Prion protein—Semisynthetic prion protein (PrP) variants with posttranslational modifications
نویسندگان
چکیده
منابع مشابه
Polythiophenes inhibit prion propagation by stabilizing prion protein (PrP) aggregates.
Luminescent conjugated polymers (LCPs) interact with ordered protein aggregates and sensitively detect amyloids of many different proteins, suggesting that they may possess antiprion properties. Here, we show that a variety of anionic, cationic, and zwitterionic LCPs reduced the infectivity of prion-containing brain homogenates and of prion-infected cerebellar organotypic cultured slices and de...
متن کاملRNA aptamers specifically interact with the prion protein PrP.
We have isolated RNA aptamers which are directed against the recombinant Syrian golden hamster prion protein rPrP23-231 (rPrPc) fused to glutathione S-transferase (GST). The aptamers did not recognize the fusion partner GST or the fusion protein GST::rPrP90-231 (rPrP27-30), which lacks 67 amino acids from the PrP N terminus. The aptamer-interacting region of PrPc was mapped to the N-terminal am...
متن کاملPrion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie.
The 'protein only' hypothesis postulates that the prion, the agent causing transmissible spongiform encephalopathies, is PrP(Sc), an isoform of the host protein PrP(C). Protease treatment of prion preparations cleaves off approximately 60 N-terminal residues of PrP(Sc) but does not abrogate infectivity. Disruption of the PrP gene in the mouse abolishes susceptibility to scrapie and prion replic...
متن کاملPrion protein gene (PrP) polymorphisms in healthy sheep in Turkey.
Scrapie, a transmissible spongiform encephalopathy (TSE) or prion disease, is a fatal, neurodegenerative disease in sheep and goats. This disease has been known in Europe for more than 250 years. Susceptibility to scrapie is associated with polymorphisms in the sheep prion protein gene (PrP) gene. In sheep, polymorphism in the PrP gene has been identified at a number of codons, and polymorphism...
متن کاملContext dependent neuroprotective properties of prion protein (PrP).
Although it has been known for more than twenty years that an aberrant conformation of the prion protein (PrP) is the causative agent in prion diseases, the role of PrP in normal biology is undetermined. Numerous studies have suggested a protective function for PrP, including protection from ischemic and excitotoxic lesions and several apoptotic insults. On the other hand, many observations hav...
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ژورنال
عنوان ژورنال: Journal of Peptide Science
سال: 2019
ISSN: 1075-2617,1099-1387
DOI: 10.1002/psc.3216