메뉴 건너뛰기




Volumn 21, Issue 6, 2012, Pages 1230-1247

A TAT-frataxin fusion protein increases lifespan and cardiac function in a conditional Friedreich's ataxia mouse model

Author keywords

[No Author keywords available]

Indexed keywords

ACONITATE HYDRATASE; CASPASE 3; FRATAXIN; HYBRID PROTEIN; MITOCHONDRIA PROCESSING PEPTIDASE; MITOCHONDRIAL ENZYME; TAT FRATAXIN FUSION PROTEIN; TRANSACTIVATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84863278400     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddr554     Document Type: Article
Times cited : (82)

References (99)
  • 1
    • 0019782799 scopus 로고
    • Friedreich's ataxia: a clinical and genetic study of 90 families with an analysis of early diagnostic criteria and intrafamilial clustering of clinical features
    • Harding, A.E. (1981) Friedreich's ataxia: a clinical and genetic study of 90 families with an analysis of early diagnostic criteria and intrafamilial clustering of clinical features. Brain, 104, 589-620.
    • (1981) Brain , vol.104 , pp. 589-620
    • Harding, A.E.1
  • 4
    • 1842370633 scopus 로고    scopus 로고
    • Friedreich's ataxia. Revision of the phenotype according to molecular genetics
    • Schols, L., Amoiridis, G., Przuntek, H., Frank, G., Epplen, J.T. and Epplen, C. (1997) Friedreich's ataxia. Revision of the phenotype according to molecular genetics. Brain, 120 (Pt 12), 2131-2140.
    • (1997) Brain , vol.120 , Issue.PART 12 , pp. 2131-2140
    • Schols, L.1    Amoiridis, G.2    Przuntek, H.3    Frank, G.4    Epplen, J.T.5    Epplen, C.6
  • 7
    • 0016734732 scopus 로고
    • Friedreich's ataxia in Western Norway
    • Skre, H. (1975) Friedreich's ataxia in Western Norway. Clin. Genet., 7, 287-298.
    • (1975) Clin. Genet. , vol.7 , pp. 287-298
    • Skre, H.1
  • 8
    • 0031009267 scopus 로고    scopus 로고
    • Differential stability of the (GAA)n tract in the Friedreich ataxia (STM7) gene
    • Epplen, C., Epplen, J.T., Frank, G., Miterski, B., Santos, E.J. and Schols, L. (1997) Differential stability of the (GAA)n tract in the Friedreich ataxia (STM7) gene. Hum. Genet., 99, 834-836.
    • (1997) Hum. Genet. , vol.99 , pp. 834-836
    • Epplen, C.1    Epplen, J.T.2    Frank, G.3    Miterski, B.4    Santos, E.J.5    Schols, L.6
  • 9
    • 54049142098 scopus 로고    scopus 로고
    • Friedreich ataxia
    • Pandolfo, M. (2008) Friedreich ataxia. Arch. Neurol., 65, 1296-1303.
    • (2008) Arch. Neurol. , vol.65 , pp. 1296-1303
    • Pandolfo, M.1
  • 10
    • 0034969491 scopus 로고    scopus 로고
    • Friedreich ataxia: from GAA triplet-repeat expansion to frataxin deficiency
    • Patel, P.I. and Isaya, G. (2001) Friedreich ataxia: from GAA triplet-repeat expansion to frataxin deficiency. Am. J. Hum. Genet., 69, 15-24.
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 15-24
    • Patel, P.I.1    Isaya, G.2
  • 11
  • 12
    • 0035920101 scopus 로고    scopus 로고
    • Sticky DNA, a self-associated complex formed at long GAA * TTC repeats in intron 1 of the frataxin gene, inhibits transcription
    • Sakamoto, N., Ohshima, K., Montermini, L., Pandolfo, M. and Wells, R.D. (2001) Sticky DNA, a self-associated complex formed at long GAA * TTC repeats in intron 1 of the frataxin gene, inhibits transcription. J. Biol. Chem., 276, 27171-27177.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27171-27177
    • Sakamoto, N.1    Ohshima, K.2    Montermini, L.3    Pandolfo, M.4    Wells, R.D.5
  • 16
    • 33747330134 scopus 로고    scopus 로고
    • Mrs3p, Mrs4p, and frataxin provide iron for Fe-S cluster synthesis in mitochondria
    • Zhang, Y., Lyver, E.R., Knight, S.A., Pain, D., Lesuisse, E. and Dancis, A. (2006) Mrs3p, Mrs4p, and frataxin provide iron for Fe-S cluster synthesis in mitochondria. J. Biol. Chem., 281, 22493-22502.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22493-22502
    • Zhang, Y.1    Lyver, E.R.2    Knight, S.A.3    Pain, D.4    Lesuisse, E.5    Dancis, A.6
  • 17
    • 70349504414 scopus 로고    scopus 로고
    • Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant
    • Huang, M.L., Becker, E.M., Whitnall, M., Rahmanto, Y.S., Ponka, P. and Richardson, D.R. (2009) Elucidation of the mechanism of mitochondrial iron loading in Friedreich's ataxia by analysis of a mouse mutant. Proc. Natl Acad. Sci. USA, 106, 16381-16386.
