Janet E. Lovett

1.9k total citations
37 papers, 1.3k citations indexed

About

Janet E. Lovett is a scholar working on Biophysics, Materials Chemistry and Electronic, Optical and Magnetic Materials. According to data from OpenAlex, Janet E. Lovett has authored 37 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 28 papers in Biophysics, 18 papers in Materials Chemistry and 13 papers in Electronic, Optical and Magnetic Materials. Recurrent topics in Janet E. Lovett's work include Electron Spin Resonance Studies (28 papers), Lanthanide and Transition Metal Complexes (16 papers) and Magnetism in coordination complexes (13 papers). Janet E. Lovett is often cited by papers focused on Electron Spin Resonance Studies (28 papers), Lanthanide and Transition Metal Complexes (16 papers) and Magnetism in coordination complexes (13 papers). Janet E. Lovett collaborates with scholars based in United Kingdom, United States and Germany. Janet E. Lovett's co-authors include Edward A. Anderson, Christiane R. Timmel, Susan M. Lea, Jeffrey R. Harmer, Matthew R. Hicks, Marcella Orwick‐Rydmark, Anthony Watts, Andrea Graziadei, Pietro Roversi and Steven Johnson 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

Janet E. Lovett

36 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Janet E. Lovett United Kingdom 18 483 435 432 193 180 37 1.3k
Marina Gobbo Italy 21 249 0.5× 374 0.9× 562 1.3× 181 0.9× 92 0.5× 84 1.3k
Д. В. Пышный Russia 25 372 0.8× 424 1.0× 1.6k 3.7× 263 1.4× 135 0.8× 200 2.3k
Sarah D. Cady United States 21 193 0.4× 526 1.2× 1.1k 2.5× 60 0.3× 744 4.1× 26 2.1k
Jana Humpolíčková Czechia 25 225 0.5× 353 0.8× 1.2k 2.7× 63 0.3× 123 0.7× 62 2.0k
Jörg S. Hartig Germany 34 227 0.5× 301 0.7× 3.9k 9.0× 115 0.6× 119 0.7× 114 4.3k
Gail E. Fanucci United States 25 716 1.5× 630 1.4× 850 2.0× 306 1.6× 354 2.0× 85 2.2k
Alexander A. Nevzorov United States 21 276 0.6× 426 1.0× 932 2.2× 43 0.2× 1.0k 5.7× 55 1.7k
Pascal Didier France 22 168 0.3× 780 1.8× 1.1k 2.5× 69 0.4× 259 1.4× 79 2.2k
Riccardo Nifosı̀ Italy 24 563 1.2× 418 1.0× 940 2.2× 81 0.4× 156 0.9× 53 1.7k
Markus Weingarth Netherlands 29 222 0.5× 737 1.7× 802 1.9× 40 0.2× 1.1k 6.1× 79 2.2k

Countries citing papers authored by Janet E. Lovett

Since Specialization
Citations

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

Fields of papers citing papers by Janet E. Lovett

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Janet E. Lovett. 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 Janet E. Lovett. The network helps show where Janet E. Lovett may publish in the future.

