Key Publications

  1. Jenny, K. A.; Ruggles, E. L.; Liptak, M.; Masterson, D. S.; Hondal, R. J. “Ergothioneine in a Peptide:  Substitution of Histidine with 2-Thiohistindine in Bioactive Petides”, J. Pept. Sci. 2021, 27, e3339 (
  2. Jenny, K. A.; St. Marie E. J.; Mose, G.; Ruggles E. L.; Hondal, R. J. “Facile Removal of 4-methoxybenzyl protecting group from selenocysteine”, J. Pept. Sci. 2019, 25, e3209 (
  3. Payne, N. C.; Barber, D.; Ruggles, E. L.; Hondal, R. J.  “Can dimedone be used to study selenoproteins?  An investigation into the reactivity of dimedone toward oxidized forms of selenocysteine”, Protein Sci. 2019, 28, 41-55. 
  4. Payne, N. C.; Geissler, A.; Button,  A.; Sasuclark, A. R.; Schroll, A. L.; Ruggles, E. L.; Gladyshev, V. N.; Hondal, R. J.  “Comparison of the redox chemistry of sulfur and selenium containing analogs of uracil”, Free Rad. Biol. Med. 2017, 104, 249-261.
  5. St. Marie, E.; Ruggles, E. L.; Hondal, R. J.  “Removal of the 5-nitro-2-pyridine-sulfenyl protecting group from selenocysteine and cysteine by ascorbolysis”, J. Pept. Sci., 2016, 22, 571-576.
  6. Ruggles, E. L.; Deker, P. B.; Hondal, R. J.  “Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy”, J. Pept. Sci. 2014, 20, 349-360.
  7. Lothrop, A. P.; Snider, G. W.; Flemer, S. Jr.; Ruggles, E. L.; Davidson, R. S.; Lamb, A.; Hondal, R. J.  “Compensating for the absence of selenocysteine in high Mr thioredoxin reductases: The electrophilic activation hypothesis”, Biochemistry 2014, 53, 664-674.
  8. Lothrop, A. P.; Snider, G. W.; Ruggles, E. L.; Patel, A. S.; Lees, W. J.; Hondal, R. J.  “Selenium as an electron acceptor during the catalytic mechanism of thioredoxin reductase”, Biochemistry 2014, 53, 654-663.
  9. Snider, G. W.; Dustin, C. M.; Ruggles, E. L.; Hondal, R. J.  “A mechanistic investigation of the C-terminal redox motif of thioredoxin reductase from Plasmodium falciparum”, Biochemistry 2014, 53, 601-609.
  10. Lothrop, A. P.; Snider, G. W.; Ruggles, E. L.; Hondal, R. J.  “Why is mammalian thioredoxin reductase-1 so dependent upon the use of selenium?”, Biochemistry 2014, 53, 554-565.
  11. Snider, G. W.; Ruggles, E. L.; Khan, N.; Hondal, R. J.  “Selenocysteine Confers Resistance to Inactivation by Oxidation in Thioredoxin Reductase: Comparison of Selenium and Sulfur Enzymes”, Biochemistry 2013, 52, 5472-5481.
  12. Ruggles, E. L.; Snider, G.; Hondal, R. J. Chapter Six, Chemical Basis for the Use of Selenocysteine, In Selenium:  Its Molecular Biology and Role in Human Health; Hatfield, D. L., Berry, M. J., Gladyshev, V. N., Eds.; Springer: New York, 2012, 73-83.  
  13. Hondal, R. J.; Ruggles, E. L. “Differing views of the role of selenium in thioredoxin reductase” Amino Acids 2011, 41, 73-89.
  14. Snider, G.; Grout, L.; Ruggles, E. L.; Hondal, R. J. “Methaneseleninic Acid is a Substrate for Truncated Mammalian Thioredoxin Reductase: Implications for the Catalytic Mechanism and Redox Signaling”, Biochemistry 2010, 49, 10329-10338.
  15. Lothrop, A. P.; Ruggles, E. L.; Hondal, R. J.  “No Selenium Required:  Reactions Catalyzed by Mammalian Thioredoxin Reductase That Are Independent of a Selenocyteine Residue”, Biochemistry 2009, 48, 6213-6123.  
  16. Ruggles, E. L.; Deker, P. B.; Hondal. R. J.  “Synthesis, Redox Properteis, and Conformational Analysis of Vicinal Disulfide Ring Mimics”, Tetrahedron 2009, 65, 1257-1267
  17. Ruggles, E. L.; Flemer Jr., S.; Hondal, R. J.  “Viable Synthesis of N-Methyl Cysteine”, Biopolymers (Peptide Science) 2008, 90, 61-68. 
  18. Ruggles, E. L.; Hondal, R. J.  “Synthesis and Properties of Disulfide-Bond Containing Eight-Membered Rings”, Tetrahedron Lett. 2006, 47, 4281-4284.

All Publications

Dr. Erik Ruggles