Erik C. Ralph

555 total citations
16 papers, 459 citations indexed

About

Erik C. Ralph is a scholar working on Molecular Biology, Plant Science and Biochemistry. According to data from OpenAlex, Erik C. Ralph has authored 16 papers receiving a total of 459 indexed citations (citations by other indexed papers that have themselves been cited), including 8 papers in Molecular Biology, 5 papers in Plant Science and 4 papers in Biochemistry. Recurrent topics in Erik C. Ralph's work include Amino Acid Enzymes and Metabolism (4 papers), Pesticide Exposure and Toxicity (4 papers) and Metabolism and Genetic Disorders (3 papers). Erik C. Ralph is often cited by papers focused on Amino Acid Enzymes and Metabolism (4 papers), Pesticide Exposure and Toxicity (4 papers) and Metabolism and Genetic Disorders (3 papers). Erik C. Ralph collaborates with scholars based in United States, United Kingdom and Germany. Erik C. Ralph's co-authors include John R. Cashman, Jarosław Kalisiak, Paul F. Fitzpatrick, W. W. Cleland, Jun Zhang, Mark A. Anderson, Shaoxian Sun, Mark A. Anderson, Daniel A. Singleton and Jennifer S. Hirschi and has published in prestigious journals such as Biochemistry, Journal of Medicinal Chemistry and Journal of Pharmacology and Experimental Therapeutics.

In The Last Decade

Erik C. Ralph

16 papers receiving 455 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Erik C. Ralph United States	10	227	149	133	82	56	16	459
Mary MacDonald United States	11	208 0.9×	98 0.7×	82 0.6×	25 0.3×	135 2.4×	14	388
Małgorzata Juszczak Poland	11	177 0.8×	60 0.4×	24 0.2×	21 0.3×	126 2.3×	20	374
René M. de Jong Netherlands	15	706 3.1×	64 0.4×	61 0.5×	31 0.4×	79 1.4×	22	884
J.H.T.M. Ploemen Netherlands	15	547 2.4×	41 0.3×	28 0.2×	96 1.2×	69 1.2×	21	724
Zoltán Pataj Hungary	20	354 1.6×	81 0.5×	49 0.4×	58 0.7×	32 0.6×	33	888
Gwendolyn D. Fate United States	11	133 0.6×	121 0.8×	54 0.4×	13 0.2×	52 0.9×	21	468
Ben Bruyneel Netherlands	15	268 1.2×	18 0.1×	77 0.6×	19 0.2×	47 0.8×	21	550
Nobuo Miki Japan	10	178 0.8×	127 0.9×	25 0.2×	28 0.3×	31 0.6×	25	412
Ekaterina Darii France	14	414 1.8×	51 0.3×	42 0.3×	80 1.0×	68 1.2×	31	576
Robert H. McClanahan United States	9	128 0.6×	105 0.7×	29 0.2×	17 0.2×	28 0.5×	16	363

Countries citing papers authored by Erik C. Ralph

Since Specialization

Citations

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

Fields of papers citing papers by Erik C. Ralph

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Erik C. Ralph. 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 Erik C. Ralph. The network helps show where Erik C. Ralph may publish in the future.

Co-authorship network of co-authors of Erik C. Ralph

This figure shows the co-authorship network connecting the top 25 collaborators of Erik C. Ralph. A scholar is included among the top collaborators of Erik C. Ralph 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 Erik C. Ralph. Erik C. Ralph is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

16 of 16 papers shown

Jové, Veronica, Heather E. Wheeler, David R. Healy, et al.. (2024). Type I interferon regulation by USP18 is a key vulnerability in cancer. iScience. 27(4). 109593–109593. 6 indexed citations

Nestl, Bettina M., Robert J. Haselbeck, Michael A. Noble, et al.. (2017). Structural and functional insights into asymmetric enzymatic dehydration of alkenols. Nature Chemical Biology. 13(3). 275–281. 31 indexed citations

