.2    Cabantchik, Z.I.3    Fibach, E.4    Rovault, T.A.5    Hershko, C.6    Konijn, A.M.7
  • 91
    • 0036182252 scopus 로고    scopus 로고
    • Denatured H-ferritin subunit is a major constituent of haemosiderin in the liver of patients with iron overload
    • Miyazaki E, Kato J, Kobune M, Okumura K, Sasaki K, Shintani N, Arosio P, Niitsu Y. 2002. Denatured H-ferritin subunit is a major constituent of haemosiderin in the liver of patients with iron overload. Gut 50:413-19.
    • (2002) Gut , vol.50 , pp. 413-419
    • Miyazaki, E.1    Kato, J.2    Kobune, M.3    Okumura, K.4    Sasaki, K.5    Shintani, N.6    Arosio, P.7    Niitsu, Y.8
  • 92
    • 0029146534 scopus 로고
    • A role for ferritin in hematopoiesis and the immune system
    • Morikawa K, Oseko F, Morikawa S. 1995. A role for ferritin in hematopoiesis and the immune system. Leuk Lymphoma 18:429-33.
    • (1995) Leuk Lymphoma , vol.18 , pp. 429-433
    • Morikawa, K.1    Oseko, F.2    Morikawa, S.3
  • 93
    • 0028090195 scopus 로고
    • The endocytic pathway for H-ferritin established in live MOLT-4 cells by laser scanning confocal microscopy
    • Moss D, Hibbs AR, Stenzel D, Powell LW, Halliday JW. 1994. The endocytic pathway for H-ferritin established in live MOLT-4 cells by laser scanning confocal microscopy. Br J Haematol 88:746-53.
    • (1994) Br J Haematol , vol.88 , pp. 746-753
    • Moss, D.1    Hibbs, A.R.2    Stenzel, D.3    Powell, L.W.4    Halliday, J.W.5
  • 94
    • 14944358625 scopus 로고    scopus 로고
    • Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis
    • Nie G, Sheftel AD, Kim SF, Ponka P. 2005. Overexpression of mitochondrial ferritin causes cytosolic iron depletion and changes cellular iron homeostasis. Blood 105(5):2161-7.
    • (2005) Blood , vol.105 , Issue.5 , pp. 2161-2167
    • Nie, G.1    Sheftel, A.D.2    Kim, S.F.3    Ponka, P.4
  • 97
    • 0035057746 scopus 로고    scopus 로고
    • Novel cellular defences against iron and oxidation: Ferritin and autophagocytosis preserve lysosomal stability in airway epithelium
    • 6(1):57-63
    • Persson HL, Nilsson KJ, Brunk UT. 2001. Novel cellular defences against iron and oxidation: ferritin and autophagocytosis preserve lysosomal stability in airway epithelium. Redox Report 6(1):57-63.
    • (2001) Redox Report
    • Persson, H.L.1    Nilsson, K.J.2    Brunk, U.T.3
  • 98
    • 0034692328 scopus 로고    scopus 로고
    • Interleukin-1β increases binding of the iron regulatory protein and the synthesis of ferritin by increasing the labile iron pool
    • Pifiero DJ, Hu J, Cook BM, Scaduto Jr, RC, Connor JR. 2000. Interleukin-1β increases binding of the iron regulatory protein and the synthesis of ferritin by increasing the labile iron pool. Biochim Biophys Acta 1497:279-88.
    • (2000) Biochim Biophys Acta , vol.1497 , pp. 279-288
    • Pifiero, D.J.1    Hu, J.2    Cook, B.M.3    Scaduto Jr, R.C.4    Connor, J.R.5
  • 99
    • 18944406393 scopus 로고    scopus 로고
    • Nanophase iron phosphate, iron arsenate, iron vanadate and iron molybdate minerals synthesized within the protein cage of ferritin
    • Polanams J, Ray AD, Watt RK. 2005. Nanophase iron phosphate, iron arsenate, iron vanadate and iron molybdate minerals synthesized within the protein cage of ferritin. Inorg Chem 44(9):3203-9.
    • (2005) Inorg Chem , vol.44 , Issue.9 , pp. 3203-3209
    • Polanams, J.1    Ray, A.D.2    Watt, R.K.3
  • 100
    • 0031963449 scopus 로고    scopus 로고
    • Function and regulation of transferrin and ferritin
    • Ponka P, Beaumont C, Richardson DR. 1998. Function and regulation of transferrin and ferritin. Sem Hematol 35(1):35-54.
