% 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{Yang:841860,
      author       = {Yang, Ge and Yu, Kun and Kaitatzi, Christina-Symina and
                      Singh, Abhilasha and Labahn, Jörg},
      title        = {{I}nfluence of solubilization and {AD}-mutations on
                      stability and structure of human presenilins},
      journal      = {Scientific reports},
      volume       = {7},
      number       = {1},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2018-00157},
      pages        = {17970},
      year         = {2017},
      abstract     = {Presenilin (PS1 or PS2) functions as the catalytic subunit
                      of γ-secretase, which produces the toxic amyloid beta
                      peptides in Alzheimer’s disease (AD). The dependence of
                      folding and structural stability of PSs on the lipophilic
                      environment and mutation were investigated by far UV CD
                      spectroscopy. The secondary structure content and stability
                      of PS2 depended on the lipophilic environment. PS2 undergoes
                      a temperature-dependent structural transition from
                      α-helical to β-structure at 331 K. The restructured
                      protein formed structures which tested positive in
                      spectroscopic amyloid fibrils assays. The AD mutant
                      PS1L266F, PS1L424V and PS1ΔE9 displayed reduced stability
                      which supports a proposed ‘loss of function’ mechanism
                      of AD based on protein instability. The exon 9 coded
                      sequence in the inhibitory loop of the zymogen was found to
                      be required for the modulation of the thermal stability of
                      PS1 by the lipophilic environment.},
      cin          = {ICS-6},
      ddc          = {000},
      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},
      pubmed       = {pmid:29269939},
      UT           = {WOS:000418562100010},
      doi          = {10.1038/s41598-017-18313-x},
      url          = {https://juser.fz-juelich.de/record/841860},
}