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			<title>ScienceDaily: Prion News</title>
			<link>http://www.sciencedaily.com/news/plants_animals/prions/</link>
			<description>Learn all about prions and prion disease. How are prions linked to mad cow disease, TSE, Creutzfeldt-Jacob disease and chronic wasting disease?</description>
			<language>en-us</language>
			<pubDate>Wed, 15 Feb 2012 21:05:01 EST</pubDate>
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				<title>ScienceDaily: Prion News</title>
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				<link>http://www.sciencedaily.com/news/plants_animals/prions/</link>
				<description>For more science articles, visit ScienceDaily.</description>
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				<title>Most lethal known species of prion protein identified</title>
				<link>http://www.sciencedaily.com/releases/2012/02/120209152814.htm</link>
				<description>Scientists have identified a single prion protein that causes neuronal death similar to that seen in &quot;mad cow&quot; disease, but is at least 10 times more lethal than larger prion species.</description>
				<pubDate>Thu, 09 Feb 2012 15:28:28 EST</pubDate>
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				<title>New findings about the prion protein and its interaction with the immune system</title>
				<link>http://www.sciencedaily.com/releases/2011/12/111229091638.htm</link>
				<description>Scrapie is a neurodegenerative disease which can function as a model for other diseases caused by an accumulation of proteins resulting in tissue malformations (proteinpathies), such as Alzheimer&#39;s and Parkinson&#39;s disease. Many questions regarding these diseases still remain unanswered. A new study has uncovered a number of factors relating to the uptake of the prion protein (PrPSc) associated with the development of this disease and how this protein interacts with the immune cells in the intestines.</description>
				<pubDate>Thu, 29 Dec 2011 09:16:16 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/12/111229091638.htm</guid>
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				<title>Cellular stress can induce yeast to promote prion formation</title>
				<link>http://www.sciencedaily.com/releases/2011/07/110722213431.htm</link>
				<description>Biochemists have identified a yeast protein called Lsb2 that can promote spontaneous prion formation. Prions can cause neurodegenerative disorders, such as mad cow/Creutzfeld-Jakob disease, in humans and animals.</description>
				<pubDate>Fri, 22 Jul 2011 21:34:34 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/07/110722213431.htm</guid>
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				<title>Tracking down BSE and Creutzfeldt-Jakob disease</title>
				<link>http://www.sciencedaily.com/releases/2011/06/110630091701.htm</link>
				<description>Researchers have identified an altered expression of endogenous retroviruses in BSE-infected macaques.</description>
				<pubDate>Thu, 30 Jun 2011 09:17:17 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/06/110630091701.htm</guid>
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				<title>Two gene classes linked to new prion formation</title>
				<link>http://www.sciencedaily.com/releases/2011/05/110526122911.htm</link>
				<description>Researchers have discovered two classes of yeast genes that may hold clues as to why proteins take on the misfolded prion form, a condition associated with several neurodegenerative diseases, such as &quot;mad cow.&quot;</description>
				<pubDate>Thu, 26 May 2011 12:29:29 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/05/110526122911.htm</guid>
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				<title>Potential human exposure to prion diseases assessed</title>
				<link>http://www.sciencedaily.com/releases/2011/05/110523075314.htm</link>
				<description>Researchers have examined the potential for human exposure to prion diseases, looking at hunting, venison consumption, and travel to areas in which prion diseases have been reported in animals. Three prion diseases in particular -- bovine spongiform encephalopathy, variant Creutzfeldt-Jakob disease and chronic wasting disease -- were specified in the investigation.</description>
				<pubDate>Mon, 23 May 2011 07:53:53 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/05/110523075314.htm</guid>
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				<title>Lichens may aid in combating deadly chronic wasting disease in wildlife</title>
				<link>http://www.sciencedaily.com/releases/2011/05/110518141710.htm</link>
