메뉴 건너뛰기




Volumn 23, Issue 3, 2006, Pages 644-652

Characterization of the l-ferritin variant 460InsA responsible of a hereditary ferritinopathy disorder

Author keywords

Ferritin; Hereditary ferritinopathy; Iron; Oxidative stress

Indexed keywords

FERRITIN; IRON; POLYMER; PROTEIN DERIVATIVE;

EID: 33747154110     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbd.2006.05.004     Document Type: Article
Times cited : (34)

References (34)
  • 1
    • 0037101879 scopus 로고    scopus 로고
    • Ferritin, iron homeostasis, and oxidative damage
    • Arosio P., and Levi S. Ferritin, iron homeostasis, and oxidative damage. Free Radical Biol. Med. 33 (2002) 457-463
    • (2002) Free Radical Biol. Med. , vol.33 , pp. 457-463
    • Arosio, P.1    Levi, S.2
  • 2
    • 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., and Chasteen N.D. The putative "nucleation site" in human H-chain ferritin is not required for mineralization of the iron core. Biochemistry 43 (2004) 4332-4337
    • (2004) Biochemistry , vol.43 , pp. 4332-4337
    • Bou-Abdallah, F.1    Biasiotto, G.2    Arosio, P.3    Chasteen, N.D.4
  • 3
    • 14544267566 scopus 로고    scopus 로고
    • Role of ferritin and ferroportin genes in unexplained hyperferritinaemia
    • Cazzola M. Role of ferritin and ferroportin genes in unexplained hyperferritinaemia. Best Pract. Res., Clin. Haematol. 18 (2005) 251-263
    • (2005) Best Pract. Res., Clin. Haematol. , vol.18 , pp. 251-263
    • Cazzola, M.1
  • 5
    • 0029092802 scopus 로고
    • A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains
    • Connor J.R., Snyder B.S., Arosio P., Loeffler D.A., and LeWitt P. A quantitative analysis of isoferritins in select regions of aged, parkinsonian, and Alzheimer's diseased brains. J. Neurochem. 65 (1995) 717-724
    • (1995) J. Neurochem. , vol.65 , pp. 717-724
    • Connor, J.R.1    Snyder, B.S.2    Arosio, P.3    Loeffler, D.A.4    LeWitt, P.5
  • 6
    • 0024429683 scopus 로고
    • Development of an immunoassay for all human isoferritins, and its application to serum ferritin evaluation
    • Cozzi A., Levi S., Bazzigaluppi E., Ruggeri G., and Arosio P. Development of an immunoassay for all human isoferritins, and its application to serum ferritin evaluation. Clin. Chim. Acta 184 (1989) 197-206
    • (1989) Clin. Chim. Acta , vol.184 , pp. 197-206
    • Cozzi, A.1    Levi, S.2    Bazzigaluppi, E.3    Ruggeri, G.4    Arosio, P.5
  • 7
    • 0034682761 scopus 로고    scopus 로고
    • Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferritin ferroxidase activity
    • Cozzi A., Corsi B., Levi S., Santambrogio P., Albertini A., and Arosio P. Overexpression of wild type and mutated human ferritin H-chain in HeLa cells: in vivo role of ferritin ferroxidase activity. J. Biol. Chem. 275 (2000) 25122-25129
    • (2000) 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
  • 9
    • 1542373640 scopus 로고    scopus 로고
    • Analysis of the biologic functions of H- and l-ferritins in HeLa cells by transfection with siRNAs and cDNAs: evidence for a proliferative role of l-ferritin
    • Cozzi A., Corsi B., Levi S., Santambrogio P., Biasiotto G., and Arosio P. Analysis of the biologic functions of H- and l-ferritins in HeLa cells by transfection with siRNAs and cDNAs: evidence for a proliferative role of l-ferritin. Blood 103 (2004) 2377-2383
    • (2004) Blood , vol.103 , pp. 2377-2383
    • Cozzi, A.1    Corsi, B.2    Levi, S.3    Santambrogio, P.4    Biasiotto, G.5    Arosio, P.6
  • 14
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., and Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1275 (1996) 161-203
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 15
    • 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., and Kuhn L.C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 8175-8182
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 16
    • 33745752320 scopus 로고    scopus 로고
    • Mutations of Ferritin H Chain C-Terminus produced by nucleotide insertions have altered stability and functional properties
    • Ingrassia R., Gerardi G., Biasiotto G., and Arosio P. Mutations of Ferritin H Chain C-Terminus produced by nucleotide insertions have altered stability and functional properties. J. Biochem. 139 (2006) 1-5
    • (2006) J. Biochem. , vol.139 , pp. 1-5
