Lori Emert-Sedlak, PhD
Research Assistant Professor
533 Bridgeside Point II
450 Technology Drive
Education
PhD in Pharmacology, University of Pittsburgh, School of Medicine
BS in Biochemistry and Molecular Biology, Pennsylvania State University
Research Summary
My research focuses on high-throughput drug discovery for inhibitors of the HIV-1 Nef and Vif accessory proteins. In addition to developing new assays that are compatible for screening large compound libraries, I work to define the biological relevance and the mechanism of the compounds that we discover. My project aims to develop the first drugs that target HIV-1 Nef.
Research Lab Affiliation
Why I Chose Pitt
In addition to being a beautiful and family-friendly city, Pittsburgh boasts a world-class medical center with outstanding researchers. I want to work in a laboratory where I think my work might actually make a difference, so I chose an outstanding mentor that has the same goals.
Selected Abstracts:
- Emert-Sedlak L. Screening for Small Molecule Inhibitors of HIV-1 Nef Function via Src-Family Kinase Coupling In Vitro Identifies a Novel Inhibitor of HIV-1 Replication. 12th Annual Symposium on Antiviral Drug Resistance. November 2011, Hershey PA. Oral presentation.
- Emert-Sedlak L, Lazo JS, Johnston P, and Smithgall TE. High-throughput Screening for Small Molecule Inhibitors of HIV-1 Nef via Nef-Src Family Kinase Coupling in vitro. Keystone Symposium: HIV Evolution, Genomics and Pathogenesisjoint with Protection from HIV: Targeted Intervention Strategies. March 2011, Whistler, British Columbia, Canada.
- Emert-Sedlak L, Johnston P, Lazo JS, and Smithgall TE. High-throughput Screening for Small Molecule Inhibitors of HIV-1 Nef Function. 11th Annual Symposium on Antiviral Drug Resistance. November 2010, Hershey PA.
- Emert-Sedlak L, Kodama T, Lerner E, Die W, Foster C, Day BW, Lazo JS, and Smithgall TE. Chemical library screens targeting an HIV-1 accessory factor/host cell kinase complex identify novel antiretroviral compounds. 10th Annual Symposium on Antiviral Drug Resistance: Targets and Mechansisms. November 2009, Richmond VA.
Publications
Marcsisin, S. R; Narute, P. S; Emert-Sedlak, L. A; Kloczewiak, M; Smithgall, T. E; and Engen, J. R. (2011) On the solution conformation and dynamics of the HIV-1 Virion Infectivity Factor. J. Mol. Biol. 410: 1008-1022. | View Abstract
Dikeakos, J. D; Atkins, K. M; Thomas, L; Emert-Sedlak, L; Byeon, I. J; Jung, J; Ahn, J; Wortman, M. D; Kukull, B; Saito, M; Koizumi, H; Williamson, D. M; Hiyoshi, M; Barklis, E; Takiguchi, M; Suzu, S; Gronenborn, A. M; Smithgall, T. E; and Thomas, G. (2010) Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action. Mol Biol Cell. 21: 3279-3292. | View Abstract
Schmaier, A. A; Zou, Z; Kazlauskas, A; Emert-Sedlak, L; Fong, K. P; Neeves, K. B; Maloney, S. F; Diamond, S. L; Kunapuli, S. P; Ware, J; Brass, L. F; Smithgall, T. E; Saksela, K; and Kahn, M. L. (2009) Molecular priming of Lyn by GPVI enables an immune receptor to adopt a hemostatic role. Proc Natl Acad Sci USA. 106: 21167-21672. | View Abstract
Emert-Sedlak, L; Kodama, T; Lerner, E. C; Dai, W; Foster, C; Day, B. W; Lazo, J. S; and Smithgall, T. E. (2009) Chemical library screens targeting an HIV-1 accessory factor/host cell kinase complex identify novel antiretroviral compounds. ACS Chem Biol. 4: 939-947. | View Abstract
Trible, R. P; Emert-Sedlak, L; Wales, T. E; Ayyavoo, V; Engen, J. R; and Smithgall, T. E. (2007) Allosteric Loss-of-function Mutations in HIV-1 Nef from a Long-Term Non-Progressor. J of Mol Biol. 374: 121-129. | View Abstract
Mitchell, J. L; Trible, R. P; Emert-Sedlak, L. A; Weis, D. D; Lerner, E. C; Applen, J. J; Sefton, B. M; Smithgall, T. E; and Engen, J. R. (2007) Functional characterization and conformational analysis of the Herpesvirus saimiri Tip-C484 protein. J Mol Biol. 366: 1282-1293. | View Abstract
Trible, R. P; Emert-Sedlak, L; and Smithgall, T. E. (2006) HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction. J Biol Chem. 281: 27029-27038. | View Abstract