J.A. Fee

3.3k total citations
46 papers, 2.7k citations indexed

About

J.A. Fee is a scholar working on Molecular Biology, Inorganic Chemistry and Health, Toxicology and Mutagenesis. According to data from OpenAlex, J.A. Fee has authored 46 papers receiving a total of 2.7k indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Molecular Biology, 16 papers in Inorganic Chemistry and 7 papers in Health, Toxicology and Mutagenesis. Recurrent topics in J.A. Fee's work include Photosynthetic Processes and Mechanisms (19 papers), Metal-Catalyzed Oxygenation Mechanisms (15 papers) and Electrochemical Analysis and Applications (7 papers). J.A. Fee is often cited by papers focused on Photosynthetic Processes and Mechanisms (19 papers), Metal-Catalyzed Oxygenation Mechanisms (15 papers) and Electrochemical Analysis and Applications (7 papers). J.A. Fee collaborates with scholars based in United States, United Kingdom and Sweden. J.A. Fee's co-authors include Christopher Bull, Tatsuro Yoshida, Eckard Münck, William Dunham, Katherine Bradley, Eric C. Niederhoffer, T. Kent Kirk, Ming Tien, Karen L. Findling and Michael W. Mather and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Applied and Environmental Microbiology.

In The Last Decade

J.A. Fee

46 papers receiving 2.5k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
J.A. Fee United States	32	1.4k	782	454	338	285	46	2.7k
Christopher Dennison United Kingdom	35	1.8k 1.2×	775 1.0×	513 1.1×	312 0.9×	574 2.0×	130	3.4k
W. John Ingledew United Kingdom	34	2.5k 1.7×	373 0.5×	438 1.0×	191 0.6×	608 2.1×	103	4.1k
Francis E. Jenney United States	34	1.9k 1.4×	780 1.0×	808 1.8×	261 0.8×	688 2.4×	70	3.4k
Shinnichiro Suzuki Japan	32	1.7k 1.1×	810 1.0×	584 1.3×	232 0.7×	579 2.0×	176	3.5k
Elinor T. Adman United States	41	3.1k 2.2×	1.3k 1.7×	1.3k 2.9×	359 1.1×	1.1k 3.8×	78	5.3k
Edward A. Berry United States	34	4.2k 2.9×	633 0.8×	606 1.3×	438 1.3×	575 2.0×	65	5.5k
Vilmos Fülöp United Kingdom	35	2.5k 1.7×	607 0.8×	221 0.5×	411 1.2×	644 2.3×	120	4.7k
Carlos Gómez‐Moreno Spain	36	2.8k 1.9×	1.1k 1.4×	751 1.7×	427 1.3×	601 2.1×	129	3.6k
V.V. Barynin Russia	28	1.3k 0.9×	834 1.1×	161 0.4×	294 0.9×	623 2.2×	42	2.6k
Yukiteru Katsube Japan	28	1.3k 0.9×	418 0.5×	398 0.9×	263 0.8×	440 1.5×	114	2.3k

Countries citing papers authored by J.A. Fee

Since Specialization

Citations

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

Fields of papers citing papers by J.A. Fee

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J.A. Fee. 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 J.A. Fee. The network helps show where J.A. Fee may publish in the future.

Co-authorship network of co-authors of J.A. Fee

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

All Works

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20 of 20 papers shown

Karpefors, Martin, J.A. Fee, Roland Aasa, et al.. (1996). Electron paramagnetic resonance studies of the soluble CuA protein from the cytochrome ba3 of Thermus thermophilus. Biophysical Journal. 71(5). 2823–2829. 27 indexed citations

Brown, Olen R., Elzbieta M. Smyk-Randall, Bozena Draczynska‐Lusiak, & J.A. Fee. (1995). Dihydroxy-acid Dehydratase, a (4Fe-4S) Cluster-Containing Enzyme in Escherichia coli: Effects of Intracellular Superoxide Dismutase on Its Inactivation by Oxidant Stress. Archives of Biochemistry and Biophysics. 319(1). 10–22. 33 indexed citations

Fee, J.A., W.E. Antholine, Chaoliang Fan, et al.. (1992). High field endor studies of the CuA and CuB sites in cytochrome oxidase. Journal of Inorganic Biochemistry. 47(3-4). 12–12. 1 indexed citations

