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Volumn 63, Issue , 2013, Pages 351-360

In vivo detection of free radicals using molecular MRI and immuno-spin trapping in a mouse model for amyotrophic lateral sclerosis

Author keywords

Amyotrophic lateral sclerosis; Anti DMPO probe; DMPO; Free radicals; Gd DTPA albumin anti DMPO biotin probe; Immuno spin trapping; In vivo; Molecular magnetic resonance imaging

Indexed keywords

5,5 DIMETHYL 1 PYRROLINE 1 OXIDE; ALBUMIN; BIOTIN; FREE RADICAL; GADOLINIUM; PENDETIDE; SODIUM CHLORIDE; STREPTAVIDIN;

EID: 84879478576     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2013.05.026     Document Type: Article
Times cited : (33)

References (56)
  • 1
    • 1942520360 scopus 로고    scopus 로고
    • Using anti-5,5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immuno-spin trapping
    • DOI 10.1016/j.freeradbiomed.2004.02.077, PII S0891584904001959
    • Mason, R. P. Using anti-5,5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immune-spin trapping. Free Radic. Biol. Med 36: 1214-1223; 2004. (Pubitemid 38526315)
    • (2004) Free Radical Biology and Medicine , vol.36 , Issue.10 , pp. 1214-1223
    • Mason, R.P.1
  • 2
    • 58249088828 scopus 로고    scopus 로고
    • Cu, Zn-superoxide dismutase-driven free radical modifications: Copper- and carbonate radical anion-initiated protein radical chemistry
    • Ramirez, D. C.; Gomez-Mejiba, S. E.; Corbett, J. T.; Deterding, L. J.; Tomer, K. B.; Mason, R. P. Cu, Zn-superoxide dismutase-driven free radical modifications: copper- and carbonate radical anion-initiated protein radical chemistry. Biochem. J. 417: 341-353; 2009.
    • (2009) Biochem J. , vol.417 , pp. 341-353
    • Ramirez, D.C.1    Gomez-Mejiba, S.E.2    Corbett, J.T.3    Deterding, L.J.4    Tomer, K.B.5    Mason, R.P.6
  • 4
    • 0035906260 scopus 로고    scopus 로고
    • Oxidative damage to mitochondrial DNA in spinal motoneurons of transgenic ALS mice
    • Warita, H.; Hayashi, T.; Murakami, T.; Manabe, Y.; Abe, K. Oxidative damage to mitochondrial DNA in spinal motoneurons of transgenic ALS mice. Brain Res. Mol. Brain Res. 89: 147-152; 2011.
    • (2011) Brain Res. Mol. Brain Res , vol.89 , pp. 147-152
    • Warita, H.1    Hayashi, T.2    Murakami, T.3    Manabe, Y.4    Abe, K.5
  • 5
    • 18144387600 scopus 로고    scopus 로고
    • Increased oxidative damage to DNA in an animal model of amyotrophic lateral sclerosis
    • DOI 10.1080/10715760400027979
    • Aguirre, N.; Beal, M. F.; Matson, W. R.; Bogdanov, M. B. Increased oxidative damage to DNA in an animal model of amyotrophic lateral sclerosis. Free Radic. Res. 39: 383-388; 2005. (Pubitemid 40613717)
    • (2005) Free Radical Research , vol.39 , Issue.4 , pp. 383-388
    • Aguirre, N.1    Beal, M.F.2    Matson, W.R.3    Bogdanov, M.B.4
  • 6
    • 14644400490 scopus 로고    scopus 로고
    • Proteomic analysis of 4-hydroxy-2-nonenal-modified proteins in G93A-SOD1 transgenic mice - A model of familial amyotrophic lateral sclerosis
    • DOI 10.1016/j.freeradbiomed.2004.12.021
    • Perluigi, M.; Fai Poon, H.; Hensley, K.; Pierce, W. M.; Klein, J. B.; Calabrese, V.; De Marco, C.; Butterfield, D. A. Proteomic analysis of 4-hydroxy-2-nonenal-modified proteins in G93A-SOD1 transgenic mice: a model of familial amyotrophic lateral sclerosis. Free Radic. Biol. Med. 38: 960-968; 2005. (Pubitemid 40321087)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.7 , pp. 960-968
    • Perluigi, M.1    Poon, H.F.2    Hensley, K.3    Pierce, W.M.4    Klein, J.B.5    Calabrese, V.6    De Marco, C.7    Butterfield, D.A.8
