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Roden Receives High Honor

National society honors Blakely

Conn to hold newly endowed chair honoring Limbird

Hamm on NIH peer review committee

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Chair's Welcome

I am pleased to welcome you to the Department of Pharmacology. We are one of the most distinguished Pharmacology departments in the country and have placed in the top two NIH ranking positions for sixteen of the last twenty years. Research interests in the Department include five major areas: signal transduction, neuroscience, bioactive lipid metabolism, genetic basis of cardiovascular dysfunction, and drug metabolism. Molecules under investigation include G-protein coupled receptors (rhodopsin, adrenergic, serotonin and receptors), heterotrimeric G-proteins, ion channels, transporters and regulatory proteins such as arrestins, protein kinases and protein phosphatases. A strength in our research and training environment is that Vanderbilt University has a world-acclaimed Division of Clinical Pharmacology, which links the Department of Medicine with the Department of Pharmacology. Faculty members in the Division of Clinical Pharmacology focus on human disease and clinical enigmas as the origin of their questions for research. Basic scientists who pursue their inquiries in this environment are continually informed by their colleagues of the pathophysiological and potential therapeutic relevance that can be achieved by appropriate focus of their efforts. We have created one of the first programs in the country to answer the call from the National Institutes of Health (NIH) for more scientists trained in the area of drug discovery and development.

-Heidi Hamm, Ph.D., Department Chair 

Friends, colleagues remember Morrow

Jason Morrow, M.D., chief of the Division of Clinical Pharmacology in Vanderbilt Medical Center's Department of Medicine, was remembered last week as a gifted scientist and generous friend.

Dr. Morrow, 51, died on July 8. Six hundred people attended his funeral on July 11 at Congregation Micah in Brentwood.  Read Full Article



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Conformational changes associated with GTP binding and hydrolysis. This movie starts with the inactive guanosine diphosphate (GDP)-bound form of the subunit of bovine transducin (G t) bound to the βγ subunit shown in grey. In the G subunit, the helical domain is shown in red, and the GTPase domain is shown in green. The exchange of GDP for guanosine triphosphate (GTP) is followed by the changes associated with GTPase activity. Upon GTP binding and hydrolysis, regions in yellow color (switch regions) undergo dramatic conformational changes. Note the opening and closing of the switch regions that accompanies the GDP- and GTP-bound states.

Mission Statement

We engage in scientific discovery to elucidate biological mechanisms and develop novel therapeutics. We provide training focused on critical thinking to promote innovation, scholarship and integrity. To this end, we foster creativity, collegiality, and leadership.