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 16381-16386
    • Huang, M.L.1    Becker, E.M.2    Whitnall, M.3    Rahmanto, Y.S.4    Ponka, P.5    Richardson, D.R.6
  • 18
    • 2942744572 scopus 로고    scopus 로고
    • Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis
    • Yoon, T. and Cowan, J.A. (2004) Frataxin-mediated iron delivery to ferrochelatase in the final step of heme biosynthesis. J. Biol. Chem., 279, 25943-25946.
    • (2004) J. Biol. Chem. , vol.279 , pp. 25943-25946
    • Yoon, T.1    Cowan, J.A.2
  • 19
    • 76549093324 scopus 로고    scopus 로고
    • Iron-binding activity in yeast frataxin entails a trade off with stability in the alpha1/beta1 acidic ridge region
    • Correia, A.R., Wang, T., Craig, E.A. and Gomes, C.M. (2010) Iron-binding activity in yeast frataxin entails a trade off with stability in the alpha1/beta1 acidic ridge region. Biochem. J., 426, 197-203.
    • (2010) Biochem. J. , vol.426 , pp. 197-203
    • Correia, A.R.1    Wang, T.2    Craig, E.A.3    Gomes, C.M.4
  • 20
    • 78049305276 scopus 로고    scopus 로고
    • Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
    • Tsai, C.L. and Barondeau, D.P. (2010) Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex. Biochemistry, 49, 9132-9139.
    • (2010) Biochemistry , vol.49 , pp. 9132-9139
    • Tsai, C.L.1    Barondeau, D.P.2
  • 21
    • 77956248535 scopus 로고    scopus 로고
    • Frataxin and mitochondrial FeS cluster biogenesis
    • Stemmler, T.L., Lesuisse, E., Pain, D. and Dancis, A. (2010) Frataxin and mitochondrial FeS cluster biogenesis. J. Biol. Chem., 285, 26737-26743.
    • (2010) J. Biol. Chem. , vol.285 , pp. 26737-26743
    • Stemmler, T.L.1    Lesuisse, E.2    Pain, D.3    Dancis, A.4
  • 22
    • 79551514731 scopus 로고    scopus 로고
    • Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex
    • Schmucker, S., Martelli, A., Colin, F., Page, A., Wattenhofer-Donze, M., Reutenauer, L. and Puccio, H. (2011) Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex. PLoS One, 6, e16199.
    • (2011) PLoS One , vol.6
    • Schmucker, S.1    Martelli, A.2    Colin, F.3    Page, A.4    Wattenhofer-Donze, M.5    Reutenauer, L.6    Puccio, H.7
  • 25
    • 0034839688 scopus 로고    scopus 로고
    • Cardiac energetics are abnormal in Friedreich ataxia patients in the absence of cardiac dysfunction and hypertrophy: an in vivo 31P magnetic resonance spectroscopy study
    • Lodi, R., Rajagopalan, B., Blamire, A.M., Cooper, J.M., Davies, C.H., Bradley, J.L., Styles, P. and Schapira, A.H. (2001) Cardiac energetics are abnormal in Friedreich ataxia patients in the absence of cardiac dysfunction and hypertrophy: an in vivo 31P magnetic resonance spectroscopy study. Cardiovasc. Res., 52, 111-119.
    • (2001) Cardiovasc. Res. , vol.52 , pp. 111-119
    • Lodi, R.1    Rajagopalan, B.2    Blamire, A.M.3    Cooper, J.M.4    Davies, C.H.5    Bradley, J.L.6    Styles, P.7    Schapira, A.H.8
  • 27
    • 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. (2000) Two-step processing of human frataxin by mitochondrial processing peptidase. Precursor and intermediate forms are cleaved at different rates. J. Biol. Chem., 275, 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
  • 30
    • 0037317490 scopus 로고    scopus 로고
    • Friedreich's ataxia: iron chelators that target the mitochondrion as a therapeutic strategy?
    • Richardson, D.R. (2003) Friedreich's ataxia: iron chelators that target the mitochondrion as a therapeutic strategy? Expert. Opin. Investig. Drugs, 12, 235-245.
