L
Laquasha Gaddis
Researcher at Georgia State University
Publications - 3
Citations - 658
Laquasha Gaddis is an academic researcher from Georgia State University. The author has contributed to research in topics: Amprenavir & HIV-1 protease. The author has an hindex of 3, co-authored 3 publications receiving 626 citations.
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Journal ArticleDOI
Novel bis-tetrahydrofuranylurethane-containing nonpeptidic protease inhibitor (PI) UIC-94017 (TMC114) with potent activity against multi-PI-resistant human immunodeficiency virus in vitro
Yasuhiro Koh,Hirotomo Nakata,Kenji Maeda,Hiromi Ogata,Geoffrey Bilcer,Thippeswamy Devasamudram,John F. Kincaid,Péter Boross,Yuan-Fang Wang,Yunfeng Tie,Patra Volarath,Laquasha Gaddis,Robert W. Harrison,Irene T. Weber,Arun K. Ghosh,Hiroaki Mitsuya,Hiroaki Mitsuya +16 more
TL;DR: Considering the favorable pharmacokinetics of UIC-94017 when administered with ritonavir, the present data warrant that UIC -94017 be further developed as a potential therapeutic agent for the treatment of primary and multi-PI-resistant HIV-1 infections.
Journal ArticleDOI
High Resolution Crystal Structures of HIV-1 Protease with a Potent Non-Peptide Inhibitor (Uic-94017) Active Against Multi-Drug-Resistant Clinical Strains.
Yunfeng Tie,Péter Boross,Péter Boross,Yuan-Fang Wang,Laquasha Gaddis,Azhar K. Hussain,Sofiya Leshchenko,Arun K. Ghosh,John M. Louis,Robert W. Harrison,Irene T. Weber +10 more
TL;DR: The compound UIC-94017 (TMC-114) is a second-generation HIV protease inhibitor with improved pharmacokinetics that is chemically related to the clinical inhibitor amprenavir and proposed to be critical for the potency of this compound against HIV isolates that are resistant to multiple protease inhibitors.
Journal ArticleDOI
Molecular basis for substrate recognition and drug resistance from 1.1 to 1.6 Å resolution crystal structures of HIV-1 protease mutants with substrate analogs
Yunfeng Tie,Péter Boross,Péter Boross,Yuan-Fang Wang,Laquasha Gaddis,Fengling Liu,Xianfeng Chen,József Tözsér,Robert W. Harrison,Irene T. Weber +9 more
TL;DR: The structures suggest that the binding affinity for mutants is modulated by the conformational flexibility of the substrate analogs, which helps to explain how HIV can develop drug resistance while retaining the ability of PR to hydrolyze natural substrates.