Saturday, April 11, 2009

Tid bits. I mean TWIT BITS

Huntington's Chorea

Twit Bit-
http://bit.ly/qLlOj

Howard Hughes Medical Institute researchers have designed tiny RNA molecules that shut off the gene that causes Huntington's disease without damaging that gene's healthy counterpart, which maintains the health and vitality of neurons. Laboratory studies suggest that a single small interfering RNA could reduce production of the damaging Huntingtin protein in nearly half of people with the disease. Another 25 percent of patients might benefit from one of a set of four additional small interfering RNAs.
Phillip D. Zamore, an HHMI investigator at the University of Massachusetts Medical School in Worcester, and his colleagues reported their findings in an article published April 9, 2009, in the journal Current Biology.
There is no treatment for Huntington's disease, which is caused by a mutant form of the Huntingtin gene. Huntingtin is required for healthy nerve cells, but the mutant gene makes a toxic protein that contains excess amounts of the amino acid glutamine.
The key to whether the Huntingtin gene is normal or defective lies in a kind of genetic stutter: a repetitive sequence of the DNA triplet CAG, which codes for the amino acid glutamine. Stretches of CAG "repeats" appear in every human being's Huntingtin gene, but the length varies. Whereas the normal gene has a sequence of between six and 34 CAG repeats, the abnormal gene contains many more. In fact, any stretch of DNA containing more than 40 of these repeats ensures that its bearer will develop Huntington'sthe greater the number of repeats, the earlier the disease strikes and the greater its ferocity. The abnormal Huntingtin protein causes movement disorders, cognitive failure, and ultimately, death. Children who have a parent with Huntington's disease have a 50 percent chance of inheriting the disease themselves.
Zamore studies how RNA interference can be used to silence genes selectively. In the 1990s, he and other scientists
Contact: Jennifer Michalowski
mailto:Michalowskimichalow@hhmi.org
301-215-8576
Howard Hughes Medical InstituteSource:Eurekalert

On Globlastomas
Could Antineoplastins work the same way?
Twit BIT-
http://bit.ly/1IYCC

CHAPEL HILL Researchers at the University of North Carolina at Chapel Hill School of Medicine have identified a compound that could be modified to treat one of the most deadly types of cancer, and discovered how a particular gene mutation contributes to tumor growth.
The findings and potential treatment apply to a type of brain tumor called secondary glioblastoma multiforme (GBM). GBMs are part of a larger group of brain tumors called malignant gliomas, which is the type of cancer Senator Edward Kennedy suffers from.
A report of the research will appear in the April 10, 2009 issue of the journal Science. In experiments with tumor cells, the researchers reversed the effects of a mutation in a gene called isocitrate dehydrogenase-1 (IDH1) by replenishing a compound called α-ketoglutarate (α-KG).
"When the IDH1 gene is mutated, the level of α-KG is reduced, which in turn contributes to tumor growth by helping to increase the supply of nutrients and oxygen to tumor cells. When we added the α-KG to tumor cells, the effects caused by the IDH1 mutation were reversed," said Yue Xiong, Ph.D., William R. Kenan Jr., Distinguished Professor of Biochemistry and Biophysics and a member of the UNC Lineberger Comprehensive Cancer Center.
"If scientists can develop α-KG into a clinical drug, it could potentially be used for treating brain tumor patients who have this specific gene mutation. The α-KG compound is already there; it only needs to be modified to be used clinically, so that may save a lot of time," Xiong said.
Xiong is a corresponding author of the study along with Kun-Liang Guan, Ph.D., professor of pharmacology at the University of California, San Diego. The findings and potential treatment apply mostly to secondary GBM, rather than a different type of tumor called primary GBM. About 75 percent of secondary GBMs have mutations in the IDH1 gene, but only 5 percent of primary GBMs
Contact: Dianne Shawdgs@med.unc.edu919-966-7834University of North Carolina School of MedicineSource:Eurekalert

On Cloud computing of protein ressearh
Twit bit -
http://bit.ly/tOmf

Researchers at the Medical College of Wisconsin Biotechnology and Bioengineering Center in Milwaukee have just made the very expensive and promising area of protein research more accessible to scientists worldwide.
They have developed a set of free tools called ViPDAC (virtual proteomics data analysis cluster), to be used in combination with Amazon's inexpensive "cloud computing" service, which provides the option to rent processing time on its powerful servers; and free open-source software from the National Institutes of Health (NIH) and the University of Manitoba.
Their research appears online in Journal of Proteomic Research and is funded by the NIH Heart Lung and Blood Institute's Proteomics Innovation Center at the Medical College. Proteomics is a biomedical research term used to describe the large-scale study of all the proteins expressed by an organism. It usually involves the identification of proteins and determination of their modifications in both normal and disease states.
One of the major challenges for many laboratories setting up proteomics programs has been obtaining and maintaining the very costly computational infrastructure required for analysis of the vast flow of proteomics data generated by mass spectrometry instruments used to determine the elemental composition as well as chemical structure of a molecule, according to senior investigator, Simon Twigger, Ph.D., assistant professor of physiology.
"We're applying this technology in our Proteomics Center to study cardiovascular disease, the effects of radiation damage, and in our collaboration with the University of Wisconsin- Madison stem cell research group," he says.
With cloud computing making the analysis less expensive and more accessible, many more users can set up and customize their own systems. Investigators can analyze their data in greater depth than previously possible, making it possible for them to learn more about t'/>"/>

Contact: Eileen La Susalasusa@mcw.edu414-456-4700Medical College of WisconsinSource:Eurekalert

ON Protein Increase in PLANTS for FOOD
For my Twitters - http://bit.ly/KTcME
RIVERSIDE, Calif. The small flowering plant Arabidopsis is widely used in laboratories as a model organism in plant biology.
A member of the mustard family, Arabidopsis offers researchers several advantages such as a completely sequenced genome, a compact size, a life-cycle of about only six weeks from seed to seed, easy cultivation and high seed production.
Now Daniel Gallie, a professor of biochemistry at UC Riverside, has received a three-year grant of nearly $1.75 million from the National Science Foundation to study how each Arabidopsis gene is converted into protein and how plants control this process.
The research can help improve protein production in crops. Protein-rich crops improve the diet of humans directly and promote livestock productivity for a growing world population. Besides their nutritional advantages, these crops also reduce the environmental impact of livestock production by potentially reducing the acreage required for agriculture.
"Understanding how most genes, out of the more than 25,000 genes in Arabidopsis, are converted into protein will be important in understanding how plants control protein synthesis," Gallie said. "This knowledge is essential in improving protein production in crops."
With the advent of the complete sequence of the genome of Arabidopsis and other plant species, researchers are now in a position of being able to understand how every gene in an organism is converted into protein.
"This, in conjunction with the development of other recent technologies, such as the ability to identify mutants in most genes as well as to analyze virtually all genes in Arabidopsis on a chip no larger than a fingertip, makes such a study possible for the first time," Gallie said.
He explained that the process of protein producti'/>"/>

Contact: Iqbal Pittalwalaiqbal@ucr.edu951-827-6050University of California - RiversideSource:Eurekalert

On Information transfer

URL- http://www.youtube.com/watch?v=VQ3d3KigPQM

Bit - http://bit.ly/1AbtCW

On Dancing
URL - http://www.youtube.com/watch?v=cL9Wu2kWwSY
Bit- http://bit.ly/MbliY

I love you! I love you in Jesus name and there is nothing that you can do about it!

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