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Which Of The Following Statements Concerning Prion Diseases Is True

Atypical proteins in the brain are one of the hallmarks of prion diseases. These proteins can withstand boiling and disinfectants, but they can still be infectious if they are transferred from one brain into another. These proteins are misfolded proteins that damage cells and eventually kill the brain. Although the exact mechanism by which these proteins infect other cells and tissues is not known, it does cause brain damage.

Scientists have long speculated about the properties of prions and whether they are dangerous. One of the most famous prion diseases is the mad cow disease (BSE), which has affected the consumption of hundreds of thousands of Europeans for the past decade. Despite the serious threat, it is important to note that the normal incidence of BSE in cattle is so low that there’s virtually no risk to humans.

As far as the theory of prion diseases is concerned, the cellular protein PrP is the only cause. Prions theory states that this protein is usually in a stable form, but can be altered to cause the disease. It then associates with the abnormal pN, which converts into pD. The higher the risk of developing a new disease, the more pDs it associates.

A new class of diseases called prion is emerging. It is characterized by a unique glycoprotein that can clump in the brain. It can cause brain damage and even death once it is inside the brain. While prion diseases are rare, they can be fatal, and 300 cases are reported annually in the U.S. However, some researchers argue that these diseases could be caused by prion contamination.

Prion disease, a rare neurodegenerative disorder, is caused by abnormally folded proteins within the brain. It is most common in people who eat infected animal products, but can also be caused by genetics. Affected individuals suffer from progressive memory loss, personality changes, and movement problems. There’s no known cure for prion disease, but treatments are available to help those with the disorder.

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