The U.S. Defense Advanced Research Projects Agency (DARPA) has awarded $6 million to a team of researchers to develop nanotechnology therapies for the treatment of traumatic brain injury and associated infections. The award brings together a multi-disciplinary team of renowned experts in laboratory research, translational investigation, and clinical medicine. The team includes Sanford-Burnham’s Erkki Ruoslahti, M.D., Ph.D., and is led by Professor Michael J. Sailor, Ph.D., from the University of California San Diego. Also on the team are Sangeeta N. Bhatia, M.D., Ph.D., of Massachusetts Institute of Technology, and Clark C. Chen, M.D., Ph.D., of UC San Diego School of Medicine.
These nanoparticles of porous silicon, each 100 times smaller than a human hair, contain microscopic reservoirs that can hold and protect sensitive drugs. The surface of the particles can be covered with targeting molecules. (Photo by Chia-Chen Wu, UC San Diego)
#RallyMedRes
What: Rally for Medical Research
When: April 8, 2013, 11 a.m – 12:15 p.m. ET
Where: Carnegie Library, Washington, D.C. and webcast live at www.rallyformedicalresearch.org
On Twitter at #RallyMedRes
San Diego is a powerhouse for cancer research, home to two National Cancer Institute (NCI)-designated centers for basic research—our Cancer Center and the Salk Institute Cancer Center—and the University of California, San Diego Moores Cancer Center, the region’s only NCI-designated comprehensive cancer center.
Sanford-Burnham Medical Research Institute Board of Directors (trustees) announced today that John C. Reed, M.D., Ph.D., has accepted the position of Head of Roche Pharma Research and Early Development and member of the Corporate Executive Committee. Kristiina Vuori, M.D., Ph.D., president of Sanford-Burnham, will assume all leadership responsibilities on an interim basis.
“John has led Sanford-Burnham through a decade of tremendous success and growth, particularly in translational research, and we wish him the best as he moves to a new stage of his career,” said M. Wainwright Fishburn, Jr., chairman of Sanford-Burnham’s Board of Trustees. “We have a strong foundation for continued growth, and we have complete confidence in Kristiina’s ability to lead through the management transition.”
Added Dr. Reed, “I am grateful to have led Sanford-Burnham over the past decade, especially in the growth of the Institute’s work in translational research. While I am sad to be leaving the Institute, I look forward to the potential for collaborations in the future between the two organizations. I am confident in the financial strength of the Institute following the strongest year of grant revenue in its history, as well as in Dr. Vuori’s ability to lead through the time ahead. We have worked side-by-side in leading Sanford-Burnham, so she is uniquely qualified to guide a smooth transition and continued excellence.”
![3D structure of CXCR1, a G protein-coupled receptor that transmits inflammatory signals [Image courtesy of Stanley Opella, UCSD]](http://beaker.sanfordburnham.org/wp-content/uploads/2012/12/CXCR11_top10.jpg)
3D structure of CXCR1, a G protein-coupled receptor that transmits inflammatory signals [Image courtesy of Stanley Opella, UCSD]
Cellular sensor’s 3D structure reveals new clues for combating cancer
Originally published October 23, 2012
Scientists have, for the first time, determined the three-dimensional structure of a complete, unmodified G-protein-coupled receptor (GPCR) in its native environment: embedded in a lipid membrane.
The team, led by Stanley Opella, Ph.D. at the University of California, San Diego and Francesca Marassi, Ph.D. at Sanford-Burnham Medical Research Institute, used a technique called NMR spectroscopy to map the arrangement of atoms in one particular GPCR, called CXCR1. Their finding was published by Nature on October 21.
Lung X-ray, with a possible tumor shown on the right (Image courtesy of National Cancer Institute)
Researchers discover mechanism that promotes lung cancer growth and survival
Originally published June 18, 2012
Sanford-Burnham researchers and their collaborators uncovered a new mechanism that may lead to unique treatments for lung cancer, one of the leading causes of death worldwide.
