David T. Clarke

2.9k total citations
69 papers, 2.0k citations indexed

About

David T. Clarke is a scholar working on Molecular Biology, Biophysics and Materials Chemistry. According to data from OpenAlex, David T. Clarke has authored 69 papers receiving a total of 2.0k indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Molecular Biology, 21 papers in Biophysics and 19 papers in Materials Chemistry. Recurrent topics in David T. Clarke's work include Advanced Fluorescence Microscopy Techniques (19 papers), Protein Structure and Dynamics (16 papers) and Enzyme Structure and Function (14 papers). David T. Clarke is often cited by papers focused on Advanced Fluorescence Microscopy Techniques (19 papers), Protein Structure and Dynamics (16 papers) and Enzyme Structure and Function (14 papers). David T. Clarke collaborates with scholars based in United Kingdom, United States and Switzerland. David T. Clarke's co-authors include Gareth R. Jones, Marisa L. Martin-Fernandez, Daniel J. Rolfe, Laura C. Zanetti-Domingues, Christopher J. Tynan, Paul D. Griffiths, Carl Holt, David McNulty, Sharon Brownlow and Mark J. Tobin and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Nature Communications and PLoS ONE.

In The Last Decade

David T. Clarke

68 papers receiving 2.0k citations

Peers

David T. Clarke

RNMI

BIOPH

Gareth R. Jones United Kingdom

Giovanni B. Strambini Spain

Tiansheng Li United States

Cristian Ionescu‐Zanetti United States

Gregory B. Young United States

Shota Mochizuki Japan

Moeava Tehei Australia

Bogdan E. Chapman Australia

B. George Barisas United States

J. Kruuv Canada

Gareth R. Jones United Kingdom

David T. Clarke

1.1k ×1.0

304 ×1.1

121 ×0.5

RNMI

242 ×1.0

75 ×0.3

BIOPH

Citations per year, relative to David T. Clarke David T. Clarke (= 1×) peers Gareth R. Jones

Countries citing papers authored by David T. Clarke

Since Specialization

Citations

This map shows the geographic impact of David T. Clarke'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 T. Clarke with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites David T. Clarke more than expected).

Fields of papers citing papers by David T. Clarke

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David T. Clarke

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

Roberts, Selene K., et al.. (2025). Targeting mutant EGFR in non-small cell lung cancer in the context of cell adaptation and resistance. Drug Discovery Today. 30(7). 104407–104407. 1 indexed citations

Brouwers, Bas, Edson Mendes de Oliveira, Maria Martí-Solano, et al.. (2021). Human MC4R variants affect endocytosis, trafficking and dimerization revealing multiple cellular mechanisms involved in weight regulation. Cell Reports. 34(12). 108862–108862. 52 indexed citations

Bateman, Benji, Laura C. Zanetti-Domingues, Sarah R. Needham, et al.. (2019). Super-resolution Microscopy at Cryogenic Temperatures Using Solid Immersion Lenses. BIO-PROTOCOL. 9(22). e3426–e3426. 4 indexed citations

Tynan, Christopher J., Laura C. Zanetti-Domingues, Sarah R. Needham, et al.. (2015). A tale of the epidermal growth factor receptor: The quest for structural resolution on cells. Methods. 95. 86–93. 14 indexed citations

Zanetti-Domingues, Laura C., Michael Hirsch, Christopher J. Tynan, et al.. (2015). Determining the geometry of oligomers of the human epidermal growth factor family on cells with 7 nm resolution. Progress in Biophysics and Molecular Biology. 118(3). 139–152. 6 indexed citations

Needham, Sarah R., Michael Hirsch, Daniel J. Rolfe, et al.. (2013). Measuring EGFR Separations on Cells with ∼10 nm Resolution via Fluorophore Localization Imaging with Photobleaching. PLoS ONE. 8(5). e62331–e62331. 32 indexed citations

