Prions - Prion, Fatal Familial Insomnia, Stanley B. Prusiner, Bovine Spongiform Encephalopathy, Transmissible Spongiform Encephalopathy, Kuru (Paperback)

Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Pages: 24. Chapters: Prion, Fatal familial insomnia, Stanley B. Prusiner, Bovine spongiform encephalopathy, Transmissible spongiform encephalopathy, Kuru, Fungal prions, Chronic wasting disease, Scrapie, Sup35p, National Prion Clinic, Gerstmann-Straussler-Scheinker syndrome, Specified risk material, Laura Manuelidis, Protease-sensitive prionopathy, Feline spongiform encephalopathy, Transmissible mink encephalopathy, Exotic ungulate encephalopathy, Protein Misfolding Cyclic Amplification, Ure2p. Excerpt: A prion () is an infectious agent composed of protein in a misfolded form. This is in contrast to all other known infectious agents, which must contain nucleic acids (either DNA, RNA, or both). The word prion, coined in 1982 by Stanley B. Prusiner, is a portmanteau derived from the words protein and infection. Prions are responsible for the transmissible spongiform encephalopathies 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 universally fatal. Prions propagate by transmitting a misfolded protein state. When a prion enters a healthy organism, it induces existing, properly-folded proteins to convert into the disease-associated, prion form; the prion acts as a template to guide the misfolding of more protein into prion form. These newly-formed prions can then go on to convert more proteins themselves, this triggers a chain reaction that produces large amounts of the prion 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. Amyloid aggregates are fibrils, growing at their ends, and replicating when brea...