  • 7
    • 0036062628 scopus 로고    scopus 로고
    • Temporal patterns of cytokine and apoptosis-related gene expression in spinal cords of the G93A-SOD1 mouse model of amyotrophic lateral sclerosis
    • DOI 10.1046/j.1471-4159.2002.00968.x
    • Hensley, K.; Floyd, R. A.; Gordon, B.; Mou, S.; Pye, Q. N.; Stewart, C.; West, M.; Williamson, K. Temporal patterns of cytokine and apoptosis-related gene expression in spinal cords of the G93A-SOD1 mouse model of amyotrophic lateral sclerosis. J. Neurochem. 82: 365-374; 2002. (Pubitemid 34774627)
    • (2002) Journal of Neurochemistry , vol.82 , Issue.2 , pp. 365-374
    • Hensley, K.1    Floyd, R.A.2    Gordon, B.3    Mou, S.4    Pye, Q.N.5    Stewart, C.6    West, M.7    Williamson, K.8
  • 8
    • 7244223437 scopus 로고    scopus 로고
    • Oxidative damage to proteins in the spinal cord in amyotrophic lateral sclerosis (ALS)
    • Niebroj-Dobosz, I.; Dziewulska, D.; Kwiecinski, H. Oxidative damage to proteins in the spinal cord in amyotrophic lateral sclerosis (ALS). Folia Neuropathol 42: 151-156; 2004. (Pubitemid 39433400)
    • (2004) Folia Neuropathologica , vol.42 , Issue.3 , pp. 151-156
    • Niebroj-Dobosz, I.1    Dziewulska, D.2    Kwiecinski, H.3
  • 9
    • 37849007550 scopus 로고    scopus 로고
    • Oxidized/misfolded superoxide dismutase-1: The cause of all amyotrophic lateral sclerosis?
    • Kabashi, E.; Valdmanis, P. N.; Dion, P.; Rouleau, G. A. Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis? Ann Neurol 62: 553-559; 2007.
    • (2007) Ann Neurol , vol.62 , pp. 553-559
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3    Rouleau, G.A.4
  • 10
  • 12
    • 10644225292 scopus 로고    scopus 로고
    • Mechanism of hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation as explored by immuno-spin trapping: The role of copper- and carbonate radical anion-mediated oxidations
    • DOI 10.1016/j.freeradbiomed.2004.10.008, PII S089158490400810X
    • Ramirez, D. C.; Gomez Mejiba, S. E.; Mason, R. P. Mechanism of hydrogen peroxide-induced Cu,Zn-superoxide dismutase-centered radical formation as explored by immune-spin trapping: the role of copper- and carbonate radical anion-mediated oxidations. Free Radic. Biol. Med 38: 201-214; 2005. (Pubitemid 39656131)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.2 , pp. 201-214
    • Ramirez, D.C.1    Gomez Mejiba, S.E.2    Mason, R.P.3
  • 13
    • 0036667549 scopus 로고    scopus 로고
    • Immunological identification of the heart myoglobin radical formed by hydrogen peroxide
    • DOI 10.1016/S0891-5849(02)00895-X, PII S089158490200895X
    • Detweiler, C. D.; Deterding, L. J.; Tomer, K. B.; Chignell, C. F.; Germolec, D.; Mason, R. P. Immunological identification of the heart myoglobin radical formed by hydrogen peroxide. Free Radic. Biol. Med. 33: 364-369; 2002. (Pubitemid 34786275)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.3 , pp. 364-369
    • Detweiler, C.D.1    Deterding, L.J.2    Tomer, K.B.3    Chignell, C.F.4    Germolec, D.5    Mason, R.P.6
  • 18
    • 77049083474 scopus 로고    scopus 로고
    • Molecular MRI approaches used to aid in the understanding of the tissue regeneration marker Met in vivo: Implications for tissue engineering
    • Towner, R. A.; Smith., N.; Asano, Y.; Doblas, S.; Saunders, D. Molecular MRI approaches used to aid in the understanding of the tissue regeneration marker Met in vivo: implications for tissue engineering. Tissue Eng. A 16: 365-371; 2010.