Tynan, Christopher J., et al.. (2012). Multicolour Single Molecule Imaging in Cells with Near Infra-Red Dyes. PLoS ONE. 7(4). e36265–e36265. 32 indexed citations

Zanetti-Domingues, Laura C., Marisa L. Martin-Fernandez, Sarah R. Needham, Daniel J. Rolfe, & David T. Clarke. (2012). A Systematic Investigation of Differential Effects of Cell Culture Substrates on the Extent of Artifacts in Single-Molecule Tracking. PLoS ONE. 7(9). e45655–e45655. 21 indexed citations

Jelinska, Clare, Manca Kenig, Eva Žerovnik, et al.. (2011). Modulation of Contact Order Effects in the Two-State Folding of Stefins A and B. Biophysical Journal. 100(9). 2268–2274. 8 indexed citations

10.

Rudd, Timothy R., Mark A. Skidmore, Scott E. Guimond, et al.. (2008). Site-specific interactions of copper(II) ions with heparin revealed with complementary (SRCD, NMR, FTIR and EPR) spectroscopic techniques. Carbohydrate Research. 343(12). 2184–2193. 31 indexed citations

11.

Miles, Andrew J., Robert W. Janes, Alan Brown, et al.. (2008). Light flux density threshold at which protein denaturation is induced by synchrotron radiation circular dichroism beamlines. Journal of Synchrotron Radiation. 15(4). 420–422. 86 indexed citations

12.

Rudd, Timothy R., Scott E. Guimond, Mark A. Skidmore, et al.. (2007). Influence of substitution pattern and cation binding on conformation and activity in heparin derivatives. Glycobiology. 17(9). 983–993. 54 indexed citations

13.

Webb, S, Selene K. Roberts, Sarah R. Needham, et al.. (2007). Single-Molecule Imaging and Fluorescence Lifetime Imaging Microscopy Show Different Structures for High- and Low-Affinity Epidermal Growth Factor Receptors in A431 Cells. Biophysical Journal. 94(3). 803–819. 67 indexed citations

14.

Gales, Luı́s, Luísa Cortes, Carla Almeida, et al.. (2005). Towards a Structural Understanding of the Fibrillization Pathway in Machado-Joseph's Disease: Trapping Early Oligomers of Non-expanded Ataxin-3. Journal of Molecular Biology. 353(3). 642–654. 60 indexed citations

15.

Clarke, David T. & Gareth Jones. (2004). CD12: a new high-flux beamline for ultraviolet and vacuum-ultraviolet circular dichroism on the SRS, Daresbury. Journal of Synchrotron Radiation. 11(2). 142–149. 46 indexed citations

16.

Stanley, Will A., Anna Sokolova, Alan Brown, et al.. (2004). Synergistic use of synchrotron radiation techniques for biological samples in solution: a case study on protein-ligand recognition by the peroxisomal import receptor Pex5p. Journal of Synchrotron Radiation. 11(6). 490–496. 15 indexed citations

17.

Jones, Gareth R. & David T. Clarke. (2003). Applications of extended ultra-violet circular dichroism spectroscopy in biology and medicine. Faraday Discussions. 126. 223–223. 29 indexed citations

18.

Martin-Fernandez, Marisa L., et al.. (2002). Preformed Oligomeric Epidermal Growth Factor Receptors Undergo an Ectodomain Structure Change during Signaling. Biophysical Journal. 82(5). 2415–2427. 91 indexed citations

19.

Cerasoli, Eleonora, et al.. (2002). The refolding of type II shikimate kinase fromErwinia chrysanthemiafter denaturation in urea. European Journal of Biochemistry. 269(8). 2124–2132. 3 indexed citations

20.

Richards, K. Sylvia, et al.. (1988). Comparison of synchrotron and laser sources in X-ray contact microscopy of metal-contaminated biological tissue. Nuclear Instruments and Methods in Physics Research Section A Accelerators Spectrometers Detectors and Associated Equipment. 272(3). 889–894. 1 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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