Hall, J. Perry, Erik C. Ralph, Suman Shanker, et al.. (2017). The catalytic mechanism of cyclic GMP‐AMP synthase (cGAS) and implications for innate immunity and inhibition. Protein Science. 26(12). 2367–2380. 55 indexed citations

Zhang, Jun, et al.. (2012). pH dependence on functional activity of human and mouse flavin-containing monooxygenase 5. Biochemical Pharmacology. 83(7). 962–968. 8 indexed citations

Zhang, Jun, Sigeng Chen, Erik C. Ralph, Mary A. Dwyer, & John R. Cashman. (2012). Identification of Human Butyrylcholinesterase Organophosphate-Resistant Variants through a Novel Mammalian Enzyme Functional Screen. Journal of Pharmacology and Experimental Therapeutics. 343(3). 673–682. 3 indexed citations

Ralph, Erik C., Longkuan Xiang, John R. Cashman, & Jun Zhang. (2011). His-tag truncated butyrylcholinesterase as a useful construct for in vitro characterization of wild-type and variant butyrylcholinesterases. Protein Expression and Purification. 80(1). 22–27. 7 indexed citations

Kalisiak, Jarosław, Erik C. Ralph, Jun Zhang, & John R. Cashman. (2011). Amidine−Oximes: Reactivators for Organophosphate Exposure. Journal of Medicinal Chemistry. 54(9). 3319–3330. 84 indexed citations

Kalisiak, Jarosław, Erik C. Ralph, & John R. Cashman. (2011). Nonquaternary Reactivators for Organophosphate-Inhibited Cholinesterases. Journal of Medicinal Chemistry. 55(1). 465–474. 74 indexed citations

Ralph, Erik C., et al.. (2010). Characterization of Human Flavin-Containing Monooxygenase (FMO) 3 and FMO5 Expressed as Maltose-Binding Protein Fusions. Drug Metabolism and Disposition. 38(12). 2239–2245. 11 indexed citations

10.

Ralph, Erik C., et al.. (2010). Characterization of human FMO3 and FMO5 expressed as maltose binding protein fusions. 1 indexed citations

11.

Ralph, Erik C. & Shaoxian Sun. (2009). Biochemical Characterization of MODY2 Glucokinase Variants V62M and G72R Reveals Reduced Enzymatic Activities Relative to Wild Type. Biochemistry. 48(11). 2514–2521. 7 indexed citations

12.

Ralph, Erik C., J. D. Thomson, Jonathan Almaden, & Shaoxian Sun. (2008). Glucose Modulation of Glucokinase Activation by Small Molecules. Biochemistry. 47(17). 5028–5036. 28 indexed citations

13.

Ralph, Erik C., Jennifer S. Hirschi, Mark A. Anderson, et al.. (2007). Insights into the Mechanism of Flavoprotein-Catalyzed Amine Oxidation from Nitrogen Isotope Effects on the Reaction of N-Methyltryptophan Oxidase. Biochemistry. 46(25). 7655–7664. 68 indexed citations

14.

Ralph, Erik C., Mark A. Anderson, W. W. Cleland, & Paul F. Fitzpatrick. (2006). Mechanistic Studies of the Flavoenzyme Tryptophan 2-Monooxygenase: Deuterium and ¹⁵N Kinetic Isotope Effects on Alanine Oxidation by an l-Amino Acid Oxidase. Biochemistry. 45(51). 15844–15852. 42 indexed citations

15.

Ralph, Erik C. & Paul F. Fitzpatrick. (2005). pH and Kinetic Isotope Effects on Sarcosine Oxidation by N-Methyltryptophan Oxidase. Biochemistry. 44(8). 3074–3081. 20 indexed citations

16.

Fitzpatrick, Paul F., et al.. (2003). Characterization of Metal Ligand Mutants of Tyrosine Hydroxylase: Insights into the Plasticity of a 2-Histidine-1-Carboxylate Triad. Biochemistry. 42(7). 2081–2088. 14 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.

Explore authors with similar magnitude of impact