    • (1998) Sem Hematol , vol.35 , Issue.1 , pp. 35-54
    • Ponka, P.1    Beaumont, C.2    Richardson, D.R.3
  • 101
  • 102
    • 0031605349 scopus 로고    scopus 로고
    • Ferritin. Its mineralization
    • Powell AK. 1998. Ferritin. Its mineralization. Met Ions Biol Syst 35:515-61.
    • (1998) Met Ions Biol Syst , vol.35 , pp. 515-561
    • Powell, A.K.1
  • 103
    • 0032533549 scopus 로고    scopus 로고
    • Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts
    • Radisky DC, Kaplan J. 1998. Iron in cytosolic ferritin can be recycled through lysosomal degradation in human fibroblasts. Biochem J 336:201-5.
    • (1998) Biochem J , vol.336 , pp. 201-205
    • Radisky, D.C.1    Kaplan, J.2
  • 104
    • 0018095305 scopus 로고
    • The iron-loaded cell-the cytopathology of iron storage
    • Richter GW. 1978. The iron-loaded cell-the cytopathology of iron storage. Am J Pathol 91(2):363-404.
    • (1978) Am J Pathol , vol.91 , Issue.2 , pp. 363-404
    • Richter, G.W.1
  • 105
    • 0021321754 scopus 로고
    • Studies of iron overload; rat liver siderosome ferritin
    • Richter GW. 1984. Studies of iron overload; rat liver siderosome ferritin. Lab Invest 50(1):26-35.
    • (1984) Lab Invest , vol.50 , Issue.1 , pp. 26-35
    • Richter, G.W.1
  • 108
    • 0033938488 scopus 로고    scopus 로고
    • Ferritin oxidation in vitro: Implication of iron release and degradation by the 20S proteasome
    • Rudeck M, Volk T, Sitte N, Grune, T. 2000. Ferritin oxidation in vitro: implication of iron release and degradation by the 20S proteasome. IUBMB Life 49:451-6.
    • (2000) IUBMB Life , vol.49 , pp. 451-456
    • Rudeck, M.1    Volk, T.2    Sitte, N.3    Grune, T.4
  • 109
  • 111
    • 14644424533 scopus 로고    scopus 로고
    • Catechol releases iron(III) from ferritin by direct chelation without iron(II) production
    • Sánchez P, Gálvez N, Colacio E, Miñones E, Domínguez-Vera JM. 2005. Catechol releases iron(III) from ferritin by direct chelation without iron(II) production. Dalton Trans 4:811-13.
    • (2005) Dalton Trans , vol.4 , pp. 811-813
    • Sánchez, P.1    Gálvez, N.2    Colacio, E.3    Miñones, E.4    Domínguez-Vera, J.M.5
  • 112
    • 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, Arosio P. 1993. Production and characterization of recombinant heteropolymers of human ferritin H and L chains. J Biol Chem 268(7):12744-48.
    • (1993) J Biol Chem , vol.268 , Issue.7 , pp. 12744-12748
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Rovida, E.4    Albertini, A.5    Arosio, P.6
  • 113
    • 0030020621 scopus 로고    scopus 로고
    • Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres
    • Santambrogio P, Levi S, Cozzi A, Corsi B, Arosio P. 1996. Evidence that the specificity of iron incorporation into homopolymers of human ferritin L- and H-chains is conferred by the nucleation and ferroxidase centres. Biochem J 314: 139-44.
    • (1996) Biochem J , vol.314 , pp. 139-144
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Corsi, B.4    Arosio, P.5
  • 115
    • 0018779087 scopus 로고
    • Ferritin as a cytosol iron transport intermediate in human reticulocytes
    • Speyer BE, Fielding J. 1979. Ferritin as a cytosol iron transport intermediate in human reticulocytes. Br J Haematol 42:255-67.
    • (1979) Br J Haematol , vol.42 , pp. 255-267
    • Speyer, B.E.1    Fielding, J.2
  • 117
    • 21744461905 scopus 로고    scopus 로고
    • Characterization of nuclear ferritin and mechanism of translocation
    • Surguladze N, Patton S, Cozzi A, Fried MG, Connor JR. 2005. Characterization of nuclear ferritin and mechanism of translocation. Biochem J 388:731-40.
