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Archive - Sep 28, 2015

Famed Physician-Geneticist Helen Hobbs to Receive Prestigious Award from Rockefeller University; Annual $100,000 Prize Celebrates Achievements of Outstanding Women in Biomedical Science; TV Host Rachel Maddow Will Present Award at Rockefeller November 17

University of Texas (UT) Southwestern Medical Center physician-geneticist Helen Helen Hobbs, M.D., is the 2015 recipient of the prestigious Pearl Meister Greengard Prize. The prize recognizes Dr. Hobbs’ research, which advances understanding of heart disease and other complex disorders. The work of Dr. Hobbs, Director of the Eugene McDermott Center for Human Growth and Development at UT Southwestern and a Howard Hughes Medical Institute Investigator, is credited with leading to new therapeutics to lower LDL cholesterol. She will receive the prize on November 17 in a ceremony at The Rockefeller University in New York City. The international award from Rockefeller, which celebrates the achievements of outstanding women in biomedical science, was established by Dr. Paul Greengard, a biophysicist and Vincent Astor Professor at the Rockefeller, and his wife, Ursula von Rydingsvard, a sculptor. The $100,000 annual prize is named in honor of Dr. Greengard’s mother, who died giving birth to him. It is funded by Dr. Greengard’s donation of his monetary share of the 2000 Nobel Prize in Physiology or Medicine (shared among three scientists for discoveries concerning signal transduction in the nervous system), as well as donations from other generous Rockefeller supporters. “Dr. Hobbs’ work is nothing short of inspirational – she is unraveling the genetic underpinnings of cardiovascular disease and changing the way we look at one of the most common, complex health issues of our time,” said Dr. Greengard. Since 1999, Dr. Hobbs has led the Dallas Heart Study, a longitudinal, multiethnic, population-based investigation of risk factors underlying cardiovascular disease, the nation’s leading cause of death for both men and women. The study, originally funded by the Donald W.

New Technology Developed for Rapid and Efficient Targeted Functionalization of Proteins; May Enable Improved Attachment of Chemotherapeutic Drugs to Antibodies; Wide Range of Additional Therapeutic Applications Envisioned

Researchers from Ludwig-Maximilians-Universitaet (LMU) in Munich, together with colleagues based in Berlin, have developed a rapid and efficient technique for targeted chemoenzymatic functionalization of proteins. The new method has a wide range of potential therapeutic applications. Selective intermolecular recognition is at the heart of all biological processes. Thus, proteins that bind specifically to complementary chemical structures are also indispensable for many biochemical and biotechnological applications. Targeted modification of such proteins therefore plays a significant role in medical diagnostics and therapies. Now, researchers led by Professor Heinrich Leonhardt at LMU's Biocenter and Professor Christian Hackenberger of the Leibniz Institute for Molecular Pharmacology in Berlin have developed a new strategy that permits specific chemical modification of virtually any protein more rapidly and more efficiently than was hitherto possible. Their results were published online on September 25, 2015 in the journal Angewandte Chemie. The article is titled “Versatile and Efficient Site-Specific Protein Functionalization by Tubulin Tyrosine Ligase.” Many of the methods routinely used in the biosciences are based on the specific modification of proteins, in particular antibodies, to endow them with novel properties for specific purposes. For example, chemotherapeutic agents used in the treatment of cancer are often chemically linked to antibodies that recognize antigens found only on the surface of the target tumor. In this way, the cytoxic drug can be delivered directly to the cells it is intended to eradicate. Ideally, the methods used to introduce such modifications should be as specific, efficient and versatile as possible. Unfortunately, the techniques currently in use fulfill these criteria only in part.

Green Storage for Green Energy (Solar & Wind); Harvard Scientists Develop New Alkaline Quinone Flow Battery Using High-Performance, Non-Flammable, Non-Toxic, Non-Corrosive, Low-Cost Chemicals; Rapid Commercial Introduction Predicted

A team of Harvard scientists and engineers has demonstrated a rechargeable battery that could make storage of electricity from intermittent energy sources like solar and wind safe and cost-effective for both residential and commercial use. The new research builds on earlier work by members of the same team that could enable cheaper and more reliable electricity storage at the grid level. The mismatch between the availability of intermittent wind or sunshine and the variability of demand is a great obstacle to getting a large fraction of our electricity from renewable sources. This problem could be solved by a cost-effective means of storing large amounts of electrical energy for delivery over the long periods when the wind isn't blowing and the sun isn't shining. In the operation of the newly-developed battery, electrons are picked up and released by compounds composed of inexpensive, earth-abundant elements (carbon, oxygen, nitrogen, hydrogen, iron, and potassium) dissolved in water. The compounds are non-toxic, non-flammable, and widely available, making them safer and cheaper than those used in other battery systems. "This is chemistry I'd be happy to put in my basement," says Dr. Michael J. Aziz, Gene and Tracy Sykes Professor of Materials and Energy Technologies at Harvard Paulson School of Engineering and Applied Sciences (SEAS), and project Principal Investigator. "The non-toxicity and cheap, abundant materials placed in water solution mean that it's safe -- it can't catch on fire -- and that's huge when you're storing large amounts of electrical energy anywhere near people." The research was published in the September 25, 2015 issue of the journal Science. The article is titled “Alkaline Quinone Flow Battery.” This new battery chemistry was developed by post-doctoral fellow Dr.