| Year |
Citation |
Score |
| 2023 |
Corteselli EM, Sharafi M, Hondal R, MacPherson M, White S, Lam YW, Gold C, Manuel AM, van der Vliet A, Schneebeli ST, Anathy V, Li J, Janssen-Heininger YMW. Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility. Nature Communications. 14: 4550. PMID 37507364 DOI: 10.1038/s41467-023-39664-2 |
0.301 |
|
| 2021 |
Ste Marie EJ, Hondal RJ. Application of alpha-methyl selenocysteine as a tool for the study of selenoproteins. Methods in Enzymology. 662: 297-329. PMID 35101216 DOI: 10.1016/bs.mie.2021.10.016 |
0.395 |
|
| 2021 |
Jenny KA, Ruggles EL, Liptak MD, Masterson DS, Hondal RJ. Ergothioneine in a peptide: Substitution of histidine with 2-thiohistidine in bioactive peptides. Journal of Peptide Science : An Official Publication of the European Peptide Society. e3339. PMID 34008255 DOI: 10.1002/psc.3339 |
0.33 |
|
| 2020 |
Ste Marie EJ, Wehrle RJ, Haupt DJ, Wood NB, van der Vliet A, Previs MJ, Masterson DS, Hondal RJ. Can Selenoenzymes Resist Electrophilic Modification? Evidence from Thioredoxin Reductase and a Mutant Containing α-Methylselenocysteine. Biochemistry. PMID 32845139 DOI: 10.1021/Acs.Biochem.0C00608 |
0.408 |
|
| 2019 |
Ste Marie EJ, Hondal RJ. 2,2'-Dipyridyl diselenide: A chemoselective tool for cysteine deprotection and disulfide bond formation. Journal of Peptide Science : An Official Publication of the European Peptide Society. e3236. PMID 31856422 DOI: 10.1002/Psc.3236 |
0.472 |
|
| 2019 |
Jenny KA, Ste Marie EJ, Mose G, Ruggles EL, Hondal RJ. Facile removal of 4-methoxybenzyl protecting group from selenocysteine. Journal of Peptide Science : An Official Publication of the European Peptide Society. e3209. PMID 31410953 DOI: 10.1002/Psc.3209 |
0.434 |
|
| 2019 |
Wehrle RJ, Ste Marie EJ, Hondal RJ, Masterson DS. Synthesis of alpha-methyl selenocysteine and its utilization as a glutathione peroxidase mimic. Journal of Peptide Science : An Official Publication of the European Peptide Society. e3173. PMID 31074180 DOI: 10.1002/Psc.3173 |
0.462 |
|
| 2018 |
Ste Marie EJ, Hondal RJ. Reduction of cysteine-S-protecting groups by triisopropylsilane. Journal of Peptide Science : An Official Publication of the European Peptide Society. 24: e3130. PMID 30353614 DOI: 10.1002/Psc.3130 |
0.424 |
|
| 2018 |
Barber DR, Hondal RJ. Gain of function conferred by selenocysteine: Catalytic enhancement of one-electron transfer reactions by thioredoxin reductase. Protein Science : a Publication of the Protein Society. PMID 30052295 DOI: 10.1002/Pro.3480 |
0.456 |
|
| 2018 |
Maroney MJ, Hondal RJ. Selenium versus sulfur: Reversibility of chemical reactions and resistance to permanent oxidation in proteins and nucleic acids. Free Radical Biology & Medicine. PMID 29588180 DOI: 10.1016/J.Freeradbiomed.2018.03.035 |
0.36 |
|
| 2018 |
O'Keefe JP, Dustin CM, Barber DR, Snider GW, Hondal RJ. A "seleno-effect" differentiates the roles of redox active cysteine residues in Plasmodium falciparum thioredoxin reductase. Biochemistry. PMID 29485860 DOI: 10.1021/Acs.Biochem.8B00004 |
0.438 |
|
| 2018 |
Payne NC, Barber DR, Ruggles EL, Hondal RJ. Can Dimedone be Used to Study Selenoproteins? An Investigation into the Reactivity of Dimedone Towards Oxidized Forms of Selenocysteine. Protein Science : a Publication of the Protein Society. PMID 29451338 DOI: 10.1002/Pro.3390 |
0.438 |
|
| 2017 |
Fredericks GJ, Hoffmann FW, Hondal RJ, Rozovsky S, Urschitz J, Hoffmann PR. Selenoprotein K Increases Efficiency of DHHC6 Catalyzed Protein Palmitoylation by Stabilizing the Acyl-DHHC6 Intermediate. Antioxidants (Basel, Switzerland). 7. PMID 29286308 DOI: 10.3390/Antiox7010004 |
0.486 |
|
| 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 |
0.392 |
|
| 2016 |
Ste Marie EJ, Ruggles EL, Hondal RJ. Removal of the 5-nitro-2-pyridine-sulfenyl protecting group from selenocysteine and cysteine by ascorbolysis. Journal of Peptide Science : An Official Publication of the European Peptide Society. PMID 27480992 DOI: 10.1002/Psc.2908 |
0.434 |
|
| 2016 |
Reich HJ, Hondal RJ. Why Nature Chose Selenium. Acs Chemical Biology. PMID 26949981 DOI: 10.1021/Acschembio.6B00031 |
0.357 |
|
| 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 |
0.351 |
|
| 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 |
0.36 |
|
| 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 |
0.414 |
|
| 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 |
0.446 |
|
| 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 |
0.447 |
|
| 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 |
0.421 |
|
| 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 |
0.343 |
|
| 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 |
0.363 |
|
| 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 |
0.305 |
|
| 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 |
0.424 |
|
| 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 |
0.439 |
|
| 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 |
0.465 |
|
| 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 |
0.387 |
|
| 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 |
0.425 |
|
| 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 |
0.421 |
|
| 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 |
0.404 |
|
| 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 |
0.474 |
|
| 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 |
0.44 |
|
| 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 |
0.444 |
|
| 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 |
0.5 |
|
| 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 |
0.443 |
|
| 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 |
0.452 |
|
| 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 |
0.466 |
|
| 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 |
0.395 |
|
| 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 |
0.389 |
|
| 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 |
0.429 |
|
| 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 |
0.627 |
|
| 2005 |
Hondal RJ. Incorporation of selenocysteine into proteins using peptide ligation. Protein and Peptide Letters. 12: 757-64. PMID 16305545 DOI: 10.2174/0929866054864319 |
0.487 |
|
| 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 |
0.684 |
|
| 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 |
0.531 |
|
| 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 |
0.627 |
|
| 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 |
0.419 |
|
| 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. |
0.331 |
|
| 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 |
0.304 |
|
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