J. L. Ross Anderson

4.6k total citations
68 papers, 2.6k citations indexed

About

J. L. Ross Anderson is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, J. L. Ross Anderson has authored 68 papers receiving a total of 2.6k indexed citations (citations by other indexed papers that have themselves been cited), including 43 papers in Molecular Biology, 14 papers in Cell Biology and 11 papers in Materials Chemistry. Recurrent topics in J. L. Ross Anderson's work include Photosynthetic Processes and Mechanisms (16 papers), Protein Structure and Dynamics (12 papers) and Hemoglobin structure and function (12 papers). J. L. Ross Anderson is often cited by papers focused on Photosynthetic Processes and Mechanisms (16 papers), Protein Structure and Dynamics (12 papers) and Hemoglobin structure and function (12 papers). J. L. Ross Anderson collaborates with scholars based in United Kingdom, United States and Australia. J. L. Ross Anderson's co-authors include Stephen Mann, P. Leslie Dutton, Christopher C. Moser, Craig T. Armstrong, Stephen K. Chapman, Adrian J. Mulholland, Lee A. Solomon, H. Adrian Bunzel, Ronald L. Koder and F. Javier Nieto and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

J. L. Ross Anderson

65 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. L. Ross Anderson United Kingdom	26	1.4k	437	330	225	222	68	2.6k
Young‐Ho Lee Japan	31	3.4k 2.4×	649 1.5×	61 0.2×	264 1.2×	283 1.3×	126	5.6k
Maurizio Paci Italy	38	1.7k 1.2×	303 0.7×	219 0.7×	158 0.7×	409 1.8×	181	3.7k
William Furey United States	38	2.0k 1.4×	581 1.3×	170 0.5×	46 0.2×	330 1.5×	86	6.2k
Vishal Trivedi India	32	664 0.5×	446 1.0×	385 1.2×	253 1.1×	206 0.9×	130	3.2k
Jesús Mosquera Venezuela	35	1.1k 0.8×	926 2.1×	330 1.0×	468 2.1×	1.0k 4.5×	120	3.9k
Alexander B. Taylor United States	35	2.4k 1.7×	453 1.0×	240 0.7×	58 0.3×	586 2.6×	87	4.6k
Yuka Kobayashi Japan	37	1.2k 0.9×	809 1.9×	271 0.8×	367 1.6×	889 4.0×	207	4.5k
Ryan A. Mehl United States	41	3.8k 2.7×	525 1.2×	128 0.4×	216 1.0×	1.7k 7.6×	113	5.3k
Christophe Dugave France	24	1.3k 0.9×	376 0.9×	376 1.1×	82 0.4×	847 3.8×	60	3.2k

Countries citing papers authored by J. L. Ross Anderson

Since Specialization

Citations

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

Fields of papers citing papers by J. L. Ross Anderson

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J. L. Ross Anderson. 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. L. Ross Anderson. The network helps show where J. L. Ross Anderson may publish in the future.

Co-authorship network of co-authors of J. L. Ross Anderson

This figure shows the co-authorship network connecting the top 25 collaborators of J. L. Ross Anderson. A scholar is included among the top collaborators of J. L. Ross Anderson 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. L. Ross Anderson. J. L. Ross Anderson 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

Horne, Benjamin D., Thomas W. Wilson, Joseph B. Muhlestein, et al.. (2024). Contemporary Predictors of Major Adverse Cardiovascular Events Following Percutaneous Coronary Intervention: A Nationally Representative US Sample. Journal of Clinical Medicine. 13(10). 2844–2844. 1 indexed citations

Williams, Christopher, Christopher J. Arthur, Matthew J. Guberman‐Pfeffer, et al.. (2024). Delineating redox cooperativity in water‐soluble and membrane multiheme cytochromes through protein design. Protein Science. 33(8). 4 indexed citations

Ford, Holly C., et al.. (2024). Polymer nanodiscs support the functional extraction of an artificial transmembrane cytochrome. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1867(1). 184392–184392.

