JoAnne Stubbe

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

About

JoAnne Stubbe is a scholar working on Inorganic Chemistry, Molecular Biology and Oncology. According to data from OpenAlex, JoAnne Stubbe has authored 69 papers receiving a total of 4.0k indexed citations (citations by other indexed papers that have themselves been cited), including 52 papers in Inorganic Chemistry, 39 papers in Molecular Biology and 26 papers in Oncology. Recurrent topics in JoAnne Stubbe's work include Metal-Catalyzed Oxygenation Mechanisms (52 papers), Metal complexes synthesis and properties (25 papers) and Electron Spin Resonance Studies (13 papers). JoAnne Stubbe is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (52 papers), Metal complexes synthesis and properties (25 papers) and Electron Spin Resonance Studies (13 papers). JoAnne Stubbe collaborates with scholars based in United States, Germany and France. JoAnne Stubbe's co-authors include Wilfred A. van der Donk, Daniel G. Nocera, Mohammad R. Seyedsayamdost, Brian M. Hoffman, Amy C. Rosenzweig, Alexander T. Taguchi, Joseph A. Cotruvo, Amie K. Boal, J.A. Gerlt and Catherine L. Drennan and has published in prestigious journals such as Science, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

JoAnne Stubbe

69 papers receiving 3.9k citations

Hit Papers

Protein Radicals in Enzym... 1998 2026 2007 2016 1998 250 500 750 1000
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. Protein Radicals in Enzyme Catalysis
    1998 1.2k citations JoAnne Stubbe, Wilfred A. van der Donk profile →

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
JoAnne Stubbe United States 32 2.2k 2.0k 890 778 689 69 4.0k
James W. Whittaker United States 42 2.1k 1.0× 2.8k 1.4× 1.2k 1.4× 819 1.1× 762 1.1× 91 5.8k
David M. Dooley United States 46 3.8k 1.8× 1.8k 0.9× 739 0.8× 588 0.8× 582 0.8× 148 6.0k
J. Stubbe United States 31 1.9k 0.9× 1.2k 0.6× 724 0.8× 567 0.7× 389 0.6× 47 3.1k
Joann Sanders–Loehr United States 44 2.3k 1.1× 2.1k 1.0× 974 1.1× 928 1.2× 785 1.1× 91 4.7k
Jürgen Hüttermann Germany 28 1.3k 0.6× 576 0.3× 383 0.4× 479 0.6× 352 0.5× 126 2.7k
Enrica Bordignon Germany 40 2.0k 0.9× 752 0.4× 955 1.1× 1.3k 1.6× 194 0.3× 171 5.0k
Richard W. Strange United Kingdom 40 2.0k 0.9× 1.1k 0.5× 532 0.6× 1.1k 1.5× 561 0.8× 115 4.6k
Angel J. Di Bilio United States 28 1.2k 0.5× 692 0.3× 546 0.6× 748 1.0× 433 0.6× 45 2.8k
Jeffrey R. Harmer Australia 40 798 0.4× 1.7k 0.9× 477 0.5× 1.4k 1.7× 951 1.4× 149 4.6k
Shinnichiro Suzuki Japan 32 1.7k 0.8× 810 0.4× 514 0.6× 579 0.7× 584 0.8× 176 3.5k

Countries citing papers authored by JoAnne Stubbe

Since Specialization
Citations

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

Fields of papers citing papers by JoAnne Stubbe

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by JoAnne Stubbe. 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 JoAnne Stubbe. The network helps show where JoAnne Stubbe may publish in the future.

