Judith N. Burstyn

4.7k total citations · 1 hit paper
86 papers, 4.0k citations indexed

About

Judith N. Burstyn is a scholar working on Molecular Biology, Cell Biology and Oncology. According to data from OpenAlex, Judith N. Burstyn has authored 86 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 53 papers in Molecular Biology, 25 papers in Cell Biology and 20 papers in Oncology. Recurrent topics in Judith N. Burstyn's work include Hemoglobin structure and function (24 papers), Metal complexes synthesis and properties (19 papers) and Metal-Catalyzed Oxygenation Mechanisms (16 papers). Judith N. Burstyn is often cited by papers focused on Hemoglobin structure and function (24 papers), Metal complexes synthesis and properties (19 papers) and Metal-Catalyzed Oxygenation Mechanisms (16 papers). Judith N. Burstyn collaborates with scholars based in United States, Slovakia and Canada. Judith N. Burstyn's co-authors include Eric L. Hegg, Kim A. Deal, Elizabeth A. Dierks, Joan Selverstone Valentine, Omar Green, Anita E. Yu, Thomas G. Spiro, Robert L. Kerby, Peter Legzdins and George B. Richter‐Addo and has published in prestigious journals such as Chemical Reviews, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Judith N. Burstyn

86 papers receiving 4.0k citations

Hit Papers

Toward the development of... 1998 2026 2007 2016 1998 100 200 300 400 500
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Toward the development of metal-based synthetic nucleases and peptidases: a rationale and progress report in applying the principles of coordination chemistry
    1998 526 citations Judith N. Burstyn et al. profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Judith N. Burstyn United States 37 1.9k 1.4k 932 826 768 86 4.0k
David E. Heppner United States 26 1.4k 0.7× 933 0.7× 611 0.7× 1.1k 1.3× 631 0.8× 50 3.3k
Richard W. Strange United Kingdom 40 2.0k 1.0× 532 0.4× 364 0.4× 1.1k 1.3× 1.1k 1.5× 115 4.6k
Kenton R. Rodgers United States 34 1.5k 0.8× 325 0.2× 605 0.6× 853 1.0× 651 0.8× 92 3.5k
George B. Richter‐Addo United States 32 522 0.3× 308 0.2× 843 0.9× 887 1.1× 976 1.3× 135 3.1k
Yong Zhang United States 43 1.4k 0.7× 340 0.3× 2.8k 3.0× 1.2k 1.5× 897 1.2× 196 5.3k
M.A. Maestro Spain 47 1.6k 0.8× 1.1k 0.8× 2.3k 2.4× 1.8k 2.1× 1.1k 1.4× 203 6.9k
Yoshiki Higuchi Japan 44 2.9k 1.5× 693 0.5× 711 0.8× 768 0.9× 2.1k 2.8× 225 7.4k
David M. Dooley United States 46 3.8k 2.0× 739 0.5× 487 0.5× 1.8k 2.2× 588 0.8× 148 6.0k
Boi Hanh Huynh United States 51 3.4k 1.7× 836 0.6× 238 0.3× 3.1k 3.8× 1.6k 2.0× 100 6.9k
Takafumi Ueno Japan 38 2.5k 1.3× 652 0.5× 1.1k 1.2× 955 1.2× 1.3k 1.7× 144 4.9k

Countries citing papers authored by Judith N. Burstyn

Since Specialization
Citations

This map shows the geographic impact of Judith N. Burstyn'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 Judith N. Burstyn with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Judith N. Burstyn more than expected).

Fields of papers citing papers by Judith N. Burstyn

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Judith N. Burstyn. 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 Judith N. Burstyn. The network helps show where Judith N. Burstyn may publish in the future.