Co-authorship network of co-authors of Janet E. Lovett

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

All Works

20 of 20 papers shown
1.
Hunter, Robert I., Xun‐Cheng Su, Stephen J. Butler, et al.. (2025). Robustness and Sensitivity of Gd(III)–Gd(III) Double Electron–Electron Resonance (DEER) Measurements: Comparative Study of High-Frequency EPR Spectrometer Designs and Spin Label Variants. Applied Magnetic Resonance. 56(5). 591–611. 1 indexed citations
2.
Cordes, David B., et al.. (2025). Sigmatropic rearrangement enables access to a highly stable spirocyclic nitroxide for protein spin labelling. Chemical Communications. 61(37). 6755–6758.
3.
Cordes, David B., et al.. (2024). Spirocyclic Pyrrolidinyl Nitroxides with Exo ‐Methylene Substituents. ChemPlusChem. 89(12). e202400387–e202400387. 2 indexed citations
4.
Wilson, C. Blake, Arnab Mukherjee, Matthieu Starck, et al.. (2023). Triggered Functional Dynamics of AsLOV2 by Time‐Resolved Electron Paramagnetic Resonance at High Magnetic Fields. Angewandte Chemie. 135(13). 1 indexed citations
5.
Wilson, C. Blake, Arnab Mukherjee, Matthieu Starck, et al.. (2023). Triggered Functional Dynamics of AsLOV2 by Time‐Resolved Electron Paramagnetic Resonance at High Magnetic Fields. Angewandte Chemie International Edition. 62(13). e202212832–e202212832. 8 indexed citations
6.
Hopmann, Kathrin H., et al.. (2023). Conformational tuning improves the stability of spirocyclic nitroxides with long paramagnetic relaxation times. Communications Chemistry. 6(1). 111–111. 6 indexed citations
7.
Sotorríos, Lía, Kenneth G. McKendrick, Stuart A. Macgregor, et al.. (2023). The Photochemical Mediated Ring Contraction of 4H-1,2,6-Thiadiazines To Afford 1,2,5-Thiadiazol-3(2H)-one 1-Oxides. Organic Letters. 25(37). 6907–6912. 2 indexed citations
8.
Anbu, Sellamuthu, Sofía Díaz‐Moreno, Hassane El Mkami, et al.. (2023). Design of the elusive proteinaceous oxygen donor copper site suggests a promising future for copper for MRI contrast agents. Proceedings of the National Academy of Sciences. 120(27). e2219036120–e2219036120. 5 indexed citations
9.
10.
Oganesyan, Vasily S., et al.. (2021). DEER and RIDME Measurements of the Nitroxide-Spin Labelled Copper-Bound Amine Oxidase Homodimer from Arthrobacter Globiformis. Applied Magnetic Resonance. 52(8). 995–1015. 12 indexed citations
11.
Mkami, Hassane El, Robert I. Hunter, P.A.S. Cruickshank, et al.. (2020). High-sensitivity Gd 3+ –Gd 3+ EPR distance measurements that eliminate artefacts seen at short distances. SHILAP Revista de lepidopterología. 1(2). 301–313. 9 indexed citations
12.
El‐Sagheer, Afaf H., Denis Ptchelkine, Frank Beierlein, et al.. (2020). 2′-Alkynyl spin-labelling is a minimally perturbing tool for DNA structural analysis. Nucleic Acids Research. 48(6). 2830–2840. 9 indexed citations
13.
Jamshad, Mohammed, Mark Jeeves, Ashley Robinson, et al.. (2020). Iron is a ligand of SecA-like metal-binding domains in vivo. Journal of Biological Chemistry. 295(21). 7516–7528. 7 indexed citations
14.
Corey, Robin A., Zainab Ahdash, Euan Pyle, et al.. (2019). ATP-induced asymmetric pre-protein folding as a driver of protein translocation through the Sec machinery. eLife. 8. 25 indexed citations
15.
Roux, Amandine, Matthieu Starck, Jackie A. Mosely, et al.. (2019). A Gadolinium Spin Label with Both a Narrow Central Transition and Short Tether for Use in Double Electron Electron Resonance Distance Measurements. Inorganic Chemistry. 58(5). 3015–3025. 43 indexed citations
16.
Gil‐Ramírez, Guzmán, Hassane El Mkami, Kyriakos Porfyrakis, et al.. (2018). Distance Measurement of a Noncovalently Bound Y@C82 Pair with Double Electron Electron Resonance Spectroscopy. Journal of the American Chemical Society. 140(24). 7420–7424. 10 indexed citations
17.
Lovett, Janet E., et al.. (2017). Advances in the synthesis of nitroxide radicals for use in biomolecule spin labelling. Chemical Society Reviews. 47(3). 668–680. 101 indexed citations
18.
Drummond, Nicola J., Janet E. Lovett, Mark R. Miller, et al.. (2017). A synthetic cell permeable antioxidant protects neurons against acute oxidative stress. Scientific Reports. 7(1). 11857–11857. 22 indexed citations
19.
Mora, E. De la, Janet E. Lovett, Christopher F. Blanford, et al.. (2012). Structural changes caused by radiation-induced reduction and radiolysis: the effect of X-ray absorbed dose in a fungal multicopper oxidase. Acta Crystallographica Section D Biological Crystallography. 68(5). 564–577. 47 indexed citations
20.
Lillington, James, Janet E. Lovett, Steven Johnson, et al.. (2010). Shigella flexneri Spa15 Crystal Structure Verified in Solution by Double Electron Electron Resonance. Journal of Molecular Biology. 405(2). 427–435. 19 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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