News tagged with prion
Scientists identify most lethal known species of prion protein
Scientists from the Florida campus of The Scripps Research Institute have identified a single prion protein that causes neuronal death similar to that seen in "mad cow" disease, but is at least 10 times more ...
Feb 09, 2012 |
4.7 / 5 (7) |
2
|
Making memories last: Prion-like protein plays key role in storing long-term memories
Memories in our brains are maintained by connections between neurons called "synapses". But how do these synapses stay strong and keep memories alive for decades? Neuroscientists at the Stowers Institute for ...
Jan 27, 2012 |
4.9 / 5 (14) |
1
|
New study shows prions able to jump between species more easily than thought
(PhysOrg.com) -- A group of French researchers has found that prions are more easily able to jump between species than has been previously thought. In their paper published in Science, they show that prions ...
Jan 27, 2012 |
4.8 / 5 (12) |
2
|
Blood test for human form of mad cow disease developed
(Medical Xpress) -- Mad cow disease is serious business in the U.K., the human form, known as Creutzfeldt-Jakob after Hans Gerhard Creutzfeldt and Alfons Maria Jakob (CJD), who independently first described its existence ...
Jan 16, 2012 |
4 / 5 (4) |
0
|
New findings about the prion protein and its interaction with the immune system
(Medical Xpress) -- 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 ...
Dec 21, 2011 |
5 / 5 (1) |
0
Protein sheds insight into vCJD
A protein linked to the immune system could play a key role in helping scientists understand how vCJD spreads throughout the body.
Dec 02, 2011 |
not rated yet |
0
|
Medical researchers discover hidden side of prion diseases
Medical researchers in Canada and the United States recently published their joint findings that fatal prion diseases, which include BSE or "mad cow disease," have a hidden signature.
Nov 30, 2011 |
4 / 5 (1) |
0
Researchers discover possible key to degenerative nerve diseases
(Medical Xpress) -- Researchers at the University of Wisconsin-Madison and collaborators have discovered a powerful new protein in the eye of the fruit fly that may shed light on blinding diseases and other ...
Medicine & Health / Neuroscience
Nov 17, 2011 |
5 / 5 (2) |
0
|
Alzheimer's might be transmissible in similar way as infectious prion diseases: study
The brain damage that characterizes Alzheimer's disease may originate in a form similar to that of infectious prion diseases such as bovine spongiform encephalopathy (mad cow) and Creutzfeldt-Jakob, according to newly published ...
Oct 04, 2011 |
5 / 5 (3) |
1
|
Screen finds an antidepressant, other drugs, opens possibility of treating brain-wasting mad cow disease
In a new study NYU School of Medicine researchers report that they have found several chemical compounds, including an antidepressant, that have powerful effects against brain-destroying prion infections in mice, opening ...
Sep 14, 2011 |
not rated yet |
0
|
'Good' prion-like proteins boost immune response
(Medical Xpress) -- A person's ability to battle viruses at the cellular level remarkably resembles the way deadly infectious agents called prions misfold and cluster native proteins to cause disease, UT Southwestern Medical ...
Aug 09, 2011 |
not rated yet |
0
|
Cellular stress can induce yeast to promote prion formation
It's a chicken and egg question. Where do the infectious protein particles called prions come from? Essentially clumps of misfolded proteins, prions cause neurodegenerative disorders, such as mad cow/Creutzfeld-Jakob disease, ...
Jul 23, 2011 |
5 / 5 (3) |
0
|
Study finds two gene classes linked to new prion formation
Unlocking the mechanisms that cause neurodegenerative prion diseases may require a genetic key, suggest new findings reported by University of Illinois at Chicago distinguished professor of biological sciences Susan Liebman.
May 26, 2011 |
not rated yet |
0
|
CDC assesses potential human exposure to prion diseases
Researchers from the Centers for Disease Control and Prevention (CDC) have examined the potential for human exposure to prion diseases, looking at hunting, venison consumption, and travel to areas in which prion diseases ...
May 23, 2011 |
not rated yet |
0
Lichens may aid in combating deadly chronic wasting disease in wildlife
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, according ...
May 18, 2011 |
not rated yet |
0
Prion
A prion (pronounced /ˈpriː.ɒn/ ( listen)) is an infectious agent that is composed of protein. To date, all such agents that have been discovered propagate by transmitting a mis-folded protein state; the protein does not itself self-replicate and the process is dependent on the presence of the polypeptide in the host organism. The mis-folded form of the prion protein has been implicated in a number of diseases in a variety of mammals, including bovine spongiform encephalopathy (BSE, also known as "mad cow disease") in cattle and Creutzfeldt-Jakob disease (CJD) in humans. All known prion diseases affect the structure of the brain or other neural tissue, and all are currently untreatable and are always fatal. In general usage, prion refers to the theoretical unit of infection. In scientific notation, PrPC refers to the endogenous form of prion protein (PrP), which is found in a multitude of tissues, while PrPSC refers to the misfolded form of PrP, that is responsible for the formation of amyloid plaques that lead to neurodegeneration.
Prions are hypothesized to infect and propagate by refolding abnormally into a structure which is able to convert normal molecules of the protein into the abnormally structured form. All known prions induce the formation of an amyloid fold, in which the protein polymerises into an aggregate consisting of tightly packed beta sheets. This altered structure is extremely stable and accumulates in infected tissue, causing tissue damage and cell death. This stability means that prions are resistant to denaturation by chemical and physical agents, making disposal and containment of these particles difficult.
Proteins showing prion-type behavior are also found in some fungi and this has been important in helping to understand mammalian prions. However, fungal prions do not appear to cause disease in their hosts and may even confer an evolutionary advantage through a form of protein-based inheritance.
The word prion is a compound word derived from the initial letters of the words proteinaceous and infectious, with -on added by analogy to the word virion.
For more information about Prion, read the full article at
Wikipedia.
This text uses material from Wikipedia and is available under the GNU Free Documentation License.
