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@ARTICLE{SilvaCorreia:169154,
      author       = {Silva-Correia, Susana and Schmitz, Matthias and Fischer,
                      Andre and Hermann, Peter and Zerr, Inga},
      title        = {{R}ole of different recombinant {P}r{P} substrates in the
                      diagnostic accuracy of the {CSF} {RT}-{Q}u{IC} assay in
                      {C}reutzfeldt-{J}akob disease.},
      journal      = {Cell $\&$ tissue research},
      volume       = {392},
      number       = {1},
      issn         = {2192-5917},
      address      = {Heidelberg},
      publisher    = {Springer},
      reportid     = {DZNE-2023-00033},
      pages        = {301-306},
      year         = {2023},
      abstract     = {The development of the real-time quaking-induced conversion
                      (RT-QuIC), an in vitro protein misfolding amplification
                      assay, was an innovation in the scientific field of protein
                      misfolding diseases. In prion diseases, these types of
                      assays imitate the pathological conversion of the cellular
                      prion protein (PrPC) into a protease-resistant and/or
                      amyloid form of PrP, called PrP resistant (PrPRes). The
                      RT-QuIC is an automatic assay system based on real-time
                      measuring of thioflavin-T (Th-T) incorporation into amyloid
                      fibrils using shaking for disaggregation. It has already
                      been applied in diagnostics, drug pre-screening, and to
                      distinguish between different prion strains. The seeded
                      conversion efficiency and the diagnostic accuracy of the
                      RT-QuIC assay strongly depend on the kind of recombinant PrP
                      (rec PrP) substrate. The DNA sequences of different
                      substrates may originate from different species, such as
                      human, bank vole, and hamster, or from a combination of two
                      species, e.g., hamster-sheep chimera. In routine use, either
                      full-length (FL) or truncated substrates are applied which
                      can accelerate the conversion reaction, e.g., to a more
                      sensitive version of RT-QuIC assay. In the present review,
                      we provide an overview on the different types of PrP
                      substrates (FL and truncated forms), recapitulate the
                      production and purification process of different rec PrP
                      substrates, and discuss the diagnostic value of CSF RT-QuIC
                      in human prion disease diagnostics.},
      subtyp        = {Review Article},
      keywords     = {Cricetinae / Humans / Animals / Sheep / Creutzfeldt-Jakob
                      Syndrome: diagnosis / Prions: metabolism / Prion Proteins:
                      metabolism / Prions (NLM Chemicals) / Creutzfeldt-Jakob
                      disease (Other) / Diagnostics (Other) / Real-time
                      quaking-induced conversion (Other) / Recombinant prion
                      protein substrates (Other) / Prion Proteins (NLM Chemicals)},
      cin          = {AG Zerr / Ext UMG Zerr / AG Fischer 1 ; AG Fischer /
                      Clinical Dementia Research Göttingen},
      ddc          = {610},
      cid          = {I:(DE-2719)1440011-1 / I:(DE-2719)5000037 /
                      I:(DE-2719)1410002 / I:(DE-2719)1440015},
      pnm          = {353 - Clinical and Health Care Research (POF4-353) / 352 -
                      Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-353 / G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC10113290},
      pubmed       = {pmid:36536226},
      doi          = {10.1007/s00441-022-03715-9},
      url          = {https://pub.dzne.de/record/169154},
}