Jonathan A. R. Worrall

2.7k total citations
79 papers, 2.1k citations indexed

About

Jonathan A. R. Worrall is a scholar working on Molecular Biology, Inorganic Chemistry and Cell Biology. According to data from OpenAlex, Jonathan A. R. Worrall has authored 79 papers receiving a total of 2.1k indexed citations (citations by other indexed papers that have themselves been cited), including 57 papers in Molecular Biology, 19 papers in Inorganic Chemistry and 15 papers in Cell Biology. Recurrent topics in Jonathan A. R. Worrall's work include Photosynthetic Processes and Mechanisms (28 papers), Metal-Catalyzed Oxygenation Mechanisms (18 papers) and Hemoglobin structure and function (15 papers). Jonathan A. R. Worrall is often cited by papers focused on Photosynthetic Processes and Mechanisms (28 papers), Metal-Catalyzed Oxygenation Mechanisms (18 papers) and Hemoglobin structure and function (15 papers). Jonathan A. R. Worrall collaborates with scholars based in United Kingdom, Netherlands and United States. Jonathan A. R. Worrall's co-authors include Marcellus Ubbink, Alexander N. Volkov, Michael T. Wilson, Michael A. Hough, Erik Vijgenboom, Amanda K. Chaplin, Dimitri A. Svistunenko, Gerard W. Canters, Ben F. Luisi and Peter Nicholls and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Nucleic Acids Research.

In The Last Decade

Jonathan A. R. Worrall

76 papers receiving 2.1k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Jonathan A. R. Worrall United Kingdom	27	1.5k	468	251	227	222	79	2.1k
Li-Shar Huang United States	24	2.6k 1.8×	354 0.8×	299 1.2×	373 1.6×	363 1.6×	49	3.3k
Federico I. Rosell Canada	25	1.4k 0.9×	323 0.7×	394 1.6×	217 1.0×	71 0.3×	44	2.1k
Jeffrey L. Urbauer United States	24	1.3k 0.9×	446 1.0×	242 1.0×	106 0.5×	75 0.3×	56	1.8k
Gordon V. Louie United States	30	3.2k 2.1×	700 1.5×	427 1.7×	118 0.5×	406 1.8×	44	4.0k
Dan E. Robertson United States	34	3.0k 2.0×	599 1.3×	295 1.2×	345 1.5×	641 2.9×	53	4.0k
Jon N. Rumbley United States	22	1.5k 1.0×	438 0.9×	293 1.2×	134 0.6×	62 0.3×	45	1.9k
Françoise Guerlesquin France	31	1.6k 1.1×	315 0.7×	263 1.0×	197 0.9×	93 0.4×	97	2.3k
R. Haser France	20	1.4k 0.9×	566 1.2×	331 1.3×	179 0.8×	323 1.5×	45	2.2k
Kengo Okada Japan	22	2.2k 1.5×	576 1.2×	215 0.9×	175 0.8×	82 0.4×	43	3.0k
Jacques Gallay France	29	1.6k 1.1×	263 0.6×	180 0.7×	79 0.3×	76 0.3×	103	2.3k

Countries citing papers authored by Jonathan A. R. Worrall

Since Specialization

Citations

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

Fields of papers citing papers by Jonathan A. R. Worrall

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jonathan A. R. Worrall. 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 Jonathan A. R. Worrall. The network helps show where Jonathan A. R. Worrall may publish in the future.

Co-authorship network of co-authors of Jonathan A. R. Worrall

This figure shows the co-authorship network connecting the top 25 collaborators of Jonathan A. R. Worrall. A scholar is included among the top collaborators of Jonathan A. R. Worrall 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 Jonathan A. R. Worrall. Jonathan A. R. Worrall 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

1.

Thompson, Amy J., Philipp Dijkstal, Martin V. Appleby, et al.. (2025). Damage before destruction? X-ray-induced changes in single-pulse serial femtosecond crystallography. IUCrJ. 12(3). 358–371. 2 indexed citations

2.

Sen, Kakali, Marcus J. Edwards, You Lü, et al.. (2025). Double crossed? Structural and computational studies of an unusually crosslinked haem in Methylococcus capsulatus cytochrome P460. Chemical Science. 16(35). 16266–16283.

3.

Wilson, Michael T., et al.. (2025). The cytochrome P450 decarboxylase from Staphylococcus aureus can produce a diene from a C18 monounsaturated fatty acid: A spectroscopic, structural and kinetic characterisation. Journal of Inorganic Biochemistry. 275. 113117–113117.

4.

Wilson, Michael T., et al.. (2023). New insights into controlling radical migration pathways in heme enzymes gained from the study of a dye-decolorising peroxidase. Chemical Science. 14(44). 12518–12534. 5 indexed citations

5.

