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204 related items for PubMed ID: 29686043

  • 1. 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]

  • 2. Alterations in local stability and dynamics of A4V SOD1 in the presence of trifluoroethanol.
    Kumar V, Prakash A, Lynn AM.
    Biopolymers; 2018 Mar 18; 109(3):e23102. PubMed ID: 29369331
    [Abstract] [Full Text] [Related]

  • 3. Solvent sensitivity of protein aggregation in Cu, Zn superoxide dismutase: a molecular dynamics simulation study.
    Prakash A, Kumar V, Pandey P, Bharti DR, Vishwakarma P, Singh R, Hassan MI, Lynn AM.
    J Biomol Struct Dyn; 2018 Aug 18; 36(10):2605-2617. PubMed ID: 28782426
    [Abstract] [Full Text] [Related]

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

  • 5. 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]

  • 6. Trifluoroethanol Partially Unfolds G93A SOD1 Leading to Protein Aggregation: A Study by Native Mass Spectrometry and FPOP Protein Footprinting.
    Niu B, Mackness BC, Zitzewitz JA, Matthews CR, Gross ML.
    Biochemistry; 2020 Oct 06; 59(39):3650-3659. PubMed ID: 32924445
    [Abstract] [Full Text] [Related]

  • 7. Local structural unfolding at the edge-strands of beta sheets is the molecular basis for instability and aggregation of G85R and G93A mutants of superoxide dismutase 1.
    Kumar Ghosh D, Nanaji Shrikondawar A, Ranjan A.
    J Biomol Struct Dyn; 2020 Feb 06; 38(3):647-659. PubMed ID: 30806161
    [Abstract] [Full Text] [Related]

  • 8. Local unfolding of Cu, Zn superoxide dismutase monomer determines the morphology of fibrillar aggregates.
    Ding F, Furukawa Y, Nukina N, Dokholyan NV.
    J Mol Biol; 2012 Aug 24; 421(4-5):548-60. PubMed ID: 22210350
    [Abstract] [Full Text] [Related]

  • 9. 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 24; 85(7):1276-1286. PubMed ID: 28321933
    [Abstract] [Full Text] [Related]

  • 10. Conformational dynamics of superoxide dismutase (SOD1) in osmolytes: a molecular dynamics simulation study.
    Jahan I, Nayeem SM.
    RSC Adv; 2020 Jul 21; 10(46):27598-27614. PubMed ID: 35516947
    [Abstract] [Full Text] [Related]

  • 11. Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior.
    Tompa DR, Kadhirvel S.
    J Biomol Struct Dyn; 2018 Nov 21; 36(15):4085-4098. PubMed ID: 29157189
    [Abstract] [Full Text] [Related]

  • 12. The unfolding mechanism of monomeric mutant SOD1 by simulated force spectroscopy.
    Habibi M, Rottler J, Plotkin SS.
    Biochim Biophys Acta Proteins Proteom; 2017 Nov 21; 1865(11 Pt B):1631-1642. PubMed ID: 28629863
    [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]

  • 14. Molecular dynamics using atomic-resolution structure reveal structural fluctuations that may lead to polymerization of human Cu-Zn superoxide dismutase.
    Strange RW, Yong CW, Smith W, Hasnain SS.
    Proc Natl Acad Sci U S A; 2007 Jun 12; 104(24):10040-4. PubMed ID: 17548825
    [Abstract] [Full Text] [Related]

  • 15. 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]

  • 16. 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]

  • 17. Metalation of the amyotrophic lateral sclerosis mutant glycine 37 to arginine superoxide dismutase (SOD1) apoprotein restores its structural and dynamical properties in solution to those of metalated wild-type SOD1.
    Banci L, Bertini I, D'Amelio N, Libralesso E, Turano P, Valentine JS.
    Biochemistry; 2007 Sep 04; 46(35):9953-62. PubMed ID: 17683122
    [Abstract] [Full Text] [Related]

  • 18. 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 04; 1854(2):118-26. PubMed ID: 25463043
    [Abstract] [Full Text] [Related]

  • 19. Computational Investigation on Electrostatic Loop Mutants Instigating Destabilization and Aggregation on Human SOD1 Protein Causing Amyotrophic Lateral Sclerosis.
    Srinivasan E, Rajasekaran R.
    Protein J; 2019 Feb 04; 38(1):37-49. PubMed ID: 30701485
    [Abstract] [Full Text] [Related]

  • 20. 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 04; 145():40-51. PubMed ID: 30543828
    [Abstract] [Full Text] [Related]

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