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Journal Abstract Search

189 related items for PubMed ID: 35516947

  • 21. The structure of holo and metal-deficient wild-type human Cu, Zn superoxide dismutase and its relevance to familial amyotrophic lateral sclerosis.
    Strange RW, Antonyuk S, Hough MA, Doucette PA, Rodriguez JA, Hart PJ, Hayward LJ, Valentine JS, Hasnain SS.
    J Mol Biol; 2003 May 09; 328(4):877-91. PubMed ID: 12729761
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  • 22. 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
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  • 25. 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
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  • 26. Molecular dynamics of a far positioned SOD1 mutant V14M reveals pathogenic misfolding behavior.
    Tompa DR, Kadhirvel S.
    J Biomol Struct Dyn; 2018 Nov 20; 36(15):4085-4098. PubMed ID: 29157189
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  • 27. Effect of metal loading and subcellular pH on net charge of superoxide dismutase-1.
    Shi Y, Mowery RA, Shaw BF.
    J Mol Biol; 2013 Nov 15; 425(22):4388-404. PubMed ID: 23871896
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  • 29. 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 15; 151(Pt B):106319. PubMed ID: 36446187
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  • 30. 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 15; 38(1):37-49. PubMed ID: 30701485
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  • 33. Calorimetric analysis of thermodynamic stability and aggregation for apo and holo amyotrophic lateral sclerosis-associated Gly-93 mutants of superoxide dismutase.
    Stathopulos PB, Rumfeldt JA, Karbassi F, Siddall CA, Lepock JR, Meiering EM.
    J Biol Chem; 2006 Mar 10; 281(10):6184-93. PubMed ID: 16407238
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  • 34. 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
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  • 37. 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 13; 7(2):333-46. PubMed ID: 25554447
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  • 38. A common property of amyotrophic lateral sclerosis-associated variants: destabilization of the copper/zinc superoxide dismutase electrostatic loop.
    Molnar KS, Karabacak NM, Johnson JL, Wang Q, Tiwari A, Hayward LJ, Coales SJ, Hamuro Y, Agar JN.
    J Biol Chem; 2009 Nov 06; 284(45):30965-73. PubMed ID: 19635794
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  • 39. Solid-state NMR studies of metal-free SOD1 fibrillar structures.
    Banci L, Blaževitš O, Cantini F, Danielsson J, Lang L, Luchinat C, Mao J, Oliveberg M, Ravera E.
    J Biol Inorg Chem; 2014 Jun 06; 19(4-5):659-66. PubMed ID: 24719206
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  • 40. Unfolding and aggregation of oxidized metal-deficient superoxide dismutase and isoflavone inhibition based on ion mobility mass spectrometry and ThT fluorescence assay.
    Bian X, Zhuang X, Zheng Z, Liu S, Liu Z, Song F.
    Arch Biochem Biophys; 2022 Sep 30; 727():109306. PubMed ID: 35667444
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