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CROSS-SPECIES PRION INFECTIVITY. "CJD from humans can infect laboratory rodents. BSE from cattle has been used to infect macaques. And, in 1996, clinicians in the United Kingdom described new variant CJD (nvCJD), a prion disease in humans that was believed to be caused by eating beef from BSE-infected cattle." http://www.strangehorizons.com/2004/20040216/killer.shtml View in LinkedIn

"THE PRION ISOFORM is resistant to being degraded by cellular enzymes, so the newly-formed prions accumulate in the central nervous system. They then form aggregates, and these clumps of prions continue to increase in number. The aggregates in the brain tissue are called "amyloid plaques." http://www.strangehorizons.com/2004/20040216/killer.shtml View in LinkedIn

INFECTIOUS PRION. "If you ingest a prion, it may not be "flushed away" the next morning. It's capable of crossing some species barriers. It's resistant to food-preparation treatments such as high heat and ultraviolet irradiation. It's stubbornly insoluble. And it knows how to find its way from your digestive system into your nervous system." http://www.strangehorizons.com/2004/20040216/killer.shtml View in LinkedIn

TOXIC ISOFORM (PRION). "Now: don't change the gene that codes for PrP. Don't even change the sequence of amino acids that make up the protein. Just take that perfectly normal PrP protein and tweak the 3-D structure a bit -- uncoil some of the helices and re-fold them into flat sheets. Chemically and genetically, this new PrP is identical to the old one. It's simply shaped differently, like a person who has changed from a sitting to a standing position. It's a new "isoform": different in physical appearance but not in genetic or chemical makeup. Don't eat this one." http://www.strangehorizons.com/2004/20040216/killer.shtml View in LinkedIn

SAFE NORMAL PRION PROTEIN ISOFORM. "If you happen to eat some PrP, it will be denatured by the cooking heat, then chopped up by enzymes in your digestive system. Tomorrow, its leftover bits will be flushed away -- literally. No harm done." http://www.strangehorizons.com/2004/20040216/killer.shtml View in LinkedIn

NORMAL PRION PROTEIN ISOFORMS. "PrP is a perfectly normal protein produced by nerve cells. When the cell needs more PrP protein, the gene that codes for PrP gets "turned on" and a new PrP molecule is synthesized. Inside the cell, PrP gets folded into its normal three-dimensional configuration. It's then excreted and anchored to the outside of the nerve cell, where it is believed to play a role in synaptic function." http://www.strangehorizons.com/2004/20040216/killer.shtml View in LinkedIn

"THE TWO ISOFORMS of the PrP protein are technically designated PrPC and PrPSc. The "C" stands for cellular; the "Sc" stands for scrapie. PrPSc is believed to be the main, and probably the only, component of the prion (a term derived from "proteinaceous infectious particle")." https://lnkd.in/ekPJGXx View in LinkedIn

DNA INDEPENDENT. "Prion diseases are caused by conversion of a normal cell-surface glycoprotein (PrPC) into a conformationally altered isoform (PrPSc) that is infectious in the absence of nucleic acid." https://lnkd.in/eJBJ5gT View in LinkedIn

"PRIONS are not considered living organisms because they are misfolded protein molecules which may propagate by transmitting a misfolded protein state. If a prion enters a healthy organism, it induces existing, properly folded proteins to convert into the misfolded prion form. In this way, the prion acts as a template to guide the misfolding of more proteins into prion form." https://en.m.wikipedia.org/wiki/Prion View in LinkedIn

ROGUE PROTEIN ISOFORMS. "The best-known attribute of the prion protein (PrP) is its tendency to misfold into a rogue isoform. Neurodegeneration in prion disease is often seen as a consequence of abnormal PrP function yet, amazingly little is known about the normal, physiological role of PrP. In particular, the absence of obvious phenotypes in PrP knockout mice has prevented scientists from answering this important question." https://lnkd.in/eBQR5Bd View in LinkedIn