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Volumn 390, Issue 3, 2009, Pages 1007-1011

The conserved Trp155 in human frataxin as a hotspot for oxidative stress related chemical modifications

Author keywords

Frataxin; Friedreich's ataxia; Metallochaperone; Oxidative stress; Protein flexibility; Protein folding

Indexed keywords

CHAPERONE; FRATAXIN; REACTIVE OXYGEN METABOLITE; TRYPTOPHAN; TYROSINE;

EID: 70449705810     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.095     Document Type: Article
Times cited : (12)

References (31)
  • 2
    • 0035504444 scopus 로고    scopus 로고
    • The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly
    • Huynen M.A., Snel B., Bork P., and Gibson T.J. The phylogenetic distribution of frataxin indicates a role in iron-sulfur cluster protein assembly. Hum. Mol. Genet. 10 (2001) 2463-2468
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 2463-2468
    • Huynen, M.A.1    Snel, B.2    Bork, P.3    Gibson, T.J.4
  • 3
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • Yoon T., and Cowan J.A. Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. J. Biol. Chem. 279 (2004) 25943-25946
    • (2004) J. Biol. Chem. , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 4
    • 0037613459 scopus 로고    scopus 로고
    • Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins
    • Yoon T., and Cowan J.A. Iron-sulfur cluster biosynthesis. Characterization of frataxin as an iron donor for assembly of [2Fe-2S] clusters in ISU-type proteins. J. Am. Chem. Soc. 125 (2003) 6078-6084
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6078-6084
    • Yoon, T.1    Cowan, J.A.2
  • 5
    • 0037101845 scopus 로고    scopus 로고
    • The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins
    • Muhlenhoff U., Richhardt N., Ristow M., Kispal G., and Lill R. The yeast frataxin homolog Yfh1p plays a specific role in the maturation of cellular Fe/S proteins. Hum. Mol. Genet. 11 (2002) 2025-2036
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2025-2036
    • Muhlenhoff, U.1    Richhardt, N.2    Ristow, M.3    Kispal, G.4    Lill, R.5
  • 8
    • 0034642214 scopus 로고    scopus 로고
    • Increased levels of plasma malondialdehyde in Friedreich ataxia
    • Emond M., Lepage G., Vanasse M., and Pandolfo M. Increased levels of plasma malondialdehyde in Friedreich ataxia. Neurology 55 (2000) 1752-1753
    • (2000) Neurology , vol.55 , pp. 1752-1753
    • Emond, M.1    Lepage, G.2    Vanasse, M.3    Pandolfo, M.4
  • 9
    • 0036603021 scopus 로고    scopus 로고
    • Friedreich ataxia: a paradigm for mitochondrial diseases
    • Puccio H., and Koenig M. Friedreich ataxia: a paradigm for mitochondrial diseases. Curr. Opin. Genet. Dev. 12 (2002) 272-277
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 272-277
    • Puccio, H.1    Koenig, M.2
  • 11
    • 27944495710 scopus 로고    scopus 로고
    • RNAi-mediated suppression of the mitochondrial iron chaperone, frataxin, in Drosophila
    • Anderson P.R., Kirby K., Hilliker A.J., and Phillips J.P. RNAi-mediated suppression of the mitochondrial iron chaperone, frataxin, in Drosophila. Hum. Mol. Genet. 14 (2005) 3397-3405
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3397-3405
    • Anderson, P.R.1    Kirby, K.2    Hilliker, A.J.3    Phillips, J.P.4
  • 14
    • 50549100932 scopus 로고    scopus 로고
    • Dynamics stability and iron-binding activity of frataxin clinical mutants
    • Correia A.R., Pastore C., Adinolfi S., Pastore A., and Gomes C.M. Dynamics stability and iron-binding activity of frataxin clinical mutants. FEBS J. 275 (2008) 3680-3690
    • (2008) FEBS J. , vol.275 , pp. 3680-3690
    • Correia, A.R.1    Pastore, C.2    Adinolfi, S.3    Pastore, A.4    Gomes, C.M.5
  • 15
    • 33748745306 scopus 로고    scopus 로고
    • Conformational stability of human frataxin and effect of Friedreich's ataxia-related mutations on protein folding
    • Correia A.R., Adinolfi S., Pastore A., and Gomes C.M. Conformational stability of human frataxin and effect of Friedreich's ataxia-related mutations on protein folding. Biochem. J. 398 (2006) 605-611
    • (2006) Biochem. J. , vol.398 , pp. 605-611
    • Correia, A.R.1    Adinolfi, S.2    Pastore, A.3    Gomes, C.M.4
  • 17
    • 0025730414 scopus 로고
    • Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide
    • Radi R., Beckman J.S., Bush K.M., and Freeman B.A. Peroxynitrite oxidation of sulfhydryls. The cytotoxic potential of superoxide and nitric oxide. J. Biol. Chem. 266 (1991) 4244-4250
    • (1991) J. Biol. Chem. , vol.266 , pp. 4244-4250
