메뉴 건너뛰기




Volumn 94, Issue 4, 2008, Pages 491-497

Lateral-flow immunoassay for the frataxin protein in Friedreich's ataxia patients and carriers

Author keywords

Diagnostic; Frataxin; Friedreich's ataxia; Lateral flow immunoassay; Mitochondria; Prognostic; Theranostic

Indexed keywords

FRATAXIN; RECOMBINANT FRATAXIN; RECOMBINANT PROTEIN;

EID: 46749124616     PISSN: 10967192     EISSN: 10967206     Source Type: Journal    
DOI: 10.1016/j.ymgme.2008.03.019     Document Type: Article
Times cited : (48)

References (42)
  • 1
    • 0020641096 scopus 로고
    • Classification of the hereditary ataxias and paraplegias
    • Harding A.E. Classification of the hereditary ataxias and paraplegias. Lancet 1 (1983) 1151-1155
    • (1983) Lancet , vol.1 , pp. 1151-1155
    • Harding, A.E.1
  • 4
    • 33846782071 scopus 로고    scopus 로고
    • Friedreich ataxia: Detection of GAA repeat expansions and frataxin point mutations
    • Pandolfo M. Friedreich ataxia: Detection of GAA repeat expansions and frataxin point mutations. Methods Mol. Med. 126 (2006) 197-216
    • (2006) Methods Mol. Med. , vol.126 , pp. 197-216
    • Pandolfo, M.1
  • 5
    • 0034969491 scopus 로고    scopus 로고
    • Friedreich ataxia: from GAA triplet-repeat expansion to frataxin deficiency
    • Patel P.I., and Isaya G. Friedreich ataxia: from GAA triplet-repeat expansion to frataxin deficiency. Am. J. Hum. Genet. 69 (2001) 15-24
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 15-24
    • Patel, P.I.1    Isaya, G.2
  • 8
    • 0030895266 scopus 로고    scopus 로고
    • Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet-repeat expansion
    • Bidichandani S.I., Ashizawa T., and Patel P.I. Atypical Friedreich ataxia caused by compound heterozygosity for a novel missense mutation and the GAA triplet-repeat expansion. Am. J. Hum. Genet. 60 (1997) 1251-1256
    • (1997) Am. J. Hum. Genet. , vol.60 , pp. 1251-1256
    • Bidichandani, S.I.1    Ashizawa, T.2    Patel, P.I.3
  • 13
    • 0033951420 scopus 로고    scopus 로고
    • Very late-onset Friedreich ataxia despite large GAA triplet repeat expansions
    • Bidichandani S.I., Garcia C.A., Patel P.I., and Dimachkie M.M. Very late-onset Friedreich ataxia despite large GAA triplet repeat expansions. Arch. Neurol. 57 (2000) 246-251
    • (2000) Arch. Neurol. , vol.57 , pp. 246-251
    • Bidichandani, S.I.1    Garcia, C.A.2    Patel, P.I.3    Dimachkie, M.M.4
  • 14
    • 0031941447 scopus 로고    scopus 로고
    • The GAA triplet-repeat expansion in Friedreich ataxia interferes with transcription and may be associated with an unusual DNA structure
    • Bidichandani S.I., Ashizawa T., and Patel P.I. The GAA triplet-repeat expansion in Friedreich ataxia interferes with transcription and may be associated with an unusual DNA structure. Am. J. Hum. Genet. 62 (1998) 111-121
    • (1998) Am. J. Hum. Genet. , vol.62 , pp. 111-121
    • Bidichandani, S.I.1    Ashizawa, T.2    Patel, P.I.3
  • 16
    • 0032486276 scopus 로고    scopus 로고
    • Inhibitory effects of expanded GAA.TTC triplet repeats from intron I of the Friedreich ataxia gene on transcription and replication in vivo
    • Ohshima K., Montermini L., Wells R.D., and Pandolfo M. Inhibitory effects of expanded GAA.TTC triplet repeats from intron I of the Friedreich ataxia gene on transcription and replication in vivo. J. Biol. Chem. 273 (1998) 14588-14595
    • (1998) J. Biol. Chem. , vol.273 , pp. 14588-14595
    • Ohshima, K.1    Montermini, L.2    Wells, R.D.3    Pandolfo, M.4
  • 20
    • 33845693952 scopus 로고    scopus 로고
    • Frataxin knockdown causes loss of cytoplasmic iron-sulfur cluster functions, redox alterations and induction of heme transcripts
    • Lu C., and Cortopassi G. Frataxin knockdown causes loss of cytoplasmic iron-sulfur cluster functions, redox alterations and induction of heme transcripts. Arch. Biochem. Biophys. 457 (2007) 111-122