In the study, published May 15 in the journal Genes & Development, the team discovered that a protein called Bax Inhibitor-1 (BI-1) protects lung cancer cells and promotes tumor growth by regulating autophagy, a mechanism by which cells break down their own components and recycle the parts. Autophagy, which literally means “to eat oneself,” is essential to cell survival, particularly when food is scarce.
“Cancer cells are remarkably adaptive and depend on a variety of mechanisms to ensure their survival and continued growth when challenged by their environment,” says John C. Reed, M.D., Ph.D., Sanford-Burnham’s CEO and senior author of the study. “By reducing levels of BI-1, it appears we were able to modulate intracellular signals and starve lung cancer cells of the energy needed to carry out one of their most important survival mechanisms—autophagy.”
Liam
Finding the cause of Liam’s metabolic disease
Originally published February 7, 2012
Sequencing a patient’s entire genome to discover the source of his or her disease is not routine – yet. But geneticists are getting close.
A case report, published February 2 in the American Journal of Human Genetics, shows how researchers can combine a simple blood test with an “executive summary” scan of the genome to diagnose a type of severe metabolic disease. In the study, researchers at Emory University School of Medicine and Sanford-Burnham used whole-exome sequencing to find the mutations causing a glycosylation disorder affecting Liam, a boy born in 2004.
Whole-exome sequencing reads only the parts of the human genome that encode proteins, leaving the other 99 percent of the genome unread. This method is cheaper and faster than whole-genome sequencing, but is still an efficient strategy for reading the parts of the genome scientists believe are the most important for diagnosing disease. It is estimated that most disease-causing mutations (around 85 percent) are found within the regions of the genome that encode proteins, the workhorse machinery of the cell. The report illustrates how whole-exome sequencing, which was first offered commercially for clinical diagnosis in 2011, is entering medical practice. Emory Genetics Laboratory is now gearing up to start offering whole-exome sequencing as a clinical diagnostic service.
![3D structure of CXCR1, a G protein-coupled receptor that transmits inflammatory signals [Image courtesy of Stanley Opella, UCSD]](http://beaker.sanfordburnham.org/wp-content/uploads/2012/10/CXCR11.jpg)
3D structure of CXCR1, a G protein-coupled receptor that transmits inflammatory signals [Image courtesy of Stanley Opella, UCSD]
Scientists have, for the first time, determined the three-dimensional structure of a complete, unmodified G-protein-coupled receptor (GPCR) in its native environment: embedded in a lipid membrane.
The team, led by Stanley Opella, Ph.D. at the University of California, San Diego and Francesca Marassi, Ph.D. at Sanford-Burnham Medical Research Institute, used a technique called NMR spectroscopy to map the arrangement of atoms in one particular GPCR, called CXCR1. Their finding was published by Nature on October 21.
What are GPCRs?
Scientists have long known that cells must have some sort of sensor that allows them to detect external signals like aromas, hormones, and neurotransmitters. Adrenalin, for example, hits the outside of a cell yet manages to trigger changes inside the cell—the “flight or fight” response—without actually entering it. For decades, the link between the outside of a cell and the inside remained unknown—until GPCRs were discovered by Robert J. Lefkowitz, M.D. and Brian K. Kobilka, M.D., a finding for which they were awarded the 2012 Nobel Prize in Chemistry earlier this month.
Ring forms of the Plasmodium falciparum (malaria) parasite, inside red blood cells (Image by Michael Zahniser)
An international team of scientists, including researchers at the University of California, San Diego (UCSD) and Sanford-Burnham Medical Research Institute, have identified the first reported inhibitors of a key enzyme involved in survival of the parasite responsible for malaria. Their findings, which may provide the basis for anti-malarial drug development, were published July 19 in the Journal of Medicinal Chemistry.
According to the World Health Organization, there were 216 million cases of malaria worldwide in 2010. Severe forms of the disease are mainly caused by the parasite Plasmodium falciparum, transmitted to humans by female Anopheles mosquitoes. Malaria eradication has not been possible due to the lack of vaccines and the parasite’s ability to develop resistance to most drugs.
