Jordan awarded prize for breast cancer research
V. Craig Jordan, scientific director at the Lombardi Comprehensive Cancer Center at Georgetown University Medical Center, has received the St. Gallen Breast Cancer Award in Clinical Breast Cancer Research for his contributions to developing the scientific principles used in the effective antihormonal adjuvant therapy for early breast cancer.
The Swiss prize recognizes Jordan’s strategy of targeting the estrogen receptor and administering long-term (five-year) adjuvant tamoxifen therapy resulting in increased patient survivorship around the world. Millions of women continue to benefit from the use of tamoxifen.
To celebrate Jordan’s prize, the U.S. ambassador to Switzerland, Don Beyer, is hosting an event in his honor at the ambassador’s residence in Washington, D.C.
The St. Gallen Breast Cancer Award is given every two years to a scientist who has made exceptional contributions to the field of breast cancer research.
Poulter honored with Nakanishi Prize
C. Dale Poulter, the John A. Widtsoe distinguished professor of chemistry at the University of Utah, has been awarded the 2011 Nakanishi Prize from the American Chemical Society.
The prize, which recognizes significant work that extends chemical and spectroscopic methods to the study of important biological phenomena, was established in 1995 by the students and colleagues of Koji Nakanishi.
Poulter studies the reactions catalyzed by enzymes in the isoprene biosynthetic pathway with special emphasis on establishing the mechanisms of the enzyme-catalyzed transformations and how the enzymes promote the reactions. One of the most important isoprenoid reactions Poulter has studied is protein prenylation, in which isoprenoids attach to soluble proteins. This interaction allows the proteins to bind to cellular membranes and thus become pivotal in signal transduction networks.
Recently, Poulter has been investigating the link between modern enzymes and a common ancestor. He has found that by perturbing some isoprenoid enzymes he is able to make them lose their characteristic selectivity. Thus, by intermixing parts of two different isoprenoid enzymes or eliminating their cofactors, he is able to make new enzymes that lack selectivity and then identify the amino acid changes required to restore selectivity.
“Simply put, Poulter, for almost four decades, has continuously been the single scientist with the largest impact in deciphering the logic and mechanism by which nature assembles isoprenoid natural products,” commented Christopher T. Walsh, a professor at Harvard Medical School, in C&E News.