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@ARTICLE{Funke:20882,
      author       = {Funke, S.A. and Liu, H. and Sehl, T. and Bartnik, D. and
                      Brener, O. and Nagel-Steger, L. and Wiesehan, K. and
                      Willbold, D.},
      title        = {{I}dentification and characterization of an {A}ß; oligomer
                      precipitating peptide that may be useful to explore gene
                      therapeutic approaches to {A}lzheimer's disease},
      journal      = {Rejuvenation research},
      volume       = {15},
      issn         = {1549-1684},
      address      = {Larchmont, NY},
      publisher    = {Liebert},
      reportid     = {PreJuSER-20882},
      pages        = {144 - 147},
      year         = {2012},
      note         = {The authors gratefully acknowledge support from the
                      "Helmholtz-CSC (China Scholarship Council) Junior Scientists
                      Exchange Program" for Hongmei Liu.},
      abstract     = {A key feature of Alzheimer disease (AD) is the pathologic
                      self-association of the amyloid-β (Aβ) peptide, leading to
                      the formation of diffusible toxic Aβ oligomers and
                      extracellular amyloid plaques. Next to extracellular Aβ,
                      intraneuronal Aβ has important pathological functions in
                      AD. Agents that specifically interfere with the
                      oligomerization processes either outside or inside of
                      neurons are highly desired for the elucidation of the
                      pathologic mechanisms of AD and might even pave the way for
                      new AD gene therapeutic approaches. Here, we characterize
                      the Aβ binding peptide L3 and its influence on Aβ
                      oligomerization in vitro. Preliminary studies in cell
                      culture demonstrate that stably expressed L3 reduces cell
                      toxicity of externally added Aβ in neuroblastoma cells.},
      keywords     = {Alzheimer Disease: genetics / Alzheimer Disease: therapy /
                      Amyloid beta-Peptides: chemistry / Animals / Cell Line,
                      Tumor / Centrifugation, Density Gradient / Disease Models,
                      Animal / Gene Therapy: methods / Humans / Mice /
                      Nephelometry and Turbidimetry / Neurons: metabolism /
                      Peptides: chemistry / Sequence Analysis, DNA / Thiazoles:
                      chemistry / Amyloid beta-Peptides (NLM Chemicals) / Peptides
                      (NLM Chemicals) / Thiazoles (NLM Chemicals) / thioflavin T
                      (NLM Chemicals) / J (WoSType)},
      cin          = {ICS-6},
      ddc          = {610},
      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    = {Geriatrics $\&$ Gerontology},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22533419},
      UT           = {WOS:000303383600008},
      doi          = {10.1089/rej.2011.1262},
      url          = {https://juser.fz-juelich.de/record/20882},
}