Wilson, Michael T., Takehiko Tosha, Hiroshi Sugimoto, et al.. (2022). Serial Femtosecond Crystallography Reveals the Role of Water in the One- or Two-Electron Redox Chemistry of Compound I in the Catalytic Cycle of the B-Type Dye-Decolorizing Peroxidase DtpB. ACS Catalysis. 12(21). 13349–13359. 12 indexed citations

6.

Wilson, Michael T., et al.. (2021). Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of FeIV = O formation in bacterial dye-decolorizing peroxidases. JBIC Journal of Biological Inorganic Chemistry. 26(7). 743–761. 21 indexed citations

7.

Svistunenko, Dimitri A., Michael T. Wilson, Amanda K. Chaplin, et al.. (2020). Serial Femtosecond Zero Dose Crystallography Captures a Water‐Free Distal Heme Site in a Dye‐Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in Fe^IV=O Formation. Angewandte Chemie International Edition. 59(48). 21656–21662. 29 indexed citations

8.

Chaplin, Amanda K., Florian Dworkowski, Michael T. Wilson, et al.. (2020). A subtle structural change in the distal haem pocket has a remarkable effect on tuning hydrogen peroxide reactivity in dye decolourising peroxidases fromStreptomyces lividans. Dalton Transactions. 49(5). 1620–1636. 16 indexed citations

9.

Svistunenko, Dimitri A., Michael T. Wilson, Amanda K. Chaplin, et al.. (2020). Serial Femtosecond Zero Dose Crystallography Captures a Water‐Free Distal Heme Site in a Dye‐Decolorising Peroxidase to Reveal a Catalytic Role for an Arginine in Fe^IV=O Formation. Angewandte Chemie. 132(48). 21840–21846. 2 indexed citations

10.

Ebrahim, Ali, Danny Axford, Martin V. Appleby, et al.. (2019). High-throughput structures of protein–ligand complexes at room temperature using serial femtosecond crystallography. IUCrJ. 6(6). 1074–1085. 32 indexed citations

11.

Ebrahim, Ali, Martin V. Appleby, Amanda K. Chaplin, et al.. (2019). Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins. IUCrJ. 6(4). 543–551. 60 indexed citations

12.

Hough, Michael A., et al.. (2019). A Histidine Residue and a Tetranuclear Cuprous‐thiolate Cluster Dominate the Copper Loading Landscape of a Copper Storage Protein from Streptomyces lividans. Chemistry - A European Journal. 25(45). 10678–10688. 7 indexed citations

13.

Svistunenko, Dimitri A., et al.. (2018). Naturally Occurring Disease-Related Mutations in the 40–57 Ω-Loop of Human Cytochrome c Control Triggering of the Alkaline Isomerization. Biochemistry. 57(29). 4276–4288. 33 indexed citations

14.

Chaplin, Amanda K., Michael T. Wilson, & Jonathan A. R. Worrall. (2017). Kinetic characterisation of a dye decolourising peroxidase from Streptomyces lividans: new insight into the mechanism of anthraquinone dye decolourisation. Dalton Transactions. 46(29). 9420–9429. 25 indexed citations

15.

Chaplin, Amanda K., Caterina Bernini, Adalgisa Sinicropi, et al.. (2017). Tyrosine or Tryptophan? Modifying a Metalloradical Catalytic Site by Removal of the Cys–Tyr Cross‐Link in the Galactose 6‐Oxidase Homologue GlxA. Angewandte Chemie. 129(23). 6602–6606. 4 indexed citations

16.

Karsisiotis, Andreas Ioannis, et al.. (2017). Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids. Biomolecular NMR Assignments. 11(2). 165–168. 2 indexed citations

17.

Chaplin, Amanda K., Caterina Bernini, Adalgisa Sinicropi, et al.. (2017). Tyrosine or Tryptophan? Modifying a Metalloradical Catalytic Site by Removal of the Cys–Tyr Cross‐Link in the Galactose 6‐Oxidase Homologue GlxA. Angewandte Chemie International Edition. 56(23). 6502–6506. 14 indexed citations

18.

Vijgenboom, Erik, et al.. (2016). The DyP-type peroxidase DtpA is a Tat-substrate required for GlxA maturation and morphogenesis inStreptomyces. Open Biology. 6(1). 150149–150149. 52 indexed citations

19.

Chaplin, Amanda K., Michael A. Hough, Dimitri A. Svistunenko, et al.. (2015). GlxA is a new structural member of the radical copper oxidase family and is required for glycan deposition at hyphal tips and morphogenesis of Streptomyces lividans. Biochemical Journal. 469(3). 433–444. 52 indexed citations

20.

Volkov, Alexander N., et al.. (2006). Solution structure and dynamics of the complex between cytochrome c and cytochrome c peroxidase determined by paramagnetic NMR. Proceedings of the National Academy of Sciences. 103(50). 18945–18950. 214 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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