    • (2003) Expert. Opin. Investig. Drugs , vol.12 , pp. 235-245
    • Richardson, D.R.1
  • 31
    • 0348136710 scopus 로고    scopus 로고
    • Mitochondria-targeted antioxidants protect Friedreich ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants
    • Jauslin, M.L., Meier, T., Smith, R.A. and Murphy, M.P. (2003) Mitochondria-targeted antioxidants protect Friedreich ataxia fibroblasts from endogenous oxidative stress more effectively than untargeted antioxidants. FASEB J., 17, 1972-1974.
    • (2003) FASEB J. , vol.17 , pp. 1972-1974
    • Jauslin, M.L.1    Meier, T.2    Smith, R.A.3    Murphy, M.P.4
  • 33
    • 0035138072 scopus 로고    scopus 로고
    • Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits
    • Puccio, H., Simon, D., Cossee, M., Criqui-Filipe, P., Tiziano, F., Melki, J., Hindelang, C., Matyas, R., Rustin, P. and Koenig, M. (2001) Mouse models for Friedreich ataxia exhibit cardiomyopathy, sensory nerve defect and Fe-S enzyme deficiency followed by intramitochondrial iron deposits. Nat. Genet., 27, 181-186.
    • (2001) Nat. Genet. , vol.27 , pp. 181-186
    • Puccio, H.1    Simon, D.2    Cossee, M.3    Criqui-Filipe, P.4    Tiziano, F.5    Melki, J.6    Hindelang, C.7    Matyas, R.8    Rustin, P.9    Koenig, M.10
  • 34
    • 0033520487 scopus 로고    scopus 로고
    • In vivo protein transduction: delivery of a biologically active protein into the mouse
    • Schwarze, S.R., Ho, A., Vocero-Akbani, A. and Dowdy, S.F. (1999) In vivo protein transduction: delivery of a biologically active protein into the mouse. Science, 285, 1569-1572.
    • (1999) Science , vol.285 , pp. 1569-1572
    • Schwarze, S.R.1    Ho, A.2    Vocero-Akbani, A.3    Dowdy, S.F.4
  • 36
    • 38449084627 scopus 로고    scopus 로고
    • Cellular uptake and lysosomal delivery of galactocerebrosidase tagged with the HIV Tat protein transduction domain
    • Zhang, X.Y., Dinh, A., Cronin, J., Li, S.C. and Reiser, J. (2008) Cellular uptake and lysosomal delivery of galactocerebrosidase tagged with the HIV Tat protein transduction domain. J. Neurochem., 104, 1055-1064.
    • (2008) J. Neurochem. , vol.104 , pp. 1055-1064
    • Zhang, X.Y.1    Dinh, A.2    Cronin, J.3    Li, S.C.4    Reiser, J.5
  • 38
    • 0038730828 scopus 로고    scopus 로고
    • A novel TAT-Mitochondrial signal sequence fusion protein is processed, stays in mitochondria, and crosses the placenta
    • Del Gaizo, V. and Payne, R.M. (2003) A novel TAT-Mitochondrial signal sequence fusion protein is processed, stays in mitochondria, and crosses the placenta. Mol. Ther., 7, 720-730.
    • (2003) Mol. Ther. , vol.7 , pp. 720-730
    • Del Gaizo, V.1    Payne, R.M.2
  • 40
    • 79951671130 scopus 로고    scopus 로고
    • Successful TAT-mediated enzyme replacement therapy in a mouse model of mitochondrial E3 deficiency
    • Rapoport, M., Salman, L., Sabag, O., Patel, M.S. and Lorberboum-Galski, H. (2011) Successful TAT-mediated enzyme replacement therapy in a mouse model of mitochondrial E3 deficiency. J. Mol. Med., 89, 161-170.
    • (2011) J. Mol. Med. , vol.89 , pp. 161-170
    • Rapoport, M.1    Salman, L.2    Sabag, O.3    Patel, M.S.4    Lorberboum-Galski, H.5
  • 41
    • 33749425409 scopus 로고    scopus 로고
    • TAT-mediated intracellular delivery of purine nucleoside phosphorylase corrects its deficiency in mice
    • Toro, A. and Grunebaum, E. (2006) TAT-mediated intracellular delivery of purine nucleoside phosphorylase corrects its deficiency in mice. J. Clin. Invest., 116, 2717-2726.
    • (2006) J. Clin. Invest. , vol.116 , pp. 2717-2726
    • Toro, A.1    Grunebaum, E.2
  • 42
    • 5444224643 scopus 로고    scopus 로고
    • Efficacy of MitoTracker Green and CMXrosamine to measure changes in mitochondrial membrane potentials in living cells and tissues
    • Pendergrass, W., Wolf, N. and Poot, M. (2004) Efficacy of MitoTracker Green and CMXrosamine to measure changes in mitochondrial membrane potentials in living cells and tissues. Cytometry A, 61, 162-169.
