Robert J. Hondal

4.9k total citations · 2 hit papers
67 papers, 3.6k citations indexed

About

Robert J. Hondal is a scholar working on Molecular Biology, Biochemistry and Nutrition and Dietetics. According to data from OpenAlex, Robert J. Hondal has authored 67 papers receiving a total of 3.6k indexed citations (citations by other indexed papers that have themselves been cited), including 58 papers in Molecular Biology, 23 papers in Biochemistry and 19 papers in Nutrition and Dietetics. Recurrent topics in Robert J. Hondal's work include Redox biology and oxidative stress (36 papers), Sulfur Compounds in Biology (23 papers) and Selenium in Biological Systems (19 papers). Robert J. Hondal is often cited by papers focused on Redox biology and oxidative stress (36 papers), Sulfur Compounds in Biology (23 papers) and Selenium in Biological Systems (19 papers). Robert J. Hondal collaborates with scholars based in United States and France. Robert J. Hondal's co-authors include Hans J. Reich, Erik L. Ruggles, Ronald T. Raines, Bradley L. Nilsson, Emma J. Ste.Marie, Stevenson Flemer, Vadim N. Gladyshev, Ishraq Alim, Javier Seravalli and John W. Cave and has published in prestigious journals such as Cell, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Robert J. Hondal

65 papers receiving 3.6k citations

Hit Papers

Selenium Drives a Transcriptional Adaptive Program to Blo... 2016 2026 2019 2022 2019 2016 250 500 750

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Robert J. Hondal United States 28 2.1k 1.0k 663 573 472 67 3.6k
Aristi P. Fernandes Sweden 28 1.7k 0.8× 1.3k 1.2× 471 0.7× 134 0.2× 327 0.7× 42 3.3k
Julien Verrax Belgium 34 3.1k 1.5× 791 0.8× 369 0.6× 233 0.4× 334 0.7× 53 5.0k
Qing Cheng Sweden 26 1.4k 0.7× 442 0.4× 284 0.4× 164 0.3× 126 0.3× 58 2.1k
Jack C. Yalowich United States 38 2.9k 1.4× 344 0.3× 790 1.2× 133 0.2× 411 0.9× 114 4.5k
Tsai‐Kun Li Taiwan 39 3.5k 1.7× 167 0.2× 983 1.5× 147 0.3× 640 1.4× 82 5.3k
Geou‐Yarh Liou United States 19 2.1k 1.0× 221 0.2× 294 0.4× 323 0.6× 98 0.2× 42 4.3k
Margaret M. Briehl United States 30 1.9k 0.9× 244 0.2× 237 0.4× 146 0.3× 77 0.2× 62 2.8k
Chiara Gorrini Canada 17 3.1k 1.5× 155 0.2× 263 0.4× 349 0.6× 132 0.3× 23 4.6k
Longqin Hu United States 30 2.1k 1.0× 118 0.1× 1.2k 1.9× 244 0.4× 94 0.2× 91 3.9k

Countries citing papers authored by Robert J. Hondal

Since Specialization
Citations

This map shows the geographic impact of Robert J. Hondal's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Robert J. Hondal with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Robert J. Hondal more than expected).

Fields of papers citing papers by Robert J. Hondal

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Robert J. Hondal. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Robert J. Hondal. The network helps show where Robert J. Hondal may publish in the future.