    • (2005) Biochem J , vol.388 , pp. 731-740
    • Surguladze, N.1    Patton, S.2    Cozzi, A.3    Fried, M.G.4    Connor, J.R.5
  • 118
    • 0032563119 scopus 로고    scopus 로고
    • Localized unfolding at the junction of three ferritin subunits; a mechanism for iron release
    • Takagi H, Shi D, Ha Y, Allewell NM, Theil EC. 1998. Localized unfolding at the junction of three ferritin subunits; a mechanism for iron release. J Biol Chem 273(30):18685-8.
    • (1998) J Biol Chem , vol.273 , Issue.30 , pp. 18685-18688
    • Takagi, H.1    Shi, D.2    Ha, Y.3    Allewell, N.M.4    Theil, E.C.5
  • 119
    • 0037380857 scopus 로고    scopus 로고
    • Functional properties of three-fold and fourfold channels in ferritin deduced from electrostatic calculations
    • Takahashi T, Kuyucak S. 2003. Functional properties of three-fold and fourfold channels in ferritin deduced from electrostatic calculations. Biophys J 84:2256-63.
    • (2003) Biophys J , vol.84 , pp. 2256-2263
    • Takahashi, T.1    Kuyucak, S.2
  • 120
    • 0025112529 scopus 로고
    • The ferritin family of iron storage proteins
    • Theil EC. 1990. The ferritin family of iron storage proteins. Adv Enzymol Relat Areas Mol Biol 63:421-49.
    • (1990) Adv Enzymol Relat Areas Mol Biol , vol.63 , pp. 421-449
    • Theil, E.C.1
  • 121
    • 0025589263 scopus 로고
    • Ferritin and mRNA translation, structure, and gene transcription during development of animals and plants
    • Theil EC. 1990. Ferritin and mRNA translation, structure, and gene transcription during development of animals and plants. Enzyme 44(1-4):68-82.
    • (1990) Enzyme , vol.44 , Issue.1-4 , pp. 68-82
    • Theil, E.C.1
  • 122
    • 0037092516 scopus 로고    scopus 로고
    • Regulation, mechanisms and proposed function of ferritin translocation to cell nuclei
    • Thompson KJ, Fried MG, Ye Z, Boyer P, Connor JR. 2002. Regulation, mechanisms and proposed function of ferritin translocation to cell nuclei. J Cell Sci 115:2165-77.
    • (2002) J Cell Sci , vol.115 , pp. 2165-2177
    • Thompson, K.J.1    Fried, M.G.2    Ye, Z.3    Boyer, P.4    Connor, J.R.5
  • 123
    • 0032878232 scopus 로고    scopus 로고
    • Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation
    • Thomson AM, Rogers JT, Leedman PJ. 1999. Iron-regulatory proteins, iron-responsive elements and ferritin mRNA translation. Int J Biochem Cell Biol 31:1139-52.
    • (1999) Int J Biochem Cell Biol , vol.31 , pp. 1139-1152
    • Thomson, A.M.1    Rogers, J.T.2    Leedman, P.J.3
  • 124
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti FM, Torti SV. 2002. Regulation of ferritin genes and protein. Blood 99(10):3505-16.
    • (2002) Blood , vol.99 , Issue.10 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 125
    • 0028185766 scopus 로고
    • Iron and ferritin in inflammation and cancer
    • Torti SV, Torti FM. 1994. Iron and ferritin in inflammation and cancer. Adv Inorg Biochem 10:119-37.
    • (1994) Adv Inorg Biochem , vol.10 , pp. 119-137
    • Torti, S.V.1    Torti, F.M.2
  • 126
    • 0031029483 scopus 로고    scopus 로고
    • Dinuclear centre of ferritin: Studies of iron binding and oxidation show differences in the two iron sites
    • Trerffry A, Zhao Z, Quail MA, Guest JR, Harrison PM. 1997. Dinuclear centre of ferritin: studies of iron binding and oxidation show differences in the two iron sites. Biochem 36:432-41.
    • (1997) Biochem , vol.36 , pp. 432-441
    • Trerffry, A.1    Zhao, Z.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5
  • 127
    • 0035966122 scopus 로고    scopus 로고
    • Iron prevents ferritin turnover in hepatic cells
    • Truty J, Malpe R, Linder MC. 2001. Iron prevents ferritin turnover in hepatic cells. J Biol Chem 276(52):48775-80.
