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491 related items for PubMed ID: 27540759
21. 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; 14(6):230418. PubMed ID: 38835240 [Abstract] [Full Text] [Related]
22. 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]
23. 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]
24. Perspective on SOD1 mediated toxicity in Amyotrophic Lateral Sclerosis. Sangwan S, Eisenberg DS. Postepy Biochem; 2016 Sep 13; 62(3):362-369. PubMed ID: 28132491 [Abstract] [Full Text] [Related]
25. 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]
26. 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]
27. 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]
28. Wild-type Cu/Zn-superoxide dismutase is misfolded in cerebrospinal fluid of sporadic amyotrophic lateral sclerosis. Tokuda E, Takei YI, Ohara S, Fujiwara N, Hozumi I, Furukawa Y. Mol Neurodegener; 2019 Nov 19; 14(1):42. PubMed ID: 31744522 [Abstract] [Full Text] [Related]
29. β-Methylamino-L-alanine substitution of serine in SOD1 suggests a direct role in ALS etiology. Proctor EA, Mowrey DD, Dokholyan NV. PLoS Comput Biol; 2019 Jul 19; 15(7):e1007225. PubMed ID: 31323035 [Abstract] [Full Text] [Related]
30. 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 19; 87(9):738-747. PubMed ID: 31017342 [Abstract] [Full Text] [Related]
31. Biophysical and Spectroscopic Methods for Monitoring Protein Misfolding and Amyloid Aggregation. Cristóvão JS, Henriques BJ, Gomes CM. Methods Mol Biol; 2019 Sep 19; 1873():3-18. PubMed ID: 30341600 [Abstract] [Full Text] [Related]
32. Loss of charge mutations in solvent exposed Lys residues of superoxide dismutase 1 do not induce inclusion formation in cultured cell models. Crosby K, Crown AM, Roberts BL, Brown H, Ayers JI, Borchelt DR. PLoS One; 2018 Sep 19; 13(11):e0206751. PubMed ID: 30399166 [Abstract] [Full Text] [Related]
33. Misfolded SOD1 Accumulation and Mitochondrial Association Contribute to the Selective Vulnerability of Motor Neurons in Familial ALS: Correlation to Human Disease. Abu-Hamad S, Kahn J, Leyton-Jaimes MF, Rosenblatt J, Israelson A. ACS Chem Neurosci; 2017 Oct 18; 8(10):2225-2234. PubMed ID: 28715630 [Abstract] [Full Text] [Related]
34. Calcium ions promote superoxide dismutase 1 (SOD1) aggregation into non-fibrillar amyloid: a link to toxic effects of calcium overload in amyotrophic lateral sclerosis (ALS)? Leal SS, Cardoso I, Valentine JS, Gomes CM. J Biol Chem; 2013 Aug 30; 288(35):25219-25228. PubMed ID: 23861388 [Abstract] [Full Text] [Related]
35. Amyotrophic lateral sclerosis is a non-amyloid disease in which extensive misfolding of SOD1 is unique to the familial form. Kerman A, Liu HN, Croul S, Bilbao J, Rogaeva E, Zinman L, Robertson J, Chakrabartty A. Acta Neuropathol; 2010 Mar 30; 119(3):335-44. PubMed ID: 20111867 [Abstract] [Full Text] [Related]
36. Identification of a misfolded region in superoxide dismutase 1 that is exposed in amyotrophic lateral sclerosis. Rotunno MS, Auclair JR, Maniatis S, Shaffer SA, Agar J, Bosco DA. J Biol Chem; 2014 Oct 10; 289(41):28527-38. PubMed ID: 25164820 [Abstract] [Full Text] [Related]
37. Oxidized/misfolded superoxide dismutase-1: the cause of all amyotrophic lateral sclerosis? Kabashi E, Valdmanis PN, Dion P, Rouleau GA. Ann Neurol; 2007 Dec 10; 62(6):553-9. PubMed ID: 18074357 [Abstract] [Full Text] [Related]
38. Many roads lead to Rome? Multiple modes of Cu,Zn superoxide dismutase destabilization, misfolding and aggregation in amyotrophic lateral sclerosis. Broom HR, Rumfeldt JA, Meiering EM. Essays Biochem; 2014 Dec 10; 56():149-65. PubMed ID: 25131593 [Abstract] [Full Text] [Related]
39. 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 10; 76(1-2):231-241. PubMed ID: 28952073 [Abstract] [Full Text] [Related]
40. 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 10; 45(8):853-859. PubMed ID: 27496206 [Abstract] [Full Text] [Related] Page: [Previous] [Next] [New Search]