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Prion
PrionIn 1997 Stanley Prusiner was awarded the Nobel Prize in physiology or medicine for a revolutionary theory about the mechanisms of infection. His theory, the "prion hypothesis," concerns an unusual protein, the prion, which occurs in the complete absence of DNA and RNA. According to Prusiner's theory, the prion differs from other well-known infections agents including bacteria and viruses. While the latter rely on nucleic acid for survival and replication, the prion is made of a protein and lacks nucleic acid. Both the existence of the prion and the underlying mode of infection are unprecedented in medical sciences. While several critical issues remain to be addressed, the prion hypothesis may furnish a plausible framework to understand the pathogenesis of several deadly brain diseases of the central nervous system. A New Infectious AgentPrion is an acronym for "proteinaceous infectious particle," a term coined by Prusiner in the early 1980s to describe the nature of the agent causing the fatal brain disorders known as transmissible spongiform encephalopathies (TSE), also called prion diseases. Well-known examples of prion diseases include scrapie in sheep and goats, bovine spongiform encephalopathy (BSE, or "mad cow" disease) in cattle, and Creutzfeldt-Jakob disease (CJD) in humans. Prion diseases are infectious and can also be transmitted to healthy animals by inoculating them with extracts of diseased brain. In the mid-1960s, Tikvah Alper and colleagues reported that nucleic acid was unlikely to be a component of the infectious agent that causes scrapie . In 1967 J. S. Griffith speculated that the scrapie agent might be a protein capable of "self replication" without nucleic acid. However, Prusiner was the first, in the early 1980s, to successfully purify the infectious agent and to show that it consisted mostly of protein (technically speaking it is a glycoprotein , because it has a sugar group attached). He chose to name the new agent "prion" to distinguish it from viruses or viroids. The essential protein component of prion was later identified in 1984 as prion protein (PrP), which is encoded by a chromosome gene in the host genome. Researchers concluded that the prion is a new infectious agent that consists mostly of PrP. This view is often referred to as the "protein only" or prion hypothesis. Some scientists find this notion hard to accept and have argued that nucleic acid is needed to carry information necessary for infection. However, no one has been able to demonstrate that either DNA or RNA play a direct role in prion replication. In 1992 Charles Weissmann and colleagues obtained conclusive evidence for the central role of PrP in the transmission of prion diseases, when they created transgenic mice devoid of the PrP gene. These so-called PrP knockout mice were found to be completely resistant to infection when inoculated with scrapie brain preparations. When the PrP gene was reintroduced into the knockout mice, they once again became susceptible to prion infection. Role of Protein ConformationHow can a protein such as PrP made by a cellular gene become an infectious agent? Prusiner and associates had found that PrP could exist in two forms, a normal or cellular form (PrPC) normally expressed at low levels in neurons and other cell types, and an abnormal or scrapie form (PrPSc) built up in diseased brain. PrPC is a cell-surface glycoprotein, the function of which has yet to be established. PrPC consists of a single polypeptide chain folded into predominantly spiral conformations known as α-helices. These structures give rise to a globular shape that is soluble and can be cleared from the cell by degrading enzymes called proteases. In contrast, PrPSc that has been isolated from diseased brain is rich in an alternative conformation that resembles extended strands. These structures are known as β-sheets. The β-sheet rich PrPSc tends to aggregate and is resistant to heat and degradation by proteases. It is assumed that PrPSc can initiate the infection process by binding to predominantly-helical PrPC and converting it into more stable PrPSc with β-sheet conformation. This will set off a chain reaction leading to accumulation of large amounts of PrPSc to levels that result in brain tissue damage. The conformational conversion from α-helices to β-sheets transforms the benign PrPC into disease-causing PrPSc. This model of conformational conversion provides useful insights into the pathogenesis of prion diseases. Prion DiseasesHistorically, prion diseases have been given distinct names. Scrapie is a naturally occurring prion disease of sheep and goats that was first documented in Iceland during the eighteenth century. BSE or mad cow disease is a prion disease of cattle and is believed to be acquired through scrapie-contaminated foodstuffs. Kuru, a prion disease found among the