Emily Flashman

4.8k total citations · 1 hit paper
68 papers, 3.5k citations indexed

About

Emily Flashman is a scholar working on Molecular Biology, Cancer Research and Plant Science. According to data from OpenAlex, Emily Flashman has authored 68 papers receiving a total of 3.5k indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Molecular Biology, 29 papers in Cancer Research and 20 papers in Plant Science. Recurrent topics in Emily Flashman's work include Cancer, Hypoxia, and Metabolism (29 papers), Plant responses to water stress (17 papers) and Mitochondrial Function and Pathology (12 papers). Emily Flashman is often cited by papers focused on Cancer, Hypoxia, and Metabolism (29 papers), Plant responses to water stress (17 papers) and Mitochondrial Function and Pathology (12 papers). Emily Flashman collaborates with scholars based in United Kingdom, United States and Italy. Emily Flashman's co-authors include Christopher J. Schofield, Charles Redwood, Hugh Watkins, Mark D. White, Kirsty S. Hewitson, Rasheduzzaman Chowdhury, Johanna C. Moolman‐Smook, M.A. McDonough, Jasmin Mecinović and Christoph Loenarz and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Emily Flashman

66 papers receiving 3.5k citations

Hit Papers

Conserved N-terminal cysteine dioxygenases transduce resp... 2019 2026 2021 2023 2019 50 100 150

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Emily Flashman United Kingdom 34 2.2k 1.4k 526 471 375 68 3.5k
Anne M. Gardner United States 27 3.1k 1.4× 383 0.3× 164 0.3× 115 0.2× 246 0.7× 39 4.4k
Jonathan M. Elkins United Kingdom 30 2.8k 1.3× 827 0.6× 87 0.2× 43 0.1× 329 0.9× 73 4.0k
Michael Grusch Austria 41 2.9k 1.3× 783 0.6× 260 0.5× 49 0.1× 165 0.4× 161 4.7k
Gary L. Schieven United States 42 2.5k 1.2× 429 0.3× 96 0.2× 77 0.2× 198 0.5× 94 5.5k
Motoshi Suzuki Japan 32 3.0k 1.4× 942 0.7× 269 0.5× 59 0.1× 312 0.8× 132 4.0k
Seung Jun Kim South Korea 31 1.9k 0.9× 348 0.3× 99 0.2× 79 0.2× 213 0.6× 128 2.9k
Domenico Bordo Italy 28 1.5k 0.7× 233 0.2× 221 0.4× 39 0.1× 162 0.4× 57 2.6k
Lawrence P. Aggerbeck France 28 1.8k 0.9× 468 0.3× 196 0.4× 449 1.0× 252 0.7× 58 3.5k
Peter A. Beal United States 38 4.8k 2.2× 387 0.3× 156 0.3× 283 0.6× 195 0.5× 117 5.4k

Countries citing papers authored by Emily Flashman

Since Specialization
Citations

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

Fields of papers citing papers by Emily Flashman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Emily Flashman

