CorrespondenceA prion lexicon (out of control)
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Cited by (37)
Kinetics of the reduction of Creutzfeldt–Jakob disease prion seeding activity by steam sterilization support the use of validated 134°C programmes
2023, Journal of Hospital InfectionCitation Excerpt :Prions – the causative agents of transmissible spongiform encephalopathies (TSEs) – are infectious, self-replicating protein seeds that are thought to essentially consist of pathologically misfolded and aggregated conformational isomers of the cellular prion protein (PrPC), referred to as PrPSc or PrPTSE [1,2].
Important Steps in Microbial Pathogenesis
2017, Infectious Diseases, 2-Volume SetMicrobial and enzymatic inactivation of prions in soil environments
2013, Soil Biology and BiochemistryCitation Excerpt :Substantial evidence supports the hypothesis that abnormally folded forms of the prion protein (PrP) constitute the TSE infectious agent (Colby and Prusiner, 2011; Prusiner, 1998). The normal, benign, host-encoded forms of PrP are denoted PrPC, and the disease-associated, misfolded conformers are designated PrPTSE (Brown and Cervenakova, 2005). In this review we use PrPTSE (and the synonyms abnormally folded or misfolded PrP) to signify all abnormal forms of PrP when measured by biochemical or immunochemical means, and prion or TSE infectivity when directly referring to properties or measurements of TSE infectious agents.
Nature and pathogenicity of micro-organisms
2010, Infectious Diseases: Third EditionOpposing roles of prion protein in oxidative stress- and ER stress-induced apoptotic signaling
2008, Free Radical Biology and MedicinePrion diseases: From protein to cell pathology
2008, American Journal of PathologyCitation Excerpt :Conformational change distinguishes PrPC from PrPTSE that seems to be the main or only constituent of the infectious agent.1,14 The term PrPTSE was introduced to avoid confusion resulting from complex nomenclatures,15 but it is far from accepted in general use. PrPTSE features a predominantly β-pleated structure, whereas PrPC is α-helix dominant.1