% 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{Dammers:829949,
      author       = {Dammers, Christina and Reiss, Kerstin and Gremer, Lothar
                      and Lecher, Justin and Ziehm, Tamar and Stoldt, Matthias and
                      Schwarten, Melanie and Willbold, Dieter},
      title        = {{P}yroglutamate-{M}odified {A}myloid- β (3–42) {S}hows
                      α -{H}elical {I}ntermediates before {A}myloid {F}ormation},
      journal      = {Biophysical journal},
      volume       = {112},
      number       = {8},
      issn         = {0006-3495},
      address      = {Cambridge, Mass.},
      publisher    = {Cell Press},
      reportid     = {FZJ-2017-03553},
      pages        = {1621 - 1633},
      year         = {2017},
      abstract     = {Pyroglutamate-modified amyloid-β (pEAβ) has been
                      described as a relevant Aβ species in
                      Alzheimer’s-disease-affected brains, with pEAβ (3–42)
                      as a dominant isoform. Aβ (1–40) and Aβ (1–42) have
                      been well characterized under various solution conditions,
                      including aqueous solutions containing trifluoroethanol
                      (TFE). To characterize structural properties of pEAβ
                      (3–42) possibly underlying its drastically increased
                      aggregation propensity compared to Aβ (1–42), we started
                      our studies in various TFE-water mixtures and found striking
                      differences between the two Aβ species. Soluble pEAβ
                      (3–42) has an increased tendency to form β-sheet-rich
                      structures compared to Aβ (1–42), as indicated by
                      circular dichroism spectroscopy data. Kinetic assays
                      monitored by thioflavin-T show drastically accelerated
                      aggregation leading to large fibrils visualized by electron
                      microscopy of pEAβ (3–42) in contrast to Aβ (1–42).
                      NMR spectroscopy was performed for backbone and side-chain
                      chemical-shift assignments of monomeric pEAβ (3–42) in
                      $40\%$ TFE solution. Although the difference between pEAβ
                      (3–42) and Aβ (1–42) is purely N-terminal, it has a
                      significant impact on the chemical environment of $>20\%$ of
                      the total amino acid residues, as revealed by their NMR
                      chemical-shift differences. Freshly dissolved pEAβ (3–42)
                      contains two α-helical regions connected by a flexible
                      linker, whereas the N-terminus remains unstructured. We
                      found that these α-helices act as a transient intermediate
                      to β-sheet and fibril formation of pEAβ (3–42).},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000400505800010},
      pubmed       = {pmid:28445753},
      doi          = {10.1016/j.bpj.2017.03.007},
      url          = {https://juser.fz-juelich.de/record/829949},
}