				<description>Certain lichens can break down the infectious proteins responsible for chronic wasting disease (CWD), a troubling neurological disease fatal to wild deer and elk and spreading throughout the United States and Canada.</description>
				<pubDate>Wed, 18 May 2011 14:17:17 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/05/110518141710.htm</guid>
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				<title>Fast, sensitive blood test for human prion disease</title>
				<link>http://www.sciencedaily.com/releases/2011/05/110509171851.htm</link>
				<description>Scientists have developed a method -- 10,000 times more sensitive than other methods -- to detect variant Creutzfeldt-Jacob disease (vCJD) in blood plasma. vCJD is a type of prion disease in humans that leads to brain damage and death. The researchers also used the test to rapidly detect scrapie, a prion disease of sheep, in infected hamsters, some pre-symptomatic.</description>
				<pubDate>Mon, 09 May 2011 17:18:18 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/05/110509171851.htm</guid>
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				<title>New research focuses on prion diseases</title>
				<link>http://www.sciencedaily.com/releases/2011/03/110314163602.htm</link>
				<description>New research may shed light on possible treatments for prion diseases.</description>
				<pubDate>Mon, 14 Mar 2011 16:36:36 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/03/110314163602.htm</guid>
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				<title>Unraveling how prion proteins move along axons in the brain</title>
				<link>http://www.sciencedaily.com/releases/2011/02/110217125111.htm</link>
				<description>Researchers have identified the motors that move non-infectious prion proteins -- found within many mammalian cells -- up and down long, neuronal transport pathways. Identifying normal movement mechanisms of PrPC may help researchers understand the spread of infectious prions within and between neurons to reach the brain, and aid in development of therapies to halt the transport.</description>
				<pubDate>Thu, 17 Feb 2011 12:51:51 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/02/110217125111.htm</guid>
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				<title>Prion disease spreads in sheep via mother&#39;s milk</title>
				<link>http://www.sciencedaily.com/releases/2011/01/110119191350.htm</link>
				<description>Transmission of prion brain diseases such as bovine spongiform enecephalopathy (BSE) -- also known as mad cow disease -- and human variant Creutzfeldt-Jakob disease (vCJD) is generally attributed to the consumption of the brain or organ meat of infected animals but new research demonstrates lambs exposed to milk from prion-infected sheep with inflamed mammary glands can develop prion disease as well. The research has major implications for human and livestock health.</description>
				<pubDate>Wed, 19 Jan 2011 19:13:13 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/01/110119191350.htm</guid>
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				<title>Airborne pathogens can induce mad cow disease, new findings suggest</title>
				<link>http://www.sciencedaily.com/releases/2011/01/110113213056.htm</link>
				<description>Airborne prions are also infectious and can induce mad cow disease or Creutzfeldt-Jakob disorder, new findings suggest. Researchers recommend precautionary measures for scientific labs, slaughterhouses and animal feed plants.</description>
				<pubDate>Thu, 13 Jan 2011 21:30:30 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/01/110113213056.htm</guid>
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				<title>New drug target for prion diseases, &#39;mad cow&#39;</title>
				<link>http://www.sciencedaily.com/releases/2011/01/110110103838.htm</link>
				<description>Scientists have discovered that plasminogen, a protein used by the body to break up blood clots, speeds up the progress of prion diseases such as mad cow disease.</description>
				<pubDate>Mon, 10 Jan 2011 10:38:38 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2011/01/110110103838.htm</guid>
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				<title>Prions mutate and adapt to host environment</title>
				<link>http://www.sciencedaily.com/releases/2010/12/101217083232.htm</link>
				<description>Scientists have shown that prions, bits of infectious protein that can cause fatal neurodegenerative disease such as bovine spongiform encephalopathy (BSE) or &quot;mad cow disease,&quot; have the ability to adapt to survive in a new host environment.</description>
				<pubDate>Fri, 17 Dec 2010 08:32:32 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/12/101217083232.htm</guid>
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				<title>Early detection is possible for prion diseases, study suggests</title>
