Dr. Ruggles received his B.S. in Chemistry from Ithaca College under Heinz Koch where he synthesized highly halogenated styrene analogs. He subsequently got his M.S. in Chemistry from Bucknell University under Thomas T. Shawe where he used a tandem ozonolysis reductive amination approach for the construction of novel quinocarcin analogues. Dr. Ruggles then received his Ph.D. in Organic Chemistry in 2003 from Michigan State University in the lab of Robert E. Maleczka Jr. where he elucidated chlorinative carbocation rearrangements of vinylic carbinols. His postdoctoral training began in the lab of Gregory K. Friestad in the Chemistry Department at the University of Vermont where he studied enantioselective radical additions to N-acylhydrazones mediated by chiral Lewis acids. He then continued his postdoctoral training at UVM in the Biochemistry Department under Robert J. Hondal as a NIH University Postdoctoral Fellow where he investigated the synthesis, conformations, and redox properties of disulfide containing eight-membered rings with application to thioredoxin reductases.
2014 Kroepsch-Maurice Award for Teaching Excellence (Lecturer Category)
2013 Kroepsch-Maurice Award for Teaching Excellence (Lecturer Category)
2012 Kroepsch-Maurice Award for Teaching Excellence (Lecturer Category)
2008 Excellence in Laboratory Signage and Community Responsibility, University of Vermont
2004-2007 NIH University Postdoctoral Fellow Trainee (PHS T32 HL07594), University of Vermont
2003 Dissertation Completion Fellowship, Michigan State University
1999 Chemistry Travel Award, Michigan State University
1999 Merit Level Teaching Assistantship Award, Michigan State University
1996 Sigma Xi Inductee
1993 NSF Summer Fellowship, Ithaca College and Gorleaus Laboratory
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, 6213-6223.
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
Ruggles, E. L.; Flemer Jr., S.; Hondal, R. J. “Viable Synthesis of N-Methyl Cysteine.” Biopolymers 2008, 90, 61-68.
Ruggles, E. L.; Hondal, R. J. “Synthesis and Properties of Disulfide-Bond Containing Eight-Membered Rings,” Tetrahedron Lett. 2006, 47, 4281-4284.Snider G, Grout L, Ruggles EL, Hondal RJ (2010) Methaneseleninic acid is a substrate for truncated mammalian thioredoxin reductase: implications for the catalytic mechanism and redox signaling. Biochemistry 49(48): 10329-38.
Hondal RJ, Ruggles EL (2011) Differing views of the role of selenium in thioredoxin reductase. Amino Acids 41(1): 73-89.
Friestad GK, Shen Y, Ruggles EL (2003) Enantioselective radical addition to N-acyl hydrazones mediated by chiral Lewis acids. Angew Chem Int Ed Engl 42(41): 5061-3.
Ruggles, E., Snider, G., and Hondal, R. Chapter Six, Chemical Basis for the Use of Selenocysteine. Selenoproteins Wiley and Sons, New York, 2011
Snider, G., Grout, L., Ruggles, E., and Hondal, R. Methaneseleninic acid is a substrate for truncated mammalian thioredoxin reductase: implications for the catalytic mechanism and redox signaling. Biochemistry. 2010 Dec 7;49(48):10329-38. Epub 2010 Nov 10. PMID: 21038895
Hondal, R., and Ruggles, E. Differing views of the role of selenium in thioredoxin reductase. Amino Acids. 2011 Jun;41(1):73-89. Epub 2010 Feb 21. PMID: 20397034