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438 related items for PubMed ID: 15758154

  • 1. Mutant superoxide dismutase 1 forms aggregates in the brain mitochondrial matrix of amyotrophic lateral sclerosis mice.
    Vijayvergiya C, Beal MF, Buck J, Manfredi G.
    J Neurosci; 2005 Mar 09; 25(10):2463-70. PubMed ID: 15758154
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  • 2. Mutant SOD1 in neuronal mitochondria causes toxicity and mitochondrial dynamics abnormalities.
    Magrané J, Hervias I, Henning MS, Damiano M, Kawamata H, Manfredi G.
    Hum Mol Genet; 2009 Dec 01; 18(23):4552-64. PubMed ID: 19779023
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  • 3. Human Cu/Zn superoxide dismutase (SOD1) overexpression in mice causes mitochondrial vacuolization, axonal degeneration, and premature motoneuron death and accelerates motoneuron disease in mice expressing a familial amyotrophic lateral sclerosis mutant SOD1.
    Jaarsma D, Haasdijk ED, Grashorn JA, Hawkins R, van Duijn W, Verspaget HW, London J, Holstege JC.
    Neurobiol Dis; 2000 Dec 01; 7(6 Pt B):623-43. PubMed ID: 11114261
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  • 6. ALS-associated mutant SOD1G93A causes mitochondrial vacuolation by expansion of the intermembrane space and by involvement of SOD1 aggregation and peroxisomes.
    Higgins CM, Jung C, Xu Z.
    BMC Neurosci; 2003 Jul 15; 4():16. PubMed ID: 12864925
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  • 8. Conversion to the amyotrophic lateral sclerosis phenotype is associated with intermolecular linked insoluble aggregates of SOD1 in mitochondria.
    Deng HX, Shi Y, Furukawa Y, Zhai H, Fu R, Liu E, Gorrie GH, Khan MS, Hung WY, Bigio EH, Lukas T, Dal Canto MC, O'Halloran TV, Siddique T.
    Proc Natl Acad Sci U S A; 2006 May 02; 103(18):7142-7. PubMed ID: 16636275
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  • 9. Import, maturation, and function of SOD1 and its copper chaperone CCS in the mitochondrial intermembrane space.
    Kawamata H, Manfredi G.
    Antioxid Redox Signal; 2010 Nov 01; 13(9):1375-84. PubMed ID: 20367259
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  • 10. Transgenic mice with human mutant genes causing Parkinson's disease and amyotrophic lateral sclerosis provide common insight into mechanisms of motor neuron selective vulnerability to degeneration.
    Martin LJ.
    Rev Neurosci; 2007 Nov 01; 18(2):115-36. PubMed ID: 17593875
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  • 14. Different regulation of wild-type and mutant Cu,Zn superoxide dismutase localization in mammalian mitochondria.
    Kawamata H, Manfredi G.
    Hum Mol Genet; 2008 Nov 01; 17(21):3303-17. PubMed ID: 18703498
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  • 15. Cell culture models to investigate the selective vulnerability of motoneuronal mitochondria to familial ALS-linked G93ASOD1.
    Raimondi A, Mangolini A, Rizzardini M, Tartari S, Massari S, Bendotti C, Francolini M, Borgese N, Cantoni L, Pietrini G.
    Eur J Neurosci; 2006 Jul 01; 24(2):387-99. PubMed ID: 16903849
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  • 16. Stabilization of mutant Cu/Zn superoxide dismutase (SOD1) protein by coexpressed wild SOD1 protein accelerates the disease progression in familial amyotrophic lateral sclerosis mice.
    Fukada K, Nagano S, Satoh M, Tohyama C, Nakanishi T, Shimizu A, Yanagihara T, Sakoda S.
    Eur J Neurosci; 2001 Dec 01; 14(12):2032-6. PubMed ID: 11860498
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  • 17. Selective association of misfolded ALS-linked mutant SOD1 with the cytoplasmic face of mitochondria.
    Vande Velde C, Miller TM, Cashman NR, Cleveland DW.
    Proc Natl Acad Sci U S A; 2008 Mar 11; 105(10):4022-7. PubMed ID: 18296640
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  • 20. Minute quantities of misfolded mutant superoxide dismutase-1 cause amyotrophic lateral sclerosis.
    Jonsson PA, Ernhill K, Andersen PM, Bergemalm D, Brännström T, Gredal O, Nilsson P, Marklund SL.
    Brain; 2004 Jan 11; 127(Pt 1):73-88. PubMed ID: 14534160
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