L
Lee K. Opresko
Researcher at Pacific Northwest National Laboratory
Publications - 41
Citations - 3492
Lee K. Opresko is an academic researcher from Pacific Northwest National Laboratory. The author has contributed to research in topics: Epidermal growth factor & Receptor. The author has an hindex of 26, co-authored 41 publications receiving 3370 citations. Previous affiliations of Lee K. Opresko include University of Utah.
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Journal ArticleDOI
Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library
Michael J. Feldhaus,Robert W. Siegel,Lee K. Opresko,James R. Coleman,Jane M. Weaver Feldhaus,Yik Andy Yeung,Jennifer R. Cochran,Peter Heinzelman,David W. Colby,Jeffrey S. Swers,Christilyn P Graff,H. Steven Wiley,K. Dane Wittrup +12 more
TL;DR: The ability to use multiplex library screening demonstrates the usefulness of this approach for high-throughput antibody isolation for proteomics applications.
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ErbB-2 amplification inhibits down-regulation and induces constitutive activation of both ErbB-2 and epidermal growth factor receptors.
TL;DR: The data suggest that overexpression of erbB-2 inhibits both its down-regulation and that of the EGFR, and the net effect is increased signaling through the EGfr system.
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Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor.
Jianying Dong,Lee K. Opresko,Peter J. Dempsey,Douglas A. Lauffenburger,Robert J. Coffey,H. S. Wiley +5 more
TL;DR: Results indicate that soluble rather than membrane-anchored forms of the ligands mediate most of the biological effects of EGFR ligands, which have shown promise in preventing spread of metastatic disease.
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Rapid and sustained nuclear–cytoplasmic ERK oscillations induced by epidermal growth factor
Harish Shankaran,Danielle L Ippolito,William B. Chrisler,Haluk Resat,Nikki Bollinger,Lee K. Opresko,H. Steven Wiley,H. Steven Wiley +7 more
TL;DR: The characterization of single‐cell ERK dynamics provides a quantitative foundation for understanding the regulatory structure of this signaling cascade and revealed that negative feedback from phosphorylated ERK to the cascade input was necessary to match the robustness of the oscillation characteristics observed over a broad range of ligand concentrations.
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Quantitative analysis of the endocytic system involved in hormone-induced receptor internalization.
TL;DR: A quantitative method to evaluate the interaction between cell surface receptors and the endocytic apparatus is developed and it is found that constitutive internalization of the transferrin receptor behaves as a simple, first order process that is unaltered by ligand.