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<title>PHYSorg.com: PHYSorg news tagged with: prion</title>
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<description>Physorg.com internet news portal provides the latest news on science including: Physics, Nanotechnology, Life Sciences, Space Science, Earth Science, Environment, Health and Medicine.</description>

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     <title>Family's inherited condition links prion diseases, Alzheimer's </title>
   	 <description>(PhysOrg.com) -- A laboratory connection between Alzheimer's disease and brain-wasting diseases such as the human form of mad cow disease has moved into the clinic for what is believed to be the first time, manifesting itself in the brains of patients with a rare inherited disorder.</description>
     <link>http://www.physorg.com/news179570626.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Wed, 09 Dec 2009 08:45:01 EST</pubDate>
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     <title>Researchers find new piece of BSE puzzle</title>
   	 <description>A new treatment route for bovine spongiform encephalopathy (BSE) and its human form Creutzfeldt Jakob disease (CJD) could be a step closer based on new results from scientists at the University of Leeds. The team has found that a protein called Glypican-1 plays a key role in the development of BSE. Details are published November 20 in the open-access journal PLoS Pathogens.</description>
     <link>http://www.physorg.com/news177917282.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Fri, 20 Nov 2009 05:28:23 EST</pubDate>
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     <title>The protein Srebp2 drives cholesterol formation in prion-infected neuronal cells</title>
   	 <description>Prions are causing fatal and infectious diseases of the nervous system, such as the mad cow disease (BSE), scrapie in sheep or Creutzfeldt-Jakob disease in humans. Scientists of Helmholtz Zentrum München and Technische Universit&amp;auml;t München, Germany, have now succeeded in elucidating another disease mechanism of prion diseases: The prion-infected cell changes its gene expression and produces increased quantities of cholesterol. Prions need this for their propagation.</description>
     <link>http://www.physorg.com/news177760967.html</link>
	 <category>Chemistry</category>
	 <pubDate>Wed, 18 Nov 2009 10:03:51 EST</pubDate>
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     <title>First direct information about the prion's molecular structure reported</title>
   	 <description>(PhysOrg.com) -- A collaboration between scientists at Vanderbilt University and the University of California, San Francisco has led to the first direct information about the molecular structure of prions. In addition, the study has revealed surprisingly large structural differences between natural prions and the closest synthetic analogs that scientists have created in the lab.</description>
     <link>http://www.physorg.com/news173974213.html</link>
	 <category>Chemistry</category>
	 <pubDate>Mon, 05 Oct 2009 15:10:48 EST</pubDate>
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     <title>Scientists uncover evolutionary origins of prion disease gene</title>
   	 <description>A University of Toronto-led team has uncovered the evolutionary ancestry of the prion gene, which may reveal new understandings of how the prion protein causes diseases such as bovine spongiform encephalopathy (BSE), also known as "mad cow disease."</description>
     <link>http://www.physorg.com/news173359598.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Mon, 28 Sep 2009 12:27:22 EST</pubDate>
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     <title>Gene mutation alone causes transmissible prion disease</title>
   	 <description>For the first time, Whitehead Institute researchers have shown definitively that mutations associated with prion diseases are sufficient to cause a transmissible neurodegenerative disease.</description>
     <link>http://www.physorg.com/news170511514.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Wed, 26 Aug 2009 13:25:01 EST</pubDate>
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     <title>Impaired transport in neurons triggers prion disease</title>
   	 <description>A new study shows that nervous system integrity and axonal properties may play a key role in prion diseases. The findings, from researchers at the Rudolf Virchow Center and the Institute of Virology of the University of Würzburg, expand our understanding of the development of prion disease and suggest novel targets for therapeutic and diagnostic approaches in its early stages. Details are published August 21 in the open-access journal PLoS Pathogens.</description>
     <link>http://www.physorg.com/news170079903.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Fri, 21 Aug 2009 13:28:20 EST</pubDate>
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     <title>Prion protein identified as a novel early pancreatic cancer biomarker</title>
