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Binding of a single zinc ion to one subunit of copper-zinc superoxide dismutase apoprotein substantially influences the structure and stability of the entire homodimeric protein.
Potter SZ, Zhu H, Shaw BF, Rodriguez JA, Doucette PA, Sohn SH, Durazo A, Faull KF, Gralla EB, Nersissian AM, Valentine JS. Potter SZ, et al. Among authors: nersissian am. J Am Chem Soc. 2007 Apr 18;129(15):4575-83. doi: 10.1021/ja066690+. Epub 2007 Mar 24. J Am Chem Soc. 2007. PMID: 17381088
Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1.
Shaw BF, Lelie HL, Durazo A, Nersissian AM, Xu G, Chan PK, Gralla EB, Tiwari A, Hayward LJ, Borchelt DR, Valentine JS, Whitelegge JP. Shaw BF, et al. Among authors: nersissian am. J Biol Chem. 2008 Mar 28;283(13):8340-50. doi: 10.1074/jbc.M707751200. Epub 2008 Jan 11. J Biol Chem. 2008. PMID: 18192269 Free PMC article.
A structure-based mechanism for copper-zinc superoxide dismutase.
Hart PJ, Balbirnie MM, Ogihara NL, Nersissian AM, Weiss MS, Valentine JS, Eisenberg D. Hart PJ, et al. Among authors: nersissian am. Biochemistry. 1999 Feb 16;38(7):2167-78. doi: 10.1021/bi982284u. Biochemistry. 1999. PMID: 10026301
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