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Transmissibility necessitates the conversion of host PrPC by exogenous PrPSc.
They are characterized by the post-translational conversion of host cellular prion protein (PrPC) into an abnormal disease-related isoform designated PrPSc [1] [3], [5].
Such assays typically assess the conversion of host PrPC to a PK-resistant state when seeded by PrPTSE.
However, the efficiency of the conversion of host biomass into parasite propagules was negatively density-dependent, as demonstrated by the k-values.
The higher reproductive output in the European eel may thus represent a response pattern typical for multicellular parasites, in which increased host exploitation involves a greater conversion of host tissue into parasite tissue and parasite eggs [ 37, 38].
Previous research had demonstrated that the level of auxin (indole 3-acetic acid, IAA) increased in roots during secondary infection by P. brassicae, likely as the result of enhanced biosynthesis and conversion of host auxin precursors induced by the pathogen [ 27].
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Their central feature is the post-translational conversion of host-encoded PrPC [cellular PrP (prion protein)], into an abnormal isoform, designated PrPSc (pathogenic PrP) [ 1, 2].
Their central feature is the posttranslational conversion of host-encoded, cellular prion protein (PrPC) to an abnormal isoform, known as PrPSc.
Prion diseases are a group of fatal infectious neuronal disorders that are associated with the conversion of host-encoded PrP to misfolded pathogenic conformers and neurotoxicity (Prusiner & DeArmond, 1987).
This observation highlights the importance of a single, rare species and a specific pathway for the fate of therapeutics due to the metabolic conversion of host-targeted drugs by the gut microbiota.
Prions, the transmissible agents, consist of aggregates of abnormal conformers of the cellular prion protein (PrPC), generally referred to as PrPSc, and replicate in a self-perpetuating manner by conversion of host-encoded PrPC.
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