				<link>http://www.sciencedaily.com/releases/2010/12/101202181124.htm</link>
				<description>A fast test to diagnose fatal brain conditions such as mad cow disease in cattle and Creutzfeldt-Jakob disease in humans could be on the horizon, according to a new study. Researchers have developed a highly sensitive and rapid new method to detect and measure infectious agents called prions that cause these diseases.</description>
				<pubDate>Thu, 02 Dec 2010 18:11:11 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/12/101202181124.htm</guid>
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				<title>New prion discovery reveals drug target for mad cow disease and related illnesses</title>
				<link>http://www.sciencedaily.com/releases/2010/12/101201102601.htm</link>
				<description>In a new study, scientists have found that a protein our body uses to break up blood clots speeds up the progress of prion diseases. This substance, called plasminogen, is a new drug target for prion diseases in both humans and animals.</description>
				<pubDate>Wed, 01 Dec 2010 10:26:26 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/12/101201102601.htm</guid>
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				<title>Size of protein aggregates, not abundance, drives spread of prion-based disease</title>
				<link>http://www.sciencedaily.com/releases/2010/10/101028141751.htm</link>
				<description>In a study that challenges the conventional wisdom about infections caused by proteins called prions, researchers report that the size of protein structures, rather than their abundance, determines their transmission among cells.</description>
				<pubDate>Thu, 28 Oct 2010 14:17:17 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/10/101028141751.htm</guid>
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				<title>Eye test for neurological diseases in livestock developed</title>
				<link>http://www.sciencedaily.com/releases/2010/10/101019152606.htm</link>
				<description>Researchers have discovered that the eyes of sheep infected with scrapie return an intense, almost-white glow when they&#39;re hit with blue light. That finding suggests technologies can be developed to quickly and non-invasively test for transmissible spongiform encephalopathies, progressive and fatal neurological diseases such as mad cow disease.</description>
				<pubDate>Tue, 19 Oct 2010 15:26:26 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/10/101019152606.htm</guid>
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				<title>New sporadic prion protein disease: Variably protease-sensitive prionopathy shares genotype characteristics with Creutzfeldt-Jakob</title>
				<link>http://www.sciencedaily.com/releases/2010/08/100813110225.htm</link>
				<description>A new sporadic prion protein disease has been discovered. Variably protease-sensitive prionopathy, as it has been named, is the second type of complete sporadic disease to be identified since Creutzfeldt-Jakob disease was reported in the 1920s.</description>
				<pubDate>Fri, 13 Aug 2010 11:02:02 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/08/100813110225.htm</guid>
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				<title>Sequence and structure key to prion disease transmission</title>
				<link>http://www.sciencedaily.com/releases/2010/06/100614121556.htm</link>
				<description>Prion diseases are lethal neurodegenerative disorders that include Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy (BSE, commonly known as mad cow disease) in cows. New data generated in mice provides greater understanding of the factors that determine how easy it is for prion diseases to be transmitted to a new host species. This information provides new insight into a highly important food safety issue.</description>
				<pubDate>Mon, 14 Jun 2010 12:15:15 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/06/100614121556.htm</guid>
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				<title>Eyes of cattle may become new windows to detect mad cow disease</title>
				<link>http://www.sciencedaily.com/releases/2010/06/100602121111.htm</link>
				<description>The eyes may or may not be windows to the soul, as the old adage goes, but scientists are reporting evidence that a peek into the eyes of cattle may become the basis for a long-sought test to detect infection with the agent that causes Mad Cow Disease. That test could help prevent the disease from spreading in the food supply.</description>
				<pubDate>Wed, 02 Jun 2010 12:11:11 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/06/100602121111.htm</guid>
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				<title>New model for chronic wasting disease</title>
