David Cowburn

12.8k total citations · 3 hit papers
180 papers, 10.4k citations indexed

About

David Cowburn is a scholar working on Molecular Biology, Spectroscopy and Radiology, Nuclear Medicine and Imaging. According to data from OpenAlex, David Cowburn has authored 180 papers receiving a total of 10.4k indexed citations (citations by other indexed papers that have themselves been cited), including 118 papers in Molecular Biology, 54 papers in Spectroscopy and 30 papers in Radiology, Nuclear Medicine and Imaging. Recurrent topics in David Cowburn's work include Protein Structure and Dynamics (37 papers), Advanced NMR Techniques and Applications (32 papers) and Enzyme Structure and Function (25 papers). David Cowburn is often cited by papers focused on Protein Structure and Dynamics (37 papers), Advanced NMR Techniques and Applications (32 papers) and Enzyme Structure and Function (25 papers). David Cowburn collaborates with scholars based in United States, United Kingdom and France. David Cowburn's co-authors include David Fushman, John Kuriyan, Tom W. Muir, Alexander Shekhtman, Sean M. Cahill, Brian T. Chait, Frederick R. Cross, Yoshiya Oda, Jie Zheng and Kaushik Dutta and has published in prestigious journals such as Nature, Cell and Proceedings of the National Academy of Sciences.

In The Last Decade

David Cowburn

178 papers receiving 10.1k citations

Hit Papers

align trajectories

What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

Accurate quantitation of protein expression and site-specific phosphorylation

1999 777 citations David Cowburn et al. Proceedings of the National Academy of Sciences profile →
Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions

1994 709 citations Ke Shuai, Curt M. Horvath et al. Cell profile →
Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides

1992 551 citations David Cowburn et al. profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
David Cowburn United States	53	7.7k	2.1k	1.3k	1.2k	1.2k	180	10.4k
Edward T. Olejniczak United States	54	7.8k 1.0×	1.7k 0.8×	608 0.5×	1.5k 1.2×	1.3k 1.1×	122	10.7k
Jack S. Cohen United States	52	6.8k 0.9×	1.4k 0.7×	1.8k 1.4×	682 0.5×	1.1k 0.9×	237	10.7k
Paul C. Driscoll United Kingdom	49	7.3k 0.9×	1.0k 0.5×	757 0.6×	790 0.6×	1.1k 0.9×	147	10.2k
Michael Sattler Germany	64	13.6k 1.8×	1.5k 0.7×	662 0.5×	1.2k 0.9×	1.7k 1.4×	316	16.8k
Gerhard Wider Switzerland	54	11.8k 1.5×	3.7k 1.8×	1.2k 0.9×	610 0.5×	2.9k 2.4×	127	14.5k
Guang Zhu Hong Kong	32	13.7k 1.8×	2.3k 1.1×	1.2k 1.0×	1.1k 0.9×	3.1k 2.6×	125	18.4k
Rolf Boelens Netherlands	64	13.2k 1.7×	2.3k 1.1×	734 0.6×	888 0.7×	2.6k 2.2×	318	17.1k
Nico Tjandra United States	54	11.1k 1.4×	3.9k 1.8×	613 0.5×	580 0.5×	3.0k 2.5×	172	14.1k
Mark Rance United States	46	8.0k 1.0×	3.6k 1.7×	1.0k 0.8×	463 0.4×	2.1k 1.7×	115	11.1k
Volker Dötsch Germany	67	11.8k 1.5×	1.4k 0.7×	1.1k 0.9×	3.1k 2.5×	1.1k 0.9×	266	17.4k

Countries citing papers authored by David Cowburn

Since Specialization

Citations

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

Fields of papers citing papers by David Cowburn

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David Cowburn

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

Raveh, Barak, Daniel Russel, Ryo Hayama, et al.. (2025). Integrative mapping reveals molecular features underlying the mechanism of nucleocytoplasmic transport. Proceedings of the National Academy of Sciences. 122(42). e2507559122–e2507559122.