Fore tribe of New Guinea, was shown by D. Carleton Gajdusek to be transmitted by the consumption of human tissue, particularly brain tissue, during funerary rituals. Gajdusek was awarded the 1976 Nobel Prize in physiology or medicine for this contribution. The early symptom of Kuru is a loss of coordination, followed by mental confusion and, ultimately, death. It has virtually disappeared since 1958, when the practice of eating human tissue was more or less eradicated in New Guinea. CJD is the most common human prion disease, affecting about one in a million people. The main symptom is dementia , along with other neurological signs. There are three forms of CJD. Sporadic CJD, the cause of which has yet to be found, is a spontaneous disease that accounts for a majority of CJD cases. Familial CJD affects people who carry a mutation in the PrP gene on chromosome 20. The third form, called iatrogenic CJD, is the result of accidental transmission during medical treatments. A newly emerged CJD phenotype, commonly called variant CJD, has occurred in the United Kingdom since 1985. Variant CJD has a unique disease profile, and may result from the consumption of BSE-contaminated meat products. It has been diagnosed mostly in young people who initially seek treatment for psychiatric symptoms. Gertsmann-Sträussler-Scheinker (GSS) syndrome is a familial prion disease resulting from a mutation in the PrP gene. The main symptom of GSS is the loss of coordination and dementia. Fatal familial insomnia (FFI) is another a familial prion disease in which fatal dementia follows the loss of physiological sleep. Although human prion diseases manifest as three etiologically different forms—spontaneously (sporadic CJD), through inheritance (familial CJD, GSS, and FFI), and by infection (iatrogenic CJD, kuru, and possibly the new variant CJD), they nonetheless share a common pathogenetic event. Within the framework of "protein only" hypothesis, they all involve the protein conformational change that converts PrPC to pathogenic PrPSc. Such a structural change in PrP may be triggered by a rare spontaneous event leading to a sporadic disease, a mutation that causes a familial disease, or exposure to foreign PrPSc, leading to an acquired disease. The "protein only" hypothesis provides a plausible mechanism underlying the pathogenesis of all forms of prion diseases. Moreover, it also helps explain the tremendous variability in prion-associated disease phenotypes . Structurally distinct variants of PrPSc may accumulate in different regions of the brain and initiate pathogenic changes that may eventually lead to distinct pathology in different areas of the brain, and subsequently the particular disease symptoms. The concept of the prion and the role of protein conformation in disease pathogenesis have renewed inquiry into the causes of other and more common neurodegenerative disorders, such as Alzheimer's disease, Hunt-ington's disease, and Parkinson's disease. A common hallmark of all these diseases, as in prion diseases, is the conversion of an otherwise soluble and functional neuronal protein into a β-sheet rich and protease-resistant protein that has a higher tendency to aggregate and is harmful to the brain. These common pathogenetic features raise the hope that therapeutic interventions based on the same principles may be effective in all these diseases. see also Protein. Pierluigi Gambetti and Shu G. Chen BibliographyCohen, F. E., and S. B. Prusiner. "Pathologic Conformations of Prion Proteins."Annual Review in Biochemistry 67 (1998): 793-819. Prusiner, S. B. "Molecular Biology of Prion Diseases." Science 252 (1991): 1515-1522. ———. "The Prion Diseases." Scientific American (1995): 48-57. ———. Prion Biology and Diseases. New York: Cold Spring Harbor Laboratory Press,1999. |
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Gambetti, Pierluigi; Chen, Shu G.. "Prion." Genetics. 2003. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. Gambetti, Pierluigi; Chen, Shu G.. "Prion." Genetics. 2003. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1G2-3406500220.html Gambetti, Pierluigi; Chen, Shu G.. "Prion." Genetics. 2003. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1G2-3406500220.html |
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Prions