Co-authorship network of co-authors of Robert J. Hondal

This figure shows the co-authorship network connecting the top 25 collaborators of Robert J. Hondal. A scholar is included among the top collaborators of Robert J. Hondal based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Robert J. Hondal. Robert J. Hondal is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Hondal, Robert J., Maximilian B. MacPherson, Sheryl L. White, et al.. (2023). Structural and functional fine mapping of cysteines in mammalian glutaredoxin reveal their differential oxidation susceptibility. Nature Communications. 14(1). 4550–4550. 9 indexed citations
2.
Hondal, Robert J.. (2022). Flux versus poise: Measuring the dynamic cellular activity of the thioredoxin system with a redox probe. Redox Biology. 54. 102376–102376. 2 indexed citations
3.
Day, Brian J., Preston E. Bratcher, Joshua D. Chandler, et al.. (2019). The thiocyanate analog selenocyanate is a more potent antimicrobial pro-drug that also is selectively detoxified by the host. Free Radical Biology and Medicine. 146. 324–332. 16 indexed citations
4.
Ste.Marie, Emma J., et al.. (2019). Synthesis of alpha‐methyl selenocysteine and its utilization as a glutathione peroxidase mimic. Journal of Peptide Science. 25(6). e3173–e3173. 3 indexed citations
5.
Hondal, Robert J., et al.. (2018). Effectors of thioredoxin reductase: Brevetoxins and manumycin-A. Comparative Biochemistry and Physiology Part C Toxicology & Pharmacology. 217. 76–86. 11 indexed citations
6.
Maroney, Michael J. & Robert J. Hondal. (2018). Selenium versus sulfur: Reversibility of chemical reactions and resistance to permanent oxidation in proteins and nucleic acids. Free Radical Biology and Medicine. 127. 228–237. 65 indexed citations
7.
Payne, N. Connor, et al.. (2017). Comparison of the redox chemistry of sulfur- and selenium-containing analogs of uracil. Free Radical Biology and Medicine. 104. 249–261. 26 indexed citations
8.
Cunniff, Brian, et al.. (2014). Resolution of oxidative stress by thioredoxin reductase: Cysteine versus selenocysteine. Redox Biology. 2. 475–484. 21 indexed citations
9.
Cunniff, Brian, et al.. (2013). A direct and continuous assay for the determination of thioredoxin reductase activity in cell lysates. Analytical Biochemistry. 443(1). 34–40. 26 indexed citations
10.
Chandler, Joshua D., David P. Nichols, Jerry A. Nick, Robert J. Hondal, & Brian J. Day. (2013). Selective Metabolism of Hypothiocyanous Acid by Mammalian Thioredoxin Reductase Promotes Lung Innate Immunity and Antioxidant Defense. Journal of Biological Chemistry. 288(25). 18421–18428. 56 indexed citations
11.
Ruggles, Erik L., et al.. (2013). Selenocysteine Confers Resistance to Inactivation by Oxidation in Thioredoxin Reductase: Comparison of Selenium and Sulfur Enzymes. Biochemistry. 52(32). 5472–5481. 84 indexed citations
12.
Ruggles, Erik L. & Robert J. Hondal. (2006). Synthesis and properties of disulfide-bond containing eight-membered rings. Tetrahedron Letters. 47(25). 4281–4284. 9 indexed citations
13.
Lacey, Brian M. & Robert J. Hondal. (2006). Characterization of mitochondrial thioredoxin reductase from C. elegans. Biochemical and Biophysical Research Communications. 346(3). 629–636. 24 indexed citations
14.
Flemer, Stevenson, et al.. (2006). Studies on deprotection of cysteine and selenocysteine side‐chain protecting groups. Journal of Peptide Science. 13(2). 81–93. 91 indexed citations
15.
Hondal, Robert J.. (2005). Incorporation of Selenocysteine into Proteins Using Peptide Ligation. Protein and Peptide Letters. 12(8). 757–764. 21 indexed citations
16.
Hondal, Robert J. & Ronald T. Raines. (2002). Semisynthesis of Proteins Containing Selenocysteine. Methods in enzymology on CD-ROM/Methods in enzymology. 347. 70–83. 34 indexed citations
17.
Hondal, Robert J., Shuguang Ma, Richard M. Caprioli, Kristina E. Hill, & Raymond F. Burk. (2001). Heparin-binding Histidine and Lysine Residues of Rat Selenoprotein P. Journal of Biological Chemistry. 276(19). 15823–15831. 64 indexed citations
18.
Kubiak, Robert, et al.. (2001). Involvement of the Arg−Asp−His Catalytic Triad in Enzymatic Cleavage of the Phosphodiester Bond. Biochemistry. 40(18). 5422–5432. 28 indexed citations
19.
Hondal, Robert J., Amy K. Motley, Kristina E. Hill, & Raymond F. Burk. (1999). Failure of Selenomethionine Residues in Albumin and Immunoglobulin G to Protect against Peroxynitrite. Archives of Biochemistry and Biophysics. 371(1). 29–34. 20 indexed citations
20.
Werneburg, Brian, Jin-Woo Ahn, Xuejun Zhong, et al.. (1996). DNA Polymerase β:  Pre-Steady-State Kinetic Analysis and Roles of Arginine-283 in Catalysis and Fidelity. Biochemistry. 35(22). 7041–7050. 118 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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