   	 <description>Mad cow disease is caused by the accumulation of an abnormal protein, the prion, in the brain of an affected patient. Outside of the brain, very little is known about prions. Case Western Reserve University School of Medicine, researchers have, for the first time, identified the prion as a biomarker for pancreatic cancer. Pancreatic cancer is one of the most deadly cancers in humans; the five year survival rate is less than 10 percent.</description>
     <link>http://www.physorg.com/news169751882.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Mon, 17 Aug 2009 22:50:01 EST</pubDate>
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     <title>Species barrier may protect macaques from chronic wasting disease</title>
   	 <description>Data from an ongoing multi-year study suggest that people who consume deer and elk with chronic wasting disease (CWD) may be protected from infection by an inability of the CWD infectious agent to spread to people. The results to date show that 14 cynomolgus macaques exposed orally or intracerebrally to CWD remain healthy and symptom free after more than six years of observation, though the direct relevance to people is not definitive and remains under study.  </description>
     <link>http://www.physorg.com/news168178047.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Thu, 30 Jul 2009 13:13:59 EST</pubDate>
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     <title>A penny for your prions: Researchers study link between copper, mad cow disease</title>
   	 <description>(PhysOrg.com) -- North Carolina State University researchers have discovered a link between copper and the normal functioning of prion proteins, which are associated with transmissible spongiform encephalopathy diseases such as Cruetzfeldt-Jakob in humans or "mad cow" disease in cattle. </description>
     <link>http://www.physorg.com/news165161592.html</link>
	 <category>Chemistry</category>
	 <pubDate>Thu, 25 Jun 2009 19:20:01 EST</pubDate>
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     <title>Scientists devise accelerated method to determine infectious prion strains</title>
   	 <description>Current tests to identify specific strains of infectious prions, which cause a range of transmissible diseases (such as mad cow) in animals and humans, can take anywhere from six months to a year to yield results - a time-lag that may put human populations at risk.</description>
     <link>http://www.physorg.com/news162818825.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Fri, 29 May 2009 12:27:34 EST</pubDate>
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     <title>Study points to disruption of copper regulation as key to prion diseases</title>
   	 <description>(PhysOrg.com) -- An investigation of a rare, inherited form of Creutzfeldt-Jakob disease suggests that disrupted regulation of copper ions in the brain may be a key factor in this and other prion diseases.</description>
     <link>http://www.physorg.com/news159170135.html</link>
	 <category>Chemistry</category>
	 <pubDate>Fri, 17 Apr 2009 06:55:57 EST</pubDate>
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     <title>Prions serve as important source of variation in nature</title>
   	 <description>Special proteins known as prions, which are perhaps best known as the agents of mad cow and other neurodegenerative diseases, can also serve as an important source of beneficial variation in nature, confirms a new study in the April 3rd issue of the journal Cell, a Cell Press publication. After an extensive search through the genome of yeast for proteins with prion-like character, the researchers found two dozen prion-forming proteins, most of which had never been seen before.</description>
     <link>http://www.physorg.com/news157897000.html</link>
	 <category>Biology</category>
	 <pubDate>Thu, 02 Apr 2009 13:17:29 EST</pubDate>
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     <title>Prion discovery gives clue to control of mass gene expression</title>
   	 <description>The discovery in common brewer's yeast of a new, infectious, misfolded protein -- or prion -- by University of Illinois at Chicago molecular biologists raises new questions about the roles played by these curious molecules, often associated with degenerative brain diseases like "mad cow" and its human counterpart, Creutzfeldt-Jakob.</description>
     <link>http://www.physorg.com/news156180264.html</link>
	 <category>Biology</category>
	 <pubDate>Fri, 13 Mar 2009 16:25:13 EST</pubDate>
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     <title>Iron is involved in prion disease-associated neuronal demise</title>
   	 <description>Imbalance of iron homeostasis is a common feature of prion disease-affected human, mouse, and hamster brains, according to a new study by Dr. Neena Singh and colleagues at Case Western Reserve University School of Medicine, alongside collaborators from Creighton University. These findings, published March 13 in the open-access journal PLoS Pathogens, provide new insight into the mechanism of neurotoxicity in prion disorders, and novel avenues for the development of therapeutic strategies.</description>
