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First High-Res 3-D Structures of Mammalian HSP90 Protein Solved, Key to Better Targets for AIDS, Sepsis, Cancer Drugs
Date:10/19/2007

p HSP90 inhibitors, the same potential exists here. "This will spur a new line of inquiry into GRP94. While this work is its infancy, medicinal chemists will be interested in developing GRP94-targeted drugs," Gewirth said.

Other authors of the publication include: D. Eric Dollins, recent Ph.D. graduate from Duke University, Joshua J. Warren, post-doctoral fellow at Duke University and Robert M. Immorrino, recent Ph.D. graduate from Duke University.

About Gewirth

In addition to his position as an HWI senior research scientist, Gewirth is an associate professor of Structural Biology at the University at Buffalo. Prior to joining HWI in 2005, Gewirth was an assistant professor in the Department of Biochemistry at Duke University. He completed post-doctoral research at both Yale and Harvard, received his Ph.D. from Yale University in 1988 and his bachelor's degree from the University of Chicago in 1982. Gewirth's research is focused primarily on structural studies of HSP90 chaperones, drug design, protein folding; nuclear hormone receptors; and basal transcription factors. Gewirth and his wife live in Buffalo.

About HWI

With more than 50 years of exceptional scientific research, HWI is an independent, non-profit facility specializing in the area of fundamental biomedical research known as structural biology. Hauptman-Woodward's team of more than 75 staff members is committed to improving human health by studying the causes of diseases, as well as potential therapies, at their basic molecular level. HWI is located in the heart of the Buffalo Niagara Medical Campus in downtown Buffalo, New York, in a new state-of-the-art structural biology research center at 700 Ellicott Street. For more information, visit HWI's website at http://www.hwi.buffalo.edu or call 716-898-8600.

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SOURCE Hauptman-Woodward Medical Research Institute
Copyright©2007 PR Newswire.
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