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.

Schultz biosktech

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Dr. Duvoisin to lead Program in Molecular and Cellular Biology

Associate Dean for Graduate Studies Allison Fryer, Ph.D., announced that Robert Duvoisin, Ph.D., professor of physiology and pharmacology, OHSU School of Medicine, will be the new director for the Program in Molecular and Cellular Biology (PMCB). PMCB is the entry program to seven Ph.D. degrees in basic science in the OHSU School of Medicine. 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+.