Co-authorship network of co-authors of JoAnne Stubbe

This figure shows the co-authorship network connecting the top 25 collaborators of JoAnne Stubbe. A scholar is included among the top collaborators of JoAnne Stubbe 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 JoAnne Stubbe. JoAnne Stubbe 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.
Feliciano, Patrícia R., Gyunghoon Kang, Chang Cui, et al.. (2024). 2.6-Å resolution cryo-EM structure of a class Ia ribonucleotide reductase trapped with mechanism-based inhibitor N 3 CDP. Proceedings of the National Academy of Sciences. 121(45). e2417157121–e2417157121. 2 indexed citations
2.
Zhu, Qilei, Cyrille Costentin, JoAnne Stubbe, & Daniel G. Nocera. (2023). Disulfide radical anion as a super-reductant in biology and photoredox chemistry. Chemical Science. 14(25). 6876–6881. 16 indexed citations
3.
Cui, Chang, David Song, Catherine L. Drennan, JoAnne Stubbe, & Daniel G. Nocera. (2023). Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase. Journal of the American Chemical Society. 145(9). 5145–5154. 2 indexed citations
4.
Narasimhan, Jana, Aleksey I. Gerasyuto, Jiashi Wang, et al.. (2022). Ribonucleotide reductase, a novel drug target for gonorrhea. DSpace@MIT (Massachusetts Institute of Technology). 8 indexed citations
5.
Stubbe, JoAnne & Daniel G. Nocera. (2021). Radicals in Biology: Your Life Is in Their Hands. Journal of the American Chemical Society. 143(34). 13463–13472. 35 indexed citations
6.
Cui, Chang, Brandon L. Greene, Gyunghoon Kang, et al.. (2020). Gated Proton Release during Radical Transfer at the Subunit Interface of Ribonucleotide Reductase. Journal of the American Chemical Society. 143(1). 176–183. 16 indexed citations
7.
Ravichandran, Kanchana, et al.. (2020). Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay. Biochemistry. 59(14). 1442–1453. 12 indexed citations
8.
Greene, Brandon L., JoAnne Stubbe, & Daniel G. Nocera. (2019). Selenocysteine Substitution in a Class I Ribonucleotide Reductase. Biochemistry. 58(50). 5074–5084. 13 indexed citations
9.
Lee, Wankyu, Müge Kasan­mascheff, Michael Huynh, et al.. (2018). Properties of Site-Specifically Incorporated 3-Aminotyrosine in Proteins To Study Redox-Active Tyrosines: Escherichia coli Ribonucleotide Reductase as a Paradigm. Biochemistry. 57(24). 3402–3415. 13 indexed citations
10.
Brignole, Edward J., Kuang‐Lei Tsai, Johnathan Chittuluru, et al.. (2018). 3.3-Å resolution cryo-EM structure of human ribonucleotide reductase with substrate and allosteric regulators bound. eLife. 7. 34 indexed citations
11.
Greene, Brandon L., JoAnne Stubbe, & Daniel G. Nocera. (2018). Photochemical Rescue of a Conformationally Inactivated Ribonucleotide Reductase. Journal of the American Chemical Society. 140(46). 15744–15752. 10 indexed citations
12.
Ravichandran, Kanchana, Ellen C. Minnihan, Kenichi Yokoyama, et al.. (2017). Glutamate 350 Plays an Essential Role in Conformational Gating of Long-Range Radical Transport in Escherichia coli Class Ia Ribonucleotide Reductase. Biochemistry. 56(6). 856–868. 19 indexed citations
13.
Greene, Brandon L., Alexander T. Taguchi, JoAnne Stubbe, & Daniel G. Nocera. (2017). Conformationally Dynamic Radical Transfer within Ribonucleotide Reductase. Journal of the American Chemical Society. 139(46). 16657–16665. 37 indexed citations
14.
Ravichandran, Kanchana, et al.. (2017). Formal Reduction Potentials of Difluorotyrosine and Trifluorotyrosine Protein Residues: Defining the Thermodynamics of Multistep Radical Transfer. Journal of the American Chemical Society. 139(8). 2994–3004. 34 indexed citations
15.
Anand, Ruchi, Aaron A. Hoskins, JoAnne Stubbe, & S.E. Ealick. (2005). Stucture ofS. typhimuriumformylglycinamide ribonucleotide amidotransferase. Acta Crystallographica Section A Foundations of Crystallography. 61(a1). c205–c205. 1 indexed citations
16.
Sommerhalter, Monika, W.C. Voegtli, Deborah L. Perlstein, et al.. (2004). Structures of the Yeast Ribonucleotide Reductase Rnr2 and Rnr4 Homodimers ,. Biochemistry. 43(24). 7736–7742. 30 indexed citations
17.
Stubbe, JoAnne. (2003). Di-iron-tyrosyl radical ribonucleotide reductases. Current Opinion in Chemical Biology. 7(2). 183–188. 109 indexed citations
18.
Gerfen, Gary J., Wilfred A. van der Donk, Guixue Yu, et al.. (1998). Characterization of a Substrate-Derived Radical Detected during the Inactivation of Ribonucleotide Reductase fromEscherichia coliby 2‘-Fluoromethylene-2‘-deoxycytidine 5‘-Diphosphate. Journal of the American Chemical Society. 120(16). 3823–3835. 41 indexed citations
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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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