PrionsForensic investigations can often be focused on an illness outbreak or death that is suspected of being of infectious origin. Then, a critical task of forensic scientists is to identify the source of the illness and, if it is determined to be contagious, to track the pattern of the infection in order to help quell the present and future outbreaks. Bacteria, viruses, fungi, and protozoa are the usual causes of infections. However, within the past several decades, a protein found in the brain has been determined to be the cause of one or more similar diseases of humans and animals (variant Creutzfeld-Jacob disease in humans; Bovine Spongiform Encephalopathy [BSE] or "mad cow" in cattle) that produce a progressive destruction of brain tissue. The determination of the involvement of the protein, dubbed prion, is an example of forensic science . Post-mortem examinations of tissue samples are geared toward unearthing the indications of prion activity and in detecting the presence of the abnormal form of the protein. As in other infectious disease investigations, establishing the origin of the infection becomes a priority. Prions are proteins that are infectious. Indeed, the name prion is derived from "proteinaceous infectious particles." The forensically relevant investigations that have implicated prions in degenerative brain diseases have been revolutionary. The discovery of prions and confirmation of their infectious nature overturned a central dogma that infections were caused by intact organisms, particularly microorganisms such as bacteria, fungi, parasites, or viruses. Since prions lack genetic material, the prevailing attitude was that a protein could not cause disease. Prions were discovered and their role in brain degeneration was proposed by Stanley Pruisner. This work earned him the Nobel Prize in medicine or physiology in 1997. In contrast to infectious agents that are not normal residents of a host, prion proteins are a normal constituent of brain tissue in humans and in all mammals studied thus far. The prion normally is a constituent of the membrane that surrounds the cells. The protein is also designated PrP (for the aforementioned proteinaceous infectious particle). PrP is a small protein, being only some 250 amino acids in length. The protein is arranged with regions that have a helical conformation and other regions that adopt a flatter, zigzag arrangement of the amino acids. The normal function of the prion is still not clear. Studies from mutant mice that are deficient in prion manufacture indicate that the protein may help protect the brain tissue from destruction that occurs with increasing frequency as someone ages. The normal prions may aid in the survival of brain cells known as Purkinje cells, which predominate in the cerebellum, a region of the brain responsible for movement and coordination. The so-called prion theory states that PrP is the only cause of the prion-related diseases, and that disease results when a normally stable PrP is "flipped" into a different shape that causes disease. Regions that are helical and zigzag are still present, but their locations in the protein are altered. This confers a different three-dimensional shape to the protein. As of 2005, the mechanism by which a normally functioning protein is first triggered to become infectious is not known. One hypothesis, known as the virino hypothesis, proposes that the infectious form of a prion is formed when the PrP associates with nucleic acid from some infectious organism. Efforts to find prions associated with nucleic acid have, as of 2005, been unsuccessful. If the origin of the infectious prion is unclear, the nature of the infectious process following the creation of an infectious form of PrP is becoming clearer. The altered protein is able to stimulate a similar structural change in surrounding prions. The change in shape may result from the direct contact and binding of the altered and infectious prion with the unaltered and still-normally functioning prions. The altered proteins also become infective and encourage other proteins to undergo the conformational change. The cascade produces proteins that adversely effect neural cells, and the cells lose their ability to function and ultimately die. The death of regions of the brain cells produces holes in the tissue. This appearance led to the designation of the disease as spongiform encephalopathy. This appearance is a hallmark of forensic examinations. The weight of evidence now supports the contention that prion diseases of animals, such as scrapie in sheep and BSE in cattle, can cross the species barrier to humans. In humans, the progressive loss of brain function is clinically apparent as Creutzfeld-Jacob disease, kuru, and Gerstmann-Ströussler-Scheinker disease. Other human diseases that are candidates (but as yet not definitively proven) for a prion origin are Alzheimers disease and Parkinsons disease. In the past several years, a phenomenon that bears much similarity to prion infection has been discovered in yeast. The prion-like protein is not involved in a neurological degeneration. Rather, the microorganism is able to transfer genetic information to the daughter cell by means of a shape-changing protein, rather than by the classical means of genetic transfer. The protein is able to stimulate the change of shape of other proteins in the interior of the daughter cell, which produces proteins having a new function. The recent finding of a prion-related mechanism in yeast indicates that prions may be ubiquitous features of many organisms and that the protein may have other functions than promoting disease. see also Animal evidence; Mad cow disease investigation. |
