Eric M. Shepard

4.1k total citations · 1 hit paper
70 papers, 3.3k citations indexed

About

Eric M. Shepard is a scholar working on Renewable Energy, Sustainability and the Environment, Inorganic Chemistry and Molecular Biology. According to data from OpenAlex, Eric M. Shepard has authored 70 papers receiving a total of 3.3k indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Renewable Energy, Sustainability and the Environment, 29 papers in Inorganic Chemistry and 27 papers in Molecular Biology. Recurrent topics in Eric M. Shepard's work include Metalloenzymes and iron-sulfur proteins (47 papers), Electrocatalysts for Energy Conversion (26 papers) and Metal-Catalyzed Oxygenation Mechanisms (24 papers). Eric M. Shepard is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (47 papers), Electrocatalysts for Energy Conversion (26 papers) and Metal-Catalyzed Oxygenation Mechanisms (24 papers). Eric M. Shepard collaborates with scholars based in United States, Australia and United Kingdom. Eric M. Shepard's co-authors include Joan Broderick, John W. Peters, Benjamin R. Duffus, Kaitlin S. Duschene, David M. Dooley, David W. Mulder, Eric S. Boyd, Paul W. King, Shawn E. McGlynn and Amanda S. Byer 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

Eric M. Shepard

68 papers receiving 3.2k citations

Hit Papers

RadicalS-Adenosylmethionine Enzymes 2014 2026 2018 2022 2014 200 400 600

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Eric M. Shepard United States 28 2.1k 1.2k 933 460 315 70 3.3k
Ulrich Ermler Germany 30 1.6k 0.8× 2.2k 1.8× 859 0.9× 946 2.1× 273 0.9× 85 4.2k
Eberhard Warkentin Germany 27 1.1k 0.5× 1.0k 0.8× 693 0.7× 744 1.6× 177 0.6× 61 2.6k
Evert C. Duin United States 32 1.5k 0.7× 1.1k 0.9× 679 0.7× 797 1.7× 382 1.2× 74 3.0k
Joan Broderick United States 44 4.5k 2.2× 2.3k 1.9× 2.0k 2.1× 873 1.9× 532 1.7× 112 6.2k
Marie‐Hélène Charon France 11 1.3k 0.6× 639 0.5× 459 0.5× 424 0.9× 209 0.7× 19 2.0k
Maria‐Eirini Pandelia United States 32 1.2k 0.6× 803 0.7× 480 0.5× 442 1.0× 378 1.2× 58 2.2k
Michael K. Johnson United States 26 1.5k 0.7× 1.1k 0.9× 628 0.7× 490 1.1× 119 0.4× 45 2.8k
Susana L. A. Andrade Germany 25 2.3k 1.1× 936 0.8× 1.0k 1.1× 933 2.0× 95 0.3× 52 4.0k
Jacques Gaillard France 31 1.0k 0.5× 1.2k 1.0× 794 0.9× 550 1.2× 210 0.7× 109 2.9k
X. Vernède France 15 1.3k 0.6× 576 0.5× 405 0.4× 607 1.3× 291 0.9× 22 2.0k

Countries citing papers authored by Eric M. Shepard

Since Specialization
Citations

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

Fields of papers citing papers by Eric M. Shepard

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Eric M. Shepard. 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 Eric M. Shepard. The network helps show where Eric M. Shepard may publish in the future.