    • (2001) J Biol Chem , vol.276 , Issue.52 , pp. 48775-48780
    • Truty, J.1    Malpe, R.2    Linder, M.C.3
  • 128
    • 0025999689 scopus 로고
    • Influence of site-directed modifications on the formation of iron cores in ferritin
    • Wade VJ, Levi S, Arosio P, Treffry A, Harrison PM, Mann S. 1991. Influence of site-directed modifications on the formation of iron cores in ferritin. J Mol Biol 221:1443-52.
    • (1991) J Mol Biol , vol.221 , pp. 1443-1452
    • Wade, V.J.1    Levi, S.2    Arosio, P.3    Treffry, A.4    Harrison, P.M.5    Mann, S.6
  • 129
    • 0020471563 scopus 로고
    • Iron and isoferritins in iron overload
    • Wagstaff M, Worwood M, Jacobs A. 1982. Iron and isoferritins in iron overload. Clin Sci 62(5):529-40.
    • (1982) Clin Sci , vol.62 , Issue.5 , pp. 529-540
    • Wagstaff, M.1    Worwood, M.2    Jacobs, A.3
  • 131
    • 0022256654 scopus 로고
    • Electron microscopic studies of human haemosiderin and ferritin
    • Weir MP, Sharp GA, Peters TJ. 1985. Electron microscopic studies of human haemosiderin and ferritin. J Clin Pathol 38:915-8.
    • (1985) J Clin Pathol , vol.38 , pp. 915-918
    • Weir, M.P.1    Sharp, G.A.2    Peters, T.J.3
  • 132
    • 0035887749 scopus 로고    scopus 로고
    • Modification of ferritin during iron loading
    • Welch KD, Van Eeden MC, Aust SD. 2001. Modification of ferritin during iron loading. Free Rad Biol Med 31(8):999-1006.
    • (2001) Free Rad Biol Med , vol.31 , Issue.8 , pp. 999-1006
    • Welch, K.D.1    Van Eeden, M.C.2    Aust, S.D.3
  • 133
    • 0036667556 scopus 로고    scopus 로고
    • The role of cysteine residues in the oxidation of ferritin
    • Welch KD, Reilly CA, Aust SD. 2002. The role of cysteine residues in the oxidation of ferritin. Free Rad Biol Med 33(3):399-408.
    • (2002) Free Rad Biol Med , vol.33 , Issue.3 , pp. 399-408
    • Welch, K.D.1    Reilly, C.A.2    Aust, S.D.3
  • 134
    • 0023884191 scopus 로고
    • Induction of ferritin subunit synthesis by iron is regulated at both the transcriptional and translational levels
    • White K, Munro HN. 1988. Induction of ferritin subunit synthesis by iron is regulated at both the transcriptional and translational levels. J Biol Chem 263(18):8938-42.
    • (1988) J Biol Chem , vol.263 , Issue.18 , pp. 8938-8942
    • White, K.1    Munro, H.N.2
  • 135
    • 0019231210 scopus 로고
    • Hemosiderin: Nature, formation, and significance
    • Wixom RL, Prutkin L, Munro HN. 1980. Hemosiderin: nature, formation, and significance. Int Rev Exp Pathol 22:193-225.
    • (1980) Int Rev Exp Pathol , vol.22 , pp. 193-225
    • Wixom, R.L.1    Prutkin, L.2    Munro, H.N.3
  • 136
    • 0017065135 scopus 로고
    • The purification and properties of ferritin from human serum
    • Worwood M, Dawkins S, Wagstaff M, Jacobs A. 1976. The purification and properties of ferritin from human serum. Biochem J 157:97-103.
    • (1976) Biochem J , vol.157 , pp. 97-103
    • Worwood, M.1    Dawkins, S.2    Wagstaff, M.3    Jacobs, A.4
  • 137
    • 0020144407 scopus 로고
    • Ferritin in human tissues and serum
    • Worwood M. 1982. Ferritin in human tissues and serum. Clin Haematol 11(2):275-307.
    • (1982) Clin Haematol , vol.11 , Issue.2 , pp. 275-307
    • Worwood, M.1
  • 138
    • 0025615203 scopus 로고
    • Ferritin
    • Worwood M. 1990. Ferritin. Blood Rev 4:259-69.
    • (1990) Blood Rev , vol.4 , pp. 259-269
    • Worwood, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.