% 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{Gruning:141924,
      author       = {Gruning, C. S. R. and Klinker, S. and Wolff, M. and
                      Schneider, M. and Toksöz, K. and Klein, A. N. and
                      Nagel-Steger, L. and Willbold, D. and Hoyer, W.},
      title        = {{T}he {O}ff-rate of {M}onomers {D}issociating from
                      {A}myloid-ß {P}rotofibrils},
      journal      = {The journal of biological chemistry},
      volume       = {288},
      number       = {52},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2014-00261},
      pages        = {37104 - 37111},
      year         = {2013},
      abstract     = {The interconversion of monomers, oligomers, and amyloid
                      fibrils of the amyloid-peptide (A) has been implicated in
                      the pathogenesis of Alzheimer disease. The determination of
                      the kinetics of the individual association and dissociation
                      reactions is hampered by the fact that forward and reverse
                      reactions to/from different aggregation states occur
                      simultaneously. Here, we report the kinetics of dissociation
                      of A Monomers from protofibrils, prefibrillar high molecular
                      weight oligomers previously shown to possess pronounced
                      neurotoxicity. An engineered binding protein sequestering
                      specifically mono-meric A was employed to follow protofibril
                      dissociation by tryptophan fluorescence, precluding
                      confounding effects of reverse or competing reactions. A
                      protofibril dissociation into monomers follows exponential
                      decay kinetics with a time constant of ~2 h at 25 °C and an
                      activation energy of 80 kJ/mol, values typical for high
                      affinity biomolecular interactions. This study demonstrates
                      the high kinetic stability of A protofibrils toward
                      dissociation into monomers and supports the delineation of
                      the A folding and assembly energy landscape.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452)},
      pid          = {G:(DE-HGF)POF2-452},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000329189700030},
      doi          = {10.1074/jbc.M113.513432},
      url          = {https://juser.fz-juelich.de/record/141924},
}