TY - JOUR
AU - Asen, Daskalov
AB -  Prions Are Amyloids Prions are self-propagating amyloids. Amyloids are protein polymers with a cross-β structure, in which short β-strands from the monomers stack one on top of each other to make up a fibrillar polymer [1] , [2] . These amyloids act as templates that convert monomers to the amyloid polymerised state. Spontaneous or chaperone-assisted fragmentation of this amyloid fibril allows multiplication of the prion particle by generating novel fibril ends where templating occurs. Prions have initially been identified in the context of mammalian spongiform encephalopathies such as scrapie in sheep, Creutzfeld-Jacob disease in humans, or bovine spongiform encephalopathy (BSE) in cattle [3] . In these diseases, the host encoded GPI-anchored PrP prion protein turns into prion aggregates, leading to incurable lethal neurodegenerative diseases. The prion phenomenon is not restricted to this sole example. In particular, nine prion proteins have been identified in yeast and correspond to proteins with a wide range of cellular functions [4] . Generally, prion formation leads to loss of the cellular function of the protein. Yeast prions are thus detected as non-Mendelian genetic elements, leading to infectious and inheritable protein inactivation. More than 30 human diseases, including Alzheimer disease, are caused by accumulation 
TI - The (Het-s) Prion, an Amyloid Fold as a Cell Death Activation Trigger
JF - PLoS Pathogens
DO - 10.1371/journal.ppat.1002687
DA - 2012-05-24
UR - https://www.deepdyve.com/lp/public-library-of-science-plos-journal/the-het-s-prion-an-amyloid-fold-as-a-cell-death-activation-trigger-zkiHTId1Dh
VL - 8
IS - 5
DP - DeepDyve
ER -