    • Ingrassia, R.1    Gerardi, G.2    Biasiotto, G.3    Arosio, P.4
  • 17
    • 0026700576 scopus 로고
    • Loop mutations can cause a substantial conformational change in the carboxy terminus of the ferritin protein
    • Jappelli R., Luzzago A., Tataseo P., Pernice I., and Cesareni G. Loop mutations can cause a substantial conformational change in the carboxy terminus of the ferritin protein. J. Mol. Biol. 227 (1992) 532-543
    • (1992) J. Mol. Biol. , vol.227 , pp. 532-543
    • Jappelli, R.1    Luzzago, A.2    Tataseo, P.3    Pernice, I.4    Cesareni, G.5
  • 20
    • 14544294357 scopus 로고    scopus 로고
    • Neuroferritinopathy: a neurodegenerative disorder associated with l-ferritin mutation
    • Levi S., Cozzi A., and Arosio P. Neuroferritinopathy: a neurodegenerative disorder associated with l-ferritin mutation. Best Pract. Res. Clin. Haematol. 18 (2005) 265-276
    • (2005) Best Pract. Res. Clin. Haematol. , vol.18 , pp. 265-276
    • Levi, S.1    Cozzi, A.2    Arosio, P.3
  • 23
    • 4644223259 scopus 로고    scopus 로고
    • Mechanisms of gene silencing by double-stranded RNA
    • Meister G., and Tuschl T. Mechanisms of gene silencing by double-stranded RNA. Nature 431 (2004) 343-349
    • (2004) Nature , vol.431 , pp. 343-349
    • Meister, G.1    Tuschl, T.2
  • 24
    • 14944341764 scopus 로고    scopus 로고
    • Adult-onset generalized dystonia due to a mutation in the neuroferritinopathy gene
    • Mir P., Edwards M.J., Curtis A.R., Bhatia K.P., and Quinn N.P. Adult-onset generalized dystonia due to a mutation in the neuroferritinopathy gene. Mov. Disord. 20 (2005) 243-245
    • (2005) Mov. Disord. , vol.20 , pp. 243-245
    • Mir, P.1    Edwards, M.J.2    Curtis, A.R.3    Bhatia, K.P.4    Quinn, N.P.5
  • 25
    • 0035968305 scopus 로고    scopus 로고
    • Inducible nitric-oxide synthase is regulated by the proteasome degradation pathway
    • Musial A., and Eissa N.T. Inducible nitric-oxide synthase is regulated by the proteasome degradation pathway. J. Biol. Chem. 276 (2001) 24268-24273
    • (2001) J. Biol. Chem. , vol.276 , pp. 24268-24273
    • Musial, A.1    Eissa, N.T.2
  • 26
    • 0034194227 scopus 로고    scopus 로고
    • Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress
    • Reinheckel T., Ullrich O., Sitte N., and Grune T. Differential impairment of 20S and 26S proteasome activities in human hematopoietic K562 cells during oxidative stress. Arch. Biochem. Biophys. 377 (2000) 65-68
    • (2000) Arch. Biochem. Biophys. , vol.377 , pp. 65-68
    • Reinheckel, T.1    Ullrich, O.2    Sitte, N.3    Grune, T.4
  • 27
    • 0027198736 scopus 로고
    • Production and characterization of recombinant heteropolymers of human ferritin H and L chains
    • Santambrogio P., Levi S., Cozzi A., Rovida E., Albertini A., and Arosio P. Production and characterization of recombinant heteropolymers of human ferritin H and L chains. J. Biol. Chem. 268 (1993) 12744-12748
    • (1993) J. Biol. Chem. , vol.268 , pp. 12744-12748
    • Santambrogio, P.1    Levi, S.2    Cozzi, A.3    Rovida, E.4    Albertini, A.5    Arosio, P.6
  • 29
    • 4043144143 scopus 로고    scopus 로고
    • Neurodegenerative disease and iron storage in the brain
    • Thomas M., and Jankovic J. Neurodegenerative disease and iron storage in the brain. Curr. Opin. Neurol. 17 (2004) 437-442
    • (2004) Curr. Opin. Neurol. , vol.17 , pp. 437-442
    • Thomas, M.1    Jankovic, J.2
  • 30
    • 0035955494 scopus 로고    scopus 로고
    • Modulation of dopamine uptake in rat nucleus accumbens: effect of specific dopamine receptor antagonists and sigma ligands
    • Thompson T.L., Bridges S., and Miller C. Modulation of dopamine uptake in rat nucleus accumbens: effect of specific dopamine receptor antagonists and sigma ligands. Neurosci. Lett. 312 (2001) 169-172
    • (2001) Neurosci. Lett. , vol.312 , pp. 169-172
    • Thompson, T.L.1    Bridges, S.2    Miller, C.3
  • 31
    • 3843069669 scopus 로고    scopus 로고
    • Neurodegeneration caused by proteins with an aberrant carboxyl-terminus
    • Vidal R., Delisle M.B., and Ghetti B. Neurodegeneration caused by proteins with an aberrant carboxyl-terminus. J. Neuropathol. Exp. Neurol. 63 (2004) 787-800
    • (2004) J. Neuropathol. Exp. Neurol. , vol.63 , pp. 787-800
    • Vidal, R.1    Delisle, M.B.2    Ghetti, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.