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Journal Abstract Search

310 related items for PubMed ID: 20184893

  • 1. Disulfide-reduced ALS variants of Cu, Zn superoxide dismutase exhibit increased populations of unfolded species.
    Kayatekin C, Zitzewitz JA, Matthews CR.
    J Mol Biol; 2010 Apr 30; 398(2):320-31. PubMed ID: 20184893
    [Abstract] [Full Text] [Related]

  • 2. Metal-free ALS variants of dimeric human Cu,Zn-superoxide dismutase have enhanced populations of monomeric species.
    Svensson AK, Bilsel O, Kayatekin C, Adefusika JA, Zitzewitz JA, Matthews CR.
    PLoS One; 2010 Apr 09; 5(4):e10064. PubMed ID: 20404910
    [Abstract] [Full Text] [Related]

  • 3. The Disulfide Bond, but Not Zinc or Dimerization, Controls Initiation and Seeded Growth in Amyotrophic Lateral Sclerosis-linked Cu,Zn Superoxide Dismutase (SOD1) Fibrillation.
    Chattopadhyay M, Nwadibia E, Strong CD, Gralla EB, Valentine JS, Whitelegge JP.
    J Biol Chem; 2015 Dec 18; 290(51):30624-36. PubMed ID: 26511321
    [Abstract] [Full Text] [Related]

  • 4. Amyotrophic lateral sclerosis mutations have the greatest destabilizing effect on the apo- and reduced form of SOD1, leading to unfolding and oxidative aggregation.
    Furukawa Y, O'Halloran TV.
    J Biol Chem; 2005 Apr 29; 280(17):17266-74. PubMed ID: 15691826
    [Abstract] [Full Text] [Related]

  • 5. Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis.
    Tiwari A, Xu Z, Hayward LJ.
    J Biol Chem; 2005 Aug 19; 280(33):29771-9. PubMed ID: 15958382
    [Abstract] [Full Text] [Related]

  • 6. Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.
    Vassall KA, Stubbs HR, Primmer HA, Tong MS, Sullivan SM, Sobering R, Srinivasan S, Briere LA, Dunn SD, Colón W, Meiering EM.
    Proc Natl Acad Sci U S A; 2011 Feb 08; 108(6):2210-5. PubMed ID: 21257910
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  • 7. Mechanical probes of SOD1 predict systematic trends in metal and dimer affinity of ALS-associated mutants.
    Das A, Plotkin SS.
    J Mol Biol; 2013 Mar 11; 425(5):850-74. PubMed ID: 23291526
    [Abstract] [Full Text] [Related]

  • 8. Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.
    Tiwari A, Hayward LJ.
    Neurodegener Dis; 2005 Mar 11; 2(3-4):115-27. PubMed ID: 16909016
    [Abstract] [Full Text] [Related]

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  • 10. Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1.
    Bouldin SD, Darch MA, Hart PJ, Outten CE.
    Biochem J; 2012 Aug 15; 446(1):59-67. PubMed ID: 22651090
    [Abstract] [Full Text] [Related]

  • 11. Oxidative misfolding of Cu/Zn-superoxide dismutase triggered by non-canonical intramolecular disulfide formation.
    Anzai I, Tokuda E, Handa S, Misawa H, Akiyama S, Furukawa Y.
    Free Radic Biol Med; 2020 Feb 01; 147():187-199. PubMed ID: 31863908
    [Abstract] [Full Text] [Related]

  • 12. Conformational Disorder of the Most Immature Cu, Zn-Superoxide Dismutase Leading to Amyotrophic Lateral Sclerosis.
    Furukawa Y, Anzai I, Akiyama S, Imai M, Cruz FJ, Saio T, Nagasawa K, Nomura T, Ishimori K.
    J Biol Chem; 2016 Feb 19; 291(8):4144-55. PubMed ID: 26694608
    [Abstract] [Full Text] [Related]

  • 13. Strategies for stabilizing superoxide dismutase (SOD1), the protein destabilized in the most common form of familial amyotrophic lateral sclerosis.
    Auclair JR, Boggio KJ, Petsko GA, Ringe D, Agar JN.
    Proc Natl Acad Sci U S A; 2010 Dec 14; 107(50):21394-9. PubMed ID: 21098299
    [Abstract] [Full Text] [Related]

  • 14. Folding of Cu, Zn superoxide dismutase and familial amyotrophic lateral sclerosis.
    Khare SD, Ding F, Dokholyan NV.
    J Mol Biol; 2003 Nov 28; 334(3):515-25. PubMed ID: 14623191
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  • 16. Structural changes to monomeric CuZn superoxide dismutase caused by the familial amyotrophic lateral sclerosis-associated mutation A4V.
    Schmidlin T, Kennedy BK, Daggett V.
    Biophys J; 2009 Sep 16; 97(6):1709-18. PubMed ID: 19751676
    [Abstract] [Full Text] [Related]

  • 17. Dynamical roles of metal ions and the disulfide bond in Cu, Zn superoxide dismutase folding and aggregation.
    Ding F, Dokholyan NV.
    Proc Natl Acad Sci U S A; 2008 Dec 16; 105(50):19696-701. PubMed ID: 19052230
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  • 19. The metal cofactor zinc and interacting membranes modulate SOD1 conformation-aggregation landscape in an in vitro ALS model.
    Sannigrahi A, Chowdhury S, Das B, Banerjee A, Halder A, Kumar A, Saleem M, Naganathan AN, Karmakar S, Chattopadhyay K.
    Elife; 2021 Apr 07; 10():. PubMed ID: 33825682
    [Abstract] [Full Text] [Related]

  • 20. Loss of metal ions, disulfide reduction and mutations related to familial ALS promote formation of amyloid-like aggregates from superoxide dismutase.
    Oztug Durer ZA, Cohlberg JA, Dinh P, Padua S, Ehrenclou K, Downes S, Tan JK, Nakano Y, Bowman CJ, Hoskins JL, Kwon C, Mason AZ, Rodriguez JA, Doucette PA, Shaw BF, Valentine JS.
    PLoS One; 2009 Apr 07; 4(3):e5004. PubMed ID: 19325915
    [Abstract] [Full Text] [Related]

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