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@ARTICLE{Birkmann:60108,
      author       = {Birkmann, E. and Henke, F. and Weinmann, N and Dumpitak, C.
                      and Groshup, M. and Funke, A. and Willbold, D. and Riesner,
                      D.},
      title        = {{C}ounting of single prion particles bound to a
                      capture-antibody surface (surface-{FIDA})},
      journal      = {Veterinary microbiology},
      volume       = {123},
      issn         = {0378-1135},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier Science},
      reportid     = {PreJuSER-60108},
      pages        = {294 - 304},
      year         = {2007},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Hitherto accredited prion tests use the PK resistance of
                      PrP(Sc), the pathogenic isoform of the prion protein, as a
                      marker for the disease. Because of variations in the amount
                      of disease-related aggregated PrP, which is not
                      PK-resistant, these prion tests offer only limited
                      sensitivity. Therefore, a prion detection method that does
                      not rely on PK digestion would allow for the detection of
                      both PK-resistant as well as PK-sensitive PrP(Sc).
                      Furthermore, single particle counting is more sensitive than
                      methods measuring an integrated signal. Our new test system
                      is based on dual-colour fluorescence correlation
                      spectroscopy (FCS). This method quantifies the number of
                      protein aggregates that have been simultaneously labelled
                      with two different antibodies using dual-colour fluorescence
                      intensity distribution analysis (2D-FIDA). This only counts
                      PrP aggregates, and not PrP monomers. To increase the
                      sensitivity, PrP(Sc) was concentrated in a two-dimensional
                      space by immobilizing it so that the antibodies could be
                      captured on the surface of the slide (surface-FIDA). When
                      the surface was systematically scanned, even single prion
                      particles were detected. Using this new technique, the
                      sensitivity to identify samples from scrapie-infected
                      hamster as well as BSE-infected cattle can be dramatically
                      increased in comparison with identification using FIDA in
                      solution.},
      keywords     = {Animals / Blotting, Western: veterinary / Cattle /
                      Cricetinae / Electrophoresis, Polyacrylamide Gel: veterinary
                      / Encephalopathy, Bovine Spongiform: diagnosis /
                      Endopeptidase K: chemistry / Endopeptidase K: metabolism /
                      PrPSc Proteins: cerebrospinal fluid / PrPSc Proteins:
                      isolation $\&$ purification / Prion Diseases: diagnosis /
                      Prion Diseases: veterinary / Prions: isolation $\&$
                      purification / Scrapie: diagnosis / Sensitivity and
                      Specificity / Spectrometry, Fluorescence: methods /
                      Spectrometry, Fluorescence: veterinary / PrPSc Proteins (NLM
                      Chemicals) / Prions (NLM Chemicals) / Endopeptidase K (NLM
                      Chemicals) / J (WoSType)},
      cin          = {INB-2},
      ddc          = {630},
      cid          = {I:(DE-Juel1)VDB805},
      pnm          = {Funktion und Dysfunktion des Nervensystems},
      pid          = {G:(DE-Juel1)FUEK409},
      shelfmark    = {Microbiology / Veterinary Sciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:17499942},
      UT           = {WOS:000249306400003},
      doi          = {10.1016/j.vetmic.2007.04.001},
      url          = {https://juser.fz-juelich.de/record/60108},
}