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Gary A. Meints

Researcher at University of Illinois at Urbana–Champaign

Publications -  8
Citations -  743

Gary A. Meints is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Farnesyl diphosphate synthase & Farnesyl pyrophosphate. The author has an hindex of 7, co-authored 7 publications receiving 728 citations. Previous affiliations of Gary A. Meints include University of London.

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Quantitative Structure-Activity Relationships for γδ T Cell Activation by Bisphosphonates

TL;DR: The activation of γ δ T cells by a broad range of bisphosphonates is reported and a pharmacophore model for γδ T cell activation is developed and a comparative molecular similarity index analysis (CoMSIA) approach is used to make quantitative relationships between γ ΔT cell activation by bisph phosphonates and their three-dimensional structures.
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3-D QSAR investigations of the inhibition of Leishmania major farnesyl pyrophosphate synthase by bisphosphonates.

TL;DR: The results are of general interest since they represent the first detailed quantitative structure-activity relationship study of the inhibition of an expressed farnesyl pyrophosphate synthase enzyme by bisphosphonate inhibitors and that the activity of these inhibitors can be predicted within about a factor of 3 by using 3D-QSAR techniques.
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Activity of Bisphosphonates against Trypanosoma brucei rhodesiense

TL;DR: Several bisphosphonates were found to have large therapeutic indices (> or =200:1) as well as low IC(50) values, suggesting their further investigation as antiparasitic agents against T. b.
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Solid-state NMR, crystallographic, and computational investigation of bisphosphonates and farnesyl diphosphate synthase-bisphosphonate complexes.

TL;DR: X-ray crystallography is used to determine the structures of two potent bisphosphonate inhibitors, finding good agreement with the computational results, opening up the possibility of using the combination of NMR, quantum chemistry and molecular docking to facilitate the design of other, novel prenytransferase inhibitors.