    • (2010) Tissue Eng. A , vol.16 , pp. 365-371
    • Towner, R.A.1    Smith, N.2    Asano, Y.3    Doblas, S.4    Saunders, D.5
  • 19
    • 77049123525 scopus 로고    scopus 로고
    • Molecular MRI approaches used to aid in the understanding of angiogenesis in vivo: Implications for tissue engineering
    • Towner, R.; Smith, N.; Asano, Y.; He, T.; Doblas, S.; Saunders, D.; Silasi-Mansat, R.; Lupu, F.; Seeney, C. E. Molecular MRI approaches used to aid in the understanding of angiogenesis in vivo: implications for tissue engineering. Tissue Eng. A 16 : 357-364; 2010.
    • (2010) Tissue Eng. A , vol.16 , pp. 357-364
    • Towner, R.1    Smith, N.2    Asano, Y.3    He, T.4    Doblas, S.5    Saunders, D.6    Silasi-Mansat, R.7    Lupu, F.8    Seeney, C.E.9
  • 21
    • 0036194973 scopus 로고    scopus 로고
    • MRI and fluorescence microscopy of the acute vascular response to VEGF165: Vasodilation, hyper-permeability and lymphatic uptake, followed by rapid inactivation of the growth factor
    • DOI 10.1002/nbm.724
    • Dafni, H.; Landsman, L.; Schechter, B.; Kohen, F.; Neeman, M. MRI and fluorescence microscopy of the acute vascular response to VEGF165: vasodila-tion, hyper-permeability and lymphatic uptake, followed by rapid inactivation of the growth factor. NMR Biomed 15: 120-131; 2002. (Pubitemid 34213402)
    • (2002) NMR in Biomedicine , vol.15 , Issue.2 , pp. 120-131
    • Dafni, H.1    Landsman, L.2    Schechter, B.3    Kohen, F.4    Neeman, M.5
  • 22
    • 0342845498 scopus 로고    scopus 로고
    • Avidin-biotin systems
    • Academic Press: San Diego;
    • Hermanson, G. T. Avidin-Biotin Systems. In: Bioconjugate Techniques. Academic Press: San Diego; 494-527; 1996.
    • (1996) Bioconjugate Techniques , pp. 494-527
    • Hermanson G., .T.1
  • 24
    • 0033989243 scopus 로고    scopus 로고
    • Amyotrophic lateral sclerosis: Copper/zinc superoxide dismutase (SOD1) gene mutations
    • Orrel, R. W. Amyotrophic lateral sclerosis: copper/zinc superoxide dismutase (SOD1) gene mutations. Neuromusc. Disord 10: 63-68; 2000.
    • (2000) Neuromusc. Disord , vol.10 , pp. 63-68
    • Orrel, R.W.1
  • 27
    • 67649807405 scopus 로고    scopus 로고
    • Direct magnetic resonance evidence for peroxcymonocarbonate involvement in the Cu,Zn-superoxide dismutase peroxidase catalytic cycle
    • Bonini, M. G.; Gabel, S. A.; Ranguelova, K.; Stadler, K.; Derose, E. F.; London, R. E.; Mason, R. P. Direct magnetic resonance evidence for peroxcymonocarbonate involvement in the Cu,Zn-superoxide dismutase peroxidase catalytic cycle. J. Biol. Chem. 284: 14618-14627; 2009.
    • (2009) J. Biol. Chem , vol.284 , pp. 14618-14627
    • Bonini, M.G.1    Gabel, S.A.2    Ranguelova, K.3    Stadler, K.4    Derose, E.F.5    London, R.E.6    Mason, R.P.7
  • 28
    • 77954536371 scopus 로고    scopus 로고
    • Mechanism of the peroxidase activity of super-oxide dismutase 1
    • Medinas, D. B.; Augusto, O. Mechanism of the peroxidase activity of super-oxide dismutase 1. Free Radic. Biol. Med. 49: 682; 2010.
