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Journal Abstract Search

226 related items for PubMed ID: 26319711

  • 1. Structural basis of Cu, Zn-superoxide dismutase amyloid fibril formation involves interaction of multiple peptide core regions.
    Ida M, Ando M, Adachi M, Tanaka A, Machida K, Hongo K, Mizobata T, Yamakawa MY, Watanabe Y, Nakashima K, Kawata Y.
    J Biochem; 2016 Feb; 159(2):247-60. PubMed ID: 26319711
    [Abstract] [Full Text] [Related]

  • 2. 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]

  • 3. 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 Dec 18; 4(3):e5004. PubMed ID: 19325915
    [Abstract] [Full Text] [Related]

  • 4. Cu/Zn Superoxide Dismutase Forms Amyloid Fibrils under Near-Physiological Quiescent Conditions: The Roles of Disulfide Bonds and Effects of Denaturant.
    Khan MAI, Respondek M, Kjellström S, Deep S, Linse S, Akke M.
    ACS Chem Neurosci; 2017 Sep 20; 8(9):2019-2026. PubMed ID: 28585802
    [Abstract] [Full Text] [Related]

  • 5. Structural similarity of wild-type and ALS-mutant superoxide dismutase-1 fibrils using limited proteolysis and atomic force microscopy.
    Chan PK, Chattopadhyay M, Sharma S, Souda P, Gralla EB, Borchelt DR, Whitelegge JP, Valentine JS.
    Proc Natl Acad Sci U S A; 2013 Jul 02; 110(27):10934-9. PubMed ID: 23781106
    [Abstract] [Full Text] [Related]

  • 6. 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]

  • 7. Structure, folding, and misfolding of Cu,Zn superoxide dismutase in amyotrophic lateral sclerosis.
    Rakhit R, Chakrabartty A.
    Biochim Biophys Acta; 2006 Aug 19; 1762(11-12):1025-37. PubMed ID: 16814528
    [Abstract] [Full Text] [Related]

  • 8. Mechanism for transforming cytosolic SOD1 into integral membrane proteins of organelles by ALS-causing mutations.
    Lim L, Lee X, Song J.
    Biochim Biophys Acta; 2015 Jan 19; 1848(1 Pt A):1-7. PubMed ID: 25306968
    [Abstract] [Full Text] [Related]

  • 9. Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis.
    Kitamura F, Fujimaki N, Okita W, Hiramatsu H, Takeuchi H.
    Biochemistry; 2011 May 24; 50(20):4242-50. PubMed ID: 21506602
    [Abstract] [Full Text] [Related]

  • 10. Metal-free superoxide dismutase forms soluble oligomers under physiological conditions: a possible general mechanism for familial ALS.
    Banci L, Bertini I, Durazo A, Girotto S, Gralla EB, Martinelli M, Valentine JS, Vieru M, Whitelegge JP.
    Proc Natl Acad Sci U S A; 2007 Jul 03; 104(27):11263-7. PubMed ID: 17592131
    [Abstract] [Full Text] [Related]

  • 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 03; 7(6 Pt B):623-43. PubMed ID: 11114261
    [Abstract] [Full Text] [Related]

  • 12. Heterodimer formation of wild-type and amyotrophic lateral sclerosis-causing mutant Cu/Zn-superoxide dismutase induces toxicity independent of protein aggregation.
    Witan H, Kern A, Koziollek-Drechsler I, Wade R, Behl C, Clement AM.
    Hum Mol Genet; 2008 May 15; 17(10):1373-85. PubMed ID: 18211954
    [Abstract] [Full Text] [Related]

  • 13. 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]

  • 14. Aggregation-triggering segments of SOD1 fibril formation support a common pathway for familial and sporadic ALS.
    Ivanova MI, Sievers SA, Guenther EL, Johnson LM, Winkler DD, Galaleldeen A, Sawaya MR, Hart PJ, Eisenberg DS.
    Proc Natl Acad Sci U S A; 2014 Jan 07; 111(1):197-201. PubMed ID: 24344300
    [Abstract] [Full Text] [Related]

  • 15. 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]

  • 16. Mutation-dependent polymorphism of Cu,Zn-superoxide dismutase aggregates in the familial form of amyotrophic lateral sclerosis.
    Furukawa Y, Kaneko K, Yamanaka K, Nukina N.
    J Biol Chem; 2010 Jul 16; 285(29):22221-31. PubMed ID: 20404329
    [Abstract] [Full Text] [Related]

  • 17. Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis.
    Watanabe S, Nagano S, Duce J, Kiaei M, Li QX, Tucker SM, Tiwari A, Brown RH, Beal MF, Hayward LJ, Culotta VC, Yoshihara S, Sakoda S, Bush AI.
    Free Radic Biol Med; 2007 May 15; 42(10):1534-42. PubMed ID: 17448900
    [Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. Disruption of mitochondrial membrane integrity induced by amyloid aggregates arising from variants of SOD1.
    Oladzad Abbasabadi A, Javanian A, Nikkhah M, Meratan AA, Ghiasi P, Nemat-Gorgani M.
    Int J Biol Macromol; 2013 Oct 15; 61():212-7. PubMed ID: 23872456
    [Abstract] [Full Text] [Related]

  • 20. Common dynamical signatures of familial amyotrophic lateral sclerosis-associated structurally diverse Cu, Zn superoxide dismutase mutants.
    Khare SD, Dokholyan NV.
    Proc Natl Acad Sci U S A; 2006 Feb 28; 103(9):3147-52. PubMed ID: 16488975
    [Abstract] [Full Text] [Related]

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