Omari is a third year Ph.D. Candidate in the Program in Chemical Biology. He graduated from Morehouse College in 2014 with a B.S. in Chemistry. While at Morehouse, he did biomaterials research with Dr. Juana Mendenhall and Dr. Lawrence Bonassar at Cornell University. Omari came directly to Michigan after graduating. He is a recipient of the Rackham Merit Fellowship, GAANN fellowship, the NSF GRFP Fellowship. In the Martin lab, Omari is studying the individual role of Ras isoforms in the MAPK pathway.
In addition to his lab work, Omari likes to take photos, practice piano, and conduct technical/cycle analysis.
Cancer researchers have targeted players within the mitogen activated protein kinase (MAPK) pathway, which is a regulator of cell growth, proliferation, apoptosis, for decades to diminish cell growth and cancer progression. Yet, very little has been done to understand the auxiliary regulators of this pathway. A critical step in cancer progression involves epithelial to mesenchymal transition (EMT), which has been shown to be associated with the MAPK pathway. EMT mainly occurs due to a loss of cell polarity, junctional integrity and growth control, which supports cancer cell progression. MAPK signaling proteins such as small GTPase Ras are key mediators of cell growth and proliferation, and dysregulation of these proteins has been linked to loss of cell polarity and uncontrolled growth. Looking at the well-studied Ras-Raf interaction, a critical PPI in many cancers, could be simplified through incorporation of a photoreactive unnatural amino acid into Raf. This PPI only occurs between activated Ras (Ras-GTP) and Raf kinase and has thus been a well-established method for activated Ras isolation via a GST-RBD (Ras Binding Domain) pulldown. A UV-light reactive Raf RBD protein would allow the covalent chemical capture of activated Ras proteins which could be analyzed using mass spectrometry to identify activated Ras isoforms. This could even be further extended to understanding Ras activation with varying conditions or examination of specific inhibitory effects on Ras isoforms.