% 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{Gardon:1021672,
      author       = {Gardon, Luis and Becker, Nina and Gremer, Lothar and Heise,
                      Henrike},
      title        = {{S}tructural {I}mpact of {N}‐terminal {P}yroglutamylate
                      in an {A}myloid‐β(3‐42) {F}ibril {P}robed by
                      {S}olid‐{S}tate {NMR} {S}pectroscopy},
      journal      = {Chemistry - a European journal},
      volume       = {30},
      number       = {10},
      issn         = {0947-6539},
      address      = {Weinheim},
      publisher    = {Wiley-VCH},
      reportid     = {FZJ-2024-00927},
      pages        = {e202303007},
      year         = {2024},
      abstract     = {Extracellular amyloid-β (Aβ) plaques, primarily formed by
                      Aβ(1-40) and Aβ(1-42) fibrils, are a hallmark of
                      Alzheimer's disease. The Aβ peptide can undergo a high
                      variety of different post-translational modifications
                      including formation of a pyroglutamate (pGlu, pE) at
                      N-terminal Glu3 or Glu11 of truncated Aβ(3-x) or Aβ(11-x),
                      respectively. Here we studied structural similarities and
                      differences between pEAβ(3-42) and LS-shaped Aβ(1-42)
                      fibrils grown under identical conditions (pH 2) using
                      solid-state NMR spectroscopy. We show that the central
                      region of pEAβ(3-42) fibrils including the turn region
                      around V24 is almost identical to Aβ(1-42) showing similar
                      β-strands also at the N-terminus. The missing N-terminal
                      residues D1-A2 along with pE3 formation in pEAβ(3-42)
                      preclude a salt bridge between K28-D1' as in Aβ(1-42)
                      fibrils. G37 and G38 act as highly sensitive internal
                      sensors for the modified N-terminus, which remains rigid
                      over ~five pH units.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:001138572000001},
      doi          = {10.1002/chem.202303007},
      url          = {https://juser.fz-juelich.de/record/1021672},
}