     <link>http://www.physorg.com/news156173016.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Fri, 13 Mar 2009 14:25:12 EST</pubDate>
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     <title>What drove the cow mad? Lessons from a tiny fish</title>
   	 <description>For over twenty years, scientists have known that a normal protein in the brain, PrP, or prion protein, can turn harmful and cause deadly illnesses like Creutzfeldt-Jakob disease (CJD) in humans, and bovine spongiform encephalopathy (BSE) in cattle. What they could not explain is why large amounts of this normal protein are produced by our bodies in the first place. In a new study published in this week's PLoS Biology, researchers from the University of Konstanz in Germany reveal that PrP indeed plays a beneficial role for the organism - PrP helps cells communicate with one another during embryonic development.</description>
     <link>http://www.physorg.com/news155888796.html</link>
	 <category>Biology</category>
	 <pubDate>Tue, 10 Mar 2009 07:27:30 EST</pubDate>
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     <title>Antibody key to treating variant CJD, scientists find</title>
   	 <description>Scientists at the University of Liverpool have determined the atomic structure of the 'binding' between a brain protein and an antibody that could be key to treating patients with diseases such as variant CJD.</description>
     <link>http://www.physorg.com/news155385671.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Wed, 04 Mar 2009 10:41:36 EST</pubDate>
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     <title>Researchers find new piece in Alzheimer's puzzle</title>
   	 <description>Yale researchers have filled in a missing gap on the molecular road map of Alzheimer's disease. In the Feb. 26 issue of the journal Nature, the Yale team reports that cellular prion proteins trigger the process by which amyloid-beta peptides block brain function in Alzheimer's patients.</description>
     <link>http://www.physorg.com/news154790497.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Wed, 25 Feb 2009 13:22:13 EST</pubDate>
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     <title>Sticky antibodies block prion disease</title>
   	 <description>(PhysOrg.com) -- Antibodies that stick to a brain prion protein called PrP could be the key to treating prion diseases like variant CJD and preventing people accidentally exposed to prions from going on to develop the fatal brain disease. Using a precise visualisation technique, called X-ray crystallography, carried out at the Synchrotron Radiation Source (SRS) at the Science and Technology Facilities Councils (STFC) Daresbury Laboratory in Cheshire, scientists have identified an antibody that has the best ability to bind to PrP in the brain. Experiments using cells in the laboratory and in mice have suggested it could stop prion infection in its tracks.</description>
     <link>http://www.physorg.com/news153681509.html</link>
	 <category>Biology</category>
	 <pubDate>Thu, 12 Feb 2009 17:18:48 EST</pubDate>
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     <title>Mutant proteins result in infectious prion disease in mice</title>
   	 <description>A worldwide group of scientists has created an infectious prion disease in a mouse model, in a step that may help unravel the mystery of this progressive disease that affects the nervous system in humans and animals.  The research team, including Christina J. Sigurdson, D.V.M., Ph.D., assistant professor of pathology at the University of California, San Diego School of Medicine, also discovered that changing the structure of the prion protein by altering just two nucleic acids leads to a fatal neurological disorder in mice. Their findings will be published on line in Proceedings of the National Academy of Sciences (PNAS) the week of December 1.</description>
     <link>http://www.physorg.com/news147702312.html</link>
	 <category>Biology</category>
	 <pubDate>Fri, 05 Dec 2008 12:25:12 EST</pubDate>
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     <title>Prion infectivity found in white and brown fat tissues of mice</title>
   	 <description>Researchers from the National Institutes of Health and the Scripps Research Institute have found novel prion infectivity in white and brown fat tissues of mice.  The study appears December 5 in the open-access journal PLoS Pathogens.</description>
     <link>http://www.physorg.com/news147698270.html</link>
	 <category>Biology</category>
	 <pubDate>Fri, 05 Dec 2008 11:17:50 EST</pubDate>
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     <title>Mouse model of prion disease mimics diverse symptoms of human disorder</title>