    • (2007) Arch. Biochem. Biophys. , vol.457 , pp. 111-122
    • Lu, C.1    Cortopassi, G.2
  • 21
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau A.L., O'Neill H.A., Kennedy M.C., Ikeda-Saito M., Isaya G., and Szweda L.I. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 305 (2004) 242-245
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 22
    • 31544445770 scopus 로고    scopus 로고
    • Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
    • Gakh O., Park S., Liu G., Macomber L., Imlay J.A., Ferreira G.C., and Isaya G. Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity. Hum. Mol. Genet. 15 (2006) 467-479
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 467-479
    • Gakh, O.1    Park, S.2    Liu, G.3    Macomber, L.4    Imlay, J.A.5    Ferreira, G.C.6    Isaya, G.7
  • 23
    • 38649103446 scopus 로고    scopus 로고
    • Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia
    • Anderson P.R., Kirby K., Orr W.C., Hilliker A.J., and Phillips J.P. Hydrogen peroxide scavenging rescues frataxin deficiency in a Drosophila model of Friedreich's ataxia. Proc. Natl. Acad. Sci. USA 105 (2008) 611-616
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 611-616
    • Anderson, P.R.1    Kirby, K.2    Orr, W.C.3    Hilliker, A.J.4    Phillips, J.P.5
  • 24
    • 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
  • 26
    • 33748796912 scopus 로고    scopus 로고
    • Rational selection of small molecules that increase transcription through the GAA repeats found in Friedreich's ataxia
    • Grant L., Sun J., Xu H., Subramony S.H., Chaires J.B., and Hebert M.D. Rational selection of small molecules that increase transcription through the GAA repeats found in Friedreich's ataxia. FEBS Lett. 580 (2006) 5399-5405
    • (2006) FEBS Lett. , vol.580 , pp. 5399-5405
    • Grant, L.1    Sun, J.2    Xu, H.3    Subramony, S.H.4    Chaires, J.B.5    Hebert, M.D.6
  • 28
    • 0038448961 scopus 로고    scopus 로고
    • Upregulation of expression from the FRDA genomic locus for the therapy of Friedreich ataxia
    • Sarsero J.P., Li L., Wardan H., Sitte K., Williamson R., and Ioannou P.A. Upregulation of expression from the FRDA genomic locus for the therapy of Friedreich ataxia. J. Gene Med. 5 (2003) 72-81
    • (2003) J. Gene Med. , vol.5 , pp. 72-81
    • Sarsero, J.P.1    Li, L.2    Wardan, H.3    Sitte, K.4    Williamson, R.5    Ioannou, P.A.6
  • 29
    • 33746795976 scopus 로고    scopus 로고
    • DNA sequence-specific polyamides alleviate transcription inhibition associated with long GAA.TTC repeats in Friedreich's ataxia
    • Burnett R., Melander C., Puckett J.W., Son L.S., Wells R.D., Dervan P.B., and Gottesfeld J.M. DNA sequence-specific polyamides alleviate transcription inhibition associated with long GAA.TTC repeats in Friedreich's ataxia. Proc. Natl. Acad. Sci. USA 103 (2006) 11497-11502
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 11497-11502
    • Burnett, R.1    Melander, C.2    Puckett, J.W.3    Son, L.S.4    Wells, R.D.5    Dervan, P.B.6    Gottesfeld, J.M.7
  • 31
    • 0036472291 scopus 로고    scopus 로고
    • Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia
    • Cavadini P., O'Neill H.A., Benada O., and Isaya G. Assembly and iron-binding properties of human frataxin, the protein deficient in Friedreich ataxia. Hum. Mol. Genet. 11 (2002) 217-227
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 217-227
    • Cavadini, P.1    O'Neill, H.A.2    Benada, O.3    Isaya, G.4
  • 32
    • 0034731447 scopus 로고    scopus 로고
    • Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates
    • Cavadini P., Adamec J., Taroni F., Gakh O., and Isaya G. Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates. J. Biol. Chem. 275 (2000) 41469-41475
