% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Bartnik:9877,
      author       = {Bartnik, D. and Funke, S. A. and Andrei-Selmer, L.C. and
                      Bacher, M. and Dodel, R. and Willbold, D.},
      title        = {{D}ifferently {S}elected {D}-{E}nantiomeric {P}eptides
                      {A}ct on {D}ifferent {A} beta {S}pecies},
      journal      = {Rejuvenation research},
      volume       = {13},
      issn         = {1549-1684},
      address      = {Larchmont, NY},
      publisher    = {Liebert},
      reportid     = {PreJuSER-9877},
      year         = {2010},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {Aging is the most significant risk factor for Alzheimer
                      disease (AD). The pathological hallmark of AD is the
                      accumulation of aggregated amyloid-beta (Abeta) forms and
                      insoluble plaques, mainly composed of Abeta, in the brain of
                      the patient. Recently, we reported on the selection of
                      D-enantiomeric, Abeta-binding peptides D1 and D3. D1 was
                      selected against aggregated Abeta species to address
                      diagnosis by in vivo imaging of amyloid plaques, whereas D3
                      was selected using low-molecular-weight Abeta species,
                      therefore addressing therapeutical studies. Here, we use a
                      surface plasmon resonance method to confirm that both
                      peptides show the desired binding specificities.},
      keywords     = {Alzheimer Disease: diagnosis / Alzheimer Disease:
                      metabolism / Alzheimer Disease: pathology / Amyloid:
                      analysis / Amyloid: chemistry / Amyloid beta-Peptides:
                      chemistry / Amyloid beta-Peptides: drug effects / Amyloid
                      beta-Peptides: metabolism / Humans / Oligopeptides:
                      chemistry / Oligopeptides: metabolism / Oligopeptides:
                      pharmacology / Peptide Fragments: chemistry / Peptide
                      Fragments: isolation $\&$ purification / Peptide Fragments:
                      metabolism / Peptide Fragments: pharmacology / Plaque,
                      Amyloid: chemistry / Plaque, Amyloid: drug effects / Plaque,
                      Amyloid: metabolism / Protein Binding / Protein Isoforms:
                      analysis / Protein Isoforms: chemistry / Protein
                      Multimerization: drug effects / Substrate Specificity /
                      Surface Plasmon Resonance / Amyloid (NLM Chemicals) /
                      Amyloid beta-Peptides (NLM Chemicals) / D3 peptide (NLM
                      Chemicals) / Oligopeptides (NLM Chemicals) / Peptide
                      Fragments (NLM Chemicals) / Protein Isoforms (NLM Chemicals)
                      / J (WoSType)},
      cin          = {ISB-3 / JARA-HPC},
      ddc          = {610},
      cid          = {I:(DE-Juel1)VDB942 / $I:(DE-82)080012_20140620$},
      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:19954333},
      UT           = {WOS:000277602200017},
      doi          = {10.1089/rej.2009.0924},
      url          = {https://juser.fz-juelich.de/record/9877},
}