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Journal Abstract Search

127 related items for PubMed ID: 31702142

  • 1. Revealing Well-Defined Soluble States during Amyloid Fibril Formation by Multilinear Analysis of NMR Diffusion Data.
    Jensen KS, Linse S, Nilsson M, Akke M, Malmendal A.
    J Am Chem Soc; 2019 Nov 27; 141(47):18649-18652. PubMed ID: 31702142
    [Abstract] [Full Text] [Related]

  • 2. 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]

  • 3. 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]

  • 4. Identification of Distinct Soluble States During Fibril Formation Using Multilinear Analysis of NMR Diffusion Data.
    Jensen KS, Nilsson M, Akke M, Malmendal A.
    Methods Mol Biol; 2023 Dec 13; 2551():461-479. PubMed ID: 36310220
    [Abstract] [Full Text] [Related]

  • 5. Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange.
    Carulla N, Zhou M, Giralt E, Robinson CV, Dobson CM.
    Acc Chem Res; 2010 Aug 17; 43(8):1072-9. PubMed ID: 20557067
    [Abstract] [Full Text] [Related]

  • 6. Aberrant zinc binding to immature conformers of metal-free copper-zinc superoxide dismutase triggers amorphous aggregation.
    Leal SS, Cristóvão JS, Biesemeier A, Cardoso I, Gomes CM.
    Metallomics; 2015 Feb 17; 7(2):333-46. PubMed ID: 25554447
    [Abstract] [Full Text] [Related]

  • 7. 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 17; 159(2):247-60. PubMed ID: 26319711
    [Abstract] [Full Text] [Related]

  • 8. MIF inhibits the formation and toxicity of misfolded SOD1 amyloid aggregates: implications for familial ALS.
    Shvil N, Banerjee V, Zoltsman G, Shani T, Kahn J, Abu-Hamad S, Papo N, Engel S, Bernhagen J, Israelson A.
    Cell Death Dis; 2018 Jan 25; 9(2):107. PubMed ID: 29371591
    [Abstract] [Full Text] [Related]

  • 9. An in silico study of the effect of SOD1 electrostatic loop dynamics on amyloid‑like filament formation.
    Healy EF, Cervantes L.
    Eur Biophys J; 2016 Dec 25; 45(8):853-859. PubMed ID: 27496206
    [Abstract] [Full Text] [Related]

  • 10. Curcumin binds to the pre-fibrillar aggregates of Cu/Zn superoxide dismutase (SOD1) and alters its amyloidogenic pathway resulting in reduced cytotoxicity.
    Bhatia NK, Srivastava A, Katyal N, Jain N, Khan MA, Kundu B, Deep S.
    Biochim Biophys Acta; 2015 May 25; 1854(5):426-36. PubMed ID: 25666897
    [Abstract] [Full Text] [Related]

  • 11. Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR.
    Iwakawa N, Morimoto D, Walinda E, Kawata Y, Shirakawa M, Sugase K.
    Int J Mol Sci; 2017 Oct 28; 18(11):. PubMed ID: 29143789
    [Abstract] [Full Text] [Related]

  • 12. Large SOD1 aggregates, unlike trimeric SOD1, do not impact cell viability in a model of amyotrophic lateral sclerosis.
    Zhu C, Beck MV, Griffith JD, Deshmukh M, Dokholyan NV.
    Proc Natl Acad Sci U S A; 2018 May 01; 115(18):4661-4665. PubMed ID: 29666246
    [Abstract] [Full Text] [Related]

  • 13. α-Synuclein aggregation at low concentrations.
    Afitska K, Fucikova A, Shvadchak VV, Yushchenko DA.
    Biochim Biophys Acta Proteins Proteom; 2019 May 01; 1867(7-8):701-709. PubMed ID: 31096048
    [Abstract] [Full Text] [Related]

  • 14. 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 01; 61():212-7. PubMed ID: 23872456
    [Abstract] [Full Text] [Related]

  • 15. A hyperthermophilic protein G variant engineered via directed evolution prevents the formation of toxic SOD1 oligomers.
    Dagan B, Oren O, Banerjee V, Taube R, Papo N.
    Proteins; 2019 Sep 01; 87(9):738-747. PubMed ID: 31017342
    [Abstract] [Full Text] [Related]

  • 16. Early stages of amyloid fibril formation studied by liquid-state NMR: the peptide hormone glucagon.
    Svane AS, Jahn K, Deva T, Malmendal A, Otzen DE, Dittmer J, Nielsen NC.
    Biophys J; 2008 Jul 01; 95(1):366-77. PubMed ID: 18339765
    [Abstract] [Full Text] [Related]

  • 17. TFE-induced local unfolding and fibrillation of SOD1: bridging the experiment and simulation studies.
    Kumar V, Prakash A, Pandey P, Lynn AM, Hassan MI.
    Biochem J; 2018 May 18; 475(10):1701-1719. PubMed ID: 29686043
    [Abstract] [Full Text] [Related]

  • 18. Monitoring Early-Stage Protein Aggregation by an Aggregation-Induced Emission Fluorogen.
    Kumar M, Hong Y, Thorn DC, Ecroyd H, Carver JA.
    Anal Chem; 2017 Sep 05; 89(17):9322-9329. PubMed ID: 28795815
    [Abstract] [Full Text] [Related]

  • 19. Thermophoretic trap for single amyloid fibril and protein aggregation studies.
    Fränzl M, Thalheim T, Adler J, Huster D, Posseckardt J, Mertig M, Cichos F.
    Nat Methods; 2019 Jul 05; 16(7):611-614. PubMed ID: 31235884
    [Abstract] [Full Text] [Related]

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