Anderson, J. L. Ross, Donald Hilvert, Vickery L. Arcus, et al.. (2023). Comment on: “Computer Simulations Reveal an Entirely Entropic Activation Barrier for the Chemical Step in a Designer Enzyme”. ACS Catalysis. 13(15). 10527–10530. 6 indexed citations

Christofferson, Andrew J., J. L. Ross Anderson, A. Evans, et al.. (2023). Structure and Dynamics of Three Escherichia coli NfsB Nitro-Reductase Mutants Selected for Enhanced Activity with the Cancer Prodrug CB1954. International Journal of Molecular Sciences. 24(6). 5987–5987. 2 indexed citations

Shannon, Mark, et al.. (2023). Bienzymatic Generation of Interpenetrating Polymer Networked Engineered Living Materials with Shape Changing Properties. Advanced Materials Technologies. 8(18). 4 indexed citations

Danson, Michael J., Marc W. van der Kamp, Oliver B. Sutcliffe, et al.. (2023). Synthetic cannabinoid receptor agonists are monoamine oxidase‐A selective inhibitors. FEBS Journal. 290(12). 3243–3257. 9 indexed citations

Bunzel, H. Adrian, J. L. Ross Anderson, Donald Hilvert, et al.. (2021). Evolution of dynamical networks enhances catalysis in a designer enzyme. Nature Chemistry. 13(10). 1017–1022. 89 indexed citations

Bunzel, H. Adrian, J. L. Ross Anderson, & Adrian J. Mulholland. (2021). Designing better enzymes: Insights from directed evolution. Current Opinion in Structural Biology. 67. 212–218. 58 indexed citations

10.

Stenner, R.D., et al.. (2020). A de novo peroxidase is also a promiscuous yet stereoselective carbene transferase. Proceedings of the National Academy of Sciences. 117(3). 1419–1428. 59 indexed citations

11.

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

12.

Curnow, Paul, Virginie Dufour, Christopher J. Arthur, et al.. (2020). Small-residue packing motifs modulate the structure and function of a minimal de novo membrane protein. Scientific Reports. 10(1). 15203–15203. 6 indexed citations

13.

Armstrong, James P. K., Rameen Shakur, Sally C. Dickinson, et al.. (2015). Artificial membrane-binding proteins stimulate oxygenation of stem cells during engineering of large cartilage tissue. Nature Communications. 6(1). 7405–7405. 68 indexed citations

14.

Watkins, Daniel W., Craig T. Armstrong, Jonathan Jenkins, et al.. (2015). A suite of de novo c -type cytochromes for functional oxidoreductase engineering. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1857(5). 493–502. 15 indexed citations

15.

Armstrong, Craig T., J. L. Ross Anderson, & Richard M. Denton. (2014). Studies on the regulation of the human E1 subunit of the 2-oxoglutarate dehydrogenase complex, including the identification of a novel calcium-binding site. Biochemical Journal. 459(2). 369–381. 30 indexed citations

16.

Dutton, P. Leslie, Goutham Kodali, Joshua A. Mancini, et al.. (2014). Toward the biogenesis of manmade oxidoreductases working in cells. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1837. e9–e10. 1 indexed citations

17.

Anderson, J. L. Ross, Craig T. Armstrong, Goutham Kodali, et al.. (2013). Constructing a man-made c-type cytochrome maquette in vivo: electron transfer, oxygen transport and conversion to a photoactive light harvesting maquette.. Chemical Science. 5(2). 507–514. 70 indexed citations

18.

Anderson, J. L. Ross & Stephen K. Chapman. (2006). Molecular mechanisms of enzyme-catalysed halogenation. Molecular BioSystems. 2(8). 350–357. 36 indexed citations

19.

Anderson, J. L. Ross & Stephen K. Chapman. (2004). Ligand probes for heme proteins. Dalton Transactions. 13–13. 17 indexed citations

20.

Janecek, John, et al.. (1963). THE EFFECTS OF WITHDRAWAL OF TRIFLUOPERAZINE ON PATIENTS MAINTAINED ON THE COMBINATION OF TRANYLCYPROMINE AND TRIFLUOPERAZINE: A DOUBLE-BLIND STUDY.. PubMed. 5. 608–15. 9 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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