D.A. Keedy

22.4k total citations · 3 hit papers
46 papers, 16.0k citations indexed

About

D.A. Keedy is a scholar working on Molecular Biology, Materials Chemistry and Polymers and Plastics. According to data from OpenAlex, D.A. Keedy has authored 46 papers receiving a total of 16.0k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 25 papers in Materials Chemistry and 7 papers in Polymers and Plastics. Recurrent topics in D.A. Keedy's work include Enzyme Structure and Function (23 papers), Protein Structure and Dynamics (21 papers) and Protein Tyrosine Phosphatases (10 papers). D.A. Keedy is often cited by papers focused on Enzyme Structure and Function (23 papers), Protein Structure and Dynamics (21 papers) and Protein Tyrosine Phosphatases (10 papers). D.A. Keedy collaborates with scholars based in United States, United Kingdom and Canada. D.A. Keedy's co-authors include Jane S. Richardson, David Richardson, Jeffrey J. Headd, W.B. Arendall, Vincent B. Chen, Gary J. Kapral, Robert M. Immormino, Laura W. Murray, Christopher J. Williams and Steven M. Lewis and has published in prestigious journals such as The Journal of Chemical Physics, Bioinformatics and Journal of Applied Physics.

In The Last Decade

D.A. Keedy

46 papers receiving 15.9k citations

Hit Papers

MolProbity: all-atom stru... 2009 2026 2014 2020 2009 2017 2010 2.5k 5.0k 7.5k 10.0k

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author Last Decade Papers Cites
D.A. Keedy 11.3k 3.2k 1.6k 1.3k 1.2k 46 16.0k
Eugene Krissinel 10.7k 0.9× 4.1k 1.3× 1.6k 1.0× 1.1k 0.9× 1.1k 1.0× 28 15.0k
Harold R. Powell 9.2k 0.8× 3.9k 1.2× 1.4k 0.9× 1.0k 0.8× 991 0.8× 73 14.2k
Elizabeth Potterton 8.9k 0.8× 3.3k 1.0× 1.3k 0.8× 970 0.8× 989 0.8× 8 12.5k
Stuart McNicholas 9.6k 0.8× 3.6k 1.1× 1.4k 0.9× 973 0.8× 1.1k 0.9× 19 13.4k
Gert Vriend 15.3k 1.4× 3.7k 1.2× 1.8k 1.1× 919 0.7× 1.0k 0.9× 192 21.0k
Tom Alber 10.3k 0.9× 3.0k 0.9× 1.2k 0.8× 1.4k 1.1× 1.2k 1.1× 131 13.1k
Laura W. Murray 8.4k 0.7× 2.2k 0.7× 1.3k 0.8× 971 0.8× 934 0.8× 10 11.7k
Robert M. Immormino 9.2k 0.8× 2.3k 0.7× 1.3k 0.8× 992 0.8× 1.1k 0.9× 34 12.7k
Georg E. Schulz 15.3k 1.3× 4.4k 1.4× 2.2k 1.4× 905 0.7× 1.1k 1.0× 242 20.9k
Morten Kjeldgaard 12.1k 1.1× 3.7k 1.1× 2.1k 1.3× 736 0.6× 1.5k 1.3× 32 15.5k

Countries citing papers authored by D.A. Keedy

Since Specialization
Citations

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

Fields of papers citing papers by D.A. Keedy

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by D.A. Keedy. 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 D.A. Keedy. The network helps show where D.A. Keedy may publish in the future.