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"Prions." World of Forensic Science. 2005. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. "Prions." World of Forensic Science. 2005. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1G2-3448300458.html "Prions." World of Forensic Science. 2005. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1G2-3448300458.html |
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Prions
PrionsPrions are proteins that are infectious. Indeed, the name prion is derived from "proteinaceous infectious particles." The discovery of prions and confirmation of their infectious nature overturned a central dogma that infections were caused by intact organisms, particularly microorganisms such as bacteria , fungi , parasites , or viruses . Since prions lack genetic material, the prevailing attitude was that a protein could not cause disease. Prions were discovered and their role in brain degeneration was proposed by Stanley Pruisner. This work earned him the 1997 Nobel Prize in medicine or physiology. In contrast to infectious agents that are not normal residents of a host, prion proteins are a normal constituent of brain tissue in humans and in all mammals studied thus far. The prion normally is a constituent of the membrane that surrounds the cells. The protein is also designated PrP (for proteinaceous infectious particle). PrP is a small protein, being only some 250 amino acids in length. The protein is arranged with regions that have a helical conformation and other regions that adopt a flatter, zigzag arrangement of the amino acids. The normal function of the prion is still not clear. Studies from mutant mice that are deficient in prion manufacture indicate that the protein may help protect the brain tissue from destruction that occurs with increasing frequency as someone ages. The normal prions may aid in the survival of brain cells known as Purkinje cells, which predominate in the cerebellum, a region of the brain responsible for movement and coordination. The so-called prion theory states that PrP is the only cause of the prion-related diseases, and that these disease results when a normally stable PrP is "flipped" into a different shape that causes disease. Regions that are helical and zigzag are still present, but their locations in the protein are altered. This confers a different three-dimensional shape to the protein. As of 2002, the mechanism by which normally functioning protein is first triggered to become infectious is not known. One hypothesis, known as the virino hypothesis, proposes that the infectious form of a prion is formed when the PrP associates with nucleic acid from some infectious organism. Efforts to find prions associated with nucleic acid have, as of 2001, been unsuccessful. If the origin of the infectious prion is unclear, the nature of the infectious process following the creation of an infectious form of PrP is becoming clearer. The altered protein is able to stimulate a similar structural change in surrounding prions. The change in shape may result from the direct contact and binding of the altered and infectious prion with the unaltered and still-normally functioning prions. The altered proteins also become infective and encourage other proteins to undergo the conformational change. The cascade produces proteins that adversely effect neural cells and the cells lose their ability to function and die. The death of regions of the brain cells produces holes in the tissue. This appearance leads to the designation of the disease as spongiform encephalopathy. The weight of evidence now supports the contention that prion diseases of animals, such as scrapie in sheep and bovine spongiform encephalopathy (BSE—popularly known as Mad cow disease) can cross the species barrier to humans. In humans, the progressive loss of brain function is clinically apparent as Creutzfeld-Jacob disease, kuru, and Gerstmann-Sträussler-Scheinker disease. Other human disease that are candidates (but as yet not definitively proven) for a prion origin are Alzheimer's disease and Parkinson's disease. In the past several years, a phenomenon that bears much similarity to prion infection has been discovered in yeast . The prion-like protein is not involved in a neurological degeneration. Rather, the microorganism is able to transfer genetic information to the daughter cell by means of a shape-changing protein, rather than by the classical means of genetic transfer. The protein is able to stimulate the change of shape of other proteins in the interior of the daughter cell, which produces proteins having a new function. The recent finding of a prion-related mechanism in yeast indicates that prions my be a ubiquitous feature of many organisms and that the protein may have other functions than promoting disease. See also BSE and CJD disease; BSE and CJD disease, advances in research |
