| Literature DB >> 28817974 |
Niccolò Candelise1, Matthias Schmitz1, Susana Margarida Da Silva Correia1, Amandeep Singh Arora1, Anna Villar-Piqué1, Saima Zafar1, Franc Llorens2, Maria Cramm1, Inga Zerr1.
Abstract
INTRODUCTION: The development of in vitro protein misfolding amplification assays for the detection and analysis of abnormally folded proteins, such as proteinase K resistant prion protein (PrPres) was a major innovation in the prion field. In prion diseases, these types of assays imitate the pathological conversion of the cellular PrP (PrPC) into a proteinase resistant associated conformer or amyloid, called PrPres. Areas covered: The most prominent protein misfolding amplification assays are the protein misfolding cyclic amplification (PMCA), which is based on sonication and the real-time quaking-induced conversion (RT-QuIC) technique based on shaking. The more recently established RT-QuIC is fully automatic and enables the monitoring of misfolded protein aggregates in real-time by using a fluorescent dye. Expert commentary: RT-QuIC is a very robust and highly reproducible test system which is applicable in diagnosis, prion strain-typing, drug pre-screening and other amyloidopathies.Entities:
Keywords: Real-time quaking-induced conversion; aggregation; prion protein; protein misfolding; sporadic Creutzfeldt-Jakob disease
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Year: 2017 PMID: 28817974 DOI: 10.1080/14737159.2017.1368389
Source DB: PubMed Journal: Expert Rev Mol Diagn ISSN: 1473-7159 Impact factor: 5.225