T
Tudor I. Oprea
Researcher at University of New Mexico
Publications - 304
Citations - 21459
Tudor I. Oprea is an academic researcher from University of New Mexico. The author has contributed to research in topics: Virtual screening & Medicine. The author has an hindex of 70, co-authored 280 publications receiving 18067 citations. Previous affiliations of Tudor I. Oprea include University of Copenhagen & Technical University of Denmark.
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Journal ArticleDOI
A comprehensive map of molecular drug targets
Rita Santos,Rita Santos,Oleg Ursu,Anna Gaulton,A. Patrícia Bento,Ramesh S. Donadi,Cristian Bologa,Anneli Karlsson,Bissan Al-Lazikani,Anne Hersey,Tudor I. Oprea,John P. Overington +11 more
TL;DR: An updated comprehensive map of molecular targets of approved drugs is presented and the relationships between bioactivity class and clinical success, as well as the presence of orthologues between human and animal models and between pathogen and human genomes are explored.
Journal ArticleDOI
The Design of Leadlike Combinatorial Libraries.
TL;DR: The optimization of low-potency leads into drugs is often accompanied by an increase in molecular weight and lipophilicity, as a consequence of affinity enhancement, shown schematically by the distributions of M(r) for a leadlike library, oral drugs, and a typical combinatorial chemistry library.
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Virtual and biomolecular screening converge on a selective agonist for GPR30
Cristian Bologa,Chetana M. Revankar,Susan M. Young,Bruce S. Edwards,Jeffrey B. Arterburn,Alexander S. Kiselyov,Matthew A. Parker,Sergey E. Tkachenko,Nikolay P. Savchuck,Larry A. Sklar,Tudor I. Oprea,Eric R. Prossnitz +11 more
TL;DR: The identification of the first G PR30-specific agonist, G-1 (1), capable of activating GPR30 in a complex environment of classical and new estrogen receptors is described.
Journal ArticleDOI
Is There a Difference between Leads and Drugs? A Historical Perspective
TL;DR: Lead structures exhibit, on the average, less molecular complexity, are less hydrophobic, and less druglike (lower druglike scores), and this information should be used in the design of novel combinatorial libraries that are aimed at lead discovery.
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Estrogen Signaling through the Transmembrane G Protein–Coupled Receptor GPR30
Eric R. Prossnitz,Jeffrey B. Arterburn,Jeffrey B. Arterburn,Harriet O. Smith,Tudor I. Oprea,Larry A. Sklar,Helen J. Hathaway +6 more
TL;DR: An overview of the evidence for the cellular and physiological actions of GPR30 in estrogen-dependent processes and the relationship of G PR30 with classical estrogen receptors is provided.