JoAnne Stubbe

16.9k total citations · 3 hit papers
217 papers, 13.8k citations indexed

About

JoAnne Stubbe is a scholar working on Molecular Biology, Inorganic Chemistry and Oncology. According to data from OpenAlex, JoAnne Stubbe has authored 217 papers receiving a total of 13.8k indexed citations (citations by other indexed papers that have themselves been cited), including 134 papers in Molecular Biology, 127 papers in Inorganic Chemistry and 69 papers in Oncology. Recurrent topics in JoAnne Stubbe's work include Metal-Catalyzed Oxygenation Mechanisms (127 papers), Metal complexes synthesis and properties (66 papers) and Metalloenzymes and iron-sulfur proteins (34 papers). JoAnne Stubbe is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (127 papers), Metal complexes synthesis and properties (66 papers) and Metalloenzymes and iron-sulfur proteins (34 papers). JoAnne Stubbe collaborates with scholars based in United States, Germany and France. JoAnne Stubbe's co-authors include John W. Kozarich, Daniel G. Nocera, Jingyang Chen, Anthony J. Sinskey, Cyril S. Yee, Joseph A. Cotruvo, Michelle C. Y. Chang, Mohammad R. Seyedsayamdost, Jiamin Tian and Ellen C. Minnihan 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

215 papers receiving 13.5k citations

Hit Papers

Mechanisms of bleomycin-i... 1987 2026 2000 2013 1987 2003 2005 250 500 750

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
JoAnne Stubbe 8.2k 5.8k 3.3k 2.2k 2.2k 217 13.8k
Lucia Banci 9.9k 1.2× 2.3k 0.4× 2.8k 0.8× 2.9k 1.3× 2.0k 0.9× 430 19.9k
Vincent L. Pecoraro 4.3k 0.5× 10.0k 1.7× 5.0k 1.5× 8.0k 3.6× 1.7k 0.8× 324 18.8k
J. Peisach 7.1k 0.9× 2.3k 0.4× 2.7k 0.8× 2.0k 0.9× 779 0.4× 258 13.8k
Thomas V. O’Halloran 7.3k 0.9× 1.3k 0.2× 3.2k 1.0× 2.4k 1.1× 495 0.2× 198 19.8k
P. Nordlund 10.6k 1.3× 3.2k 0.6× 2.6k 0.8× 2.0k 0.9× 976 0.5× 181 15.4k
Peter Hildebrandt 7.1k 0.9× 1.7k 0.3× 837 0.3× 2.7k 1.2× 2.4k 1.1× 412 15.3k
J. Martin Bollinger 6.3k 0.8× 8.9k 1.6× 2.6k 0.8× 2.8k 1.2× 2.5k 1.1× 197 12.7k
Eckhard Bill 3.3k 0.4× 14.0k 2.4× 7.0k 2.2× 9.5k 4.3× 6.5k 3.0× 557 28.4k
Robert A. Scott 3.4k 0.4× 1.5k 0.3× 945 0.3× 1.8k 0.8× 1.3k 0.6× 191 7.8k
Paul V. Bernhardt 2.4k 0.3× 3.1k 0.5× 4.9k 1.5× 2.7k 1.2× 971 0.4× 492 12.3k