    • (2010) Free Radic. Biol. Med , vol.49 , pp. 682
    • Medinas, D.B.1    Augusto, O.2
  • 29
    • 0027048350 scopus 로고
    • Fatty acid radical formation in rats administered oxidized fatty acids: In vivo spin trapping investigation
    • DOI 10.1016/0003-9861(92)90288-8
    • Chamulitrat, W.; Jordan, S. J.; Mason, R. P. Fatty acid radical formation in rats administered oxidized fatty acids: in vivo spin trapping investigation. Arch. Biochem. Biophys. 299: 361-367; 1992. (Pubitemid 23029044)
    • (1992) Archives of Biochemistry and Biophysics , vol.299 , Issue.2 , pp. 361-367
    • Chamulitrat, W.1    Jordan, S.J.2    Mason, R.P.3
  • 30
    • 0035863031 scopus 로고    scopus 로고
    • Spin trapping of polyunsaturated fatty acid-derived peroxyl radicals: Reassignment to alkoxyl radical adducts
    • DOI 10.1016/S0891-5849(00)00456-1, PII S0891584900004561
    • Dikalov, S. I.; Mason, R. P. Spin trapping of polyunsaturated fatty acid-derived peroxyl radicals: reassignment to alkoxyl radical adducts. Free Radic. Biol. Med. 30: 187-197; 2001. (Pubitemid 32121796)
    • (2001) Free Radical Biology and Medicine , vol.30 , Issue.2 , pp. 187-197
    • Dikalov, S.I.1    Mason, R.P.2
  • 31
    • 33947514186 scopus 로고    scopus 로고
    • Identification of free radicals of glycerophosphatidylcholines containing 6 fatty acids using spin trapping coupled with tandem mass spectrometry
    • DOI 10.1080/10715760601118353, PII 773534592
    • Reis, A.; Domingues, P.; Ferrer-Correla, A. J.; Domingues, M. R. Identification of free radicals of glycerophosphatidylcholines containing omega-6 fatty acids using spin trapping coupled with tandem mass spectrometry. Free Radic. Res 41: 432-443; 2007. (Pubitemid 46470941)
    • (2007) Free Radical Research , vol.41 , Issue.4 , pp. 432-443
    • Reis, A.1    Domingues, P.2    Ferrer-Correia, A.J.V.3    Domingues, M.R.M.4
  • 32
    • 84055223023 scopus 로고    scopus 로고
    • Evaluation of the Forrester-Hepburn mechanism as an artefact source in ESR spin trapping
    • Leinisch, F.; Ranguelova, K.; DeRose, E. F.; Jiang, J. J.; Mason, R. P. Evaluation of the Forrester-Hepburn mechanism as an artefact source in ESR spin trapping. Chem. Res. Toxicol. 24: 2217-2226; 2011.
    • (2011) Chem. Res. Toxicol , vol.24 , pp. 2217-2226
    • Leinisch, F.1    Ranguelova, K.2    Derose, E.F.3    Jiang, J.J.4    Mason, R.P.5
  • 33
    • 79953220709 scopus 로고    scopus 로고
    • The fidelity of spin trapping with DMPO in biological systems
    • Ranguelova, K.; Mason, R. P. The fidelity of spin trapping with DMPO in biological systems. Magn. Reson. Chem. 49: 152-158; 2011.
    • (2011) Magn. Reson. Chem , vol.49 , pp. 152-158
    • Ranguelova, K.1    Mason, R.P.2
  • 34
    • 33947640544 scopus 로고    scopus 로고
    • On the relation of oxidative stress to neuroinflammation: Lessons learned from the G93A-SOD1 mouse model of amyotrophic lateral sclerosis
    • Hensley, K.; Mhatre, M.; Mou, S.; Pye, Q. N.; Stewart, C.; West, M.; Williamson, K. S. On the relation of oxidative stress to neuroinflammation: lessons learned from the G93A-SOD1 mouse model of amyotrophic lateral sclerosis. Antioxid. Redox Signaling 8: 2075-2087; 2006. (Pubitemid 46489632)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.11-12 , pp. 2075-2087
    • Hensley, K.1    Mhatre, M.2    Mou, S.3    Pye, Q.N.4    Stewart, C.5    West, M.6    Williamson, K.S.7
  • 36
    • 0030806228 scopus 로고    scopus 로고
    • Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant
