Robert J. Hondal - Publications

Affiliations: 
1998-2002 University of Wisconsin, Madison, Madison, WI 

49 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2017 Payne NC, Geissler A, Button A, Sasuclark AR, Schroll AL, Ruggles EL, Gladyshev VN, Hondal RJ. Comparison of the redox chemistry of sulfur- and selenium-containing analogs of uracil. Free Radical Biology & Medicine. PMID 28108278 DOI: 10.1016/J.Freeradbiomed.2017.01.028  0.52
2016 Gladyshev VN, Arnér ES, Berry MJ, Brigelius-Flohé R, Bruford EA, Burk RF, Carlson BA, Castellano S, Chavatte L, Conrad M, Copeland PR, Diamond AM, Driscoll DM, Ferreiro A, Flohé L, ... ... Hondal RJ, et al. Selenoprotein Gene Nomenclature. The Journal of Biological Chemistry. PMID 27645994 DOI: 10.1074/Jbc.M116.756155  0.52
2016 Reich HJ, Hondal RJ. Why Nature Chose Selenium. Acs Chemical Biology. PMID 26949981 DOI: 10.1021/Acschembio.6B00031  1
2014 Cunniff B, Snider GW, Fredette N, Stumpff J, Hondal RJ, Heintz NH. Resolution of oxidative stress by thioredoxin reductase: Cysteine versus selenocysteine. Redox Biology. 2: 475-84. PMID 24624337 DOI: 10.1016/J.Redox.2014.01.021  1
2014 Ruggles EL, Deker PB, Hondal RJ. Conformational analysis of oxidized peptide fragments of the C-terminal redox center in thioredoxin reductases by NMR spectroscopy. Journal of Peptide Science : An Official Publication of the European Peptide Society. 20: 349-60. PMID 24599608 DOI: 10.1002/Psc.2620  1
2014 Lothrop AP, Snider GW, Flemer S, Ruggles EL, Davidson RS, Lamb AL, Hondal RJ. Compensating for the absence of selenocysteine in high-molecular weight thioredoxin reductases: the electrophilic activation hypothesis. Biochemistry. 53: 664-74. PMID 24490974 DOI: 10.1021/Bi4007258  1
2014 Lothrop AP, Snider GW, Ruggles EL, Patel AS, Lees WJ, Hondal RJ. Selenium as an electron acceptor during the catalytic mechanism of thioredoxin reductase. Biochemistry. 53: 654-63. PMID 24422500 DOI: 10.1021/Bi400658G  1
2014 Snider GW, Dustin CM, Ruggles EL, Hondal RJ. A mechanistic investigation of the C-terminal redox motif of thioredoxin reductase from Plasmodium falciparum. Biochemistry. 53: 601-9. PMID 24400600 DOI: 10.1021/Bi400931K  1
2014 Lothrop AP, Snider GW, Ruggles EL, Hondal RJ. Why is mammalian thioredoxin reductase 1 so dependent upon the use of selenium? Biochemistry. 53: 554-65. PMID 24393022 DOI: 10.1021/Bi400651X  1
2013 Randall MJ, Spiess PC, Hristova M, Hondal RJ, van der Vliet A. Acrolein-induced activation of mitogen-activated protein kinase signaling is mediated by alkylation of thioredoxin reductase and thioredoxin 1. Redox Biology. 1: 265-75. PMID 24024160 DOI: 10.1016/J.Redox.2013.02.001  1
2013 Cunniff B, Snider GW, Fredette N, Hondal RJ, Heintz NH. A direct and continuous assay for the determination of thioredoxin reductase activity in cell lysates. Analytical Biochemistry. 443: 34-40. PMID 23973629 DOI: 10.1016/J.Ab.2013.08.013  1
2013 Snider GW, Ruggles E, Khan N, Hondal RJ. Selenocysteine confers resistance to inactivation by oxidation in thioredoxin reductase: comparison of selenium and sulfur enzymes. Biochemistry. 52: 5472-81. PMID 23865454 DOI: 10.1021/Bi400462J  1
2013 Chandler JD, Nichols DP, Nick JA, Hondal RJ, Day BJ. Selective metabolism of hypothiocyanous acid by mammalian thioredoxin reductase promotes lung innate immunity and antioxidant defense. The Journal of Biological Chemistry. 288: 18421-8. PMID 23629660 DOI: 10.1074/Jbc.M113.468090  1
2013 Hondal RJ, Marino SM, Gladyshev VN. Selenocysteine in thiol/disulfide-like exchange reactions. Antioxidants & Redox Signaling. 18: 1675-89. PMID 23121622 DOI: 10.1089/Ars.2012.5013  1
2012 Schroll AL, Hondal RJ, Flemer S. The use of 2,2'-dithiobis(5-nitropyridine) (DTNP) for deprotection and diselenide formation in protected selenocysteine-containing peptides. Journal of Peptide Science : An Official Publication of the European Peptide Society. 18: 155-62. PMID 22249911 DOI: 10.1002/Psc.1430  1
