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@ARTICLE{Sun:23150,
      author       = {Sun, N. and Hartmann, R. and Lecher, J. and Stoldt, M. and
                      Funke, S.A. and Gremer, L. and Ludwig, H.-H. and Demuth,
                      H.U. and Kleinschmidt, H. and Willbold, D.},
      title        = {{S}tructural analysis of the pyroglutamate modified isoform
                      of the {A}lzheimer's disease related beta-amyloid using
                      {NMR} spectroscopy},
      journal      = {Journal of peptide science},
      volume       = {18},
      issn         = {1075-2617},
      address      = {New York, NY [u.a.]},
      publisher    = {Wiley},
      reportid     = {PreJuSER-23150},
      pages        = {691 - 695},
      year         = {2012},
      note         = {Record converted from VDB: 12.11.2012},
      abstract     = {The aggregation of the Aβ plays a fundamental role in the
                      pathology of AD. Recently, N-terminally modified Aβ
                      species, pE-Aβ, have been described as major constituents
                      of Aβ deposits in the brains of AD patients. pE-Aβ has an
                      increased aggregation propensity and shows increased
                      toxicity compared with Aβ1-40 and Aβ1-42. In the present
                      work, high-resolution NMR spectroscopy was performed to
                      study pE-Aβ3-40 in aqueous TFE-containing solution.
                      Two-dimensional TOCSY and NOESY experiments were performed.
                      On the basis of NOE and chemical shift data, pE-Aβ3-40 was
                      shown to contain two helical regions formed by residues
                      14-22 and 30-36. This is similar as previously described for
                      Aβ1-40. However, the secondary chemical shift data indicate
                      decreased helical propensity in pE-Aβ3-40 when compared
                      with Aβ1-40 under exactly the same conditions. This is in
                      agreement with the observation that pE-Aβ3-40 shows a
                      drastically increased tendency to form β-sheet-rich
                      structures under more physiologic conditions. Structural
                      studies of pE-Aβ are crucial for better understanding the
                      structural basis of amyloid fibril formation in the brain
                      during development of AD, especially because an increasing
                      number of reports indicate a decisive role of pE-Aβ for the
                      pathogenesis of AD. Copyright © 2012 European Peptide
                      Society and John Wiley $\&$ Sons, Ltd.},
      cin          = {ICS-6},
      ddc          = {570},
      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},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23001756},
      UT           = {WOS:000310029900006},
      doi          = {10.1002/psc.2456},
      url          = {https://juser.fz-juelich.de/record/23150},
}