Robert Abel
Molecular Biology · 2006–2021
A researcher in the Science corpus: 12 papers; trusts 3 researchers and is trusted by 6 researchers here, as inferred from the citation graph.
Subfields
- Molecular Biology — 96 citations into it; #6,329 of 17,773 by trust here, #2,498 by citations
Whom Robert Abel trusts overall
Their strongest outbound trust, strongest first, inferred from their citations.
- Alexander D. MacKerell
- W. L. Jorgensen
- T. Darden
- Matthew P. Jacobson
- Richard A. Friesner
- Junmei Wang
- Emilio Gallicchio
- Eric J. Sorin
- Michael Feig
Who trusts Robert Abel overall
- Tatu Pantsar
- Shota Uehara
- Evanthia Lionta
- Yue Yang
- Antti Poso
- Shigenori Tanaka
- S. J. Macalino
- Tai-Sung Lee
- George M. Spyrou
- ST John
Papers from Robert Abel's perspective
Ordered by how strongly the researchers Robert Abel trusts endorse each paper. Same corpus, a different order for every researcher.
- Force Field Validation Using Protein Side Chain Prediction
- The Amber biomolecular simulation programs
- Modeling of loops in protein structures
- Current Status of the AMOEBA Polarizable Force Field (Journal of Physical Chemistry B)
- Advancing Drug Discovery through Enhanced Free Energy Calculations. (Accounts of Chemical Research)
- How well does a restrained electrostatic potential (RESP) model perform in calculating conformational energies of organic and biological molecules? (Journal of Computational Chemistry)
- Comparative protein modelling by satisfaction of spatial restraints.
- Development and Testing of the OPLS All-Atom Force Field on Conformational Energetics and Properties of Organic Liquids
- A point‐charge force field for molecular mechanics simulations of proteins based on condensed‐phase quantum mechanical calculations (Journal of Computational Chemistry)
- Practical Aspects of Free-Energy Calculations: A Review.
Their papers
- Comparison of multiple Amber force fields and development of improved protein backbone parameters (2006) — 6,725 citations
- Motifs for molecular recognition exploiting hydrophobic enclosure in protein–ligand binding (2007) — 652 citations
- Advancing Drug Discovery through Enhanced Free Energy Calculations. (2017) — 304 citations
- Accurate and reliable prediction of relative ligand binding potency in prospective drug discovery by way of a modern free-energy calculation protocol and force field. (2015) — 1,186 citations
- Role of the active-site solvent in the thermodynamics of factor Xa ligand binding. (2008) — 625 citations
- OPLS3: A Force Field Providing Broad Coverage of Drug-like Small Molecules and Proteins. (2016) — 2,754 citations
- OPLS3e: Extending Force Field Coverage for Drug-Like Small Molecules. (2019) — 1,023 citations
- Efficient Exploration of Chemical Space with Docking and Deep Learning. (2021) — 358 citations
- OPLS4: Improving Force Field Accuracy on Challenging Regimes of Chemical Space. (2021) — 1,624 citations
- Reliable and Accurate Solution to the Induced Fit Docking Problem for Protein-Ligand Binding. (2021) — 168 citations
- Docking Covalent Inhibitors: A Parameter Free Approach To Pose Prediction and Scoring (2014) — 426 citations
- The VSGB 2.0 model: A next generation energy model for high resolution protein structure modeling (2011) — 1,046 citations