    • Bruijn, L. I.; Beal, M. F.; Becher, M. W.; Schulz, J. B.; Wong, P. C.; Price, D. L.; Cleveland, D. W. Elevated free nitrotyrosine levels, but not protein-bound nitrotyrosine or hydroxyl radicals, throughout amyotrophic lateral sclerosis (ALS)-like disease implicate tyrosine nitration as an aberrant in vivo property of one familial ALS-linked superoxide dismutase 1 mutant. Proc. Natl. Acad. Sci. USA 94: 7606-7611; 1997.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7606-7611
    • Bruijn, L.I.1    Beal, M.F.2    Becher, M.W.3    Schulz, J.B.4    Wong, P.C.5    Price, D.L.6    Cleveland, D.W.7
  • 37
    • 0030851761 scopus 로고    scopus 로고
    • Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis
    • DOI 10.1002/ana.410420416
    • Beal, M. F.; Ferrante, R. J.; Browne, S. E.; Matthews, R. T.; Kowall, N. W.; Brown Jr. R. H. Increased 3-nitrotyrosine in both sporadic and familial amyotrophic lateral sclerosis. Ann. Neurol. 42: 644-654; 1997. (Pubitemid 27439028)
    • (1997) Annals of Neurology , vol.42 , Issue.4 , pp. 644-654
    • Beal, M.F.1    Ferrante, R.J.2    Browne, S.E.3    Matthews, R.T.4    Kowall, N.W.5    Brown Jr., R.H.6
  • 38
    • 0043172468 scopus 로고    scopus 로고
    • 4-Hydroxynonenal and neurodegenerative diseases
    • DOI 10.1016/S0098-2997(03)00024-4
    • Zarkovic, K. 4-Hydroxynonenal and neurodegenerative diseases. Mol. Aspects Med. 24: 293-303; 2003. (Pubitemid 36945029)
    • (2003) Molecular Aspects of Medicine , vol.24 , Issue.4-5 , pp. 293-303
    • Zarkovic, K.1
  • 40
    • 18144398928 scopus 로고    scopus 로고
    • Protein nitration in a mouse model of familial amyotrophic lateral sclerosis: Possible multifunctional role in the pathogenesis
    • DOI 10.1074/jbc.M413111200
    • Casoni, F.; Basso, M.; Massignan, T.; Gianazza, E.; Cheroni, C.; Salmonia, M.; Bonetto, V. Protein nitration in a mouse model of familial amyotrophic lateral sclerosis: possible multifunctional role in the pathogenesis. J. Biol. Chem. 280: 16295-16304; 2005. (Pubitemid 40616757)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 16295-16304
    • Casoni, F.1    Basso, M.2    Massignan, T.3    Gianazzail, E.4    Cheroni, C.5    Salmona, M.6    Bendotti, C.7    Bonetto, V.8
  • 42
    • 34247485859 scopus 로고    scopus 로고
    • Mutation of superoxide dismutase elevates reactive species: Comparison of nitration and oxidation of proteins in different brain regions of transgenic mice with amyotrophic lateral sclerosis
    • DOI 10.1016/j.neuroscience.2007.01.028, PII S030645220700005X
    • Liu, D; Bao, F; Wen, J; Liu, J. Mutation of superoxide dismutase elevates reactive species: comparison of nitration and oxidation of proteins in different brain regions of transgenic mice with amyotrophic lateral sclerosis. Neu-roscience 146: 255-264; 2007. (Pubitemid 46654601)
    • (2007) Neuroscience , vol.146 , Issue.1 , pp. 255-264
    • Liu, D.1    Bao, F.2    Wen, J.3    Liu, J.4
  • 45
    • 0027164824 scopus 로고
    • Erratum: Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis (Nature (1993) 362 (59-62))
    • Rosen, D. R. Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis. Nature 364: 362; 1993. (Pubitemid 23265284)
    • (1993) Nature , vol.364 , Issue.6435 , pp. 362
    • Rosen, D.R.1
  • 46
    • 0031960868 scopus 로고    scopus 로고
    • Homozygosity for Asn86Ser mutation in the CuZn-superoxide dismutase gene produces a severe clinical phenotype in a juvenile onset case of familial amyotrophic lateral sclerosis
    • Hayward, C.; Brock, D. J.; Minns, R. A.; Swingler, R. J. Homozygosity for Asn86Ser mutation in the CuZn-superoxide dismutase gene produces a severe clinical phenotype in a juvenile onset case of familial amyotrophic lateral sclerosis. j. Med. Genet. 35: 174 -176; 1998.
