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A prion / ˈ p r iː ɒ n / ⓘ is a misfolded protein that induces misfolding in normal variants of the same protein, leading to cellular death. Prions are responsible for prion diseases, known as transmissible spongiform encephalopathy (TSEs), which are fatal and transmissible neurodegenerative diseases affecting both humans and animals.
Familial forms of prion disease are inherited in an autosomal dominant pattern, which means one copy of the altered gene in each cell is sufficient to cause the disorder. In most cases, an affected person inherits the altered gene from one affected parent. In some people, familial forms of prion disease are caused by a new mutation in the PRNP ...
The abnormal protein PrP Sc accumulates in the brain and destroys nerve cells, which leads to the mental and behavioral features of prion diseases. [citation needed] Several other changes in the PRNP gene (called polymorphisms) do not cause prion diseases but may affect a person's risk of developing these diseases or alter the course of the ...
The secondary cell wall, a thick layer formed inside the primary cell wall after the cell is fully grown. It is not found in all cell types. It is not found in all cell types. Some cells, such as the conducting cells in xylem , possess a secondary wall containing lignin , which strengthens and waterproofs the wall.
Amyloids have been known to arise from many different proteins. [2] [7] These polypeptide chains generally form β-sheet structures that aggregate into long fibers; however, identical polypeptides can fold into multiple distinct amyloid conformations. [8] The diversity of the conformations may have led to different forms of the prion diseases. [6]
A human pathogen is a pathogen (microbe or microorganism such as a virus, bacterium, prion, or fungus) that causes disease in humans.. The human physiological defense against common pathogens (such as Pneumocystis) is mainly the responsibility of the immune system with help by some of the body's normal microbiota.
Plants uptake prions from contaminated soil and transport them into their stem and leaves, potentially transmitting the prions to herbivorous animals. [22] Additionally, wood, rocks, plastic, glass, cement, stainless steel, and aluminum have been shown binding, retaining, and releasing prions, showcasing that the proteins resist environmental ...
The majority of porins are monomers; however, some dimeric porins have been discovered, as well as an octameric porin. [4] Depending on the size of the porin, the interior of the protein may either be filled with water, have up to two β strands folded back into the interior, or contain a "stopper" segment composed of β strands.