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@ARTICLE{Funke:22156,
      author       = {Funke, S.A. and Bartnik, D. and Glück, J.M. and Pirkowska,
                      K. and Wiesehan, K. and Weber, U. and Gulyas, B. and
                      Halldin, C. and Pfeifer, A. and Spenger, C. and Muhs, A. and
                      Willbold, D.},
      title        = {{D}evelopment of a small {D}-enantiomeric {A}lzheimer's
                      amyloid-beta binding peptide ligand for future in vivo
                      imaging applications},
      journal      = {PLoS one},
      volume       = {7},
      number       = {7},
      issn         = {1932-6203},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PreJuSER-22156},
      pages        = {e41457},
      year         = {2012},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Alzheimer's disease (AD) is a devastating disease affecting
                      predominantly the aging population. One of the
                      characteristic pathological hallmarks of AD are neuritic
                      plaques, consisting of amyloid-β peptide (Aβ). While there
                      has been some advancement in diagnostic classification of AD
                      patients according to their clinical severity, no fully
                      reliable method for pre-symptomatic diagnosis of AD is
                      available. To enable such early diagnosis, which will allow
                      the initiation of treatments early in the disease progress,
                      neuroimaging tools are under development, making use of
                      Aβ-binding ligands that can visualize amyloid plaques in
                      the living brain. Here we investigate the properties of a
                      newly designed series of D-enantiomeric peptides which are
                      derivatives of ACI-80, formerly called D1, which was
                      developed to specifically bind aggregated Aβ1-42. We
                      describe ACI-80 derivatives with increased stability and Aβ
                      binding properties, which were characterized using surface
                      plasmon resonance and enzyme-linked immunosorbent assays.
                      The specific interactions of the lead compounds with amyloid
                      plaques were validated by ex vivo immunochemistry in
                      transgenic mouse models of AD. The novel compounds showed
                      increased binding affinity and are promising candidates for
                      further development into in vivo imaging compounds.},
      keywords     = {J (WoSType)},
      cin          = {ICS-6},
      ddc          = {500},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22848501},
      pmc          = {pmc:PMC3404088},
      UT           = {WOS:000306751300042},
      doi          = {10.1371/journal.pone.0041457},
      url          = {https://juser.fz-juelich.de/record/22156},
}