Mather, Michael W. & J.A. Fee. (1992). Development of plasmid cloning vectors for Thermus thermophilus HB8: expression of a heterologous, plasmid-borne kanamycin nucleotidyltransferase gene. Applied and Environmental Microbiology. 58(1). 421–425. 43 indexed citations

Fee, J.A.. (1991). Regulation of sod genes in Escherichia coli: relevance to superoxide dismutase function. Molecular Microbiology. 5(11). 2599–2610. 89 indexed citations

Niederhoffer, Eric C., et al.. (1990). Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric uptake regulation (fur) locus. Journal of Bacteriology. 172(4). 1930–1938. 232 indexed citations

Greenwood, C, Andrew J. Thomson, Jim Peterson, et al.. (1988). Some Spectroscopic Views of the Cu_A, Site in Cytochrome c Oxidase Preparationsa. Annals of the New York Academy of Sciences. 550(1). 47–52. 18 indexed citations

Fee, J.A., et al.. (1988). Isolation and Partial Sequence of the A‐Protein Gene of Thermus thermophilus Cytochrome c₁aa₃a. Annals of the New York Academy of Sciences. 550(1). 33–38. 12 indexed citations

Münck, Eckard, et al.. (1987). Evidence for structural heterogeneities and a study of exchange coupling. Mössbauer studies of cytochrome c1aa3 from Thermus thermophilus.. Journal of Biological Chemistry. 262(34). 16328–16332. 11 indexed citations

10.

Kuila, Debasish & J.A. Fee. (1986). Evidence for a redox-linked ionizable group associated with the [2Fe-2S] cluster of Thermus Rieske protein.. Journal of Biological Chemistry. 261(6). 2768–2771. 68 indexed citations

11.

Yoshida, Tatsuro, Robert M. Lorence, Miles G. Choc, et al.. (1984). Respiratory proteins from the extremely thermophilic aerobic bacterium, Thermus thermophilus. Purification procedures for cytochromes c552, c555,549, and c1aa3 and chemical evidence for a single subunit cytochrome aa3.. Journal of Biological Chemistry. 259(1). 112–123. 51 indexed citations

12.

Lieberman, Robert A., Richard H. Sands, & J.A. Fee. (1982). A study of the electron paramagnetic resonance properties of single monoclinic crystals of bovine superoxide dismutase.. Journal of Biological Chemistry. 257(1). 336–344. 31 indexed citations

13.

Kent, Thomas A., Eckard Münck, William Dunham, et al.. (1982). Mössbauer study of a bacterial cytochrome oxidase: cytochrome c1aa3 from Thermus thermophilus.. Journal of Biological Chemistry. 257(21). 12489–12492. 40 indexed citations

14.

Stallings, William C., et al.. (1981). Characterization of crystals of tetrameric manganese superoxide dismutase from Thermus thermophilus HB8.. Journal of Biological Chemistry. 256(11). 5857–5859. 8 indexed citations

15.

Fee, J.A., et al.. (1980). Oxygen stasis of bacterial growth: analogy between the stasis of E. coli by hyperbaric oxygen and by aerobic paraquat.. 1(4). 304–311. 19 indexed citations

16.

Dunham, William, et al.. (1980). Application of fast Fourier transforms to EPR spectra of free radicals in solution. Journal of Magnetic Resonance (1969). 40(2). 351–359. 25 indexed citations

17.

Fee, J.A., Miles G. Choc, Karen L. Findling, Robert M. Lorence, & Takamasa Yoshida. (1980). Properties of a copper-containing cytochrome c1aa3 complex: a terminal oxidase of the extreme thermophile Thermus thermophilus HB8.. Proceedings of the National Academy of Sciences. 77(1). 147–151. 79 indexed citations

18.

McClune, Gregory J. & J.A. Fee. (1978). A simple system for mixing miscible organic solvents with water in 10--20 ms for the study of superoxide chemistry by stopped-flow methods. Biophysical Journal. 24(1). 65–69. 15 indexed citations

19.

Fee, J.A., et al.. (1976). Physical and chemical studies on bacterial superoxide dismutases. Purification and some anion binding properties of the iron-containing protein of Escherichia coli B.. Journal of Biological Chemistry. 251(18). 5472–5477. 91 indexed citations

20.

Fritz, Jonathan A., R. E. Anderson, J.A. Fee, et al.. (1971). The iron electron-nuclear double resonance (ENDOR) of two-iron ferredoxins from spinach, parsley, pig adrenal cortex and Pseudomonas putida. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 253(1). 110–133. 82 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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