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"Prions." World of Microbiology and Immunology. 2003. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. "Prions." World of Microbiology and Immunology. 2003. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1G2-3409800457.html "Prions." World of Microbiology and Immunology. 2003. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1G2-3409800457.html |
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Prion
PrionUnlike all other infectious agents, prions contain no deoxyribonucleic acid (DNA) or ribonucleic acid (RNA). This radical difference has slowed the understanding and acceptance of the infectious properties of prions since their discovery. Prions are infectious agents composed of protein that cause fatal brain diseases. Prion diseases include scrapie in sheep, "mad cow disease" (bovine spongiform encephalopathy, or BSE) in cattle, and Creutzfeldt-Jakob disease (CJD) in humans. Prion diseases can be transmitted when an organism consumes infected brain material from another organism. This occurred in England (and elsewhere) when cows were fed processed remains of infected livestock. While the cause of most cases of CJD is unknown, a small number of European cases have been correlated with the consumption of contaminated beef. First called "slow viruses," the unusual nature of these infectious agents became clear from experiments performed in the 1960s. For example, the agents were particularly resistant to sterilization procedures that inactivated bacteria and viruses. In the early 1980s American neurologist Stanley Prusiner published biochemical purification studies suggesting that these pathogens were composed mainly of one type of protein and were thus fundamentally different—and by implication, far simpler chemically—than conventional infectious pathogens of animals and plants. Prusiner coined the term prion (derived from pro- teinaceous in fectious pathogen) to highlight this distinction. The single protein implicated as the causative agent was named the prion protein, PrP for short. Although the theory was first greeted with skepticism, Prusiner was vindicated by receiving the 1997 Nobel Prize in Biology or Medicine. Generally, and as first suggested by Norwegian-American chemist Christian Anfinsen, the linear sequence of amino acids in a protein determines its unique three-dimensional structure, or "conformation." This conformation arises from folding of the peptide chain driven by thermodynamic considerations. A normal form of PrP made in healthy animals is called PrPC and follows a predetermined pattern of folding. The folding results in three corkscrew ("α -helical") segments that compact down upon each other to form a globular core region. Surprisingly, analysis of the infectious form of the PrP referred to as PrPSc reveals a different shape. Compared to PrPC, PrPSc has a diminished amount of α-helix and an increased amount of another folding pattern called α-sheet, despite the fact that they have the same amino acid sequence. These findings defined a new mechanism of disease resulting from proteins adopting alternative, inappropriate conformations. The exact means whereby PrPSc molecules are formed from PrPC molecules is not fully understood. Nonetheless, it appears to involve a templating reaction where PrPC molecules are first unfolded and then refolded into the shape characteristic of PrPSc using preexisting PrPSc molecules as templates . Since the generation of new PrPSc molecules is equated with (and perhaps the same as) the generation of new infectious particles, it can be seen that prions "replicate" in a strange and novel manner, namely by subverting the folding of a normal cell-surface protein. see also Neurologic Diseases; Protein Structure David Westaway BibliographyPrusiner, S. B. Scientific American 272, no. 1 (January 1995): 48–57. |
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Westaway, David. "Prion." Biology. 2002. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. Westaway, David. "Prion." Biology. 2002. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1G2-3400700373.html Westaway, David. "Prion." Biology. 2002. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1G2-3400700373.html |
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prion
prion , abnormal form of a protein found in mammals, believed to cause a group of diseases known as prion diseases or transmissible spongiform encephalopathies. Well-known prion diseases are Creutzfeldt-Jakob disease (CJD) and kuru in humans, scrapie in sheep, bovine spongiform encephalopathy (BSE), also called "mad cow disease," in cattle, and chronic wasting disease in deer and elk (wapiti). There is no effective treatment for any prion disease.
