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Richard A. Friesner
Researcher at Columbia University
Publications - 376
Citations - 61378
Richard A. Friesner is an academic researcher from Columbia University. The author has contributed to research in topics: Density functional theory & Ab initio. The author has an hindex of 97, co-authored 367 publications receiving 52729 citations. Previous affiliations of Richard A. Friesner include Environmental Molecular Sciences Laboratory & Schrödinger.
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Journal ArticleDOI
Glide: a new approach for rapid, accurate docking and scoring. 1. Method and assessment of docking accuracy.
Richard A. Friesner,Jay L. Banks,Robert B. Murphy,Thomas A. Halgren,Jasna Klicic,Daniel T. Mainz,Matthew P. Repasky,Eric H. Knoll,Mee Shelley,Jason K. Perry,David E. Shaw,Perry Francis,Peter S Shenkin +12 more
TL;DR: Glide approximates a complete systematic search of the conformational, orientational, and positional space of the docked ligand to find the best docked pose using a model energy function that combines empirical and force-field-based terms.
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Glide: a new approach for rapid, accurate docking and scoring. 2. Enrichment factors in database screening.
Thomas A. Halgren,Robert B. Murphy,Richard A. Friesner,Hege S. Beard,Leah L. Frye,W. Thomas Pollard,Jay L. Banks +6 more
TL;DR: Comparisons to results for the thymidine kinase and estrogen receptors published by Rognan and co-workers show that Glide 2.5 performs better than GOLD 1.1, FlexX 1.8, or DOCK 4.01.
Journal ArticleDOI
Extra Precision Glide: Docking and Scoring Incorporating a Model of Hydrophobic Enclosure for Protein-Ligand Complexes
Richard A. Friesner,Robert B. Murphy,Matthew P. Repasky,Leah L. Frye,Jeremy R. Greenwood,Thomas A. Halgren,Paul C. Sanschagrin,Daniel T. Mainz +7 more
TL;DR: Enrichment results demonstrate the importance of the novel XP molecular recognition and water scoring in separating active and inactive ligands and avoiding false positives.
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Evaluation and Reparametrization of the OPLS-AA Force Field for Proteins via Comparison with Accurate Quantum Chemical Calculations on Peptides†
TL;DR: In this article, a fitting technique combines using accurate ab initio data as the target, choosing an efficient fitting subspace of the whole potential energy surface, and determining weights for each of the fitting points based on magnitudes of the potential energy gradient.
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OPLS3: A Force Field Providing Broad Coverage of Drug-like Small Molecules and Proteins
Edward Harder,Wolfgang Damm,Jon R. Maple,Chuanjie Wu,Mark Reboul,Jin Yu Xiang,Lingle Wang,Dmitry Lupyan,Markus K. Dahlgren,Jennifer L. Knight,Joseph W. Kaus,David S. Cerutti,Goran Krilov,William L. Jorgensen,Robert Abel,Richard A. Friesner +15 more
TL;DR: Together, the improvements made to both the small molecule and protein force field lead to a high level of accuracy in predicting protein-ligand binding measured over a wide range of targets and ligands (less than 1 kcal/mol RMS error) representing a 30% improvement over earlier variants of the OPLS force field.