The department offers a unique environment for research and training that combines Systems Physiology with Chemical Biology in a synergistic and highly collaborative atmosphere. Learn more
Dr. Carsten Schultz recruited as new chair
OHSU School of Medicine Dean Mark Richardson has appointed Carsten Schultz, Ph.D., as chair of the Department of Physiology and Pharmacology following a national recruitment search. The appointment is effective October 1, 2016. Dr. Schultz will succeed Beth Habecker, Ph.D., who has served as interim chair since 2014. Read more.
Physiology & Pharmacology students selected as Roadmap Scholars
In its third year, the Roadmap Scholar program provides graduate students with the opportunity to participate in the School of Medicine’s Research Roadmap, a process and forum for faculty and research leaders to advance research at OHSU. Learn more.
Schultz group publishes new paper in Cell Chemical Biology "High-Content Imaging Platform for Profiling Intracellular Signaling Network Activity in Living Cells"
OHSU Scientists Received Funding to Develop a Therapy for a Rare Cancer
Dr. Xiangshu Xiao and his team were recently awarded a new grant from the Elsa U. Pardee Foundation to develop a new therapy for Clear Cell Sarcoma of Soft Tissue or CCSST for short. CCSST is a rare and aggressive cancer. Once the tumor is metastasized, the 5-year survival rate is only 20%. This disease mainly affects adolescents and young adults. CCSST is caused and maintained by a specific gene fusion called EWS-ATF1. While the cause was identified more than two decades ago, no effective therapy is currently available. Dr. Xiao and his team recently developed potent small molecule drugs that inhibit ATF1. With this grant, his team will now investigate the antitumor activity of these inhibitors. Dr. Xiao believes this approach may lead to an effective therapy for this devastating disease.
Researchers develop NAD+ biosensor
Michael Cohen, Ph.D., associate professor of physiology and pharmacology in the OHSU School of Medicine, provided the key insight for this paper by recognizing that a bacterial enzyme, DNA ligase, underwent a significant structural change upon binding to NAD+.