				<link>http://www.sciencedaily.com/releases/2010/05/100526103906.htm</link>
				<description>Scientists have generated a mouse model of cervid chronic wasting disease. Chronic wasting disease is a fatal prion-induced disease, similar to mad cow disease, that affects cervids such as deer, elk, and moose. It is a neurodegenerative disease typified by chronic weight-loss leading to death.</description>
				<pubDate>Wed, 26 May 2010 10:39:39 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/05/100526103906.htm</guid>
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				<title>New form of prion disease damages brain arteries</title>
				<link>http://www.sciencedaily.com/releases/2010/03/100304202246.htm</link>
				<description>Scientists investigating how prion diseases destroy the brain have observed a new form of the disease in mice that does not cause the sponge-like brain deterioration typically seen in prion diseases. Instead, it resembles a form of human Alzheimer&#39;s disease, cerebral amyloid angiopathy, that damages brain arteries.</description>
				<pubDate>Thu, 04 Mar 2010 20:22:22 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/03/100304202246.htm</guid>
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				<title>Researchers induce a new transmissible prion disease</title>
				<link>http://www.sciencedaily.com/releases/2010/02/100226211408.htm</link>
				<description>Researchers have conducted a study on prion disease and found that transmissible spongiform encephalopathy (TSE) can be induced without an outside catalyst like a virus.</description>
				<pubDate>Fri, 26 Feb 2010 21:14:14 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/02/100226211408.htm</guid>
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				<title>Prion protein in cell culture</title>
				<link>http://www.sciencedaily.com/releases/2010/02/100205115944.htm</link>
				<description>The fatal brain disease Creutzfeldt-Jakob in humans, BSE (bovine spongiform encephalopathy) in cattle and scrapie in sheep are so-called prion diseases, whereby one of the body&#39;s normal proteins, the prion protein PrPc misfolds into a pathogenic form: PrPSc. In spite of several years of extensive research, little is still known about what actually happens in this process.</description>
				<pubDate>Fri, 05 Feb 2010 11:59:59 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/02/100205115944.htm</guid>
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				<title>Spongiform brain diseases are caused by aberrant protein, new research shows</title>
				<link>http://www.sciencedaily.com/releases/2010/01/100128142137.htm</link>
				<description>Scientists have determined how a normal protein can be converted into a prion, an infectious agent that causes fatal brain diseases in humans and mammals. The finding, in mice, is expected to advance the understanding of transmissible spongiform encephalopathies, or TSEs, a family of neurodegenerative diseases that include Creutzfeldt-Jakob Disease, kuru and fatal familial insomnia in humans, scrapie in sheep, and bovine spongiform encephalopathy in cattle, also known as &quot;mad cow disease.&quot;</description>
				<pubDate>Thu, 28 Jan 2010 14:21:21 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2010/01/100128142137.htm</guid>
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				<title>&#39;Lifeless&#39; prions capable of evolutionary change and adaptation</title>
				<link>http://www.sciencedaily.com/releases/2009/12/091231164747.htm</link>
				<description>Scientists have determined for the first time that prions, bits of infectious protein devoid of DNA or RNA that can cause fatal neurodegenerative disease, are capable of Darwinian evolution.</description>
				<pubDate>Thu, 31 Dec 2009 16:47:47 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/12/091231164747.htm</guid>
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				<title>Researchers find new piece of bovine spongiform encephalopathy (BSE) puzzle</title>
				<link>http://www.sciencedaily.com/releases/2009/11/091119210836.htm</link>
				<description>A new treatment route for bovine spongiform encephalopathy (BSE) and its human form Creutzfeldt Jakob disease could be a step closer based on new results from scientists in the UK. The team has found that a protein called Glypican-1 plays a key role in the development of BSE.</description>
				<pubDate>Thu, 19 Nov 2009 21:08:08 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/11/091119210836.htm</guid>
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				<title>Protein Srebp2 drives cholesterol formation in prion-infected neuronal cells</title>
				<link>http://www.sciencedaily.com/releases/2009/11/091118101401.htm</link>
