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Journal Abstract Search

242 related items for PubMed ID: 29649360

  • 1. Glycerolipid Headgroups Control Rate and Mechanism of Superoxide Dismutase-1 Aggregation and Accelerate Fibrillization of Slowly Aggregating Amyotrophic Lateral Sclerosis Mutants.
    Rasouli S, Abdolvahabi A, Croom CM, Plewman DL, Shi Y, Shaw BF.
    ACS Chem Neurosci; 2018 Jul 18; 9(7):1743-1756. PubMed ID: 29649360
    [Abstract] [Full Text] [Related]

  • 2. Kaplan-Meier Meets Chemical Kinetics: Intrinsic Rate of SOD1 Amyloidogenesis Decreased by Subset of ALS Mutations and Cannot Fully Explain Age of Disease Onset.
    Abdolvahabi A, Shi Y, Rasouli S, Croom CM, Aliyan A, Martí AA, Shaw BF.
    ACS Chem Neurosci; 2017 Jun 21; 8(6):1378-1389. PubMed ID: 28290665
    [Abstract] [Full Text] [Related]

  • 3. 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]

  • 4. 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
    [Abstract] [Full Text] [Related]

  • 5. Tryptophan residue 32 in human Cu-Zn superoxide dismutase modulates prion-like propagation and strain selection.
    Crown A, McAlary L, Fagerli E, Brown H, Yerbury JJ, Galaleldeen A, Cashman NR, Borchelt DR, Ayers JI.
    PLoS One; 2020 Nov 16; 15(1):e0227655. PubMed ID: 31999698
    [Abstract] [Full Text] [Related]

  • 6. Kinetic Variability in Seeded Formation of ALS-Linked SOD1 Fibrils Across Multiple Generations.
    Baumer KM, Koone JC, Shaw BF.
    ACS Chem Neurosci; 2020 Feb 05; 11(3):304-313. PubMed ID: 31895541
    [Abstract] [Full Text] [Related]

  • 7. High-Throughput Microplate-Based Fluorescence Assays for Studying Stochastic Aggregation of Superoxide Dismutase-1.
    Abdolvahabi A, Rasouli S, Croom CM, Plewman DL.
    Methods Mol Biol; 2019 Feb 05; 1873():93-108. PubMed ID: 30341605
    [Abstract] [Full Text] [Related]

  • 8. Lysine acylation in superoxide dismutase-1 electrostatically inhibits formation of fibrils with prion-like seeding.
    Rasouli S, Abdolvahabi A, Croom CM, Plewman DL, Shi Y, Ayers JI, Shaw BF.
    J Biol Chem; 2017 Nov 24; 292(47):19366-19380. PubMed ID: 28974578
    [Abstract] [Full Text] [Related]

  • 9. How Do Gyrating Beads Accelerate Amyloid Fibrillization?
    Abdolvahabi A, Shi Y, Rasouli S, Croom CM, Chuprin A, Shaw BF.
    Biophys J; 2017 Jan 24; 112(2):250-264. PubMed ID: 28122213
    [Abstract] [Full Text] [Related]

  • 10. Arresting amyloid with coulomb's law: acetylation of ALS-linked SOD1 by aspirin impedes aggregation.
    Abdolvahabi A, Shi Y, Rhodes NR, Cook NP, Martí AA, Shaw BF.
    Biophys J; 2015 Mar 10; 108(5):1199-212. PubMed ID: 25762331
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. Changes in hydrophobicity mainly promotes the aggregation tendency of ALS associated SOD1 mutants.
    Tompa DR, Kadhirvel S.
    Int J Biol Macromol; 2020 Feb 15; 145():904-913. PubMed ID: 31669277
    [Abstract] [Full Text] [Related]

  • 13. Calcium binding to gatekeeper residues flanking aggregation-prone segments underlies non-fibrillar amyloid traits in superoxide dismutase 1 (SOD1).
    Estácio SG, Leal SS, Cristóvão JS, Faísca PF, Gomes CM.
    Biochim Biophys Acta; 2015 Feb 15; 1854(2):118-26. PubMed ID: 25463043
    [Abstract] [Full Text] [Related]

  • 14. Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)?
    Leal SS, Cardoso I, Valentine JS, Gomes CM.
    J Biol Chem; 2013 Aug 30; 288(35):25219-25228. PubMed ID: 23861388
    [Abstract] [Full Text] [Related]

  • 15. SOD1 in neurotoxicity and its controversial roles in SOD1 mutation-negative ALS.
    Hayashi Y, Homma K, Ichijo H.
    Adv Biol Regul; 2016 Jan 30; 60():95-104. PubMed ID: 26563614
    [Abstract] [Full Text] [Related]

  • 16. Adsorption of unfolded Cu/Zn superoxide dismutase onto hydrophobic surfaces catalyzes its formation of amyloid fibrils.
    Khan MAI, Weininger U, Kjellström S, Deep S, Akke M.
    Protein Eng Des Sel; 2019 Dec 13; 32(2):77-85. PubMed ID: 31832682
    [Abstract] [Full Text] [Related]

  • 17. Deamidation of asparagine to aspartate destabilizes Cu, Zn superoxide dismutase, accelerates fibrillization, and mirrors ALS-linked mutations.
    Shi Y, Rhodes NR, Abdolvahabi A, Kohn T, Cook NP, Marti AA, Shaw BF.
    J Am Chem Soc; 2013 Oct 23; 135(42):15897-908. PubMed ID: 24066782
    [Abstract] [Full Text] [Related]

  • 18. Cholesterol secosterol aldehyde adduction and aggregation of Cu,Zn-superoxide dismutase: Potential implications in ALS.
    Dantas LS, Chaves-Filho AB, Coelho FR, Genaro-Mattos TC, Tallman KA, Porter NA, Augusto O, Miyamoto S.
    Redox Biol; 2018 Oct 23; 19():105-115. PubMed ID: 30142602
    [Abstract] [Full Text] [Related]

  • 19. Lipid aldehyde hydrophobicity affects apo-SOD1 modification and aggregation.
    Dantas LS, Viviani LG, Inague A, Piccirillo E, Rezende L, Ronsein GE, Augusto O, Medeiros MHG, Amaral ATD, Miyamoto S.
    Free Radic Biol Med; 2020 Aug 20; 156():157-167. PubMed ID: 32598986
    [Abstract] [Full Text] [Related]

  • 20. [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 Aug 20; 139(7):1015-1019. PubMed ID: 31257248
    [Abstract] [Full Text] [Related]

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