Robert Abel

23.0k total citations · 8 hit papers
73 papers, 16.1k citations indexed

About

Robert Abel is a scholar working on Molecular Biology, Computational Theory and Mathematics and Materials Chemistry. According to data from OpenAlex, Robert Abel has authored 73 papers receiving a total of 16.1k indexed citations (citations by other indexed papers that have themselves been cited), including 63 papers in Molecular Biology, 42 papers in Computational Theory and Mathematics and 22 papers in Materials Chemistry. Recurrent topics in Robert Abel's work include Protein Structure and Dynamics (42 papers), Computational Drug Discovery Methods (42 papers) and Enzyme Structure and Function (11 papers). Robert Abel is often cited by papers focused on Protein Structure and Dynamics (42 papers), Computational Drug Discovery Methods (42 papers) and Enzyme Structure and Function (11 papers). Robert Abel collaborates with scholars based in United States, Germany and Belgium. Robert Abel's co-authors include Viktor Horn̆ák, Carlos Simmerling, Asim Okur, Adrián E. Roitberg, Richard A. Friesner, Lingle Wang, Edward Harder, Markus K. Dahlgren, B. J. Berne and Chuanjie Wu and has published in prestigious journals such as Cell, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Robert Abel

73 papers receiving 15.9k citations

Hit Papers

5 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.

Comparison of multiple Amber force fields and development of improved protein backbone parameters

2006 5.9k citations Robert Abel et al. Proteins Structure Function and Bioinformatics profile →
OPLS3: A Force Field Providing Broad Coverage of Drug-like Small Molecules and Proteins

2015 2.4k citations Edward Harder, Wolfgang Damm et al. Journal of Chemical Theory and Computation profile →
OPLS4: Improving Force Field Accuracy on Challenging Regimes of Chemical Space

2021 1.1k citations Chao Lü, Chuanjie Wu et al. Journal of Chemical Theory and Computation profile →
The VSGB 2.0 model: A next generation energy model for high resolution protein structure modeling

2011 875 citations Robert Abel, Richard A. Friesner et al. Proteins Structure Function and Bioinformatics profile →
OPLS3e: Extending Force Field Coverage for Drug-Like Small Molecules

2019 857 citations Katarina Roos, Chuanjie Wu et al. Journal of Chemical Theory and Computation profile →
Motifs for molecular recognition exploiting hydrophobic enclosure in protein–ligand binding

2007 541 citations Tom Young, Robert Abel et al. Proceedings of the National Academy of Sciences profile →
Role of the Active-Site Solvent in the Thermodynamics of Factor Xa Ligand Binding

2008 526 citations Robert Abel, Tom Young et al. profile →
Efficient Exploration of Chemical Space with Docking and Deep Learning

2021 228 citations Karl Leswing, Robert Abel et al. Journal of Chemical Theory and Computation profile →

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Robert Abel United States	43	11.3k	4.2k	2.9k	2.3k	1.3k	73	16.1k
Holger Gohlke Germany	49	16.4k 1.5×	4.9k 1.2×	3.4k 1.2×	2.5k 1.1×	1.0k 0.8×	283	23.1k
Matthew P. Jacobson United States	63	11.4k 1.0×	2.6k 0.6×	2.3k 0.8×	2.2k 0.9×	959 0.7×	200	17.2k
Alexey V. Onufriev United States	37	13.7k 1.2×	2.5k 0.6×	3.4k 1.2×	1.7k 0.7×	2.4k 1.8×	100	19.0k
Ray Luo United States	43	12.6k 1.1×	2.3k 0.5×	3.3k 1.1×	1.4k 0.6×	2.1k 1.6×	180	17.5k
Szilárd Páll Sweden	6	13.3k 1.2×	2.3k 0.5×	4.0k 1.4×	2.8k 1.2×	2.4k 1.9×	15	24.9k
Geoffrey Hutchison United States	32	6.9k 0.6×	4.7k 1.1×	4.3k 1.5×	4.2k 1.8×	1.2k 1.0×	75	20.4k
Roland Schulz United States	13	13.0k 1.1×	2.3k 0.5×	3.8k 1.3×	2.7k 1.1×	2.3k 1.8×	23	24.7k
M Abraham Australia	6	9.5k 0.8×	1.7k 0.4×	2.8k 1.0×	2.1k 0.9×	1.6k 1.3×	6	18.2k
Amedeo Caflisch Switzerland	71	11.0k 1.0×	2.6k 0.6×	2.6k 0.9×	1.1k 0.5×	1.1k 0.8×	288	14.8k
Ulf Ryde Sweden	69	9.2k 0.8×	2.6k 0.6×	4.5k 1.6×	2.4k 1.0×	2.9k 2.3×	315	18.6k

Countries citing papers authored by Robert Abel

Since Specialization

Citations

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

Fields of papers citing papers by Robert Abel

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert Abel

This figure shows the co-authorship network connecting the top 25 collaborators of Robert Abel. A scholar is included among the top collaborators of Robert Abel 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 Robert Abel. Robert Abel is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

Sort: Min cites: Since: Top N: Style:

20 of 20 papers shown

Paull, Evan, Phani Ghanakota, Jackson Chief Elk, et al.. (2025). Predicting Resistance to Small Molecule Kinase Inhibitors. Journal of Chemical Information and Modeling. 65(5). 2543–2557. 1 indexed citations

Knight, Jennifer L., Anthony J. Clark, Jiashi Wang, et al.. (2025). Harnessing free energy calculations for kinome-wide selectivity in drug discovery campaigns with a Wee1 case study. Nature Communications. 16(1). 7962–7962. 1 indexed citations

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

Ross, Gregory A., Chao Lü, Guido Scarabelli, et al.. (2023). The maximal and current accuracy of rigorous protein-ligand binding free energy calculations. Communications Chemistry. 6(1). 222–222. 64 indexed citations

Jacobson, Leif D., James Stevenson, Farhad Ramezanghorbani, et al.. (2022). Transferable Neural Network Potential Energy Surfaces for Closed-Shell Organic Molecules: Extension to Ions. Journal of Chemical Theory and Computation. 18(4). 2354–2366. 42 indexed citations

Ross, Gregory A., Yuqing Deng, Chao Lü, et al.. (2020). Enhancing Water Sampling in Free Energy Calculations with Grand Canonical Monte Carlo. Journal of Chemical Theory and Computation. 16(10). 6061–6076. 67 indexed citations

Ghoreishi, Delaram, Wolfgang Damm, Edward Harder, et al.. (2020). Advancing Free-Energy Calculations of Metalloenzymes in Drug Discovery via Implementation of LFMM Potentials. Journal of Chemical Theory and Computation. 16(11). 6926–6937. 8 indexed citations

Albanese, Steven K., et al.. (2020). Is Structure-Based Drug Design Ready for Selectivity Optimization?. Journal of Chemical Information and Modeling. 60(12). 6211–6227. 28 indexed citations

Roos, Katarina, Chuanjie Wu, Wolfgang Damm, et al.. (2019). OPLS3e: Extending Force Field Coverage for Drug-Like Small Molecules. Journal of Chemical Theory and Computation. 15(3). 1863–1874. 857 indexed citations breakdown →

10.

Yu, Haoyu S., Cen Gao, Dmitry Lupyan, et al.. (2019). Toward Atomistic Modeling of Irreversible Covalent Inhibitor Binding Kinetics. Journal of Chemical Information and Modeling. 59(9). 3955–3967. 29 indexed citations

11.

Clark, Anthony, Christopher Negron, Kevin Hauser, et al.. (2019). Relative Binding Affinity Prediction of Charge-Changing Sequence Mutations with FEP in Protein–Protein Interfaces. Journal of Molecular Biology. 431(7). 1481–1493. 68 indexed citations

12.

Hauser, Kevin, Christopher Negron, Steven K. Albanese, et al.. (2018). Predicting resistance of clinical Abl mutations to targeted kinase inhibitors using alchemical free-energy calculations. Communications Biology. 1(1). 70–70. 64 indexed citations

13.

Abel, Robert, Eric S. Manas, Richard A. Friesner, Ramy Farid, & Lingle Wang. (2018). Modeling the value of predictive affinity scoring in preclinical drug discovery. Current Opinion in Structural Biology. 52. 103–110. 14 indexed citations

14.

Abel, Robert, Lingle Wang, David L. Mobley, & Richard A. Friesner. (2017). A Critical Review of Validation, Blind Testing, and Real- World Use of Alchemical Protein-Ligand Binding Free Energy Calculations. Current Topics in Medicinal Chemistry. 17(23). 2577–2585. 72 indexed citations

15.

Kuhn, Bernd, Michal Tichý, Lingle Wang, et al.. (2017). Prospective Evaluation of Free Energy Calculations for the Prioritization of Cathepsin L Inhibitors. Journal of Medicinal Chemistry. 60(6). 2485–2497. 101 indexed citations

16.

Steinbrecher, Thomas, Robert Abel, Anthony Clark, & Richard A. Friesner. (2017). Free Energy Perturbation Calculations of the Thermodynamics of Protein Side-Chain Mutations. Journal of Molecular Biology. 429(7). 923–929. 31 indexed citations

17.

Steinbrecher, Thomas, Lingle Wang, Robert Abel, et al.. (2016). Predicting the Effect of Amino Acid Single-Point Mutations on Protein Stability—Large-Scale Validation of MD-Based Relative Free Energy Calculations. Journal of Molecular Biology. 429(7). 948–963. 84 indexed citations

18.

Stafford, Kate A., Nikola Trbovic, Joel A. Butterwick, et al.. (2014). Conformational Preferences Underlying Reduced Activity of a Thermophilic Ribonuclease H. Journal of Molecular Biology. 427(4). 853–866. 6 indexed citations

19.

Young, Tom, Lan Hua, Xuhui Huang, et al.. (2010). Dewetting transitions in protein cavities. Proteins Structure Function and Bioinformatics. 78(8). 1856–1869. 58 indexed citations

20.

Young, Tom, Robert Abel, Byungchan Kim, B. J. Berne, & Richard A. Friesner. (2007). Motifs for molecular recognition exploiting hydrophobic enclosure in protein–ligand binding. Proceedings of the National Academy of Sciences. 104(3). 808–813. 541 indexed citations breakdown →

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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