				<description>The regulating protein Srebp2 drives cholesterol formation, which prions need for their propagation, in prion-infected neuronal cells. Scientists anticipate new approaches in drug development to combat prion infection, as a result of these new findings</description>
				<pubDate>Wed, 18 Nov 2009 10:14:14 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/11/091118101401.htm</guid>
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				<title>First Direct Information About Prion&#39;s Molecular Structure Reported</title>
				<link>http://www.sciencedaily.com/releases/2009/10/091005161324.htm</link>
				<description>Scientists have discovered 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>
				<pubDate>Mon, 05 Oct 2009 16:13:13 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/10/091005161324.htm</guid>
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				<title>Evolutionary Origins Of Prion Disease Gene Uncovered</title>
				<link>http://www.sciencedaily.com/releases/2009/09/090928131210.htm</link>
				<description>Scientists have 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, also known as &quot;mad cow disease.&quot;</description>
				<pubDate>Mon, 28 Sep 2009 13:12:12 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/09/090928131210.htm</guid>
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				<title>Can Gene Expression Profiling Make It Possible To Predict Deadly Infections In Cattle?</title>
				<link>http://www.sciencedaily.com/releases/2009/09/090910191443.htm</link>
				<description>A new study suggests that gene expression profiling may allow researchers to track the progression of bovine spongiform encephalopathy (BSE) in cattle and ultimately predict their infectious status.</description>
				<pubDate>Thu, 10 Sep 2009 19:14:14 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/09/090910191443.htm</guid>
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				<title>Gene Mutation Alone Causes Transmissible Prion Disease</title>
				<link>http://www.sciencedaily.com/releases/2009/08/090826152550.htm</link>
				<description>Researchers have shown definitively that mutations associated with prion diseases are sufficient to cause a transmissible neurodegenerative disease. Until now, two theories about the role mutations play in prion diseases have been at odds. Deciphering the origins of prion diseases could help farmers and policy-makers determine how best to control a prion disease outbreak in livestock and to prevent prion transmission to humans.</description>
				<pubDate>Wed, 26 Aug 2009 15:25:25 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/08/090826152550.htm</guid>
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				<title>People Who Eat Deer And Elk With Chronic Wasting Disease May Avoid Infection Because Of Species Barrier, Study in Monkeys Suggests</title>
				<link>http://www.sciencedaily.com/releases/2009/07/090730111152.htm</link>
				<description>Data from an ongoing study in monkeys suggest that people who consume deer and elk with chronic wasting disease may be protected from infection by an inability of the CWD infectious agent to spread to people.</description>
				<pubDate>Thu, 30 Jul 2009 11:11:11 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/07/090730111152.htm</guid>
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				<title>Mad Cow And Related Diseases: Copper Linked To Normal Functioning Of Prions</title>
				<link>http://www.sciencedaily.com/releases/2009/06/090625141506.htm</link>
				<description>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 &quot;mad cow&quot; disease in cattle. Their work could have implications for patients suffering from these diseases, as well as from other prion-related diseases such as Alzheimers or Parkinson&#39;s.</description>
				<pubDate>Thu, 25 Jun 2009 14:15:15 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/06/090625141506.htm</guid>
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				<title>Farmed Fish May Pose Risk For Mad Cow Disease</title>
				<link>http://www.sciencedaily.com/releases/2009/06/090616080143.htm</link>
				<description>Neurologists questions the safety of eating farmed fish, adding a new worry to concerns about the nation&#8217;s food supply. They suggest farmed fish could transmit Creutzfeldt Jakob disease -- commonly known as mad cow disease -- if they are fed byproducts rendered from cows.</description>
				<pubDate>Tue, 16 Jun 2009 08:01:01 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/06/090616080143.htm</guid>
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				<title>Scientists Devise Accelerated Method To Determine Infectious Prion Strains</title>
