Karl Fisher

3.9k total citations
84 papers, 2.9k citations indexed

About

Karl Fisher is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Inorganic Chemistry. According to data from OpenAlex, Karl Fisher has authored 84 papers receiving a total of 2.9k indexed citations (citations by other indexed papers that have themselves been cited), including 46 papers in Molecular Biology, 30 papers in Renewable Energy, Sustainability and the Environment and 22 papers in Inorganic Chemistry. Recurrent topics in Karl Fisher's work include Metalloenzymes and iron-sulfur proteins (29 papers), Metal-Catalyzed Oxygenation Mechanisms (19 papers) and Electrocatalysts for Energy Conversion (17 papers). Karl Fisher is often cited by papers focused on Metalloenzymes and iron-sulfur proteins (29 papers), Metal-Catalyzed Oxygenation Mechanisms (19 papers) and Electrocatalysts for Energy Conversion (17 papers). Karl Fisher collaborates with scholars based in United Kingdom, United States and Germany. Karl Fisher's co-authors include David Leys, William E. Newton, Stephen E. J. Rigby, K.A.P. Payne, David Lowe, Dennis R. Dean, John W. Peters, Sam Hay, M. J. Dilworth and Mark S. Dunstan and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Karl Fisher

81 papers receiving 2.8k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Karl Fisher United Kingdom	31	1.3k	931	506	429	353	84	2.9k
Grover L. Waldrop United States	25	1.3k 1.0×	1.6k 1.7×	418 0.8×	573 1.3×	96 0.3×	62	3.8k
Eric L. Hegg United States	32	1.6k 1.3×	861 0.9×	1.0k 2.0×	62 0.1×	209 0.6×	78	3.9k
Sean J. Elliott United States	31	1.5k 1.1×	986 1.1×	729 1.4×	102 0.2×	47 0.1×	90	3.2k
Jeffrey T. Bolin United States	26	1.6k 1.2×	332 0.4×	892 1.8×	90 0.2×	130 0.4×	45	3.1k
Gianfranco Gilardi Italy	40	2.3k 1.7×	514 0.6×	426 0.8×	49 0.1×	136 0.4×	194	4.8k
Squire J. Booker United States	50	3.5k 2.7×	2.9k 3.1×	1.6k 3.2×	334 0.8×	99 0.3×	110	5.8k
Jennifer L. DuBois United States	32	1.2k 0.9×	236 0.3×	968 1.9×	68 0.2×	236 0.7×	84	3.3k
Ulrich Ermler Germany	30	2.2k 1.7×	1.6k 1.8×	859 1.7×	116 0.3×	51 0.1×	85	4.2k
Shinnichiro Suzuki Japan	32	1.7k 1.3×	584 0.6×	810 1.6×	152 0.4×	55 0.2×	176	3.5k
Margarida Archer Portugal	24	1.1k 0.8×	623 0.7×	416 0.8×	96 0.2×	44 0.1×	66	2.1k

Countries citing papers authored by Karl Fisher

Since Specialization

Citations

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

Fields of papers citing papers by Karl Fisher

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Karl Fisher

This figure shows the co-authorship network connecting the top 25 collaborators of Karl Fisher. A scholar is included among the top collaborators of Karl Fisher 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 Karl Fisher. Karl Fisher 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

Gahloth, Deepankar, Karl Fisher, Stephen Marshall, & David Leys. (2024). The prFMNH2-binding chaperone LpdD assists UbiD decarboxylase activation. Journal of Biological Chemistry. 300(2). 105653–105653. 2 indexed citations

Ortmayer, Mary, Florence J. Hardy, Matthew G. Quesne, et al.. (2021). A Noncanonical Tryptophan Analogue Reveals an Active Site Hydrogen Bond Controlling Ferryl Reactivity in a Heme Peroxidase. SHILAP Revista de lepidopterología. 1(7). 913–918. 15 indexed citations

Gautom, Trishnamoni, Dharmendra S. Dheeman, Colin Levy, et al.. (2021). Structural basis of terephthalate recognition by solute binding protein TphC. Nature Communications. 12(1). 6244–6244. 22 indexed citations

Ortmayer, Mary, Karl Fisher, Jaswir Basran, et al.. (2020). Rewiring the “Push-Pull” Catalytic Machinery of a Heme Enzyme Using an Expanded Genetic Code. ACS Catalysis. 10(4). 2735–2746. 32 indexed citations

Marshall, Stephen, K.A.P. Payne, Karl Fisher, et al.. (2019). The UbiX flavin prenyltransferase reaction mechanism resembles class I terpene cyclase chemistry. Nature Communications. 10(1). 2357–2357. 28 indexed citations