Co-authorship network of co-authors of D.A. Keedy

This figure shows the co-authorship network connecting the top 25 collaborators of D.A. Keedy. A scholar is included among the top collaborators of D.A. Keedy 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 D.A. Keedy. D.A. Keedy 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.
Case, David A., Julian C.‐H. Chen, Lillian T. Chong, et al.. (2025). Structure-Based Experimental Datasets for Benchmarking Protein Simulation Force Fields [Article v1.0]. PubMed. 6(1). 3871–3871. 1 indexed citations
2.
Aleshin, Alexander E., Lester J. Lambert, Ranajit Das, et al.. (2025). Fragment Screening Identifies Novel Allosteric Binders and Binding Sites in the VHR (DUSP3) Phosphatase. ACS Omega. 10(5). 4912–4926. 4 indexed citations
3.
Ebrahim, Ali, et al.. (2025). Three STEPs Forward: A Trio of Unexpected Structures of PTPN5. Proteins Structure Function and Bioinformatics. 93(12). 2112–2127. 1 indexed citations
4.
Vlimmeren, Anne E. van, et al.. (2024). Allosteric regulation of the tyrosine phosphatase PTP1B by a protein–protein interaction. Protein Science. 34(1). e70016–e70016. 4 indexed citations
5.
Wankowicz, Stephanie A., et al.. (2024). Automated multiconformer model building for X-ray crystallography and cryo-EM. eLife. 12. 5 indexed citations
6.
Ebrahim, Ali, et al.. (2024). Pushed to extremes: distinct effects of high temperature versus pressure on the structure of STEP. Communications Biology. 7(1). 59–59. 10 indexed citations
7.
Boivin, Benoît, et al.. (2023). High-resolution double vision of the allosteric phosphatase PTP1B. Acta Crystallographica Section F Structural Biology Communications. 80(1). 1–12. 1 indexed citations
8.
Biel, J.T., Louise Dunnett, Neil G. Paterson, et al.. (2023). Room-temperature crystallography reveals altered binding of small-molecule fragments to PTP1B. eLife. 12. 37 indexed citations
9.
Wankowicz, Stephanie A., et al.. (2023). Automated multiconformer model building for X-ray crystallography and cryo-EM. eLife. 12. 13 indexed citations
10.
Ebrahim, Ali, et al.. (2022). Room-temperature serial synchrotron crystallography of the human phosphatase PTP1B. Acta Crystallographica Section F Structural Biology Communications. 79(1). 23–30. 8 indexed citations
11.
Ebrahim, Ali, Blake T. Riley, D. Kumaran, et al.. (2022). The temperature-dependent conformational ensemble of SARS-CoV-2 main protease (Mpro). IUCrJ. 9(5). 682–694. 35 indexed citations
12.
Riley, Blake T., Stephanie A. Wankowicz, Gydo C. P. van Zundert, et al.. (2020). qFit 3: Protein and ligand multiconformer modeling for X‐ray crystallographic and single‐particle cryo‐EM density maps. Protein Science. 30(1). 270–285. 35 indexed citations
13.
Keedy, D.A., Z.B. Hill, J.T. Biel, et al.. (2018). An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tethering. eLife. 7. 117 indexed citations
14.
Zundert, Gydo C. P. van, Brandi M. Hudson, D.A. Keedy, et al.. (2018). qFit-ligand Reveals Widespread Conformational Heterogeneity of Drug-Like Molecules in X-Ray Electron Density Maps. Journal of Medicinal Chemistry. 61(24). 11183–11198. 43 indexed citations
15.
Williams, Christopher J., Jeffrey J. Headd, Nigel W. Moriarty, et al.. (2017). MolProbity: More and better reference data for improved all‐atom structure validation. Protein Science. 27(1). 293–315. 2815 indexed citations breakdown →
16.
Russi, Silvia, Ana González, Lukas Kenner, et al.. (2016). Conformational variation of proteins at room temperature is not dominated by radiation damage. Journal of Synchrotron Radiation. 24(1). 73–82. 47 indexed citations
17.
Gaínza, Pablo, Kyle E. Roberts, Ivelin S. Georgiev, et al.. (2013). osprey. Methods in enzymology on CD-ROM/Methods in enzymology. 523. 87–107. 86 indexed citations
18.
Chen, Vincent B., W.B. Arendall, Jeffrey J. Headd, et al.. (2009). MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallographica Section D Biological Crystallography. 66(1). 12–21. 11415 indexed citations breakdown →
19.
Georgiev, Ivelin S., D.A. Keedy, Jane S. Richardson, David Richardson, & Bruce R. Donald. (2008). Algorithm for backrub motions in protein design. Bioinformatics. 24(13). i196–i204. 65 indexed citations
20.
Keedy, D.A., et al.. (1960). THE USE OF AN INSTRON TESTING MACHINE FOR THE DETERMINATION OF STRESS AND STRAIN-OPTICAL COEFFICIENTS. Defense Technical Information Center (DTIC). 4 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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