				<link>http://www.sciencedaily.com/releases/2009/05/090528203819.htm</link>
				<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>
				<pubDate>Thu, 28 May 2009 20:38:38 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/05/090528203819.htm</guid>
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				<title>Closing In On Goat Scrapie</title>
				<link>http://www.sciencedaily.com/releases/2009/04/090419201836.htm</link>
				<description>Goats are tough, spirited animals, but they&#39;re no match for scrapie, a form of transmissible spongiform encephalopathy. Now, with a &quot;helping hand&quot; from science, the animals&#39; plight could take a turn for the better.</description>
				<pubDate>Sun, 19 Apr 2009 20:18:18 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/04/090419201836.htm</guid>
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				<title>Disruption Of Copper Regulation As Key To Prion Diseases</title>
				<link>http://www.sciencedaily.com/releases/2009/04/090417084124.htm</link>
				<description>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>
				<pubDate>Fri, 17 Apr 2009 08:41:41 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/04/090417084124.htm</guid>
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			<item>
				<title>Large Number Of New Prions Discovered: Scientists Redefining What It Means To Be A Prion</title>
				<link>http://www.sciencedaily.com/releases/2009/04/090402124320.htm</link>
				<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. Researchers have found a large number of new prions, greatly expanding scientists&#39; notion of how important prions might be in normal biology and demonstrating that they play many and varied roles in the inheritance of biological traits. Prions are misfolded proteins that clump together in cells. The most infamous known prion -- PrP -- causes bovine spongiform encephalitis, also known as &quot;mad cow&quot; disease.</description>
				<pubDate>Thu, 02 Apr 2009 12:43:43 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/04/090402124320.htm</guid>
			</item>
			<item>
				<title>Prion Discovery Gives Clue To Control Of Mass Gene Expression</title>
				<link>http://www.sciencedaily.com/releases/2009/03/090313171316.htm</link>
				<description>The discovery of a new yeast prion may provide clues on whether prions, like proteins, can affect mass activation of gene expression.</description>
				<pubDate>Fri, 13 Mar 2009 17:13:13 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/03/090313171316.htm</guid>
			</item>
			<item>
				<title>Iron Is Involved In Prion Disease-associated Neuronal Demise</title>
				<link>http://www.sciencedaily.com/releases/2009/03/090313145954.htm</link>
				<description>Imbalance of iron homeostasis is a common feature of prion disease-affected human, mouse, and hamster brains, according to a new study. These findings provide new insight into the mechanism of neurotoxicity in prion disorders, and novel avenues for the development of therapeutic strategies.</description>
				<pubDate>Fri, 13 Mar 2009 14:59:59 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/03/090313145954.htm</guid>
			</item>
			<item>
				<title>What Drove The Cow Mad? Lessons From A Tiny Fish</title>
				<link>http://www.sciencedaily.com/releases/2009/03/090309205323.htm</link>
				<description>Scientists have known for some time that a normal protein in the brain, prion protein (PrP), can turn harmful and cause deadly illnesses like CJD in humans, and BSE in cattle. What they could not explain is why this normal protein is produced by our bodies.</description>
				<pubDate>Mon, 09 Mar 2009 20:53:53 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/03/090309205323.htm</guid>
			</item>
			<item>
				<title>Potential Health Risks Associated With Stressed Foodstuffs Such As Foie Gras</title>
				<link>http://www.sciencedaily.com/releases/2009/02/090210092736.htm</link>
				<description>Harmful proteins fragments known as amyloid fibrils associated with damage to brain cells in Alzheimer&#39;s disease and to pancreatic cells in Type II diabetes can be present in the meat of poultry and mammals. These amyloids are not destroyed even with high-temperature cooking process.</description>
				<pubDate>Tue, 10 Feb 2009 09:27:27 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/02/090210092736.htm</guid>
			</item>
			<item>
				<title>New Disease, Comparable To BSE, Created In Laboratory Mice</title>
				<link>http://www.sciencedaily.com/releases/2009/01/090127214430.htm</link>
				<description>Scientists have created a new disease, comparable to BSE, in laboratory mice. They have shown that exchanging just two amino acids in the structure of the prion protein is enough to trigger a disease.</description>