   	 <description>A comprehensive mouse model of inherited prion disease exhibits cognitive, motor, and neurophysiological deficits that bear a striking resemblance to the symptoms experienced by patients with the human version of "mad cow disease," Creutzfeldt-Jakob disease (CJD). The research, published by Cell Press in the November 26th issue of the journal Neuron, provides exciting insight into the mechanism of disease and may lead to the development of new therapeutic strategies for this devastating neurodegenerative disorder.</description>
     <link>http://www.physorg.com/news146922723.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Wed, 26 Nov 2008 11:52:03 EST</pubDate>
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     <title>Prion switching in response to environmental stress</title>
   	 <description>If you have had a hard day at work, you may change your eating habits, perhaps favoring comfort food, but you don't suddenly develop the ability to eat the plate and cutlery. A new paper, published in this week's issue of PLoS Biology, describes an evolutionary mechanism in yeast that allows cells to respond to environmental stress in novel ways, including digesting materials that they were previously unable to use  - though admittedly, they aren't eating crockery just yet! The work shows that a protein-misfolding mechanism that can reveal hidden genetic variation is far more likely to be triggered when yeast is under environmental stress, and is therefore an evolutionary strategy to trigger rapid evolution. </description>
     <link>http://www.physorg.com/news146813034.html</link>
	 <category>Biology</category>
	 <pubDate>Tue, 25 Nov 2008 05:23:54 EST</pubDate>
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     <title>Tracking Down the Cause of Mad Cow Disease</title>
   	 <description>(PhysOrg.com) -- The cause of diseases such as BSE in cattle and Creutzfeld -Jakob disease in humans is a prion protein. This protein attaches to cell membranes by way of an anchor made of sugar and lipid components (a glycosylphosphatidylinositol, GPI) anchor. The anchoring of the prions seems to have a strong influence on the transformation of the normal form of the protein into its pathogenic form, which causes scrapie and mad cow disease.</description>
     <link>http://www.physorg.com/news142595542.html</link>
	 <category>Chemistry</category>
	 <pubDate>Tue, 07 Oct 2008 10:52:22 EST</pubDate>
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     <title>Is there more to prion protein than mad cow disease?</title>
   	 <description>Prion protein, a form of protein that triggers BSE, is associated with other brain diseases in cattle, raising the possibility of a significant increase in the range of prion disease. Publishing their findings in the open access journal BMC Veterinary Research, scientists have detected changes in the production and accumulation of the prion protein in the brains of cattle with a rare neurodegenerative disorder.</description>
     <link>http://www.physorg.com/news141989399.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Tue, 30 Sep 2008 10:29:59 EST</pubDate>
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     <title>Protective pathway in stressed cells not so helpful when it comes to prions</title>
   	 <description>Scientists at the National Institutes of Health (NIH) have discovered that an important cellular quality control mechanism may actually be toxic to some brain cells during prion infection. The research, published by Cell Press in the September 16th issue of the journal Developmental Cell, proposes a new general mechanism of cellular dysfunction that can contribute to the devastating and widespread neuronal death characteristic of slowly progressing neurodegenerative diseases.</description>
     <link>http://www.physorg.com/news140701320.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Mon, 15 Sep 2008 12:42:00 EST</pubDate>
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     <title>Newresearch shows mad cow disease also caused by genetic mutation</title>
   	 <description>New findings about the causes of mad cow disease show that sometimes it may be genetic. "We now know it's also in the genes of cattle," said Juergen A. Richt, Regents Distinguished Professor of Diagnostic Medicine and Pathobiology at Kansas State University's College of Veterinary Medicine.</description>
     <link>http://www.physorg.com/news140411184.html</link>
	 <category>Medicine &amp; Health</category>
	 <pubDate>Fri, 12 Sep 2008 04:06:24 EST</pubDate>
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     <title>A novel approach in the molecular differentiation of prion strains</title>
   	 <description>A team from the French Food Safety Agency, Lyon, France, has identified a prion protein characteristic that is unique to some natural but unusual sheep scrapie cases.   This finding, reported August 29th in the open-access journal PLoS Pathogens, may provide a novel method by which to study prion diversity and their possible changes during cross-species transmission.</description>
     <link>http://www.physorg.com/news139206108.html</link>
	 <category>Biology</category>
	 <pubDate>Fri, 29 Aug 2008 05:21:48 EST</pubDate>
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