    • (2004) Cytometry A , vol.61 , pp. 162-169
    • Pendergrass, W.1    Wolf, N.2    Poot, M.3
  • 44
    • 0033214787 scopus 로고    scopus 로고
    • Complementation between mitochondrial processing peptidase (MPP) subunits from different species
    • Adamec, J., Gakh, O., Spizek, J. and Kalousek, F. (1999) Complementation between mitochondrial processing peptidase (MPP) subunits from different species. Arch. Biochem. Biophys., 370, 77-85.
    • (1999) Arch. Biochem. Biophys. , vol.370 , pp. 77-85
    • Adamec, J.1    Gakh, O.2    Spizek, J.3    Kalousek, F.4
  • 45
    • 0024383393 scopus 로고
    • Synthetic transit peptides inhibit import and processing of mitochondrial precursor proteins
    • Chu, T.W., Eftime, R., Sztul, E. and Strauss, A.W. (1989) Synthetic transit peptides inhibit import and processing of mitochondrial precursor proteins. J. Biol. Chem., 264, 9552-9558.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9552-9558
    • Chu, T.W.1    Eftime, R.2    Sztul, E.3    Strauss, A.W.4
  • 46
    • 0023696451 scopus 로고
    • Import of the malate dehydrogenase precursor by mitochondria. Cleavage within leader peptide by matrix protease leads to formation of intermediate-sized form
    • Sztul, E.S., Chu, T.W., Strauss, A.W. and Rosenberg, L.E. (1988) Import of the malate dehydrogenase precursor by mitochondria. Cleavage within leader peptide by matrix protease leads to formation of intermediate-sized form. J. Biol. Chem., 263, 12085-12091.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12085-12091
    • Sztul, E.S.1    Chu, T.W.2    Strauss, A.W.3    Rosenberg, L.E.4
  • 47
    • 0025821619 scopus 로고
    • Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide
    • Isaya, G., Kalousek, F., Fenton, W.A. and Rosenberg, L.E. (1991) Cleavage of precursors by the mitochondrial processing peptidase requires a compatible mature protein or an intermediate octapeptide. J. Cell. Biol., 113, 65-76.
    • (1991) J. Cell. Biol. , vol.113 , pp. 65-76
    • Isaya, G.1    Kalousek, F.2    Fenton, W.A.3    Rosenberg, L.E.4
  • 48
    • 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. (2007) Frataxin knockdown causes loss of cytoplasmic iron-sulfur cluster functions, redox alterations and induction of heme transcripts. Arch. Biochem. Biophys., 457, 111-122.
    • (2007) Arch. Biochem. Biophys. , vol.457 , pp. 111-122
    • Lu, C.1    Cortopassi, G.2
  • 49
    • 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. (2004) Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science, 305, 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
  • 50
    • 0031885039 scopus 로고    scopus 로고
    • Antioxidant properties of 2,3-dimethoxy-5-methyl-6-(10-hydroxydecyl)-1,4-benzoquinone (idebenone)
    • Mordente, A., Martorana, G.E., Minotti, G. and Giardina, B. (1998) Antioxidant properties of 2,3-dimethoxy-5-methyl-6-(10-hydroxydecyl)-1,4-benzoquinone (idebenone). Chem. Res. Toxicol., 11, 54-63.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 54-63
    • Mordente, A.1    Martorana, G.E.2    Minotti, G.3    Giardina, B.4
  • 52
    • 34547760795 scopus 로고    scopus 로고
    • Understanding the binding properties of an unusual metal-binding protein-a study of bacterial frataxin
    • Pastore, C., Franzese, M., Sica, F., Temussi, P. and Pastore, A. (2007) Understanding the binding properties of an unusual metal-binding protein-a study of bacterial frataxin. Febs J, 274, 4199-4210.
    • (2007) Febs J , vol.274 , pp. 4199-4210
    • Pastore, C.1    Franzese, M.2    Sica, F.3    Temussi, P.4    Pastore, A.5
  • 53
    • 0033582421 scopus 로고    scopus 로고
    • The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle
    • Radisky, D.C., Babcock, M.C. and Kaplan, J. (1999) The yeast frataxin homologue mediates mitochondrial iron efflux. Evidence for a mitochondrial iron cycle. J. Biol. Chem., 274, 4497-4499.
