Dr. Hondal received his Ph.D. in Chemistry from the Ohio State University in 1997. He then spent one year in the laboratory of Raymond Burk at Vanderbilt University studying the chemistry of selenomethionine and the structure of selenoprotein P. He continued his postdoctoral study under the direction of Ronald Raines at the University of Wisconsin-Madison as a NIH Postdoctoral Fellow. His work there focused on state of the art protein engineering techniques, including native chemical ligation and expressed protein ligation. His postdoctoral work at UW-Madison focused on methods for inserting non-natural amino acids into proteins as a means of addressing important structure-function questions in enzymology.
The Paul D. Boyer Memorial Award for Post-Doctoral Fellows 2001Best Publication Award, Journal of Peptide Science The prize is awarded by the Editorial Board of the Journal of Peptide Science to the communicating author for a paper published in the 2007-2009 time period in the Journal of Peptide Science. 2009
Flemer, SJ, Lacey, BM and Hondal RJ. (2007). Synthesis of peptide substrates for mammalian thioredoxin reductase. J. Pept. Sci. 14(5):637-47.
Eckenroth, BE, Lacey, BM, Lothrop, AP, Harris, KM, and Hondal, RJ. (2007). Investigation of the C-terminal Redox Center of High Mr Thioredoxin Reductases by Protein Engineering and Semisynthesis. Biochemistry 46, 9472-9483.
Eckenroth, BE, Rould, MA, Hondal, RJ, and Everse SJ. (2007). Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases. Biochemistry 46, 4694-4705.
Harris, KM, Flemer, S and Hondal, RJ. (2007). Studies on deprotection of cysteine and selenocysteine side chain protecting groups. J. Pept. Sci, 13, 81-93.
Eckenroth, BE, Harris, K, Turanov, AA, Gladyshev, VN, Raines, RT, and Hondal, RJ. (2006). Semisynthesis and characterization of mammalian thioredoxin reductase. Biochemistry 45, 5158-5170.
Ruggles, EL, and Hondal, RJ. (2006). Synthesis and properties of disulfide-bond containing eight-membered rings. Tet. Lett. 47, 4281-4284.
Harris, KM and Hondal RJ. Deprotection of the p-methoxybenzyl group of selenocysteine by neighboring group participation. (2006). In Understanding Biology Using Peptides: Proceedings of the 19th American Peptide Symposium (Sylvie E. Blondelle, Ed.). Springer, New York, pgs 91-92.
Randall MJ, Spiess PC, Hristova M, Hondal RJ, van der Vliet A (2013) Acrolein-induced activation of mitogen-activated protein kinase signaling is mediated by alkylation of thioredoxin reductase and thioredoxin 1. Redox Biol 1(1): 265-75.
Cunniff B, Snider GW, Fredette N, Hondal RJ, Heintz NH (2013) A direct and continuous assay for the determination of thioredoxin reductase activity in cell lysates1. Anal Biochem : .
Snider GW, Ruggles E, Khan N, Hondal RJ (2013) Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: comparison of selenium and sulfur enzymes. Biochemistry 52(32): 5472-81.
Chandler JD, Nichols DP, Nick JA, Hondal RJ, Day BJ (2013) Selective metabolism of hypothiocyanous acid by mammalian thioredoxin reductase promotes lung innate immunity and antioxidant defense. J Biol Chem 288(25): 18421-8.
Hondal RJ, Marino SM, Gladyshev VN (2013) Selenocysteine in thiol/disulfide-like exchange reactions. Antioxid Redox Signal 18(13): 1675-89.
Schroll AL, Hondal RJ, Flemer S Jr (2012) The use of 2,2'-dithiobis(5-nitropyridine) (DTNP) for deprotection and diselenide formation in protected selenocysteine-containing peptides. J Pept Sci 18(3): 155-62.
Schroll AL, Hondal RJ, Flemer S Jr (2012) 2,2'-Dithiobis(5-nitropyridine) (DTNP) as an effective and gentle deprotectant for common cysteine protecting groups. J Pept Sci 18(1): 1-9.