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@ARTICLE{Funke:12404,
      author       = {Funke, S. A. and van Groen, T. and Kadish, I. and Bartnik,
                      D. and Nagel-Steger, L. and Brener, O. and Sehl, T. and
                      Batra-Safferling, R. and Moriscot, C. and Schoehn, G. and
                      Horn, A.H.C. and Müller-Schiffmann, A. and Korth, C. and
                      Sticht, H. and Willbold, D.},
      title        = {{O}ral {T}reatment with the {D}-{E}nantiomeric {P}eptide
                      {D}3 {I}mproves {P}athology and {B}ehavior of {A}lzheimers
                      disease {T}ransgenic {M}ice},
      journal      = {ACS chemical neuroscience},
      volume       = {1},
      issn         = {1948-7193},
      address      = {Washington, DC},
      publisher    = {Soc.},
      reportid     = {PreJuSER-12404},
      pages        = {639 - 648},
      year         = {2010},
      note         = {This work has been supported by a grant from
                      Volkswagen-Stiftung to D.W., C.K., and H.S. (I/82 649).
                      Support from the "Prasidentenfond der Helmholtzgemeinschaft"
                      (HGF, "Virtual Institute of Structural Biology") to D.W. is
                      acknowledged. C.M. was supported by a DGCIS grant (French
                      state). The electron microscopy facility used for this work
                      is part of the Partnership for Structural Biology (PSB).
                      Part of this research was supported by P30 NS47466. I.K. and
                      T.v.G have been supported by 5P50 AG16582-10.},
      abstract     = {Several lines of evidence suggest that the
                      amyloid-β-peptide (Aβ) plays a central role in the
                      pathogenesis of Alzheimer's disease (AD). Not only Aβ
                      fibrils but also small soluble Aβ oligomers in particular
                      are suspected to be the major toxic species responsible for
                      disease development and progression. The present study
                      reports on in vitro and in vivo properties of the Aβ
                      targeting d-enantiomeric amino acid peptide D3. We show that
                      next to plaque load and inflammation reduction, oral
                      application of the peptide improved the cognitive
                      performance of AD transgenic mice. In addition, we provide
                      in vitro data elucidating the potential mechanism underlying
                      the observed in vivo activity of D3. These data suggest that
                      D3 precipitates toxic Aβ species and converts them into
                      nonamyloidogenic, nonfibrillar, and nontoxic aggregates
                      without increasing the concentration of monomeric Aβ. Thus,
                      D3 exerts an interesting and novel mechanism of action that
                      abolishes toxic Aβ oligomers and thereby supports their
                      decisive role in AD development and progression.},
      keywords     = {J (WoSType)},
      cin          = {ISB-3},
      ddc          = {540},
      cid          = {I:(DE-Juel1)VDB942},
      pnm          = {Funktion und Dysfunktion des Nervensystems / BioSoft:
                      Makromolekulare Systeme und biologische
                      Informationsverarbeitung},
      pid          = {G:(DE-Juel1)FUEK409 / G:(DE-Juel1)FUEK505},
      shelfmark    = {Biochemistry $\&$ Molecular Biology / Chemistry, Medicinal
                      / Neurosciences},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22778851},
      pmc          = {pmc:PMC3368690},
      UT           = {WOS:000281891700007},
      doi          = {10.1021/cn100057j},
      url          = {https://juser.fz-juelich.de/record/12404},
}