Payer, Stefan E., Stephen Marshall, Xiang Sheng, et al.. (2017). Regioselective para‐Carboxylation of Catechols with a Prenylated Flavin Dependent Decarboxylase. Angewandte Chemie International Edition. 56(44). 13893–13897. 64 indexed citations

Payer, Stefan E., Stephen Marshall, Xiang Sheng, et al.. (2017). Regioselektive para‐Carboxylierung von Catecholen mit einer Prenylflavin‐abhängigen Decarboxylase. Angewandte Chemie. 129(44). 14081–14085. 6 indexed citations

Menon, Binuraj R. K., et al.. (2015). Glutamate 338 is an electrostatic facilitator of C–Co bond breakage in a dynamic/electrostatic model of catalysis by ornithine aminomutase. FEBS Journal. 282(7). 1242–1255.

Sjuts, Hanno, Mark S. Dunstan, Karl Fisher, & David Leys. (2015). Structures of the methyltransferase component ofDesulfitobacterium hafnienseDCB-2O-demethylase shed light on methyltetrahydrofolate formation. Acta Crystallographica Section D Biological Crystallography. 71(9). 1900–1908. 5 indexed citations

10.

Payne, K.A.P., Mark D. White, Karl Fisher, et al.. (2015). New cofactor supports α,β-unsaturated acid decarboxylation via 1,3-dipolar cycloaddition. Nature. 522(7557). 497–501. 170 indexed citations

11.

Menon, Binuraj R. K., Karl Fisher, Stephen E. J. Rigby, Nigel S. Scrutton, & David Leys. (2014). A Conformational Sampling Model for Radical Catalysis in Pyridoxal Phosphate- and Cobalamin-dependent Enzymes. Journal of Biological Chemistry. 289(49). 34161–34174. 2 indexed citations

12.

McLean, Kirsty J., Karl Fisher, Stephen E. J. Rigby, et al.. (2014). Structure and Biochemical Properties of the Alkene Producing Cytochrome P450 OleTJE (CYP152L1) from the Jeotgalicoccus sp. 8456 Bacterium. Journal of Biological Chemistry. 289(10). 6535–6550. 143 indexed citations

13.

Dunstan, Mark S., et al.. (2013). Research article: The transcriptional regulator CprK detects chlorination by combining direct and indirect readout mechanisms. Philosophical Transactions of the Royal Society B Biological Sciences. 368(1616). 1–6. 94 indexed citations

14.

Dunstan, Mark S., et al.. (2013). The transcriptional regulator CprK detects chlorination by combining direct and indirect readout mechanisms. Philosophical Transactions of the Royal Society B Biological Sciences. 368(1616). 20120323–20120323. 13 indexed citations

15.

Fryszkowska, Anna, Karl Fisher, John M. Gardiner, & Gill Stephens. (2009). A short, chemoenzymatic route to chiral β-aryl-γ-amino acids using reductases from anaerobic bacteria. Organic & Biomolecular Chemistry. 8(3). 533–535. 26 indexed citations

16.

Petersen, Jan, et al.. (2008). Structural basis for VO2+-inhibition of nitrogenase activity: (B) pH-sensitive inner-sphere rearrangements in the 1H-environment of the metal coordination site of the nitrogenase Fe–protein identified by ENDOR spectroscopy. JBIC Journal of Biological Inorganic Chemistry. 13(4). 637–650. 2 indexed citations

17.

Toogood, Helen S., Anna Fryszkowska, Karl Fisher, et al.. (2008). Structure‐Based Insight into the Asymmetric Bioreduction of the CC Double Bond of α,β‐Unsaturated Nitroalkenes by Pentaerythritol Tetranitrate Reductase. Advanced Synthesis & Catalysis. 350(17). 2789–2803. 77 indexed citations

18.

Fisher, Karl, David Lowe, & Jan Petersen. (2006). Vanadium(v) is reduced by the ‘as isolated’ nitrogenase Fe-protein at neutral pH. Chemical Communications. 2807–2809. 5 indexed citations

19.

Dilworth, M. J., Karl Fisher, Chul‐Hwan Kim, & William E. Newton. (1998). Effects on Substrate Reduction of Substitution of Histidine-195 by Glutamine in the α-Subunit of the MoFe Protein of Azotobacter vinelandii Nitrogenase. Biochemistry. 37(50). 17495–17505. 49 indexed citations

20.

Lanzilotta, William N., Karl Fisher, & Lance C. Seefeldt. (1997). Evidence for Electron Transfer-dependent Formation of a Nitrogenase Iron Protein-Molybdenum-Iron Protein Tight Complex. Journal of Biological Chemistry. 272(7). 4157–4165. 36 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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