    • (1999) J. Biol. Chem. , vol.274 , pp. 4497-4499
    • Radisky, D.C.1    Babcock, M.C.2    Kaplan, J.3
  • 54
    • 0031567601 scopus 로고    scopus 로고
    • Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
    • Foury, F. and Cazzalini, O. (1997) Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria. FEBS Lett., 411, 373-377.
    • (1997) FEBS Lett. , vol.411 , pp. 373-377
    • Foury, F.1    Cazzalini, O.2
  • 55
    • 0033054177 scopus 로고    scopus 로고
    • The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • Wong, A., Yang, J., Cavadini, P., Gellera, C., Lonnerdal, B., Taroni, F. and Cortopassi, G. (1999) The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet., 8, 425-430.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Gellera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 56
    • 0031260335 scopus 로고    scopus 로고
    • Elevated ferritin production, iron containment, and oxidant resistance in hemin-treated leukemia cells
    • Lin, F. and Girotti, A.W. (1997) Elevated ferritin production, iron containment, and oxidant resistance in hemin-treated leukemia cells. Arch. Biochem. Biophys., 346, 131-141.
    • (1997) Arch. Biochem. Biophys. , vol.346 , pp. 131-141
    • Lin, F.1    Girotti, A.W.2
  • 57
    • 0030218886 scopus 로고    scopus 로고
    • Effects of increasing intracellular reactive iron level on cardiac function and oxidative injury in the isolated rat heart
    • Oubidar, M., Marie, C., Mossiat, C. and Bralet, J. (1996) Effects of increasing intracellular reactive iron level on cardiac function and oxidative injury in the isolated rat heart. J. Mol. Cell. Cardiol., 28, 1769-1776.
    • (1996) J. Mol. Cell. Cardiol. , vol.28 , pp. 1769-1776
    • Oubidar, M.1    Marie, C.2    Mossiat, C.3    Bralet, J.4
  • 58
    • 0029744364 scopus 로고    scopus 로고
    • Differential cytoprotection by glycine against oxidant damage to proximal tubule cells
    • Sogabe, K., Roeser, N.F., Venkatachalam, M.A. and Weinberg, J.M. (1996) Differential cytoprotection by glycine against oxidant damage to proximal tubule cells. Kidney Int., 50, 845-854.
    • (1996) Kidney Int. , vol.50 , pp. 845-854
    • Sogabe, K.1    Roeser, N.F.2    Venkatachalam, M.A.3    Weinberg, J.M.4
  • 61
    • 0035215598 scopus 로고    scopus 로고
    • Cre-mediated transgene activation in the developing and adult mouse brain
    • Cinato, E., Mirotsou, M. and Sablitzky, F. (2001) Cre-mediated transgene activation in the developing and adult mouse brain. Genesis, 31, 118-125.
    • (2001) Genesis , vol.31 , pp. 118-125
    • Cinato, E.1    Mirotsou, M.2    Sablitzky, F.3
  • 62
    • 0035543875 scopus 로고    scopus 로고
    • Immunohistochemical demonstration of Leu-7 (HNK-1), Neurone-specific Enolase (NSE) and Protein-Gene Peptide (PGP) 9. 5 in the developing camel (Camelus dromedarius) heart
    • El Sharaby, A.A., Egerbacher, M., Hammoda, A.K. and Bock, P. (2001) Immunohistochemical demonstration of Leu-7 (HNK-1), Neurone-specific Enolase (NSE) and Protein-Gene Peptide (PGP) 9.5 in the developing camel (Camelus dromedarius) heart. Anat. Histol. Embryol., 30, 321-325.
    • (2001) Anat. Histol. Embryol. , vol.30 , pp. 321-325
    • El Sharaby, A.A.1    Egerbacher, M.2    Hammoda, A.K.3    Bock, P.4
  • 63
    • 0025287940 scopus 로고
    • Physiological expression of neural marker proteins in the heart of young rats
    • Semba, R., Asano, T. and Kato, K. (1990) Physiological expression of neural marker proteins in the heart of young rats. Brain Res. Dev. Brain Res., 54, 217-220.
    • (1990) Brain Res. Dev. Brain Res. , vol.54 , pp. 217-220
    • Semba, R.1    Asano, T.2    Kato, K.3
  • 65
    • 33644676105 scopus 로고    scopus 로고
    • Accuracy of methods for calculating postnatal growth velocity for extremely low birth weight infants
    • Patel, A.L., Engstrom, J.L., Meier, P.P. and Kimura, R.E. (2005) Accuracy of methods for calculating postnatal growth velocity for extremely low birth weight infants. Pediatrics, 116, 1466-1473.
