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305 related items for PubMed ID: 34076319

  • 1. Free energy calculations of ALS-causing SOD1 mutants reveal common perturbations to stability and dynamics along the maturation pathway.
    Wells NGM, Tillinghast GA, O'Neil AL, Smith CA.
    Protein Sci; 2021 Sep; 30(9):1804-1817. PubMed ID: 34076319
    [Abstract] [Full Text] [Related]

  • 2. 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]

  • 3. Exploring the cause of aggregation and reduced Zn binding affinity by G85R mutation in SOD1 rendering amyotrophic lateral sclerosis.
    Srinivasan E, Rajasekaran R.
    Proteins; 2017 Jul 07; 85(7):1276-1286. PubMed ID: 28321933
    [Abstract] [Full Text] [Related]

  • 4. Computational investigation of the human SOD1 mutant, Cys146Arg, that directs familial amyotrophic lateral sclerosis.
    Srinivasan E, Rajasekaran R.
    Mol Biosyst; 2017 Jul 25; 13(8):1495-1503. PubMed ID: 28621357
    [Abstract] [Full Text] [Related]

  • 5. 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]

  • 6. A faulty interaction between SOD1 and hCCS in neurodegenerative disease.
    Wright GS, Antonyuk SV, Hasnain SS.
    Sci Rep; 2016 Jun 10; 6():27691. PubMed ID: 27282955
    [Abstract] [Full Text] [Related]

  • 7. Regression model for predicting pathogenic properties of SOD1 mutants based on the analysis of conformational stability and conservation of hydrogen bonds.
    Alemasov NA, Ivanisenko NV, Ivanisenko VA.
    J Mol Graph Model; 2017 Oct 10; 77():378-385. PubMed ID: 28950184
    [Abstract] [Full Text] [Related]

  • 8. Molecular binding response of naringin and naringenin to H46R mutant SOD1 protein in combating protein aggregation using density functional theory and discrete molecular dynamics.
    Srinivasan E, Rajasekaran R.
    Prog Biophys Mol Biol; 2019 Aug 10; 145():40-51. PubMed ID: 30543828
    [Abstract] [Full Text] [Related]

  • 9. Amyloidogenic regions in beta-strands II and III modulate the aggregation and toxicity of SOD1 in living cells.
    McAlary L, Nan JR, Shyu C, Sher M, Plotkin SS, Cashman NR.
    Open Biol; 2024 Jun 10; 14(6):230418. PubMed ID: 38835240
    [Abstract] [Full Text] [Related]

  • 10. An Allosteric Pathway in Copper, Zinc Superoxide Dismutase Unravels the Molecular Mechanism of the G93A Amyotrophic Lateral Sclerosis-Linked Mutation.
    Souza PCT, Thallmair S, Marrink SJ, Mera-Adasme R.
    J Phys Chem Lett; 2019 Dec 19; 10(24):7740-7744. PubMed ID: 31747286
    [Abstract] [Full Text] [Related]

  • 11. 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]

  • 12. Amyotrophic lateral sclerosis disease-related mutations disrupt the dimerization of superoxide dismutase 1 - A comparative molecular dynamics simulation study.
    Basith S, Manavalan B, Lee G.
    Comput Biol Med; 2022 Dec 16; 151(Pt B):106319. PubMed ID: 36446187
    [Abstract] [Full Text] [Related]

  • 13. The Role of Metal Binding in the Amyotrophic Lateral Sclerosis-Related Aggregation of Copper-Zinc Superoxide Dismutase.
    Sirangelo I, Iannuzzi C.
    Molecules; 2017 Aug 29; 22(9):. PubMed ID: 28850080
    [Abstract] [Full Text] [Related]

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  • 15. Mutations in Superoxide Dismutase 1 (Sod1) Linked to Familial Amyotrophic Lateral Sclerosis Can Disrupt High-Affinity Zinc-Binding Promoted by the Copper Chaperone for Sod1 (Ccs).
    Boyd SD, Ullrich MS, Calvo JS, Behnia F, Meloni G, Winkler DD.
    Molecules; 2020 Feb 28; 25(5):. PubMed ID: 32121118
    [Abstract] [Full Text] [Related]

  • 16. 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]

  • 17. Superoxide Dismutase 1 Folding Stability as a Target for Molecular Tweezers in SOD1-Related Amyotrophic Lateral Sclerosis.
    Samanta N, Ruiz-Blanco YB, Fetahaj Z, Gnutt D, Lantz C, Loo JA, Sanchez-Garcia E, Ebbinghaus S.
    Chembiochem; 2022 Nov 04; 23(21):e202200396. PubMed ID: 36083789
    [Abstract] [Full Text] [Related]

  • 18. 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]

  • 19. Cysteine to Serine Conversion at 111th Position Renders the Disaggregation and Retains the Stabilization of Detrimental SOD1 A4V Mutant Against Amyotrophic Lateral Sclerosis in Human-A Discrete Molecular Dynamics Study.
    Srinivasan E, Rajasekaran R.
    Cell Biochem Biophys; 2018 Jun 18; 76(1-2):231-241. PubMed ID: 28952073
    [Abstract] [Full Text] [Related]

  • 20. 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 Jun 18; 1658():357-367. PubMed ID: 28861801
    [Abstract] [Full Text] [Related]

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