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"prion." The Columbia Encyclopedia, 6th ed.. 2011. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. "prion." The Columbia Encyclopedia, 6th ed.. 2011. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1E1-prion.html "prion." The Columbia Encyclopedia, 6th ed.. 2011. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1E1-prion.html |
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Prions
PRIONSPrions are infectious proteinaceous particles or, more simply, proteins that lack nucleic acid. They were discovered by Stanley Prusiner, who received the Nobel Prize in medicine in 1997 for his work on them. Prions are biologically unique, existing somewhere in the border zone between living things and nonliving matter. Although they show none of the characteristics associated with life, such as the need to metabolize and the capacity to reproduce, they are in some manner capable of replication in the body of a human or certain other mammals. Prions apparently gain entry to the body mainly by ingestion, or else in contaminated human growth hormone, or, possibly, in contaminated blood or blood products. They selectively attack the central nervous system, causing a relentless and progressive destruction of neural tissue, leaving in its place microscopic vesicular globules. The pathological name for this is spongiform encephalopathy. Conditions in this category, all of them invariably fatal, are all transmissible. They include kuru, Creutzfeldt-Jakob disease, scrapie (a degenerative neural disease of sheep), bovine spongiform encephalopathy (mad cow disease), and variant Creutzfeldt-Jakob disease, which appears to be acquired by ingesting beef contaminated by the prions that cause mad cow disease. As of September 2000, it remains unknown what other mammalian species are vulnerable to prions; in research laboratories they have been shown to infect rodents and primates. It is possible that all domestic farm animals are at risk, though so far only sheep, beef and dairy cattle, and wild ungulates such as deer and elk have been confirmed as vulnerable. There is no vaccine or serum to protect against infection, and no agent that can arrest or retard the progress of the spongiform degeneration once it begins. John M. Last (see also: Transmissible Spongiform Encephalopathy ) |
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Last, John M.. "Prions." Encyclopedia of Public Health. 2002. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. Last, John M.. "Prions." Encyclopedia of Public Health. 2002. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1G2-3404000688.html Last, John M.. "Prions." Encyclopedia of Public Health. 2002. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1G2-3404000688.html |
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prion
prion An abnormal form of a normal cell protein (PrP) found in the brain of mammals that is believed to be the agent responsible for the diseases scrapie in sheep, bovine spongiform encephalopathy (BSE) in cattle, and Creutzfeldt–Jakob disease in humans. Produced by mutation of the normal PrP gene, the abnormal prion protein induces the normal protein to fold incorrectly, causing it to form aggregates. These accumulate in the brain and progressively damage and destroy brain cells. Prion protein can be transmitted to other individuals of the same or closely related species, by injection or ingestion of infected tissue, and appears to be transmissible between species that are not closely related, e.g. between cattle and humans.
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"prion." A Dictionary of Biology. 2004. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. "prion." A Dictionary of Biology. 2004. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1O6-prion.html "prion." A Dictionary of Biology. 2004. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1O6-prion.html |
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prion
prion Infective agent that appears to consist simply of a protein. Prions are thought to cause diseases such as Creutzfeldt-Jakob disease (CJD) and kuru in humans, bovine spongiform encephalopathy (BSE) in cattle, and scrapie in sheep. It is not yet understood how prions work; unlike viruses and bacteria, they do not contain dna or rna. A virus is a hundred times larger than a prion. The US neurologist Stanley Prusiner won the 1997 Nobel Prize for developing the prion theory in 1982.
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"prion." World Encyclopedia. 2005. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. "prion." World Encyclopedia. 2005. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1O142-prion.html "prion." World Encyclopedia. 2005. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1O142-prion.html |
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prion
prion (pree-on) n. a constituent protein of brain cells that, in an abnormal form, accumulates in and destroys brain tissue. This form is very stable and resistant to radiation and sterilization; it is thought to interact with normal prion protein in such a way as to convert it to abnormal prion. Prions are now widely accepted as being the causal agents of Creutzfeldt-Jakob disease and other spongiform encephalopathies.