    • (2005) Pediatrics , vol.116 , pp. 1466-1473
    • Patel, A.L.1    Engstrom, J.L.2    Meier, P.P.3    Kimura, R.E.4
  • 66
    • 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. (2004) Iron-sulfur protein maturation in human cells: evidence for a function of frataxin. Hum. Mol. Genet., 13, 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
  • 67
    • 47749130452 scopus 로고    scopus 로고
    • The MCK mouse heart model of Friedreich's ataxia: alterations in iron-regulated proteins and cardiac hypertrophy are limited by iron chelation
    • Whitnall, M., Rahmanto, Y.S., Sutak, R., Xu, X., Becker, E.M., Mikhael, M.R., Ponka, P. and Richardson, D.R. (2008) The MCK mouse heart model of Friedreich's ataxia: alterations in iron-regulated proteins and cardiac hypertrophy are limited by iron chelation. Proc. Natl Acad. Sci. USA, 105, 9757-9762.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 9757-9762
    • Whitnall, M.1    Rahmanto, Y.S.2    Sutak, R.3    Xu, X.4    Becker, E.M.5    Mikhael, M.R.6    Ponka, P.7    Richardson, D.R.8
  • 70
    • 47249094614 scopus 로고    scopus 로고
    • Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases
    • Lill, R. and Muhlenhoff, U. (2008) Maturation of iron-sulfur proteins in eukaryotes: mechanisms, connected processes, and diseases. Annu. Rev. Biochem., 77, 669-700.
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 669-700
    • Lill, R.1    Muhlenhoff, U.2
  • 71
    • 0014800861 scopus 로고
    • The demonstration of alternating contractile state in pulsus alternans
    • Noble, R.J. and Nutter, D.O. (1970) The demonstration of alternating contractile state in pulsus alternans. J. Clin. Invest., 49, 1166-1177.
    • (1970) J. Clin. Invest. , vol.49 , pp. 1166-1177
    • Noble, R.J.1    Nutter, D.O.2
  • 72
    • 84863237181 scopus 로고    scopus 로고
    • Echocardiographic assessment of diastolic function
    • Solomon, S.D. and Bulwer, B.E. (eds), Humana Press, New York
    • Ho, C.Y. (2007) Echocardiographic assessment of diastolic function. In Solomon, S.D. and Bulwer, B.E. (eds), Essential Echocardiography: A Practical Handbook. Humana Press, New York, pp. 119-131.
    • (2007) Essential Echocardiography: A Practical Handbook , pp. 119-131
    • Ho, C.Y.1
  • 73
    • 0034641655 scopus 로고    scopus 로고
    • Echocardiographic characterization of cardiomyopathy in Friedreich's ataxia with tissue Doppler echocardiographically derived myocardial velocity gradients
    • Dutka, D.P., Donnelly, J.E., Palka, P., Lange, A., Nunez, D.J. and Nihoyannopoulos, P. (2000) Echocardiographic characterization of cardiomyopathy in Friedreich's ataxia with tissue Doppler echocardiographically derived myocardial velocity gradients. Circulation, 102, 1276-1282.
    • (2000) Circulation , vol.102 , pp. 1276-1282
    • Dutka, D.P.1    Donnelly, J.E.2    Palka, P.3    Lange, A.4    Nunez, D.J.5    Nihoyannopoulos, P.6
  • 74
    • 0014128470 scopus 로고
    • Fine structure of myocardial mitochondria in rats after exercise for one-half to two hours
    • Laguens, R.P. and Gomez-Dumm, C.L. (1967) Fine structure of myocardial mitochondria in rats after exercise for one-half to two hours. Circ. Res., 21, 271-279.
    • (1967) Circ. Res. , vol.21 , pp. 271-279
    • Laguens, R.P.1    Gomez-Dumm, C.L.2
  • 75
    • 0018575129 scopus 로고
    • Ultrastructural and morphometric study of the human heart muscle cell in acute coronary insufficiency
    • Laguens, R.P., Weinschelbaun, R. and Favaloro, R. (1979) Ultrastructural and morphometric study of the human heart muscle cell in acute coronary insufficiency. Hum. Pathol., 10, 695-705.
    • (1979) Hum. Pathol. , vol.10 , pp. 695-705
    • Laguens, R.P.1    Weinschelbaun, R.2    Favaloro, R.3
  • 76
    • 59049091824 scopus 로고    scopus 로고
    • Acute doxorubicin cardiotoxicity is associated with p53-induced inhibition of the mammalian target of rapamycin pathway
    • Zhu, W., Soonpaa, M.H., Chen, H., Shen, W., Payne, R.M., Liechty, E.A., Caldwell, R.L., Shou, W. and Field, L.J. (2009) Acute doxorubicin cardiotoxicity is associated with p53-induced inhibition of the mammalian target of rapamycin pathway. Circulation, 119, 99-106.
