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Journal Abstract Search

1387 related items for PubMed ID: 26563614

  • 1. SOD1 in neurotoxicity and its controversial roles in SOD1 mutation-negative ALS.
    Hayashi Y, Homma K, Ichijo H.
    Adv Biol Regul; 2016 Jan; 60():95-104. PubMed ID: 26563614
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  • 2. Wild-type Cu/Zn-superoxide dismutase is misfolded in cerebrospinal fluid of sporadic amyotrophic lateral sclerosis.
    Tokuda E, Takei YI, Ohara S, Fujiwara N, Hozumi I, Furukawa Y.
    Mol Neurodegener; 2019 Nov 19; 14(1):42. PubMed ID: 31744522
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  • 3. [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 Nov 19; 139(7):1015-1019. PubMed ID: 31257248
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  • 4. 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 19; 132(6):827-840. PubMed ID: 27704280
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  • 10. Perspective on SOD1 mediated toxicity in Amyotrophic Lateral Sclerosis.
    Sangwan S, Eisenberg DS.
    Postepy Biochem; 2016 Dec 19; 62(3):362-369. PubMed ID: 28132491
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  • 11. 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 19; 7(6 Pt B):623-43. PubMed ID: 11114261
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  • 12. Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis.
    Tokuda E, Anzai I, Nomura T, Toichi K, Watanabe M, Ohara S, Watanabe S, Yamanaka K, Morisaki Y, Misawa H, Furukawa Y.
    Mol Neurodegener; 2017 Jan 05; 12(1):2. PubMed ID: 28057013
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  • 13. The molecular tweezer CLR01 inhibits aberrant superoxide dismutase 1 (SOD1) self-assembly in vitro and in the G93A-SOD1 mouse model of ALS.
    Malik R, Meng H, Wongkongkathep P, Corrales CI, Sepanj N, Atlasi RS, Klärner FG, Schrader T, Spencer MJ, Loo JA, Wiedau M, Bitan G.
    J Biol Chem; 2019 Mar 08; 294(10):3501-3513. PubMed ID: 30602569
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  • 16. Superoxide dismutase 1 mutants related to amyotrophic lateral sclerosis induce endoplasmic stress in neuro2a cells.
    Oh YK, Shin KS, Yuan J, Kang SJ.
    J Neurochem; 2008 Feb 08; 104(4):993-1005. PubMed ID: 18233996
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  • 18. ALS-linked mutant SOD1 proteins promote Aβ aggregates in ALS through direct interaction with Aβ.
    Jang JY, Cho H, Park HY, Rhim H, Kang S.
    Biochem Biophys Res Commun; 2017 Nov 04; 493(1):697-707. PubMed ID: 28864422
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  • 19. Endoplasmic reticulum stress leads to accumulation of wild-type SOD1 aggregates associated with sporadic amyotrophic lateral sclerosis.
    Medinas DB, Rozas P, Martínez Traub F, Woehlbier U, Brown RH, Bosco DA, Hetz C.
    Proc Natl Acad Sci U S A; 2018 Aug 07; 115(32):8209-8214. PubMed ID: 30038021
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  • 20. Cu/Zn superoxide dismutase (SOD1) mutations associated with familial amyotrophic lateral sclerosis (ALS) affect cellular free radical release in the presence of oxidative stress.
    Cookson MR, Menzies FM, Manning P, Eggett CJ, Figlewicz DA, McNeil CJ, Shaw PJ.
    Amyotroph Lateral Scler Other Motor Neuron Disord; 2002 Jun 07; 3(2):75-85. PubMed ID: 12215229
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