IN THIS ISSUE .
October 15, 2008
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This tropical scene, reminiscent of a postcard from Key West, is actually a petri dish containing an artistic arrangement of genetically engineered bacteria. The image showcases eight of the fluorescent proteins created in the laboratory of Roger Y. Tsien, a cell biologist at the University of California, San Diego. Tsien, along with Osamu Shimomura of the Marine Biology Laboratory and Martin Chalfie of Columbia University, share the 2008 Nobel Prize in chemistry for their work on green fluorescent protein—a naturally glowing molecule from jellyfish that has become a powerful tool for studying molecules inside living cells. Courtesy of Nathan Shaner, Monterey Bay Aquarium Research Institute.
Many commercial chemical products are manufactured with the help of catalysts, substances that increase the rate of chemical reactions with a small amount of energy. To develop a more direct method for making useful chemical building blocks, Princeton University chemists David MacMillan and David Nicewicz brought together two independent catalytic processes. Joining the processes in a clever fashion led to the synthesis of an entire class of chemical products previously much more difficult to obtain. Because the method is catalytic, it required little added energy—just the light from a 15-watt bulb. Efficient, versatile, inexpensive, and environmentally friendly, the method could improve many chemistry-based processes, including drug manufacturing.
Cholesterol often gets a bad rap, but cells need this waxy substance to function properly. Research on this role of cholesterol has focused mainly on the membranes enclosing cells, but new molecular simulations suggest that cholesterol may directly affect proteins. University of Pennsylvania researchers led by computational biophysicist Michael Klein developed simulations of a well studied receptor protein linked to many neurological disorders. The work showed that cholesterol buries deep inside the protein structure, explaining why the protein needs the substance to function. The surprising finding could transform our understanding of this and other receptors as well as the medications designed to interact with them.
story (no longer available)
Klein lab home page (no longer available)
Article abstract (from the September 23 issue of PNAS)
Scientists have long known that the nervous system and the immune system influence one another, but the exact means of communication has been elusive. Now, geneticist Alejandro Aballay of Duke University has revealed the identity of a key link between the systems. Working in roundworms, his team found that nerve cells use a receptor called NPR-1 to send signals that heighten the worms' innate immune response, the first line of defense against invading pathogens. This work represents an important step toward understanding how the nervous system can regulate immunity and offers possible new therapeutic targets for treating infectious diseases.
NIH's National Institute of Allergy and Infectious Diseases also supported this work.
Full story (no longer available)
Aballay lab home page
Article abstract (from the September 18 online issue of Science)
Did you know that ingredients from tree bark can treat cancer and molecules in poppies can ease its pain? That hundreds of life-saving medicines originally came from plants or fungi? Find out about chemist Erik Sorensen's quest to find new drugs from nature. In the September 2008 issue of Findings, you'll also meet molecular biologist Cynthia McMurray, whose research on Huntington's disease helps to explain this mysterious brain disorder and offers hope for new treatments and even a cure.