HIV (gold) infecting a T cell (Image credit: NIAID)
The U.S. National Institutes of Health’s National Institute of Allergy and Infectious Diseases awarded a new seven-year grant to a team of researchers at The Scripps Research Institute, Sanford-Burnham Medical Research Institute, and several other institutions around the country. The funding—expected to total more than $77 million—will be used to establish the Center for HIV/AIDS Vaccine Immunology & Immunogen Discovery (CHAVI-ID).
CHAVI-ID researchers will study immune responses that prevent infection with HIV—the virus that causes AIDS—or control the virus in infected individuals. The team will also generate vaccine components to induce such immune responses and provide broad protection against HIV.
The World Health Organization estimates that 34 million people worldwide are living with HIV.
Lung X-ray, with a possible tumor shown on the right (Image courtesy of National Cancer Institute)
Sanford-Burnham researchers and their collaborators uncovered a new mechanism that may lead to unique treatments for lung cancer, one of the leading causes of death worldwide.
In the study, published May 15 in the journal Genes & Development, the team discovered that a protein called Bax Inhibitor-1 (BI-1) protects lung cancer cells and promotes tumor growth by regulating autophagy, a mechanism by which cells break down their own components and recycle the parts. Autophagy, which literally means “to eat oneself,” is essential to cell survival, particularly when food is scarce.
“Cancer cells are remarkably adaptive and depend on a variety of mechanisms to ensure their survival and continued growth when challenged by their environment,” says John C. Reed, M.D., Ph.D., Sanford-Burnham’s CEO and senior author of the study. “By reducing levels of BI-1, it appears we were able to modulate intracellular signals and starve lung cancer cells of the energy needed to carry out one of their most important survival mechanisms—autophagy.”
Normal cells containing green fluorescent protein (left) don't glow. In contrast, cells from a child with a glycosylation disorder (right) light up, signaling a genetic defect.
Just as Gotham City uses the Bat Signal to call for Batman’s aid, a new tool developed by Sanford-Burnham scientists should serve as the cellular equivalent for children with genetic diseases known as congenital disorders of glycosylation (CDG). In a new report appearing online June 12 in The FASEB Journal, the scientists describe how they used a green fluorescent protein originally isolated from jellyfish to identify the presence of genes—known and unknown—associated with CDG. By being able to identify exactly which genes are defective, researchers can develop therapies to correct the root causes of these diseases, rather than merely treating the symptoms.
John Reed (right) interviews Eric Topol in the latest "Medscape One-on-One" episode
In the latest episode of Medscape One-on-One, Sanford-Burnham CEO John Reed, M.D., Ph.D. interviews Eric Topol, M.D., author of The Creative Destruction of Medicine, about how technology is changing medicine, making diagnosis and treatment faster, better, and more accurate. In his book, Topol, chief academic officer of Scripps Health and director of the Scripps Translational Science Institute, discusses this digital revolution and how it can change medicine for the better—but only if we let it or if we have the will to do it.
Click here to watch the full interview or read the transcript.
Read the English version of this post here.
El 5 de junio de California tendra las ellecciones primarias, los votantes tendrán la oportunidad de considerar la Proposición 29 de la Ley de Investigación de Cáncer de California (CCRA). CCRA tiene como objetivo proporcionar fondos para la investigación del cáncer mediante el aumento de impuesto de $1 sobre una cajetilla de cigarrillos. Actualmente el impuesto de California sobre un paquete de cigarillos es de solo 87 centavos es uno de los mas bajos de la nacion.
Read the Spanish version of this post here.
On California’s June 5 primary ballot, voters will have an opportunity to consider Proposition 29, the California Cancer Research Act (CCRA). CCRA’s goal is to provide funding for cancer research by increasing the tax on a pack of cigarettes by $1. At 87 cents per pack, California’s tax on cigarettes is currently among the lowest in the nation.
California Cancer Research Act by the numbers:
June 5, 2012
Passing Proposition 29 would mean:
$1 increase in tax per-pack of cigarettes
$735 million total generated annually
$441 million per year for research on cancer and tobacco-related diseases
$110 million per year for facilities and equipment to support research
9-member Citizen’s Oversight Committee, including 3 directors from California’s National Cancer Institute-designated Cancer Centers