				<pubDate>Tue, 27 Jan 2009 21:44:44 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/01/090127214430.htm</guid>
			</item>
			<item>
				<title>Intestinal Lymphatic Tissue Important For The Absorption And Spread Of The Scrapie Prion</title>
				<link>http://www.sciencedaily.com/releases/2009/01/090109095115.htm</link>
				<description>Scrapie is a transmissible, degenerative and ultimately fatal disease of the nervous system of sheep. The cause of the disease is a prion protein, and absorption from the intestine is assumed to be the natural route of infection. Lymphatic tissue associated with the intestine is important for the early accumulation of prion protein and its subsequent spread to the central nervous system.</description>
				<pubDate>Fri, 09 Jan 2009 09:51:51 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2009/01/090109095115.htm</guid>
			</item>
			<item>
				<title>New Mouse Model Of Prion Disease: Mutant Proteins Result In Infectious Prion Disease In Mice</title>
				<link>http://www.sciencedaily.com/releases/2008/12/081205122936.htm</link>
				<description>Scientists have 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.</description>
				<pubDate>Fri, 05 Dec 2008 12:29:29 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/12/081205122936.htm</guid>
			</item>
			<item>
				<title>Prion Infectivity Found In White And Brown Fat Tissues Of Mice</title>
				<link>http://www.sciencedaily.com/releases/2008/12/081205094509.htm</link>
				<description>Researchers have found novel prion infectivity in white and brown fat tissues of mice. Prion diseases, also known as transmissible spongiform encephalopathies, are infectious progressive fatal neurodegenerative diseases which affect humans as well as wild and domestic animals.</description>
				<pubDate>Fri, 05 Dec 2008 09:45:45 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/12/081205094509.htm</guid>
			</item>
			<item>
				<title>Mouse Model Of Prion Disease Mimics Diverse Symptoms Of Human Disorder</title>
				<link>http://www.sciencedaily.com/releases/2008/11/081126133300.htm</link>
				<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 &quot;mad cow disease,&quot; Creutzfeldt-Jakob disease. The research, published in 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>
				<pubDate>Wed, 26 Nov 2008 13:33:33 EST</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/11/081126133300.htm</guid>
			</item>
			<item>
				<title>Tracking Down The Cause Of Mad Cow Disease: First Synthetic Prion Protein With An Anchor</title>
				<link>http://www.sciencedaily.com/releases/2008/10/081008113430.htm</link>
				<description>Researchers in Germany and Switzerland have developed a new general method for the synthesis of anchored proteins, such as GPI-anchored prions, which cause scrapie and mad cow disease.</description>
				<pubDate>Wed, 08 Oct 2008 11:34:34 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/10/081008113430.htm</guid>
			</item>
			<item>
				<title>Is There More To Prion Protein Than Mad Cow Disease?</title>
				<link>http://www.sciencedaily.com/releases/2008/09/080929212926.htm</link>
				<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. Scientists have detected changes in the production and accumulation of the prion protein in the brains of cattle with a rare neurodegenerative disorder.</description>
				<pubDate>Mon, 29 Sep 2008 21:29:29 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/09/080929212926.htm</guid>
			</item>
			<item>
				<title>Mad Cow Disease Also Caused By Genetic Mutation</title>
				<link>http://www.sciencedaily.com/releases/2008/09/080912075208.htm</link>
				<description>New findings about the causes of mad cow disease show that sometimes it may be genetic. Until several years ago, it was thought that the cattle prion disease bovine spongiform encephalopathy -- also called BSE or mad cow disease -- was a foodborne disease.</description>
				<pubDate>Fri, 12 Sep 2008 07:52:52 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/09/080912075208.htm</guid>
			</item>
			<item>
				<title>Changes In Urine Could Lead To BSE Test For Live Animals</title>
				<link>http://www.sciencedaily.com/releases/2008/09/080905153643.htm</link>
				<description>Researchers have demonstrated that protein levels in urine samples can indicate both the presence and progress of Bovine Spongiform Encephalopathy disease in cattle. The scientists hope that their discovery might lead to the development of a urine-based test that could prevent the precautionary slaughter of many animals as now occurs when the disease is detected.</description>
				<pubDate>Fri, 05 Sep 2008 15:36:36 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/09/080905153643.htm</guid>
