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242 related items for PubMed ID: 22542526

  • 21. Nonnative structure in a peptide model of the unfolded state of superoxide dismutase 1 (SOD1): Implications for ALS-linked aggregation.
    Cohen NR, Zitzewitz JA, Bilsel O, Matthews CR.
    J Biol Chem; 2019 Sep 13; 294(37):13708-13717. PubMed ID: 31341015
    [Abstract] [Full Text] [Related]

  • 22. Cysteine residues in Cu,Zn-superoxide dismutase are essential to toxicity in Caenorhabditis elegans model of amyotrophic lateral sclerosis.
    Ogawa M, Shidara H, Oka K, Kurosawa M, Nukina N, Furukawa Y.
    Biochem Biophys Res Commun; 2015 Aug 07; 463(4):1196-202. PubMed ID: 26086102
    [Abstract] [Full Text] [Related]

  • 23. Destabilization of the dimer interface is a common consequence of diverse ALS-associated mutations in metal free SOD1.
    Broom HR, Rumfeldt JA, Vassall KA, Meiering EM.
    Protein Sci; 2015 Dec 07; 24(12):2081-9. PubMed ID: 26362407
    [Abstract] [Full Text] [Related]

  • 24. Monomeric Cu,Zn-superoxide dismutase is a common misfolding intermediate in the oxidation models of sporadic and familial amyotrophic lateral sclerosis.
    Rakhit R, Crow JP, Lepock JR, Kondejewski LH, Cashman NR, Chakrabartty A.
    J Biol Chem; 2004 Apr 09; 279(15):15499-504. PubMed ID: 14734542
    [Abstract] [Full Text] [Related]

  • 25. Voltage-Induced Misfolding of Zinc-Replete ALS Mutant Superoxide Dismutase-1.
    Shi Y, Acerson MJ, Shuford KL, Shaw BF.
    ACS Chem Neurosci; 2015 Oct 21; 6(10):1696-707. PubMed ID: 26207449
    [Abstract] [Full Text] [Related]

  • 26. 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]

  • 27. Exposure of Solvent-Inaccessible Regions in the Amyloidogenic Protein Human SOD1 Determined by Hydroxyl Radical Footprinting.
    Sheng Y, Capri J, Waring A, Valentine JS, Whitelegge J.
    J Am Soc Mass Spectrom; 2019 Feb 25; 30(2):218-226. PubMed ID: 30328005
    [Abstract] [Full Text] [Related]

  • 28. 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]

  • 29. An immunological epitope selective for pathological monomer-misfolded SOD1 in ALS.
    Rakhit R, Robertson J, Vande Velde C, Horne P, Ruth DM, Griffin J, Cleveland DW, Cashman NR, Chakrabartty A.
    Nat Med; 2007 Jun 11; 13(6):754-9. PubMed ID: 17486090
    [Abstract] [Full Text] [Related]

  • 30. Quercitrin and quercetin 3-β-d-glucoside as chemical chaperones for the A4V SOD1 ALS-causing mutant.
    Ip P, Sharda PR, Cunningham A, Chakrabartty S, Pande V, Chakrabartty A.
    Protein Eng Des Sel; 2017 Jun 01; 30(6):431-440. PubMed ID: 28475686
    [Abstract] [Full Text] [Related]

  • 31. Cu/Zn superoxide dismutase (SOD1) mutations associated with familial amyotrophic lateral sclerosis (ALS) affect cellular free radical release in the presence of oxidative stress.
    Cookson MR, Menzies FM, Manning P, Eggett CJ, Figlewicz DA, McNeil CJ, Shaw PJ.
    Amyotroph Lateral Scler Other Motor Neuron Disord; 2002 Jun 01; 3(2):75-85. PubMed ID: 12215229
    [Abstract] [Full Text] [Related]

  • 32. Hydrogen Peroxide and Amyotrophic Lateral Sclerosis: From Biochemistry to Pathophysiology.
    Sanghai N, Tranmer GK.
    Antioxidants (Basel); 2021 Dec 27; 11(1):. PubMed ID: 35052556
    [Abstract] [Full Text] [Related]

  • 33. Oligomerization of Cu,Zn-Superoxide Dismutase (SOD1) by Docosahexaenoic Acid and Its Hydroperoxides In Vitro: Aggregation Dependence on Fatty Acid Unsaturation and Thiols.
    Appolinário PP, Medinas DB, Chaves-Filho AB, Genaro-Mattos TC, Cussiol JR, Netto LE, Augusto O, Miyamoto S.
    PLoS One; 2015 Dec 27; 10(4):e0125146. PubMed ID: 25928076
    [Abstract] [Full Text] [Related]

  • 34. 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]

  • 35. Decreased stability and increased formation of soluble aggregates by immature superoxide dismutase do not account for disease severity in ALS.
    Vassall KA, Stubbs HR, Primmer HA, Tong MS, Sullivan SM, Sobering R, Srinivasan S, Briere LA, Dunn SD, Colón W, Meiering EM.
    Proc Natl Acad Sci U S A; 2011 Feb 08; 108(6):2210-5. PubMed ID: 21257910
    [Abstract] [Full Text] [Related]

  • 36. 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]

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  • 38. Immunodetection of disease-associated conformers of mutant cu/zn superoxide dismutase 1 selectively expressed in degenerating neurons in amyotrophic lateral sclerosis.
    Sábado J, Casanovas A, Hernández S, Piedrafita L, Hereu M, Esquerda JE.
    J Neuropathol Exp Neurol; 2013 Jul 15; 72(7):646-61. PubMed ID: 23771221
    [Abstract] [Full Text] [Related]

  • 39. Effects of maturation on the conformational free-energy landscape of SOD1.
    Culik RM, Sekhar A, Nagesh J, Deol H, Rumfeldt JAO, Meiering EM, Kay LE.
    Proc Natl Acad Sci U S A; 2018 Mar 13; 115(11):E2546-E2555. PubMed ID: 29483249
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