    • (2009) Circulation , vol.119 , pp. 99-106
    • Zhu, W.1    Soonpaa, M.H.2    Chen, H.3    Shen, W.4    Payne, R.M.5    Liechty, E.A.6    Caldwell, R.L.7    Shou, W.8    Field, L.J.9
  • 78
    • 79959547500 scopus 로고    scopus 로고
    • Early changes in left ventricular long-axis function in Friedreich ataxia: relation with the FXN gene mutation and cardiac structural change
    • Mottram, P.M., Delatycki, M.B., Donelan, L., Gelman, J.S., Corben, L. and Peverill, R.E. (2011) Early changes in left ventricular long-axis function in Friedreich ataxia: relation with the FXN gene mutation and cardiac structural change. J. Am. Soc. Echocardiogr., 24, 782-789.
    • (2011) J. Am. Soc. Echocardiogr. , vol.24 , pp. 782-789
    • Mottram, P.M.1    Delatycki, M.B.2    Donelan, L.3    Gelman, J.S.4    Corben, L.5    Peverill, R.E.6
  • 80
    • 0033525773 scopus 로고    scopus 로고
    • Mitochondrial diseases in man and mouse
    • Wallace, D.C. (1999) Mitochondrial diseases in man and mouse. Science, 283, 1482-1488.
    • (1999) Science , vol.283 , pp. 1482-1488
    • Wallace, D.C.1
  • 81
    • 34249873947 scopus 로고    scopus 로고
    • Translocation of proteins into mitochondria
    • Neupert, W. and Herrmann, J.M. (2007) Translocation of proteins into mitochondria. Annu. Rev. Biochem., 76, 723-749.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 723-749
    • Neupert, W.1    Herrmann, J.M.2
  • 82
    • 0026099940 scopus 로고
    • Immunocytochemical identification of neuroendocrine markers in human cardiac paraganglion-like structures
    • Gobbi, H., Barbosa, A.J., Teixeira, V.P. and Almeida, H.O. (1991) Immunocytochemical identification of neuroendocrine markers in human cardiac paraganglion-like structures. Histochemistry, 95, 337-340.
    • (1991) Histochemistry , vol.95 , pp. 337-340
    • Gobbi, H.1    Barbosa, A.J.2    Teixeira, V.P.3    Almeida, H.O.4
  • 83
    • 0017230254 scopus 로고
    • Human enolase isozymes: electrophoretic and biochemical evidence for three loci
    • Pearce, J.M., Edwards, Y.H. and Harris, H. (1976) Human enolase isozymes: electrophoretic and biochemical evidence for three loci. Ann. Hum. Genet., 39, 263-276.
    • (1976) Ann. Hum. Genet. , vol.39 , pp. 263-276
    • Pearce, J.M.1    Edwards, Y.H.2    Harris, H.3
  • 84
    • 0344628532 scopus 로고    scopus 로고
    • Presence of bone-marrow- and neural-crest-derived cells in intimal hyperplasia at the time of clinical in-stent restenosis
    • Skowasch, D., Jabs, A., Andrie, R., Dinkelbach, S., Luderitz, B. and Bauriedel, G. (2003) Presence of bone-marrow- and neural-crest-derived cells in intimal hyperplasia at the time of clinical in-stent restenosis. Cardiovasc. Res., 60, 684-691.
    • (2003) Cardiovasc. Res. , vol.60 , pp. 684-691
    • Skowasch, D.1    Jabs, A.2    Andrie, R.3    Dinkelbach, S.4    Luderitz, B.5    Bauriedel, G.6
  • 85
    • 0021955067 scopus 로고
    • Immunohistochemical localization of gamma-enolase in normal human tissues other than nervous and neuroendocrine tissues
    • Haimoto, H., Takahashi, Y., Koshikawa, T., Nagura, H. and Kato, K. (1985) Immunohistochemical localization of gamma-enolase in normal human tissues other than nervous and neuroendocrine tissues. Lab. Invest., 52, 257-263.
    • (1985) Lab. Invest. , vol.52 , pp. 257-263
    • Haimoto, H.1    Takahashi, Y.2    Koshikawa, T.3    Nagura, H.4    Kato, K.5
  • 86
    • 0025063668 scopus 로고
    • Transgenic mice expressing beta-galactosidase in mature neurons under neuron-specific enolase promoter control
    • Forss-Petter, S., Danielson, P.E., Catsicas, S., Battenberg, E., Price, J., Nerenberg, M. and Sutcliffe, J.G. (1990) Transgenic mice expressing beta-galactosidase in mature neurons under neuron-specific enolase promoter control. Neuron, 5, 187-197.