Cowburn, David & Michael P. Rout. (2023). Improving the hole picture: towards a consensus on the mechanism of nuclear transport. Biochemical Society Transactions. 51(2). 871–886. 22 indexed citations

Sparks, Samuel, et al.. (2017). Effects of FGFR2 kinase activation loop dynamics on catalytic activity. PLoS Computational Biology. 13(2). e1005360–e1005360. 10 indexed citations

Xu, Rong, Dongsheng Liu, & David Cowburn. (2012). Abl kinase constructs expressed in bacteria: facilitation of structural and functional studies including segmental labeling by expressed protein ligation. Molecular BioSystems. 8(7). 1878–1885. 6 indexed citations

Bhattacharya, Shibani, Hongtao Zhang, David Cowburn, & Asim K. Debnath. (2011). Novel structures of self‐associating stapled peptides. Biopolymers. 97(5). 253–264. 18 indexed citations

Ferrage, Fabien, et al.. (2010). On the measurement of 15N–{1H} nuclear Overhauser effects. 2. Effects of the saturation scheme and water signal suppression. Journal of Magnetic Resonance. 207(2). 294–303. 36 indexed citations

Ferrage, Fabien, Andrea Piserchio, David Cowburn, & Ranajeet Ghose. (2008). On the measurement of 15N–{1H} nuclear Overhauser effects. Journal of Magnetic Resonance. 192(2). 302–313. 39 indexed citations

Liu, Dongsheng, Rong Xu, Kaushik Dutta, & David Cowburn. (2008). N‐terminal cysteinyl proteins can be prepared using thrombin cleavage. FEBS Letters. 582(7). 1163–1167. 27 indexed citations

Valentine, Elizabeth R., Fabien Ferrage, Francesca Massi, David Cowburn, & Arthur G. Palmer. (2007). Joint composite-rotation adiabatic-sweep isotope filtration. Journal of Biomolecular NMR. 38(1). 11–22. 4 indexed citations

10.

Camarero, Julio A., Alexander Shekhtman, Elizabeth A. Campbell, et al.. (2002). Autoregulation of a bacterial σ factor explored by using segmental isotopic labeling and NMR. Proceedings of the National Academy of Sciences. 99(13). 8536–8541. 92 indexed citations

11.

Shekhtman, Alexander & David Cowburn. (2002). A ubiquitin-interacting motif from Hrs binds to and occludes the ubiquitin surface necessary for polyubiquitination in monoubiquitinated proteins. Biochemical and Biophysical Research Communications. 296(5). 1222–1227. 52 indexed citations

12.

Shekhtman, Alexander, Ranajeet Ghose, Dongxia Wang, Philip A. Cole, & David Cowburn. (2001). Novel mechanism of regulation of the non-receptor protein tyrosine kinase csk: insights from NMR mapping studies and site-directed mutagenesis. Journal of Molecular Biology. 314(1). 129–138. 31 indexed citations

13.

NICHOLAS, PETER C., et al.. (2000). The Virtual NMR Spectrometer: A Computer Program for Efficient Simulation of NMR Experiments Involving Pulsed Field Gradients. Journal of Magnetic Resonance. 145(2). 262–275. 30 indexed citations

14.

Fushman, David, et al.. (1999). Impact of Cl and Na ions on simulated structure and dynamics of βARK1 PH domain. Proteins Structure Function and Bioinformatics. 35(2). 206–217.

15.

Fushman, David, et al.. (1999). Impact of Cl? and Na+ ions on simulated structure and dynamics of ?ARK1 PH domain. Proteins Structure Function and Bioinformatics. 35(2). 206–217. 23 indexed citations

16.

Shuai, Ke, et al.. (1994). Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions. Cell. 76(5). 821–828. 709 indexed citations breakdown →

17.

Koutcher, Jason A., Alan Alfieri, M. Devitt, et al.. (1992). Quantitative changes in tumor metabolism, partial pressure of oxygen, and radiobiological oxygenation status postradiation.. PubMed. 52(17). 4620–7. 58 indexed citations

18.

Koutcher, Jason A., et al.. (1990). Relationship of changes in pH and energy status to hypoxic cell fraction and hyperthermia sensitivity. International Journal of Radiation Oncology*Biology*Physics. 18(6). 1429–1435. 42 indexed citations

19.

Glushka, John, Francis Barany, & David Cowburn. (1989). Observation of arginyl-deoxyoligonucleotide interactions in TaqI endonuclease by detection of specific 1H NMR signals from 140kD [Nη1, Nη2, 15N Arg]TaqI/oligomer complexes. Biochemical and Biophysical Research Communications. 164(1). 88–93. 7 indexed citations

20.

Live, David, David Cowburn, & Esther Breslow. (1987). Binding of oxytocin and 8-arginine-vasopressin to neurophysin studied by nitrogen-15 NMR using magnetization transfer and indirect detection via protons. Biochemistry. 26(20). 6415–6422. 11 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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