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Journal Abstract Search

240 related items for PubMed ID: 33326235

  • 1. Exposure of β6/β7-Loop in Zn/Cu Superoxide Dismutase (SOD1) Is Coupled to Metal Loss and Is Transiently Reversible During Misfolding.
    Bakavayev S, Argueti S, Venkatachalam N, Yehezkel G, Stavsky A, Barak Z, Israelson A, Engel S.
    ACS Chem Neurosci; 2021 Jan 06; 12(1):49-62. PubMed ID: 33326235
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  • 4. A copper-deficient form of mutant Cu/Zn-superoxide dismutase as an early pathological species in amyotrophic lateral sclerosis.
    Tokuda E, Nomura T, Ohara S, Watanabe S, Yamanaka K, Morisaki Y, Misawa H, Furukawa Y.
    Biochim Biophys Acta Mol Basis Dis; 2018 Jun 06; 1864(6 Pt A):2119-2130. PubMed ID: 29551730
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  • 5. 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
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  • 6. The metal cofactor zinc and interacting membranes modulate SOD1 conformation-aggregation landscape in an in vitro ALS model.
    Sannigrahi A, Chowdhury S, Das B, Banerjee A, Halder A, Kumar A, Saleem M, Naganathan AN, Karmakar S, Chattopadhyay K.
    Elife; 2021 Apr 07; 10():. PubMed ID: 33825682
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  • 9. SOD1 oxidation and formation of soluble aggregates in yeast: relevance to sporadic ALS development.
    Martins D, English AM.
    Redox Biol; 2014 Apr 07; 2():632-9. PubMed ID: 24936435
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  • 10. Blocking an epitope of misfolded SOD1 ameliorates disease phenotype in a model of amyotrophic lateral sclerosis.
    Bakavayev S, Stavsky A, Argueti-Ostrovsky S, Yehezkel G, Fridmann-Sirkis Y, Barak Z, Gitler D, Israelson A, Engel S.
    Brain; 2023 Nov 02; 146(11):4594-4607. PubMed ID: 37394908
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  • 11. Aberrant localization of FUS and TDP43 is associated with misfolding of SOD1 in amyotrophic lateral sclerosis.
    Pokrishevsky E, Grad LI, Yousefi M, Wang J, Mackenzie IR, Cashman NR.
    PLoS One; 2012 Nov 02; 7(4):e35050. PubMed ID: 22493728
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  • 12. Early steps in oxidation-induced SOD1 misfolding: implications for non-amyloid protein aggregation in familial ALS.
    Mulligan VK, Kerman A, Laister RC, Sharda PR, Arslan PE, Chakrabartty A.
    J Mol Biol; 2012 Aug 24; 421(4-5):631-52. PubMed ID: 22542526
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  • 14. A copper chaperone-mimetic polytherapy for SOD1-associated amyotrophic lateral sclerosis.
    McAlary L, Shephard VK, Wright GSA, Yerbury JJ.
    J Biol Chem; 2022 Mar 24; 298(3):101612. PubMed ID: 35065969
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  • 15. 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
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  • 17. 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
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  • 18. Structural instability and Cu-dependent pro-oxidant activity acquired by the apo form of mutant SOD1 associated with amyotrophic lateral sclerosis.
    Kitamura F, Fujimaki N, Okita W, Hiramatsu H, Takeuchi H.
    Biochemistry; 2011 May 24; 50(20):4242-50. PubMed ID: 21506602
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  • 19. A Zn-dependent structural transition of SOD1 modulates its ability to undergo phase separation.
    Das B, Roychowdhury S, Mohanty P, Rizuan A, Chakraborty J, Mittal J, Chattopadhyay K.
    EMBO J; 2023 Jan 16; 42(2):e111185. PubMed ID: 36416085
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