David J. Huggins

3.2k total citations
63 papers, 2.2k citations indexed

About

David J. Huggins is a scholar working on Molecular Biology, Computational Theory and Mathematics and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, David J. Huggins has authored 63 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 50 papers in Molecular Biology, 18 papers in Computational Theory and Mathematics and 11 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in David J. Huggins's work include Protein Structure and Dynamics (24 papers), Computational Drug Discovery Methods (18 papers) and Spectroscopy and Quantum Chemical Studies (10 papers). David J. Huggins is often cited by papers focused on Protein Structure and Dynamics (24 papers), Computational Drug Discovery Methods (18 papers) and Spectroscopy and Quantum Chemical Studies (10 papers). David J. Huggins collaborates with scholars based in United States, United Kingdom and Germany. David J. Huggins's co-authors include Bruce Tidor, Woody Sherman, David R. Spring, Guy H. Grant, Ashok R. Venkitaraman, M. C. Payne, Grahame J. McKenzie, Siniša Vukovič, Malcolm M. Campbell and Christian Dubos and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Angewandte Chemie International Edition.

In The Last Decade

David J. Huggins

61 papers receiving 2.2k citations

Peers

David J. Huggins
Jong Cheol Jeong United States
Joshua Buckner United States
David L. Pincus United States
Ramu Anandakrishnan United States
Chaya S. Rapp United States
Leo S. D. Caves United Kingdom
E. Prabhu Raman United States
K. Anton Feenstra Netherlands
Jong Cheol Jeong United States
David J. Huggins
Citations per year, relative to David J. Huggins David J. Huggins (= 1×) peers Jong Cheol Jeong

Countries citing papers authored by David J. Huggins

Since Specialization
Citations

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

Fields of papers citing papers by David J. Huggins

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of David J. Huggins

This figure shows the co-authorship network connecting the top 25 collaborators of David J. Huggins. A scholar is included among the top collaborators of David J. Huggins 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 J. Huggins. David J. Huggins 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.
Michino, Mayako, Michael W. Miller, Yoshiyuki Fukase, et al.. (2024). Lead Optimization of Small Molecule ENL YEATS Inhibitors to Enable In Vivo Studies: Discovery of TDI-11055. ACS Medicinal Chemistry Letters. 15(4). 524–532. 2 indexed citations
3.
Ginn, John D., Tomasz Kochańczyk, Xiuju Jiang, et al.. (2024). Indazole to 2‐Cyanoindole Scaffold Progression for Mycobacterial Lipoamide Dehydrogenase Inhibitors Achieves Extended Target Residence Time and Improved Antibacterial Activity. Angewandte Chemie International Edition. 63(44). e202407276–e202407276. 3 indexed citations
4.
Balbach, Melanie, Carla Ritagliati, Robert W. Myers, et al.. (2023). On-demand male contraception via acute inhibition of soluble adenylyl cyclase. Nature Communications. 14(1). 637–637. 45 indexed citations
5.
Chen, Wei, Steven V. Jerome, Mayako Michino, et al.. (2023). Enhancing Hit Discovery in Virtual Screening through Absolute Protein–Ligand Binding Free-Energy Calculations. Journal of Chemical Information and Modeling. 63(10). 3171–3185. 69 indexed citations
6.
Shelton, Patrick M. M., Paul Dominic B. Olinares, Michael Grasso, et al.. (2023). Using a Function-First “Scout Fragment”-Based Approach to Develop Allosteric Covalent Inhibitors of Conformationally Dynamic Helicase Mechanoenzymes. Journal of the American Chemical Society. 146(1). 62–67. 9 indexed citations
7.
Michino, Mayako, Alexandre Beautrait, Nicholas A. Boyles, et al.. (2023). Shape-Based Virtual Screening of a Billion-Compound Library Identifies Mycobacterial Lipoamide Dehydrogenase Inhibitors. SHILAP Revista de lepidopterología. 3(6). 507–515. 7 indexed citations
8.
Finkin-Groner, Efrat, Yoshiyuki Fukase, Qingfei Zheng, et al.. (2021). Deglycase-activity oriented screening to identify DJ-1 inhibitors. RSC Medicinal Chemistry. 12(7). 1232–1238. 17 indexed citations
9.
Ginn, John D., Xiuju Jiang, Mayako Michino, et al.. (2021). Whole Cell Active Inhibitors of Mycobacterial Lipoamide Dehydrogenase Afford Selectivity over the Human Enzyme through Tight Binding Interactions. ACS Infectious Diseases. 7(2). 435–444. 5 indexed citations
10.
Huggins, David J.. (2020). Structural analysis of experimental drugs binding to the SARS-CoV-2 target TMPRSS2. Journal of Molecular Graphics and Modelling. 100. 107710–107710. 29 indexed citations
11.
Read, Cai, Duuamene Nyimanu, Thomas Williams, et al.. (2019). International Union of Basic and Clinical Pharmacology. CVII. Structure and Pharmacology of the Apelin Receptor with a Recommendation that Elabela/Toddler Is a Second Endogenous Peptide Ligand. Pharmacological Reviews. 71(4). 467–502. 83 indexed citations
12.
Mullarky, Edouard, Jiayi Xu, David J. Huggins, et al.. (2019). Inhibition of 3-phosphoglycerate dehydrogenase (PHGDH) by indole amides abrogates de novo serine synthesis in cancer cells. Bioorganic & Medicinal Chemistry Letters. 29(17). 2503–2510. 41 indexed citations
13.
Cole, Daniel J., M. Janecek, Maxim Rossmann, et al.. (2017). Computationally-guided optimization of small-molecule inhibitors of the Aurora A kinase–TPX2 protein–protein interaction. Chemical Communications. 53(67). 9372–9375. 12 indexed citations
14.
Vukovič, Siniša, Paul E. Brennan, & David J. Huggins. (2016). Exploring the role of water in molecular recognition: predicting protein ligandability using a combinatorial search of surface hydration sites. Journal of Physics Condensed Matter. 28(34). 344007–344007. 31 indexed citations
15.
Huggins, David J.. (2016). Studying the role of cooperative hydration in stabilizing folded protein states. Journal of Structural Biology. 196(3). 394–406. 12 indexed citations
16.
Huggins, David J.. (2015). Quantifying the Entropy of Binding for Water Molecules in Protein Cavities by Computing Correlations. Biophysical Journal. 108(4). 928–936. 58 indexed citations
17.
Huggins, David J.. (2013). Comparing distance metrics for rotation using thek‐nearest neighbors algorithm for entropy estimation. Journal of Computational Chemistry. 35(5). 377–385. 25 indexed citations
18.
Huggins, David J. & Bruce Tidor. (2011). Systematic placement of structural water molecules for improved scoring of protein-ligand interactions. Protein Engineering Design and Selection. 24(10). 777–789. 34 indexed citations
19.
Huggins, David J., Grahame J. McKenzie, Daniel D. Robinson, et al.. (2010). Computational Analysis of Phosphopeptide Binding to the Polo-Box Domain of the Mitotic Kinase PLK1 Using Molecular Dynamics Simulation. PLoS Computational Biology. 6(8). e1000880–e1000880. 26 indexed citations
20.
Huggins, David J., Michael D. Altman, & Bruce Tidor. (2008). Evaluation of an inverse molecular design algorithm in a model binding site. Proteins Structure Function and Bioinformatics. 75(1). 168–186. 8 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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