    • (2000) J. Biol. Chem. , vol.275 , pp. 41469-41475
    • Cavadini, P.1    Adamec, J.2    Taroni, F.3    Gakh, O.4    Isaya, G.5
  • 33
    • 0023709368 scopus 로고
    • Efficient hybridoma production using previously frozen splenocytes
    • Marusich M.F. Efficient hybridoma production using previously frozen splenocytes. J. Immunol. Methods 114 (1988) 155-159
    • (1988) J. Immunol. Methods , vol.114 , pp. 155-159
    • Marusich, M.F.1
  • 34
    • 9644284455 scopus 로고    scopus 로고
    • Supramolecular assemblies of human frataxin are formed via subunit-subunit interactions mediated by a non-conserved amino-terminal region
    • O'Neill H.A., Gakh O., and Isaya G. Supramolecular assemblies of human frataxin are formed via subunit-subunit interactions mediated by a non-conserved amino-terminal region. J. Mol. Biol. 345 (2005) 433-439
    • (2005) J. Mol. Biol. , vol.345 , pp. 433-439
    • O'Neill, H.A.1    Gakh, O.2    Isaya, G.3
  • 35
    • 0031656903 scopus 로고    scopus 로고
    • Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase
    • Koutnikova H., Campuzano V., and Koenig M. Maturation of wild-type and mutated frataxin by the mitochondrial processing peptidase. Hum. Mol. Genet. 7 (1998) 1485-1489
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1485-1489
    • Koutnikova, H.1    Campuzano, V.2    Koenig, M.3
  • 36
    • 34247643174 scopus 로고    scopus 로고
    • N-terminal iron-mediated self-cleavage of human fratax: regulation of iron binding and complex formation with target proteins
    • Yoon T., Dizin E., and Cowan J.A. N-terminal iron-mediated self-cleavage of human fratax: regulation of iron binding and complex formation with target proteins. J. Biol. Inorg. Chem. 12 (2007) 535-542
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 535-542
    • Yoon, T.1    Dizin, E.2    Cowan, J.A.3
  • 38
    • 0032800601 scopus 로고    scopus 로고
    • Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain
    • Foury F. Low iron concentration and aconitase deficiency in a yeast frataxin homologue deficient strain. FEBS Lett. 456 (1999) 281-284
    • (1999) FEBS Lett. , vol.456 , pp. 281-284
    • Foury, F.1
  • 40
    • 34447316711 scopus 로고    scopus 로고
    • Mitochondrial frataxin interacts with ISD11 of the Nfs1/ISCU complex and multiple mitochondrial chaperones
    • Shan Y., Napoli E., and Cortopassi G. Mitochondrial frataxin interacts with ISD11 of the Nfs1/ISCU complex and multiple mitochondrial chaperones. Hum. Mol. Genet. (2007)
    • (2007) Hum. Mol. Genet.
    • Shan, Y.1    Napoli, E.2    Cortopassi, G.3
  • 41
    • 9744248303 scopus 로고    scopus 로고
    • Iron-sulfur protein maturation in human cells: evidence for a function of frataxin
    • Stehling O., Elsasser H.P., Bruckel B., Muhlenhoff U., and Lill R. Iron-sulfur protein maturation in human cells: evidence for a function of frataxin. Hum. Mol. Genet. 13 (2004) 3007-3015
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 3007-3015
    • Stehling, O.1    Elsasser, H.P.2    Bruckel, B.3    Muhlenhoff, U.4    Lill, R.5
  • 42
    • 33646162871 scopus 로고    scopus 로고
    • Gene expression profiling in frataxin deficient mice: microarray evidence for significant expression changes without detectable neurodegeneration
    • Coppola G., Choi S.H., Santos M.M., Miranda C.J., Tentler D., Wexler E.M., Pandolfo M., and Geschwind D.H. Gene expression profiling in frataxin deficient mice: microarray evidence for significant expression changes without detectable neurodegeneration. Neurobiol. Dis. 22 (2006) 302-311
    • (2006) Neurobiol. Dis. , vol.22 , pp. 302-311
    • Coppola, G.1    Choi, S.H.2    Santos, M.M.3    Miranda, C.J.4    Tentler, D.5    Wexler, E.M.6    Pandolfo, M.7    Geschwind, D.H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.