Koder, R. ., Haynes, C. ., Rodgers, M. ., Rodgers, D. ., & Miller, A. . (2002). Flavin thermodynamics explain the oxygen insensitivity of enteric nitroreductases. Biochemistry, 41(48), 14197-205. https://doi.org/10.1021/bi025805t (Original work published 2002)

Yikilmaz, E. ., Xie, J. ., Brunold, T. ., & Miller, A. . (2002). Hydrogen-bond-mediated tuning of the redox potential of the non-heme Fe site of superoxide dismutase. Journal of the American Chemical Society, 124(14), 3482-3. https://doi.org/10.1021/ja011220v (Original work published 2002)

Miller, A. ., Padmakumar, K. ., Sorkin, D. ., Karapetian, A. ., & Vance, C. . (2003). Proton-coupled electron transfer in Fe-superoxide dismutase and Mn-superoxide dismutase. Journal of Inorganic Biochemistry, 93(1-2), 71-83. https://doi.org/10.1016/s0162-0134(02)00621-9 (Original work published 2003)

Miller, A. . (2004). Superoxide dismutases: active sites that save, but a protein that kills. Current Opinion in Chemical Biology, 8(2), 162-8. https://doi.org/10.1016/j.cbpa.2004.02.011

Yikilmaz, E. ., Rodgers, D. ., & Miller, A. . (2006). The crucial importance of chemistry in the structure-function link: manipulating hydrogen bonding in iron-containing superoxide dismutase. Biochemistry, 45(4), 1151-61. https://doi.org/10.1021/bi051495d (Original work published 2006)

Chellgren, B. ., Miller, A. ., & Creamer, T. . (2006). Evidence for polyproline II helical structure in short polyglutamine tracts. Journal of Molecular Biology, 361(2), 362-71. https://doi.org/10.1016/j.jmb.2006.06.044 (Original work published 2006)

RL, K. . , Jr, Walsh, J. ., Pometun, M. ., Dutton, P. ., Wittebort, R. ., & Miller, A. . (2006). 15N solid-state NMR provides a sensitive probe of oxidized flavin reactive sites. Journal of the American Chemical Society, 128(47), 15200-8. https://doi.org/10.1021/ja0648817 (Original work published 2006)

Yikilmaz, E. ., Porta, J. ., Grove, L. ., Vahedi-Faridi, A. ., Bronshteyn, Y. ., Brunold, T. ., … Miller, A. . (2007). How can a single second sphere amino acid substitution cause reduction midpoint potential changes of hundreds of millivolts?. Journal of the American Chemical Society, 129(32), 9927-40. https://doi.org/10.1021/ja069224t (Original work published 2007)

Miller, A. . (2008). Redox tuning over almost 1 V in a structurally conserved active site: lessons from Fe-containing superoxide dismutase. Accounts of Chemical Research, 41(4), 501-10. https://doi.org/10.1021/ar700237u

Boatright, W. ., Jahan, M. ., Walters, B. ., Miller, A. ., Cui, D. ., Hustedt, E. ., & Lei, Q. . (2008). Carbon-centered radicals in isolated soy proteins. Journal of Food Science, 73(3), C222-6. https://doi.org/10.1111/j.1750-3841.2008.00693.x