IN THIS ISSUE . . .
January 18, 2005
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The National Institute of General Medical Sciences (NIGMS), one of the National Institutes of Health, supports all research featured in this digest. Although only the lead scientists are named, coworkers and other collaborators also contributed to the findings.
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Cool Image: Mapping Metabolic Activity
Like a map showing heavily traveled roads, this mathematical model of metabolic activity inside an E. coli cell shows the busiest pathway in white. Reaction pathways used less frequently by the cell are marked in red (moderate activity) and green (even less activity). Visualizations like this one may help scientists identify drug targets that block key metabolic pathways in bacteria. Courtesy of Albert-László Barabási, professor of physics at the University of Notre Dame.
Barabási home page
Hi-res image (714KB PNG)
Sea Snail Research Leads to Better Pain Relief
People who suffer from severe, intractable pain may soon find relief from an unlikely source: the venom of a poisonous sea snail. For more than 25 years, University of Utah biologist Baldomero Olivera has analyzed the nerve toxins produced by these snails, and now his basic research has led to a powerful new painkiller called Prialt®. Olivera's work reveals molecular details about the snails' toxins and the deadly effects they have, and it points to hundreds of other snail toxins that might be useful as medicines or research tools.
"This work is a clear example of how investing in curiosity-driven research can lead to exciting new medical treatments. An added benefit of this and many other basic biomedical studies is the development of tools that are useful for further laboratory research." -- Jeremy M. Berg, Director, NIGMS
Image caption: Conus magus, or magician's cone snail, is native to coral reefs in the Pacific Ocean. About 2 inches long, Conus magus uses its venom to hunt fish. Some of the larger cone snails contain enough venom to kill a human with a single sting.
Hi-res image (299KB JPG)
Olivera home page
Carbohydrates are essential molecules of life that perform countless bodily functions. They coat nearly every cell in the body and help fight germs, and they make it possible for an embryo to implant into a woman's uterus and develop into a baby. Yet these important molecules have remained mysterious because many exist in complicated, branched structures that are hard for scientists to study and control. But now Carolyn Bertozzi, a molecular engineer at the University of California, Berkeley, has created a chemical switch that opens the door to studying and possibly controlling carbohydrates and the biological processes associated with them.
Bertozzi home page
Lab home page
Researchers Watch Protein Plaques Form in the Brain
In diseases like Alzheimer's and Parkinson's, clumps of proteins form in the brain. To get a better look at how proteins aggregate, researchers at North Carolina State University decided to make computer-generated movies. Led by chemical engineer Carol Hall, they used a computer simulation technique to show how small pieces of proteins called peptides can spontaneously gather into protein sheets, similar to the structures found in animals and people with certain brain diseases. These models could help scientists understand the formation of protein clusters, widening the view on how to slow or even halt this process.
Image caption: Simulation of peptides gathering to form protein cluster.
Movie (9.8MB MOV)
Hall home page
Research group home page
Researchers Find Long-Sought Gene Regulator
A team of Harvard Medical School scientists led by pathologist Yang Shi has found a long-sought key to controlling what genes are turned on and off. The researchers stumbled across the proverbial needle in the haystack when they realized that a molecule they were analyzing could be none other than the gene-regulating enzyme, called a demethylase, that researchers had searched for but never found. Flaws in the process controlled by this enzyme have been linked to several diseases, including certain forms of cancer, which make the enzyme an appealing target for drug development.
Shi home page