2012 Schroll AL, Hondal RJ, Flemer S. 2,2'-Dithiobis(5-nitropyridine) (DTNP) as an effective and gentle deprotectant for common cysteine protecting groups. Journal of Peptide Science : An Official Publication of the European Peptide Society. 18: 1-9. PMID 22083608 DOI: 10.1002/Psc.1403  1
2011 Spiess PC, Deng B, Hondal RJ, Matthews DE, van der Vliet A. Proteomic profiling of acrolein adducts in human lung epithelial cells. Journal of Proteomics. 74: 2380-94. PMID 21704744 DOI: 10.1016/J.Jprot.2011.05.039  1
2011 Hondal RJ, Ruggles EL. Differing views of the role of selenium in thioredoxin reductase. Amino Acids. 41: 73-89. PMID 20397034 DOI: 10.1007/S00726-010-0494-6  1
2011 Ruggles EL, Snider GW, Hondal RJ. Chemical basis for the use of selenocysteine Selenium: Its Molecular Biology and Role in Human Health. 73-83. DOI: 10.1007/978-1-4614-1025-6_6  1
2010 Snider G, Grout L, Ruggles EL, Hondal RJ. Methaneseleninic acid is a substrate for truncated mammalian thioredoxin reductase: implications for the catalytic mechanism and redox signaling. Biochemistry. 49: 10329-38. PMID 21038895 DOI: 10.1021/Bi101130T  1
2009 Ruggles EL, Deker PB, Hondal RJ. Synthesis, Redox Properties, and Conformational Analysis of Vicinal Disulfide Ring Mimics. Tetrahedron. 65: 1257-1267. PMID 23682198 DOI: 10.1016/J.Tet.2008.11.085  1
2009 Hondal RJ. Using chemical approaches to study selenoproteins-focus on thioredoxin reductases. Biochimica Et Biophysica Acta. 1790: 1501-12. PMID 19406205 DOI: 10.1016/J.Bbagen.2009.04.015  1
2009 Schroll AL, Hondal RJ. Further development of new deprotection chemistry for cysteine and selenocysteine side chain protecting groups. Advances in Experimental Medicine and Biology. 611: 135-6. PMID 19400127 DOI: 10.1007/978-0-387-73657-0_60  1
2009 Flemer S, Hondal RJ. An efficient protocol for on-resin, vicinal disulfide formation: applications to thioredoxin reductase. Advances in Experimental Medicine and Biology. 611: 93-4. PMID 19400108 DOI: 10.1007/978-0-387-73657-0_41  1
2009 Lothrop AP, Ruggles EL, Hondal RJ. No selenium required: reactions catalyzed by mammalian thioredoxin reductase that are independent of a selenocysteine residue. Biochemistry. 48: 6213-23. PMID 19366212 DOI: 10.1021/Bi802146W  1
2008 Lacey BM, Eckenroth BE, Flemer S, Hondal RJ. Selenium in thioredoxin reductase: a mechanistic perspective. Biochemistry. 47: 12810-21. PMID 18986163 DOI: 10.1021/Bi800951F  1
2008 Flemer S, Lacey BM, Hondal RJ. Synthesis of peptide substrates for mammalian thioredoxin reductase. Journal of Peptide Science : An Official Publication of the European Peptide Society. 14: 637-47. PMID 18035847 DOI: 10.1002/Psc.961  1
2008 Ruggles EL, Flemer S, Hondal RJ. A viable synthesis of N-methyl cysteine. Biopolymers. 90: 61-8. PMID 18008337 DOI: 10.1002/Bip.20889  1
2007 Eckenroth BE, Lacey BM, Lothrop AP, Harris KM, Hondal RJ. Investigation of the C-terminal redox center of high-Mr thioredoxin reductase by protein engineering and semisynthesis. Biochemistry. 46: 9472-83. PMID 17661444 DOI: 10.1021/Bi7004812  1
2007 Eckenroth BE, Rould MA, Hondal RJ, Everse SJ. Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases. Biochemistry. 46: 4694-705. PMID 17385893 DOI: 10.1021/Bi602394P  1
2007 Harris KM, Flemer S, Hondal RJ. Studies on deprotection of cysteine and selenocysteine side-chain protecting groups. Journal of Peptide Science : An Official Publication of the European Peptide Society. 13: 81-93. PMID 17031870 DOI: 10.1002/Psc.795  1
2006 Ruggles EL, Hondal RJ. Synthesis and Properties of Disulfide-Bond Containing Eight-Membered Rings. Tetrahedron Letters. 47: 4281-4284. PMID 23828656 DOI: 10.1016/J.Tetlet.2006.04.023  1
