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prion d. any of a group of fatal, transmissible neurodegenerative diseases caused by abnormalities of prion protein metabolism, which may result from mutations in the prion protein gene or from infection with pathogenic isoforms of the protein (see prion). Characteristics include neuronal loss, gliosis, and extensive vacuolization of the cerebral cortex. Prion diseases may be sporadic, inherited as an autosomal dominant trait, or acquired. Human diseases include Creutzfeldt-Jakob disease, Gerstmann-Sträussler syndrome, fatal familial insomnia, and kuru; animal diseases include scrapie, bovine spongiform encephalopathy, and mink encephalopathy. Called also transmissible neurodegenerative disease and subacute spongiform or transmissible spongiform encephalopathy.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
prion p. a 33–35 kD protein of uncertain function, in humans coded for by a gene on the short arm of chromosome 20. The 27–30 kD protease-resistant core is the functional, and perhaps only, component of prions; several isoforms have been identified and are responsible for prion disease. Extracellular prion protein aggregates into rod-shaped structures that resemble amyloid.
Ãâó: www.mercksource.com/pp/us/cns/cns_health_library.j...
prion disease Any transmissible neurodegenerative disease believed to be caused by a proteinaceous infectious particle (also known as prion proteins, or PrPs). PrPs change other cellular proteins, producing intracellular vacuoles (¡°spongiform ch
Ãâó:
prion An infectious form of protein that may increase in number by converting related proteins to more prions.
Ãâó: www.sbs.utexas.edu/delia/bio212/glossary.htm
prion is a contraction of the descriptive term, proteinaceous infectious proteins. Prions, unlike viruses, bacteria and fungi, have no DNA and consist only of protein and the infectious form can cause degenerative brain diseases.
Ãâó: www.axonyx.com/glossary.html
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