Co-authorship network of co-authors of Eric M. Shepard

This figure shows the co-authorship network connecting the top 25 collaborators of Eric M. Shepard. A scholar is included among the top collaborators of Eric M. Shepard 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 Eric M. Shepard. Eric M. Shepard 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.
Larson, James, Monika Tokmina‐Lukaszewska, Rachel L. Spietz, et al.. (2024). Impact of mineral and non-mineral sources of iron and sulfur on the metalloproteome of Methanosarcina barkeri. Applied and Environmental Microbiology. 90(8). e0051624–e0051624. 1 indexed citations
2.
Shepard, Eric M., et al.. (2023). Semisynthetic maturation of [FeFe]-hydrogenase using [Fe2(μ-SH)2(CN)2(CO)4]2−: key roles for HydF and GTP. Chemical Communications. 59(58). 8929–8932. 11 indexed citations
3.
Yang, Hao, Richard J. Jodts, Eric M. Shepard, et al.. (2020). Radical SAM Enzyme Spore Photoproduct Lyase: Properties of the Ω Organometallic Intermediate and Identification of Stable Protein Radicals Formed during Substrate-Free Turnover. Journal of the American Chemical Society. 142(43). 18652–18660. 10 indexed citations
4.
Yang, Hao, Richard J. Jodts, Eric M. Shepard, et al.. (2020). Active-Site Controlled, Jahn–Teller Enabled Regioselectivity in Reductive S–C Bond Cleavage of S-Adenosylmethionine in Radical SAM Enzymes. Journal of the American Chemical Society. 143(1). 335–348. 16 indexed citations
5.
Yang, Hao, et al.. (2020). S‐Adenosyl‐l‐ethionine is a Catalytically Competent Analog of S‐Adenosyl‐l‐methionine (SAM) in the Radical SAM Enzyme HydG. Angewandte Chemie International Edition. 60(9). 4666–4672. 21 indexed citations
6.
Byer, Amanda S., Eric M. Shepard, Michael W. Ratzloff, et al.. (2019). H-cluster assembly intermediates built on HydF by the radical SAM enzymes HydE and HydG. JBIC Journal of Biological Inorganic Chemistry. 24(6). 783–792. 16 indexed citations
7.
Byer, Amanda S., Hao Yang, Anna L. Vagstad, et al.. (2018). Paradigm Shift for Radical S-Adenosyl-l-methionine Reactions: The Organometallic Intermediate Ω Is Central to Catalysis. Journal of the American Chemical Society. 140(28). 8634–8638. 75 indexed citations
8.
Szilágyi, Róbert K., David W. Mulder, Michael W. Ratzloff, et al.. (2018). Compositional and structural insights into the nature of the H-cluster precursor on HydF. Dalton Transactions. 47(28). 9521–9535. 18 indexed citations
9.
Streit, Bennett R., Arianna I. Celis, Garrett C. Moraski, et al.. (2018). Decarboxylation involving a ferryl, propionate, and a tyrosyl group in a radical relay yields heme b. Journal of Biological Chemistry. 293(11). 3989–3999. 22 indexed citations
10.
Byer, Amanda S., Eric M. Shepard, John W. Peters, & Joan Broderick. (2014). Radical S-Adenosyl-l-methionine Chemistry in the Synthesis of Hydrogenase and Nitrogenase Metal Cofactors. Journal of Biological Chemistry. 290(7). 3987–3994. 22 indexed citations
11.
Silver, Sunshine C., Sunil Naik, Eric M. Shepard, et al.. (2014). Combined Mössbauer spectroscopic, multi-edge X-ray absorption spectroscopic, and density functional theoretical study of the radical SAM enzyme spore photoproduct lyase. JBIC Journal of Biological Inorganic Chemistry. 19(3). 465–483. 10 indexed citations
12.
Shepard, Eric M., et al.. (2012). Iron–sulfur cluster coordination in the [FeFe]‐hydrogenase H cluster biosynthetic factor HydF. FEBS Letters. 586(22). 3939–3943. 16 indexed citations
13.
Cumming, Graeme S., et al.. (2012). Host associations, biogeography, and phylogenetics of avian malaria in southern African waterfowl. Parasitology. 140(2). 193–201. 20 indexed citations
14.
Mulder, David W., Eric M. Shepard, Jonathan E. Meuser, et al.. (2011). Insights into [FeFe]-Hydrogenase Structure, Mechanism, and Maturation. Structure. 19(8). 1038–1052. 186 indexed citations
15.
Driesener, Rebecca C., Martin R. Challand, Shawn E. McGlynn, et al.. (2010). [FeFe]‐Hydrogenase Cyanide Ligands Derived From S ‐Adenosylmethionine‐Dependent Cleavage of Tyrosine. Angewandte Chemie International Edition. 49(9). 1687–1690. 127 indexed citations
16.
McGlynn, Shawn E., David W. Mulder, Eric M. Shepard, Joan Broderick, & John W. Peters. (2009). Hydrogenase cluster biosynthesis: organometallic chemistry nature's way. Dalton Transactions. 4274–4274. 60 indexed citations
17.
McGrath, Aaron P., Kimberly M. Hilmer, Charles A. Collyer, et al.. (2009). Structure and Inhibition of Human Diamine Oxidase. Biochemistry. 48(41). 9810–9822. 92 indexed citations
18.
Duff, Anthony P., Eric M. Shepard, David B. Langley, et al.. (2006). A C-terminal disulfide bond in the copper-containing amine oxidase from pea seedlings violates the twofold symmetry of the molecular dimer. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 62(12). 1168–1173. 5 indexed citations
19.
Duff, Anthony P., Daniel Trambaiolo, Aina E. Cohen, et al.. (2004). Using Xenon as a Probe for Dioxygen-binding Sites in Copper Amine Oxidases. Journal of Molecular Biology. 344(3). 599–607. 50 indexed citations
20.
Shepard, Eric M., Jennifer A. Smith, Bradley O. Elmore, et al.. (2002). Towards the development of selective amine oxidase inhibitors. European Journal of Biochemistry. 269(15). 3645–3658. 31 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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