    • (1998) J. Med. Genet , vol.35 , pp. 174-176
    • Hayward, C.1    Brock, D.J.2    Minns, R.A.3    Swingler, R.J.4
  • 47
    • 22044435425 scopus 로고    scopus 로고
    • Identification of three mutations in the Cu, Zn-superoxide dismutase (Cu, Zn-SOD) gene with familial amyotrophic lateral sclerosis: Transduction of human Cu, Zn-SOD into PC12 cells by HIV-1 TAT protein basic domain
    • Chou, C. M.; Huang, C. J.; Shih, C. M.; Chen, Y. P.; Liu, T. P.; Chen, C. T. Identification of three mutations in the Cu, Zn-superoxide dismutase (Cu, Zn-SOD) gene with familial amyotrophic lateral sclerosis: transduction of human Cu, Zn-SOD into PC12 cells by HIV-1 TAT protein basic domain. Ann. N. Y. Acad. Sci 1042: 303-313; 2005.
    • (2005) Ann. N. Y. Acad. Sci , vol.1042 , pp. 303-313
    • Chou, C.M.1    Huang, C.J.2    Shih, C.M.3    Chen, Y.P.4    Liu, T.P.5    Chen, C.T.6
  • 48
    • 0037111503 scopus 로고    scopus 로고
    • Do oxidatively modified proteins cause ALS?
    • DOI 10.1016/S0891-5849(02)01080-8, PII S0891584902010808
    • Valentine, J. S. Do oxidatively modified proteins cause ALS? 33: 1314-1320; 2002Free Radic. Biol. Med 33: 1314-1320; 2002. (Pubitemid 35284916)
    • (2002) Free Radical Biology and Medicine , vol.33 , Issue.10 , pp. 1314-1320
    • Valentine, J.S.1
  • 49
    • 65649103331 scopus 로고    scopus 로고
    • Pathophysiology of neurodegeneration in familial amyotrophic lateral sclerosis
    • Vucic, S.; Kiernan, M. C. Pathophysiology of neurodegeneration in familial amyotrophic lateral sclerosis. Curr. Mol. Med. 9: 255-272; 2009.
    • (2009) Curr. Mol. Med , vol.9 , pp. 255-272
    • Vucic, S.1    Kiernan, M.C.2
  • 53
    • 79961126295 scopus 로고    scopus 로고
    • Reepiration and ROS production in brain and spinal cord mitochondria of transgenic rats with mutant G93a Cu/Zn-superoxide dismu-tase gene
    • Panov, A.; Kubalik, N.; Zinchenko, N.; Hemendinger, R.; Dikalov, S.; Bonokovsky, H. L. Respiration and ROS production in brain and spinal cord mitochondria of transgenic rats with mutant G93a Cu/Zn-superoxide dismu-tase gene. Neurobiol. Dis. 44: 53-62; 2011.
    • (2011) Neurobiol. Dis , vol.44 , pp. 53-62
    • Panov, A.1    Kubalik, N.2    Zinchenko, N.3    Hemendinger, R.4    Dikalov, S.5    Bonokovsky, H.L.6
  • 54
    • 84859258363 scopus 로고    scopus 로고
    • Modulation of astrocytic mitochondrial function by dichloroacetate improves survival and motor performance in inherited amyotrophic lateral sclerosis
    • Miquel, E.; Cassina, A.; Martinez-Palma, L.; Bolatto, C.; Trías, E.; Gandelman, M.; Radi, R.; Barbeito, L.; Cassina, P. Modulation of astrocytic mitochondrial function by dichloroacetate improves survival and motor performance in inherited amyotrophic lateral sclerosis. PLoS One 7:e34776; 2012.
    • (2012) PLoS One , vol.7
    • Miquel, E.1    Cassina, A.2    Martinez-Palma, L.3    Bolatto, C.4    Trías, E.5    Gandelman, M.6    Radi, R.7    Barbeito, L.8    Cassina, P.9
  • 55
    • 79959462293 scopus 로고    scopus 로고
    • The role of mitochondria in the pathogenesis of amyotrophic lateral sclerosis
    • Duffy, L. M.; Chapman, A. L.; Shaw, P. J.; Grierson, A. J. The role of mitochondria in the pathogenesis of amyotrophic lateral sclerosis. Neuropathol. Appl. Neurobiol. 37: 336-352; 2011.
    • (2011) Neuropathol. Appl. Neurobiol , vol.37 , pp. 336-352
    • Duffy, L.M.1    Chapman, A.L.2    Shaw, P.J.3    Grierson, A.J.4


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