Much of Dr. Vivian Cody’s work is concerned with dihydrofolate reductase (DHFR), an enzyme that is a useful target for cancer chemotherapy as well as treatment of the type of pneumonia that often plagues AIDS patients.  Several of Cody’s recent papers cover various aspects of her DHFR-related work.

In the first paper, structural data reported for five antifolates reveals a previously unobserved inhibitor-binding site that may help toward the design of enzyme-specific inhibitors (PMID 21206056).  A second paper, with collaborators at Duquesne University, describes the configuration of another group of DHFR anticancer inhibitors that reveals that the enzyme can select active isomers from mixtures (PMID 21123866).  A third paper, with collaborators at the University of Minnesota and others from the University of Washington, reports the crystal structure of a novel cancer drug-delivery system that contains two DHFR molecules (PMID 21077608).

A fourth recent publication, resulting from a collaboration between Cody and the group at the University of Minnesota, concerned a different enzyme, histidine triad nucleotide binding protein, that is thought to be involved in tumor suppression (PMID 20934431).

Dr. Cody has authored or coauthored approximately 250 peer-reviewed papers during her career at the Hauptman-Woodward Institute.