    • Radi, R.1    Beckman, J.S.2    Bush, K.M.3    Freeman, B.A.4
  • 18
    • 0037064027 scopus 로고    scopus 로고
    • The ferroxidase activity of yeast frataxin
    • Park S., Gakh O., Mooney S.M., and Isaya G. The ferroxidase activity of yeast frataxin. J. Biol. Chem. 277 (2002) 38589-38595
    • (2002) J. Biol. Chem. , vol.277 , pp. 38589-38595
    • Park, S.1    Gakh, O.2    Mooney, S.M.3    Isaya, G.4
  • 19
    • 46049102185 scopus 로고    scopus 로고
    • Drosophila frataxin: an iron chaperone during cellular Fe-S cluster bioassembly
    • Kondapalli K.C., Kok N.M., Dancis A., and Stemmler T.L. Drosophila frataxin: an iron chaperone during cellular Fe-S cluster bioassembly. Biochemistry 47 (2008) 6917-6927
    • (2008) Biochemistry , vol.47 , pp. 6917-6927
    • Kondapalli, K.C.1    Kok, N.M.2    Dancis, A.3    Stemmler, T.L.4
  • 20
    • 0036570159 scopus 로고    scopus 로고
    • Oxidatively modified proteins in aging and disease
    • Beal M.F. Oxidatively modified proteins in aging and disease. Free Radic. Biol. Med. 32 (2002) 797-803
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 797-803
    • Beal, M.F.1
  • 22
    • 1642570319 scopus 로고    scopus 로고
    • Nitric oxide oxidants and protein tyrosine nitration
    • Radi R. Nitric oxide oxidants and protein tyrosine nitration. Proc. Natl. Acad. Sci. USA 101 (2004) 4003-4008
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4003-4008
    • Radi, R.1
  • 23
    • 0346100520 scopus 로고    scopus 로고
    • Peroxynitrite reactivity with amino acids and proteins
    • Alvarez B., and Radi R. Peroxynitrite reactivity with amino acids and proteins. Amino Acids 25 (2003) 295-311
    • (2003) Amino Acids , vol.25 , pp. 295-311
    • Alvarez, B.1    Radi, R.2
  • 24
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S., Stocker R., and Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324 Pt 1 (1997) 1-18
    • (1997) Biochem. J. , vol.324 , Issue.PART 1 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 25
    • 0031791713 scopus 로고    scopus 로고
    • Identification of tryptophan oxidation products in bovine alpha-crystallin
    • Finley E.L., Dillon J., Crouch R.K., and Schey K.L. Identification of tryptophan oxidation products in bovine alpha-crystallin. Protein Sci. 7 (1998) 2391-2397
    • (1998) Protein Sci. , vol.7 , pp. 2391-2397
    • Finley, E.L.1    Dillon, J.2    Crouch, R.K.3    Schey, K.L.4
  • 26
    • 0026749942 scopus 로고
    • Hydroxyl radical mediated damage to proteins with special reference to the crystallins
    • Guptasarma P., Balasubramanian D., Matsugo S., and Saito I. Hydroxyl radical mediated damage to proteins with special reference to the crystallins. Biochemistry 31 (1992) 4296-4303
    • (1992) Biochemistry , vol.31 , pp. 4296-4303
    • Guptasarma, P.1    Balasubramanian, D.2    Matsugo, S.3    Saito, I.4
  • 27
    • 34247197625 scopus 로고    scopus 로고
    • Distinct iron binding property of two putative iron donors for the iron-sulfur cluster assembly: IscA and the bacterial frataxin ortholog CyaY under physiological and oxidative stress conditions
    • Ding H., Yang J., Coleman L.C., and Yeung S. Distinct iron binding property of two putative iron donors for the iron-sulfur cluster assembly: IscA and the bacterial frataxin ortholog CyaY under physiological and oxidative stress conditions. J. Biol. Chem. 282 (2007) 7997-8004
    • (2007) J. Biol. Chem. , vol.282 , pp. 7997-8004
    • Ding, H.1    Yang, J.2    Coleman, L.C.3    Yeung, S.4
  • 28
    • 0019881197 scopus 로고
    • Formation of thiobarbituric-acid-reactive substance from deoxyribose in the presence of iron salts: the role of superoxide and hydroxyl radicals
    • Halliwell B., and Gutteridge J.M. Formation of thiobarbituric-acid-reactive substance from deoxyribose in the presence of iron salts: the role of superoxide and hydroxyl radicals. FEBS Lett. 128 (1981) 347-352
    • (1981) FEBS Lett. , vol.128 , pp. 347-352
    • Halliwell, B.1    Gutteridge, J.M.2
  • 29
    • 39749191225 scopus 로고    scopus 로고
    • Overexpression of frataxin in the mitochondria increases resistance to oxidative stress and extends lifespan in Drosophila
    • Runko A.P., Griswold A.J., and Min K.T. Overexpression of frataxin in the mitochondria increases resistance to oxidative stress and extends lifespan in Drosophila. FEBS Lett. 582 (2008) 715-719
    • (2008) FEBS Lett. , vol.582 , pp. 715-719
    • Runko, A.P.1    Griswold, A.J.2    Min, K.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.