IN THIS ISSUE .
February 18, 2009
Got research news to share? E-mail us at email@example.com.
To change your subscription options or unsubscribe, visit https://public.govdelivery.com/accounts/USNIGMS/subscriber/new?topic_id=USNIGMS_3.
Subscribe to the RSS version of Biomedical Beat by selecting this XML link and following your news reader's instructions for adding a feed.
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. To read additional news items, visit NIGMS
News. To check out free NIGMS publications, go to
the order form.
A protein called tubulin (green) accumulates in the center of a nucleus (outlined in pink) from an aging cell. Normally, this protein is kept out of the nucleus with the help of gatekeepers known as nuclear pore complexes. But a new study shows that wear and tear to long-lived components of the complexes eventually lowers the gatekeepers’ guard. As a result, cytoplasmic proteins like tubulin gain entry to the nucleus while proteins normally confined to the nucleus seep out. The work suggests that finding ways to stop the leakage could slow the cellular aging process and possibly lead to new therapies for age-related diseases. Courtesy of cell biologists Maximiliano D’Angelo and Martin Hetzer, Salk Institute.
Scientists from four continents joined to address one of the trickiest issues in prescribing medicine: how to optimize a patient’s dosage of the blood-thinner warfarin. The drug is challenging to prescribe because each person’s ideal dosage varies widely, is hard to predict and is crucial for his or her safety. Sharing anonymized data from thousands of people worldwide, the International Warfarin Pharmacogenetics Consortium used mathematical modeling to develop a gene-based warfarin dosing strategy that could work for genetically diverse patients. To test this idea, NIH is launching a large-scale clinical trial.
This work was also supported by other parts of NIH: National Heart, Lung and Blood Institute; the National Institute of Neurological Disorders and Stroke; and the National Center for Research Resources.
Automakers use steel scraps to build cars, construction companies repurpose tires to lay running tracks and now scientists are reusing previously discarded medical data to better understand our complex physiology. Through a Website called PhysioNet developed in part by Beth Israel Deaconess Medical Center cardiologist Ary Goldberger, scientists can access complete physiologic recordings, such as heart rate, respiration, brain activity and gait. They then can use free software to analyze the data and find patterns in it. The patterns could ultimately help health care professionals diagnose and treat health conditions like congestive heart failure, sleeping disorders, epilepsy and walking problems.
PhysioNet is also supported by NIH’s National Institute of Biomedical Imaging and Bioengineering.
The world celebrates Darwin Day this February. The occasion marks the 200th anniversary of naturalist Charles Darwin’s birth and the 150th anniversary of the publication of his historic book about evolution, On the Origin of Species. In tribute, the February 2009 issue of Findings is a special, all-evolution issue. Find out how two evolutionary biologists are using modern biological approaches to uncover the secrets of our past and what they can tell us about health and disease. Also check out special online games and interviews with cutting-edge scientists.
Structural biologists today working in the United States can trace their roots back to England, where many of the first techniques and labs to study the 3-D structures of proteins first emerged. While the history of protein structure determination is rich with important discoveries, a new era of rapid advance began in 1958 when British scientists John Kendrew and Max Perutz published the very first high-resolution protein structures—first of the oxygen storage protein myoglobin and then of the oxygen-transporting protein hemoglobin. Go back in time to learn about key events in the last 50 years of high-resolution protein structure determination.