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"prion." A Dictionary of Nursing. 2008. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. "prion." A Dictionary of Nursing. 2008. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1O62-prion.html "prion." A Dictionary of Nursing. 2008. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1O62-prion.html |
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prion
prion The infective agent(s) responsible for Creutzfeld‐Jacob disease, kuru and possibly other degenerative diseases of the brain in human beings, scrapie in sheep, and bovine spongiform encephalopathy (BSE). They are simple proteins, and unlike viruses do not contain any nucleic acid. Transmission occurs by ingestion of infected tissue.
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DAVID A. BENDER. "prion." A Dictionary of Food and Nutrition. 2005. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. DAVID A. BENDER. "prion." A Dictionary of Food and Nutrition. 2005. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1O39-prion.html DAVID A. BENDER. "prion." A Dictionary of Food and Nutrition. 2005. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1O39-prion.html |
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prions
prions (Pachyptila) See PROCELLARIIDAE.
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MICHAEL ALLABY. "prions." A Dictionary of Zoology. 1999. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. MICHAEL ALLABY. "prions." A Dictionary of Zoology. 1999. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1O8-prions.html MICHAEL ALLABY. "prions." A Dictionary of Zoology. 1999. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1O8-prions.html |
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prion
prion •aide-de-camp, aides-de-camp, anon, Asunción, au courant, begone, Bonn, bon vivant, Caen, Canton, Carcassonne, Ceylon, chaconne, chateaubriand, ci-devant, Colón, colon, Concepción, con (US conn), cretonne, don, Duchamp, Evonne, foregone, fromage blanc, Gabon, Garonne, gone, guenon, hereupon, Inchon, Jean, john, Jon, Le Mans, León, Luzon, Mont Blanc, Narbonne, odds-on, on, outgone, outshone, Perón, phon, piñon, Pinot Blanc, plafond, Ramón, Saigon, Saint-Saëns, Sand, Schwann, scone, shone, side-on, sine qua non, Sorbonne, spot-on, swan, thereon, thereupon, ton, Toulon, undergone, upon, Villon, wan, whereon, whereupon, won, wonton, yon, Yvonne
•crayon, rayon
•Leon, Lyons, neon, prion
•Ceredigion • Mabinogion • nucleon
•Amiens • dupion • parathion
•Laocoon
•gluon, Rouen
•bon-bon • Audubon
•Brian, cyan, Gaian, Geminian, Hawaiian, ion, iron, Ixion, lion, Lyon, Mayan, Narayan, O'Brien, Orion, Paraguayan, prion, Ryan, scion, Uruguayan, Zion
•andiron
•gridiron, midiron
•dandelion • anion • Bruneian
•cation, flatiron
•gowan, Palawan, rowen
•anthozoan, bryozoan, Goan, hydrozoan, Minoan, protozoan, protozoon, rowan, Samoan, spermatozoon
•Ohioan • Chicagoan • Virgoan
•Idahoan
•doyen, Illinoisan, Iroquoian
•Ewan, Labuan, McEwan, McLuhan, Siouan
•Saskatchewan • Papuan • Paduan
•Nicaraguan • gargantuan
•carbon, chlorofluorocarbon, graben, hydrocarbon, Laban, radiocarbon
•ebon • Melbourne • Theban
•gibbon, ribbon
•Brisbane, Lisbon
•Tyburn
•auburn, Bourbon
•Alban • Manitoban • Cuban
•stubborn
•Durban, exurban, suburban, turban, urban
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"prion." Oxford Dictionary of Rhymes. 2007. Encyclopedia.com. 27 May. 2012 <http://www.encyclopedia.com>. "prion." Oxford Dictionary of Rhymes. 2007. Encyclopedia.com. (May 27, 2012). http://www.encyclopedia.com/doc/1O233-prion.html "prion." Oxford Dictionary of Rhymes. 2007. Retrieved May 27, 2012 from Encyclopedia.com: http://www.encyclopedia.com/doc/1O233-prion.html |
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