2006 Lacey BM, Hondal RJ. Characterization of mitochondrial thioredoxin reductase from C. elegans. Biochemical and Biophysical Research Communications. 346: 629-36. PMID 16780799 DOI: 10.1016/J.Bbrc.2006.05.095  1
2006 Eckenroth B, Harris K, Turanov AA, Gladyshev VN, Raines RT, Hondal RJ. Semisynthesis and characterization of mammalian thioredoxin reductase. Biochemistry. 45: 5158-70. PMID 16618105 DOI: 10.1021/Bi0517887  1
2005 Hondal RJ. Incorporation of selenocysteine into proteins using peptide ligation. Protein and Peptide Letters. 12: 757-64. PMID 16305545 DOI: 10.2174/0929866054864319  1
2003 Nilsson BL, Hondal RJ, Soellner MB, Raines RT. Protein assembly by orthogonal chemical ligation methods. Journal of the American Chemical Society. 125: 5268-9. PMID 12720426 DOI: 10.1021/Ja029752E  1
2002 Hondal RJ, Raines RT. Semisynthesis of proteins containing selenocysteine. Methods in Enzymology. 347: 70-83. PMID 11898440 DOI: 10.1016/S0076-6879(02)47009-7  1
2001 Hondal RJ, Nilsson BL, Raines RT. Selenocysteine in native chemical ligation and expressed protein ligation. Journal of the American Chemical Society. 123: 5140-1. PMID 11457362 DOI: 10.1021/Ja005885T  1
2001 Kubiak RJ, Yue X, Hondal RJ, Mihai C, Tsai MD, Bruzik KS. Involvement of the Arg-Asp-His catalytic triad in enzymatic cleavage of the phosphodiester bond. Biochemistry. 40: 5422-32. PMID 11331006 DOI: 10.1021/Bi002371Y  1
2001 Hondal RJ, Ma S, Caprioli RM, Hill KE, Burk RF. Heparin-binding Histidine and Lysine Residues of Rat Selenoprotein P Journal of Biological Chemistry. 276: 15823-15831. PMID 11278668 DOI: 10.1074/Jbc.M010405200  1
1999 Hondal RJ, Motley AK, Hill KE, Burk RF. Failure of selenomethionine residues in albumin and immunoglobulin G to protect against peroxynitrite Archives of Biochemistry and Biophysics. 371: 29-34. PMID 10525286 DOI: 10.1006/abbi.1999.1435  1
1999 Kubiak RJ, Hondal RJ, Yue X, Tsai MD, Bruzik KS. Identification of a novel catalytic triad with dual functions in enzymatic cleavage of the P-O bond Journal of the American Chemical Society. 121: 488-489. DOI: 10.1021/Ja9834677  1
1999 Hondal RJ, Zhao Z, Kravchuk AV, Liao H, Riddle SR, Bruzik KS, Tsai MD. Mechanism of phosphatidylinositol-specific phospholipase C revealed by protein engineering and phosphorothioate analogs of phosphatidylinositol Acs Symposium Series. 718: 109-120.  1
1998 Hondal RJ, Zhao Z, Kravchuk AV, Liao H, Riddle SR, Yue X, Bruzik KS, Tsai MD. Mechanism of phosphatidylinositol-specific phospholipase C: A unified view of the mechanism of catalysis Biochemistry. 37: 4568-4580. PMID 9521777 DOI: 10.1021/Bi972646I  1
1997 Hondal RJ, Riddle SR, Kravchuk AV, Zhao Z, Liao H, Bruzik KS, Tsai MD. Phosphatidylinositol-specific phospholipase C: Kinetic and stereochemical evidence for an interaction between arginine-69 and the phosphate group of phosphatidylinositol Biochemistry. 36: 6633-6642. PMID 9184143 DOI: 10.1021/Bi962866G  1
1997 Hondal RJ, Zhao Z, Riddle SR, Kravchuk AV, Liao H, Bruzik KS, Tsai MD. Phosphatidylinositol-specific phospholipase C. 3. Elucidation of the catalytic mechanism and comparison with ribonuclease A Journal of the American Chemical Society. 119: 9933-9934. DOI: 10.1021/Ja9714402  1
1997 Hondal RJ, Bruzik KS, Zhao Z, Tsai MD. Mechanism of phosphatidylinositol-phospholipase C. 2. Reversal of a thio effect by site-directed mutagenesis [17] Journal of the American Chemical Society. 119: 5477-5478. DOI: 10.1021/Ja964217Y  1
1997 Liao H, Hondal RJ, Isai MI. Site-directed mutagenesis studies of phosphatidyl- inositol-specific phospholipase c: The substrate binding residues Faseb Journal. 11.  1
1996 Werneburg BG, Ahn J, Zhong X, Hondal RJ, Kraynov VS, Tsai MD. DNA polymerase β: Pre-steady-state kinetic analysis and roles of arginine-283 in catalysis and fidelity Biochemistry. 35: 7041-7050. PMID 8679529 DOI: 10.1021/Bi9527202  1
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