    • (1990) Neuron , vol.5 , pp. 187-197
    • Forss-Petter, S.1    Danielson, P.E.2    Catsicas, S.3    Battenberg, E.4    Price, J.5    Nerenberg, M.6    Sutcliffe, J.G.7
  • 88
    • 77952008605 scopus 로고    scopus 로고
    • Friedreich ataxia presenting as sudden cardiac death in childhood: clinical, genetic and pathological correlation, with implications for genetic testing and counselling
    • Quercia, N., Somers, G.R., Halliday, W., Kantor, P.F., Banwell, B. and Yoon, G. (2010) Friedreich ataxia presenting as sudden cardiac death in childhood: clinical, genetic and pathological correlation, with implications for genetic testing and counselling. Neuromuscul. Disord., 20, 340-342.
    • (2010) Neuromuscul. Disord. , vol.20 , pp. 340-342
    • Quercia, N.1    Somers, G.R.2    Halliday, W.3    Kantor, P.F.4    Banwell, B.5    Yoon, G.6
  • 90
    • 81255199283 scopus 로고    scopus 로고
    • Protective effects of intraperitoneal injection of TAT-SOD against focal cerebral ischemia/reperfusion injury in rats
    • Ye, N., Liu, S., Lin, Y. and Rao, P. (2011) Protective effects of intraperitoneal injection of TAT-SOD against focal cerebral ischemia/reperfusion injury in rats. Life Sciences, 89, 868-874.
    • (2011) Life Sciences , vol.89 , pp. 868-874
    • Ye, N.1    Liu, S.2    Lin, Y.3    Rao, P.4
  • 92
    • 0036663014 scopus 로고    scopus 로고
    • In vivo delivery of a Bcl-xL fusion protein containing the TAT protein transduction domain protects against ischemic brain injury and neuronal apoptosis
    • Cao, G., Pei, W., Ge, H., Liang, Q., Luo, Y., Sharp, F.R., Lu, A., Ran, R., Graham, S.H. and Chen, J. (2002) In vivo delivery of a Bcl-xL fusion protein containing the TAT protein transduction domain protects against ischemic brain injury and neuronal apoptosis. J. Neurosci., 22, 5423-5431.
    • (2002) J. Neurosci. , vol.22 , pp. 5423-5431
    • Cao, G.1    Pei, W.2    Ge, H.3    Liang, Q.4    Luo, Y.5    Sharp, F.R.6    Lu, A.7    Ran, R.8    Graham, S.H.9    Chen, J.10
  • 95
    • 0023131743 scopus 로고
    • Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenase
    • Grant, P.M., Roderick, S.L., Grant, G.A., Banaszak, L.J. and Strauss, A.W. (1987) Comparison of the precursor and mature forms of rat heart mitochondrial malate dehydrogenase. Biochemistry, 26, 128-134.
    • (1987) Biochemistry , vol.26 , pp. 128-134
    • Grant, P.M.1    Roderick, S.L.2    Grant, G.A.3    Banaszak, L.J.4    Strauss, A.W.5
  • 96
    • 0023046911 scopus 로고
    • Isolation and nucleotide sequence of a cDNA clone encoding rat mitochondrial malate dehydrogenase
    • Grant, P.M., Tellam, J., May, V.L. and Strauss, A.W. (1986) Isolation and nucleotide sequence of a cDNA clone encoding rat mitochondrial malate dehydrogenase. Nucleic Acids Res., 14, 6053-6066.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 6053-6066
    • Grant, P.M.1    Tellam, J.2    May, V.L.3    Strauss, A.W.4
  • 97
    • 47249127786 scopus 로고    scopus 로고
    • Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia
    • Li, K., Besse, E.K., Ha, D., Kovtunovych, G. and Rouault, T.A. (2008) Iron-dependent regulation of frataxin expression: implications for treatment of Friedreich ataxia. Hum. Mol. Genet., 17, 2265-2273.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 2265-2273
    • Li, K.1    Besse, E.K.2    Ha, D.3    Kovtunovych, G.4    Rouault, T.A.5
  • 98
    • 3042704342 scopus 로고    scopus 로고
    • Expression of mutant p193 and p53 permits cardiomyocyte cell cycle reentry after myocardial infarction in transgenic mice
    • Nakajima, H., Nakajima, H.O., Tsai, S.C. and Field, L.J. (2004) Expression of mutant p193 and p53 permits cardiomyocyte cell cycle reentry after myocardial infarction in transgenic mice. Circ. Res., 94, 1606-1614.
    • (2004) Circ. Res. , vol.94 , pp. 1606-1614
    • Nakajima, H.1    Nakajima, H.O.2    Tsai, S.C.3    Field, L.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.