Co-authorship network of co-authors of Judith N. Burstyn

This figure shows the co-authorship network connecting the top 25 collaborators of Judith N. Burstyn. A scholar is included among the top collaborators of Judith N. Burstyn 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 Judith N. Burstyn. Judith N. Burstyn 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.
Ramos, Sashary, et al.. (2024). Probing conformational dynamics of DNA binding by CO-sensing transcription factor, CooA. Journal of Inorganic Biochemistry. 259. 112656–112656. 2 indexed citations
2.
Burstyn, Judith N., et al.. (2023). Molecular Determinants of Efficient Cobalt-Substituted Hemoprotein Production in E. coli. ACS Synthetic Biology. 12(12). 3669–3679. 4 indexed citations
3.
Burstyn, Judith N., et al.. (2023). Carbon Monoxide-Sensing Transcription Factors: Regulators of Microbial Carbon Monoxide Oxidation Pathway Gene Expression. Journal of Bacteriology. 205(5). e0033222–e0033222. 14 indexed citations
4.
Fang, Mingxu, et al.. (2022). Redox Brake Regulator RedB and FnrL Function as Yin-Yang Regulators of Anaerobic-Aerobic Metabolism in Rhodobacter capsulatus. Microbiology Spectrum. 10(5). e0235422–e0235422. 3 indexed citations
5.
Fang, Mingxu, et al.. (2022). RedB, a Member of the CRP/FNR Family, Functions as a Transcriptional Redox Brake. Microbiology Spectrum. 10(5). e0235322–e0235322. 2 indexed citations
6.
McCaslin, Darrell R., et al.. (2022). Quaternary Structure and Deoxyribonucleic Acid-Binding Properties of the Heme-Dependent, CO-Sensing Transcriptional Regulator PxRcoM. Biochemistry. 61(8). 678–688. 6 indexed citations
7.
Buller, Andrew R., et al.. (2021). De novo biosynthesis of a nonnatural cobalt porphyrin cofactor inE. coliand incorporation into hemoproteins. Proceedings of the National Academy of Sciences. 118(16). 20 indexed citations
8.
Rau, Martina A., et al.. (2021). Adaptive support for representational competencies during technology-based problem solving in chemistry. Journal of the Learning Sciences. 30(2). 163–203. 7 indexed citations
9.
10.
Majtán, Tomáš, et al.. (2011). Purification and characterization of cystathionine β-synthase bearing a cobalt protoporphyrin. Archives of Biochemistry and Biophysics. 508(1). 25–30. 11 indexed citations
11.
Clark, Robert W., et al.. (2009). Silica-bound copper(ii)triazacyclononane as a phosphate esterase: effect of linker length and surface hydrophobicity. Dalton Transactions. 2365–2365. 16 indexed citations
12.
Lee, Andrea J., et al.. (2009). Guanidine Hydrochloride-Induced Unfolding of the Three Heme Coordination States of the CO-Sensing Transcription Factor, CooA. Biochemistry. 48(28). 6585–6597. 11 indexed citations
13.
Pazicni, Samuel, et al.. (2007). Ferrous Human Cystathionine β-Synthase Loses Activity during Enzyme Assay Due to a Ligand Switch Process. Biochemistry. 46(45). 13199–13210. 28 indexed citations
14.
Clark, Robert W., Nicholas D. Lanz, Andrea J. Lee, et al.. (2006). Unexpected NO-dependent DNA binding by the CooA homolog from Carboxydothermus hydrogenoformans. Proceedings of the National Academy of Sciences. 103(4). 891–896. 21 indexed citations
15.
Clark, Robert W., Hwan Youn, Andrea J. Lee, Gary P. Roberts, & Judith N. Burstyn. (2006). DNA binding by an imidazole-sensing CooA variant is dependent on the heme redox state. JBIC Journal of Biological Inorganic Chemistry. 12(2). 139–146. 8 indexed citations
16.
17.
Carr, Heather S., et al.. (2001). Calcium Ion Downregulates Soluble Guanylyl Cyclase Activity: Evidence for a Two-metal Ion Catalytic Mechanism. Archives of Biochemistry and Biophysics. 387(1). 47–56. 17 indexed citations
18.
Reynolds, Mark F., et al.. (1998). EPR and Electronic Absorption Spectroscopies of the CO-Sensing CooA Protein Reveal a Cysteine-Ligated Low-Spin Ferric Heme. Journal of the American Chemical Society. 120(35). 9080–9081. 45 indexed citations
19.
Dierks, Elizabeth A. & Judith N. Burstyn. (1996). Nitric oxide (NO•), the only nitrogen monoxide redox form capable of activating soluble guanylyl cyclase. Biochemical Pharmacology. 51(12). 1593–1600. 83 indexed citations
20.

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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