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.
Song, David, et al.. (2015). Direct interfacial Y731 oxidation in α2 by a photoβ2 subunit of E. coli class Ia ribonucleotide reductase. Chemical Science. 6(8). 4519–4524. 8 indexed citations
2.
Prakash, Divya, et al.. (2015). A Ferredoxin Disulfide Reductase Delivers Electrons to the to the Methanosarcina barkeri Class III Ribonucleotide Reductase. Applied Categorical Structures.
3.
Wörsdörfer, Bigna, Kenichi Yokoyama, Jovan Livada, et al.. (2013). Function of the Diiron Cluster of Escherichia coli Class Ia Ribonucleotide Reductase in Proton-Coupled Electron Transfer. DSpace@MIT (Massachusetts Institute of Technology). 1 indexed citations
4.
Brigham, Christopher J., et al.. (2012). Purification of Polyhydroxybutyrate Synthase from Its Native Organism, Ralstonia eutropha: Implications for the Initiation and Elongation of Polymer Formation in Vivo. DSpace@MIT (Massachusetts Institute of Technology). 1 indexed citations
5.
Cotruvo, Joseph A. & JoAnne Stubbe. (2011). Escherichia coli Class Ib Ribonucleotide Reductase Contains a Dimanganese(III)-Tyrosyl Radical Cofactor in Vivo. Biochemistry. 50(10). 1672–1681. 71 indexed citations
6.
Thompson, Luke, Qinglu Zeng, Libusha Kelly, et al.. (2011). Phage auxiliary metabolic genes and the redirection of cyanobacterial host carbon metabolism. Proceedings of the National Academy of Sciences. 108(39). E757–64. 361 indexed citations
7.
Yokoyama, Kenichi, Albert A. Smith, JoAnne Stubbe, Björn Corzilius, & Robert G. Griffin. (2011). Equilibration of Tyrosyl Radicals (Y[• over 356], Y[• over 731], Y[• over 730]) in the Radical Propagation Pathway of the Escherichia coli Class Ia Ribonucleotide Reductase. DSpace@MIT (Massachusetts Institute of Technology). 1 indexed citations
8.
Cotruvo, Joseph A. & JoAnne Stubbe. (2011). Escherichia coli class Ib ribonucleotide reductase contains a dimanganese(III)-tyrosyl radical cofactor in vivo. DSpace@MIT (Massachusetts Institute of Technology). 2 indexed citations
9.
Zhang, Yan & JoAnne Stubbe. (2011). Bacillus subtilis class Ib ribonucleotide reductase is a dimanganese(III)-tyrosyl radical enzyme.. PubMed. 50(25). 5615–23. 2 indexed citations
10.
Cotruvo, Joseph A. & JoAnne Stubbe. (2010). An Active Dimanganese(III)−Tyrosyl Radical Cofactor in Escherichia coli Class Ib Ribonucleotide Reductase. Biochemistry. 49(6). 1297–1309. 107 indexed citations
11.
Lohman, Gregory J. S., Gary J. Gerfen, & JoAnne Stubbe. (2010). Inactivation of Lactobacillus leichmannii ribonucleotide reductase by F2CTP: adenosylcobalamin destruction and formation of a nucleotide based radical. DSpace@MIT (Massachusetts Institute of Technology). 1 indexed citations
12.
Cotruvo, Joseph A. & JoAnne Stubbe. (2008). NrdI, a flavodoxin involved in maintenance of the diferric-tyrosyl radical cofactor in Escherichia coli class Ib ribonucleotide reductase. Proceedings of the National Academy of Sciences. 105(38). 14383–14388. 55 indexed citations
13.
Seyedsayamdost, Mohammad R., Jianming Xie, Clement T. Y. Chan, Peter G. Schultz, & JoAnne Stubbe. (2007). Site-Specific Insertion of 3-Aminotyrosine into Subunit α2 of E. coli Ribonucleotide Reductase:  Direct Evidence for Involvement of Y 730 and Y 731 in Radical Propagation. Journal of the American Chemical Society. 129(48). 15060–15071. 123 indexed citations
14.
Jiang, Wei, et al.. (2007). YfaE, a Ferredoxin Involved in Diferric-Tyrosyl Radical Maintenance in Escherichia coli Ribonucleotide Reductase. Biochemistry. 46(41). 11577–11588. 47 indexed citations
15.
Seyedsayamdost, Mohammad R. & JoAnne Stubbe. (2006). Site-Specific Replacement of Y 356 with 3,4-Dihydroxyphenylalanine in the β2 Subunit of E. coli Ribonucleotide Reductase. Journal of the American Chemical Society. 128(8). 2522–2523. 84 indexed citations
16.
Perlstein, Deborah L., Jie Ge, John H. Robblee, et al.. (2005). The Active Form of the Saccharomyces cerevisiae Ribonucleotide Reductase Small Subunit Is a Heterodimer in Vitro and in Vivo. Biochemistry. 44(46). 15366–15377. 29 indexed citations
17.
Yee, Cyril S., et al.. (2004). Turning on ribonucleotide reductase by light-initiated amino acid radical generation. Proceedings of the National Academy of Sciences. 101(18). 6882–6887. 42 indexed citations
18.
Chen, Dawei, Andreas Abend, JoAnne Stubbe, & Perry A. Frey. (2003). Epimerization at Carbon-5‘ of (5‘ R )-[5‘- 2 H]Adenosylcobalamin by Ribonucleoside Triphosphate Reductase:  Cysteine 408-Independent Cleavage of the Co−C5‘ Bond. Biochemistry. 42(15). 4578–4584. 19 indexed citations
19.
Zhang, Zhen, et al.. (2003). Subcellular localization of yeast ribonucleotide reductase regulated by the DNA replication and damage checkpoint pathways. Proceedings of the National Academy of Sciences. 100(11). 6628–6633. 124 indexed citations
20.
Bennati, Marina, et al.. (2003). Pulsed ELDOR Spectroscopy Measures the Distance between the Two Tyrosyl Radicals in the R2 Subunit of the E. coli Ribonucleotide Reductase. Journal of the American Chemical Society. 125(49). 14988–14989. 56 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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