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286 related items for PubMed ID: 11854284

  • 1. Decreased metallation and activity in subsets of mutant superoxide dismutases associated with familial amyotrophic lateral sclerosis.
    Hayward LJ, Rodriguez JA, Kim JW, Tiwari A, Goto JJ, Cabelli DE, Valentine JS, Brown RH.
    J Biol Chem; 2002 May 03; 277(18):15923-31. PubMed ID: 11854284
    [Abstract] [Full Text] [Related]

  • 2. Familial amyotrophic lateral sclerosis-associated mutations decrease the thermal stability of distinctly metallated species of human copper/zinc superoxide dismutase.
    Rodriguez JA, Valentine JS, Eggers DK, Roe JA, Tiwari A, Brown RH, Hayward LJ.
    J Biol Chem; 2002 May 03; 277(18):15932-7. PubMed ID: 11854285
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  • 4. Aberrantly increased hydrophobicity shared by mutants of Cu,Zn-superoxide dismutase in familial amyotrophic lateral sclerosis.
    Tiwari A, Xu Z, Hayward LJ.
    J Biol Chem; 2005 Aug 19; 280(33):29771-9. PubMed ID: 15958382
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  • 6. Copper and zinc metallation status of copper-zinc superoxide dismutase from amyotrophic lateral sclerosis transgenic mice.
    Lelie HL, Liba A, Bourassa MW, Chattopadhyay M, Chan PK, Gralla EB, Miller LM, Borchelt DR, Valentine JS, Whitelegge JP.
    J Biol Chem; 2011 Jan 28; 286(4):2795-806. PubMed ID: 21068388
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  • 7. Interaction of amyotrophic lateral sclerosis (ALS)-related mutant copper-zinc superoxide dismutase with the dynein-dynactin complex contributes to inclusion formation.
    Ström AL, Shi P, Zhang F, Gal J, Kilty R, Hayward LJ, Zhu H.
    J Biol Chem; 2008 Aug 15; 283(33):22795-805. PubMed ID: 18515363
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  • 9. Mutant SOD1 instability: implications for toxicity in amyotrophic lateral sclerosis.
    Tiwari A, Hayward LJ.
    Neurodegener Dis; 2005 Aug 15; 2(3-4):115-27. PubMed ID: 16909016
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  • 11. Structures of the G85R variant of SOD1 in familial amyotrophic lateral sclerosis.
    Cao X, Antonyuk SV, Seetharaman SV, Whitson LJ, Taylor AB, Holloway SP, Strange RW, Doucette PA, Valentine JS, Tiwari A, Hayward LJ, Padua S, Cohlberg JA, Hasnain SS, Hart PJ.
    J Biol Chem; 2008 Jun 06; 283(23):16169-77. PubMed ID: 18378676
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  • 12. Insights into the role of the unusual disulfide bond in copper-zinc superoxide dismutase.
    Sea K, Sohn SH, Durazo A, Sheng Y, Shaw BF, Cao X, Taylor AB, Whitson LJ, Holloway SP, Hart PJ, Cabelli DE, Gralla EB, Valentine JS.
    J Biol Chem; 2015 Jan 23; 290(4):2405-18. PubMed ID: 25433341
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  • 13. Fluorescence assay for monitoring Zn-deficient superoxide dismutase in vitro.
    Martyshkin DV, Mirov SB, Zhuang YX, Crow JP, Ermilov V, Beckman JS.
    Spectrochim Acta A Mol Biomol Spectrosc; 2003 Nov 23; 59(13):3165-75. PubMed ID: 14583292
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  • 14. Normal binding and reactivity of copper in mutant superoxide dismutase isolated from amyotrophic lateral sclerosis patients.
    Marklund SL, Andersen PM, Forsgren L, Nilsson P, Ohlsson PI, Wikander G, Oberg A.
    J Neurochem; 1997 Aug 23; 69(2):675-81. PubMed ID: 9231727
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  • 15. Structural and biophysical properties of the pathogenic SOD1 variant H46R/H48Q.
    Winkler DD, Schuermann JP, Cao X, Holloway SP, Borchelt DR, Carroll MC, Proescher JB, Culotta VC, Hart PJ.
    Biochemistry; 2009 Apr 21; 48(15):3436-47. PubMed ID: 19227972
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  • 16. Structural and biophysical properties of metal-free pathogenic SOD1 mutants A4V and G93A.
    Galaleldeen A, Strange RW, Whitson LJ, Antonyuk SV, Narayana N, Taylor AB, Schuermann JP, Holloway SP, Hasnain SS, Hart PJ.
    Arch Biochem Biophys; 2009 Dec 21; 492(1-2):40-7. PubMed ID: 19800308
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  • 17. Cupric ions induce the oxidation and trigger the aggregation of human superoxide dismutase 1.
    Li C, Xu WC, Xie ZS, Pan K, Hu J, Chen J, Pang DW, Yang FQ, Liang Y.
    PLoS One; 2013 Dec 21; 8(6):e65287. PubMed ID: 23755211
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  • 18. CuATSM Protects Against the In Vitro Cytotoxicity of Wild-Type-Like Copper-Zinc Superoxide Dismutase Mutants but not Mutants That Disrupt Metal Binding.
    Farrawell NE, Yerbury MR, Plotkin SS, McAlary L, Yerbury JJ.
    ACS Chem Neurosci; 2019 Mar 20; 10(3):1555-1564. PubMed ID: 30462490
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  • 19. Increased affinity for copper mediated by cysteine 111 in forms of mutant superoxide dismutase 1 linked to amyotrophic lateral sclerosis.
    Watanabe S, Nagano S, Duce J, Kiaei M, Li QX, Tucker SM, Tiwari A, Brown RH, Beal MF, Hayward LJ, Culotta VC, Yoshihara S, Sakoda S, Bush AI.
    Free Radic Biol Med; 2007 May 15; 42(10):1534-42. PubMed ID: 17448900
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  • 20. Chaperone-facilitated copper binding is a property common to several classes of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants.
    Corson LB, Strain JJ, Culotta VC, Cleveland DW.
    Proc Natl Acad Sci U S A; 1998 May 26; 95(11):6361-6. PubMed ID: 9600970
    [Abstract] [Full Text] [Related]

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