This figure shows the co-authorship network connecting the top 25 collaborators of Emily Flashman. A scholar is included among the top collaborators of Emily Flashman 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 Emily Flashman. Emily Flashman 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.
Khan, Mohammad Shahneawz, Antoine Wallabrègue, Edward Smith, et al.. (2025). Hypoxia‐activated fluorescent probes as markers of oxygen levels in plant cells and tissues. New Phytologist. 247(6). 2998–3009. 1 indexed citations
2.
Hintzen, Jordi C. J., Lawrence Shah, R. Sher, et al.. (2025). Evidence of an activity-enhancing conformational shift in Arabidopsis thaliana plant cysteine oxidase 4 induced by binding of substrate or substrate-mimics. Journal of Biological Chemistry. 301(11). 110770–110770.
3.
Keeley, Thomas P., Matti Myllykoski, Salma Akter, et al.. (2024). N-terminal cysteine acetylation and oxidation patterns may define protein stability. Nature Communications. 15(1). 5360–5360. 12 indexed citations
4.
Wang, Dapeng, et al.. (2024). Contrasted NCED gene expression across conifers with rising and peaking abscisic acid responses to drought. Plant Stress. 14. 100574–100574. 1 indexed citations
5.
Cervelli, Tiziana, Alvaro Galli, Pierdomenico Perata, et al.. (2023). Identification of novel plant cysteine oxidase inhibitors from a yeast chemical genetic screen. Journal of Biological Chemistry. 299(12). 105366–105366. 7 indexed citations
6.
Flashman, Emily, et al.. (2023). Kinetic Measurements to Investigate the Oxygen-Sensing Properties of Plant Cysteine Oxidases. Methods in molecular biology. 2648. 207–230. 2 indexed citations
7.
Akter, Salma, Mohammad Shahneawz Khan, Edward Smith, & Emily Flashman. (2021). Measuring ROS and redox markers in plant cells. RSC Chemical Biology. 2(5). 1384–1401. 33 indexed citations
8.
Hammarlund, Emma U., Emily Flashman, Sofie Mohlin, & Francesco Licausi. (2020). Oxygen-sensing mechanisms across eukaryotic kingdoms and their roles in complex multicellularity. Science. 370(6515). 85 indexed citations
9.
White, Mark D., Sergio Iacopino, Martin P. Edwards, et al.. (2020). Structures of Arabidopsis thaliana oxygen-sensing plant cysteine oxidases 4 and 5 enable targeted manipulation of their activity. Proceedings of the National Academy of Sciences. 117(37). 23140–23147. 38 indexed citations
10.
White, Mark D., Vinay Shukla, Alessandra Francini, et al.. (2019). Zinc Excess Induces a Hypoxia-Like Response by Inhibiting Cysteine Oxidases in Poplar Roots. PLANT PHYSIOLOGY. 180(3). 1614–1628. 17 indexed citations
11.
Masson, Norma, Thomas P. Keeley, Beatrice Giuntoli, et al.. (2019). Conserved N-terminal cysteine dioxygenases transduce responses to hypoxia in animals and plants. Science. 365(6448). 65–69. 157 indexed citations breakdown →
13.
Sánchez‐Fernández, Elena M., et al.. (2012). Kinetic investigations on the reaction of a 2-oxoglutarate dependent histone demethylase with oxygen. FEBS Journal. 279. 478–478. 1 indexed citations
14.
Chowdhury, Rasheduzzaman, M.A. McDonough, Jasmin Mecinović, et al.. (2009). Structural Basis for Binding of Hypoxia-Inducible Factor to the Oxygen-Sensing Prolyl Hydroxylases. Structure. 17(7). 981–989. 190 indexed citations
15.
McDonough, M.A., Vivian Li, Emily Flashman, et al.. (2006). Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2). Proceedings of the National Academy of Sciences. 103(26). 9814–9819. 295 indexed citations
16.
McNeill, Luke A., Emily Flashman, Matthew R. Buck, et al.. (2005). Hypoxia-inducible factor prolyl hydroxylase 2 has a high affinity for ferrous iron and 2-oxoglutarate. Molecular BioSystems. 1(4). 321–324. 100 indexed citations
17.
Flashman, Emily, M.A. McDonough, & Christopher J. Schofield. (2005). OS-9Another Piece in the HIF Complex Story. Molecular Cell. 17(4). 472–473. 2 indexed citations
18.
Flashman, Emily, M.A. McDonough, & Christopher J. Schofield. (2005). OS-9. Molecular Cell. 17(4). 472–473. 7 indexed citations
19.
Flashman, Emily, Charles Redwood, Theodor Lange, et al.. (2002). A novel interaction between the C5 and C8 domains of myosin binding protein-C and its modulation by HCM mutations. Biophysical Journal. 82. 1 indexed citations
20.
Ensminger, Stephan, Bernd M. Spriewald, Oliver Witzke, et al.. (2001). Critical Role for IL-4 in the Development of Transplant Arteriosclerosis in the Absence of CD40-CD154 Costimulation. The Journal of Immunology. 167(1). 532–541. 40 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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