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536 related items for PubMed ID: 31257248

  • 1. [Prion-like Properties of Misfolded Cu/Zn-superoxide Dismutase in Amyotrophic Lateral Sclerosis: Update and Perspectives].
    Tokuda E, Marklund SL, Furukawa Y.
    Yakugaku Zasshi; 2019; 139(7):1015-1019. PubMed ID: 31257248
    [Abstract] [Full Text] [Related]

  • 2. A Metal-Free, Disulfide Oxidized Form of Superoxide Dismutase 1 as a Primary Misfolded Species with Prion-Like Properties in the Extracellular Environments Surrounding Motor Neuron-Like Cells.
    Takashima C, Kosuge Y, Inoue M, Ono SI, Tokuda E.
    Int J Mol Sci; 2021 Apr 16; 22(8):. PubMed ID: 33923808
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  • 5. Does wild-type Cu/Zn-superoxide dismutase have pathogenic roles in amyotrophic lateral sclerosis?
    Furukawa Y, Tokuda E.
    Transl Neurodegener; 2020 Aug 19; 9(1):33. PubMed ID: 32811540
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  • 8. From molecule to molecule and cell to cell: prion-like mechanisms in amyotrophic lateral sclerosis.
    Grad LI, Fernando SM, Cashman NR.
    Neurobiol Dis; 2015 May 19; 77():257-65. PubMed ID: 25701498
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  • 9. TDP-43 or FUS-induced misfolded human wild-type SOD1 can propagate intercellularly in a prion-like fashion.
    Pokrishevsky E, Grad LI, Cashman NR.
    Sci Rep; 2016 Mar 01; 6():22155. PubMed ID: 26926802
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  • 10. The prion-like nature of amyotrophic lateral sclerosis.
    McAlary L, Yerbury JJ, Cashman NR.
    Prog Mol Biol Transl Sci; 2020 Mar 01; 175():261-296. PubMed ID: 32958236
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  • 11. Prion-like activity of Cu/Zn superoxide dismutase: implications for amyotrophic lateral sclerosis.
    Grad LI, Cashman NR.
    Prion; 2014 Mar 01; 8(1):33-41. PubMed ID: 24394345
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  • 12. Intercellular Prion-Like Conversion and Transmission of Cu/Zn Superoxide Dismutase (SOD1) in Cell Culture.
    Grad LI, Pokrishevsky E, Cashman NR.
    Methods Mol Biol; 2017 Mar 01; 1658():357-367. PubMed ID: 28861801
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  • 13. A misfolded dimer of Cu/Zn-superoxide dismutase leading to pathological oligomerization in amyotrophic lateral sclerosis.
    Anzai I, Tokuda E, Mukaiyama A, Akiyama S, Endo F, Yamanaka K, Misawa H, Furukawa Y.
    Protein Sci; 2017 Mar 01; 26(3):484-496. PubMed ID: 27977888
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  • 14. Superoxide Dismutase 1 (SOD1)-Derived Peptide Inhibits Amyloid Aggregation of Familial Amyotrophic Lateral Sclerosis SOD1 Mutants.
    Banerjee V, Shani T, Katzman B, Vyazmensky M, Papo N, Israelson A, Engel S.
    ACS Chem Neurosci; 2016 Nov 16; 7(11):1595-1606. PubMed ID: 27540759
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  • 15. Prion Properties of SOD1 in Amyotrophic Lateral Sclerosis and Potential Therapy.
    Sibilla C, Bertolotti A.
    Cold Spring Harb Perspect Biol; 2017 Oct 03; 9(10):. PubMed ID: 28096265
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  • 16. Distinct conformers of transmissible misfolded SOD1 distinguish human SOD1-FALS from other forms of familial and sporadic ALS.
    Ayers JI, Diamond J, Sari A, Fromholt S, Galaleldeen A, Ostrow LW, Glass JD, Hart PJ, Borchelt DR.
    Acta Neuropathol; 2016 Dec 03; 132(6):827-840. PubMed ID: 27704280
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  • 17. Misfolded SOD1 Accumulation and Mitochondrial Association Contribute to the Selective Vulnerability of Motor Neurons in Familial ALS: Correlation to Human Disease.
    Abu-Hamad S, Kahn J, Leyton-Jaimes MF, Rosenblatt J, Israelson A.
    ACS Chem Neurosci; 2017 Oct 18; 8(10):2225-2234. PubMed ID: 28715630
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  • 18. Spinal cord homogenates from SOD1 familial amyotrophic lateral sclerosis induce SOD1 aggregation in living cells.
    Pokrishevsky E, Hong RH, Mackenzie IR, Cashman NR.
    PLoS One; 2017 Oct 18; 12(9):e0184384. PubMed ID: 28877271
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  • 19. Prion-like propagation of mutant SOD1 misfolding and motor neuron disease spread along neuroanatomical pathways.
    Ayers JI, Fromholt SE, O'Neal VM, Diamond JH, Borchelt DR.
    Acta Neuropathol; 2016 Jan 18; 131(1):103-14. PubMed ID: 26650262
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  • 20. Endogenous macrophage migration inhibitory factor reduces the accumulation and toxicity of misfolded SOD1 in a mouse model of ALS.
    Leyton-Jaimes MF, Benaim C, Abu-Hamad S, Kahn J, Guetta A, Bucala R, Israelson A.
    Proc Natl Acad Sci U S A; 2016 Sep 06; 113(36):10198-203. PubMed ID: 27551074
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