			</item>
			<item>
				<title>Infectious, Test Tube-produced Prions Can Jump The &#39;Species Barrier&#39;</title>
				<link>http://www.sciencedaily.com/releases/2008/09/080904144830.htm</link>
				<description>Researchers have shown that they can create entirely new strains of infectious proteins known as prions in the laboratory by simply mixing infectious prions from one species with the normal prion proteins of another species.</description>
				<pubDate>Thu, 04 Sep 2008 14:48:48 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/09/080904144830.htm</guid>
			</item>
			<item>
				<title>Creutzfeldt-Jakob Disease: Humans Could Be Infected Through Blood Transfusions</title>
				<link>http://www.sciencedaily.com/releases/2008/08/080829104935.htm</link>
				<description>A nine-year study in sheep has added to the evidence that Creutzfeldt-Jakob disease (vCJD) can be transmitted through blood transfusion in humans. The likelihood of Bovine spongiform encephalopathy (BSE) being transmitted between sheep through transfusion of infected sheep blood was 36 per cent, according to new research.</description>
				<pubDate>Fri, 29 Aug 2008 10:49:49 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/08/080829104935.htm</guid>
			</item>
			<item>
				<title>Novel Approach In Molecular Differentiation Of Prion Strains</title>
				<link>http://www.sciencedaily.com/releases/2008/08/080828220507.htm</link>
				<description>Scientists have identified a prion protein characteristic that is unique to some natural but unusual sheep scrapie cases. This finding may provide a novel method by which to study prion diversity and their possible changes during cross-species transmission.</description>
				<pubDate>Thu, 28 Aug 2008 22:05:05 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/08/080828220507.htm</guid>
			</item>
			<item>
				<title>Resistant Prions: Can They Be Transmitted By Environment As Well As Direct Contact?</title>
				<link>http://www.sciencedaily.com/releases/2008/08/080811095458.htm</link>
				<description>Prions, the pathogens that cause scrapie in sheep, can survive in the ground for several years, as researchers have discovered. Animals can become infected via contaminated pastures. It is not yet known whether the pathogens that cause BSE and CWD are equally resistant.</description>
				<pubDate>Mon, 11 Aug 2008 09:54:54 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/08/080811095458.htm</guid>
			</item>
			<item>
				<title>Investigation Of Prion Folding On Cell Membranes</title>
				<link>http://www.sciencedaily.com/releases/2008/08/080811072501.htm</link>
				<description>Abnormally folded proteins cause a number of illnesses such as the Creutzfeldt-Jacob Disease, BSE (bovine spongiform encephalopathy) and Alzheimer&#8217;s. It is still unknown why this misfolding occurs. The first stages of folding and the onset of the aggregation of the proteins, the so-called oligomerisation, appear to be decisive for pathogenesis.</description>
				<pubDate>Mon, 11 Aug 2008 07:25:25 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/08/080811072501.htm</guid>
			</item>
			<item>
				<title>Infectious And Non-infectious Prions Have Clear Differences In Molecular Structures</title>
				<link>http://www.sciencedaily.com/releases/2008/06/080617111831.htm</link>
				<description>Infectious proteins known as prions have been identified as the cause of &#8220;mad cow&#8221; disease (BSE). The culprits are &#8220;incorrectly folded&#8221; proteins that can &#8220;infect&#8221; healthy proteins. The molecular bases for such prion diseases are not yet fully understood. Why are some proteins infectious while others are not? Scientists examined two different forms of a prion-forming protein domain by means of NMR spectroscopy and found that the infectious and noninfectious forms differ markedly in their molecular structure.</description>
				<pubDate>Tue, 17 Jun 2008 11:18:18 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/06/080617111831.htm</guid>
			</item>
			<item>
				<title>Prions show their good side</title>
				<link>http://www.sciencedaily.com/releases/2008/05/080507105649.htm</link>
				<description>Prions, the infamous agents behind mad cow disease and its human variation, Creutzfeldt-Jakob disease, also have a helpful side. New research shows that normally functioning prions prevent neurons from working themselves to death. The findings appear in the May 5 issue of the Journal of Cell Biology.</description>
				<pubDate>Wed, 07 May 2008 10:56:56 EDT</pubDate>
				<guid isPermaLink="true">http://www.sciencedaily.com/releases/2008/05/080507105649.htm</guid>
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