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@ARTICLE{Wsten:140214,
      author       = {Wüsten, Annick and Pasham Parameshwar, Reddy and Smiyakin,
                      Andrej and Bernis, Maria Eugenia and Tamgüney, Gültekin},
      title        = {{A} {B}ioluminescent {C}ell {A}ssay to {Q}uantify {P}rion
                      {P}rotein {D}imerization.},
      journal      = {Scientific reports},
      volume       = {8},
      number       = {1},
      issn         = {2045-2322},
      address      = {[London]},
      publisher    = {Macmillan Publishers Limited, part of Springer Nature},
      reportid     = {DZNE-2020-06536},
      pages        = {14178},
      year         = {2018},
      abstract     = {The prion protein (PrP) is a cell surface protein that in
                      disease misfolds and becomes infectious causing
                      Creutzfeldt-Jakob disease in humans, scrapie in sheep, and
                      chronic wasting disease in deer and elk. Little is known
                      regarding the dimerization of PrP and its role in disease.
                      We developed a bioluminescent prion assay (BPA) to quantify
                      PrP dimerization by bimolecular complementation of split
                      Gaussia luciferase (GLuc) halves that are each fused to PrP.
                      Fusion constructs between PrP and N- and C-terminal GLuc
                      halves were expressed on the surface of RK13 cells (RK13-DC
                      cells) and dimerized to yield a bioluminescent signal that
                      was decreased in the presence of eight different antibodies
                      to PrP. Dimerization of PrP was independent of divalent
                      cations and was induced under stress. Challenge of RK13-DC
                      cells with seven different prion strains did not lead to
                      detectable infection but was measurable by bioluminescence.
                      Finally, we used BPA to screen a compound library for
                      compounds inhibiting PrP dimerization. One of the most
                      potent compounds to inhibit PrP dimerization was JTC-801,
                      which also inhibited prion replication in RML-infected ScN2a
                      and SMB cells with an EC50 of 370 nM and 220 nM,
                      respectively. We show here that BPA is a versatile tool to
                      study prion biology and to identify anti-prion compounds.},
      keywords     = {Animals / Biological Assay: methods / Cations, Divalent:
                      metabolism / Cell Line / Cell Line, Tumor /
                      Creutzfeldt-Jakob Syndrome: metabolism / Deer / Dimerization
                      / Humans / Luminescent Measurements: methods / Mice / Prion
                      Proteins: metabolism / Protein Folding / Rabbits / Scrapie:
                      metabolism / Sheep / Wasting Disease, Chronic: metabolism /
                      Cations, Divalent (NLM Chemicals) / Prion Proteins (NLM
                      Chemicals)},
      cin          = {AG Tamgüney 2},
      ddc          = {600},
      cid          = {I:(DE-2719)1013022},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30242186},
      pmc          = {pmc:PMC6155003},
      doi          = {10.1038/s41598-018-32581-1},
      url          = {https://pub.dzne.de/record/140214},
}