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@ARTICLE{Shafiq:155621,
      author       = {Shafiq, Mohsin and Zafar, Saima and Younas, Neelam and
                      Noor, Aneeqa and Puig, Berta and Altmeppen, Hermann Clemens
                      and Schmitz, Matthias and Matschke, Jakob and Ferrer, Isidre
                      and Glatzel, Markus and Zerr, Inga},
      title        = {{P}rion protein oligomers cause neuronal cytoskeletal
                      damage in rapidly progressive {A}lzheimer's disease.},
      journal      = {Molecular neurodegeneration},
      volume       = {16},
      number       = {1},
      issn         = {1750-1326},
      address      = {London},
      publisher    = {Biomed Central},
      reportid     = {DZNE-2021-00789},
      pages        = {11},
      year         = {2021},
      abstract     = {High-density oligomers of the prion protein (HDPs) have
                      previously been identified in brain tissues of patients with
                      rapidly progressive Alzheimer's disease (rpAD). The current
                      investigation aims at identifying interacting partners of
                      HDPs in the rpAD brains to unravel the pathological
                      involvement of HDPs in the rapid progression.HDPs from the
                      frontal cortex tissues of rpAD brains were isolated using
                      sucrose density gradient centrifugation. Proteins
                      interacting with HDPs were identified by
                      co-immunoprecipitation coupled with mass spectrometry.
                      Further verifications were carried out using proteomic
                      tools, immunoblotting, and confocal laser scanning
                      microscopy.We identified rpAD-specific HDP-interactors,
                      including the growth arrest specific 2-like 2 protein
                      (G2L2). Intriguingly, rpAD-specific disturbances were found
                      in the localization of G2L2 and its associated proteins
                      i.e., the end binding protein 1, α-tubulin, and
                      β-actin.The results show the involvement of HDPs in the
                      destabilization of the neuronal actin/tubulin
                      infrastructure. We consider this disturbance to be a
                      contributing factor for the rapid progression in rpAD.},
      keywords     = {Alzheimer Disease: metabolism / Amyloid beta-Peptides:
                      metabolism / Brain: metabolism / Cytoskeleton: metabolism /
                      Cytoskeleton: pathology / Disease Progression / Humans /
                      Neurons: metabolism / Prion Proteins: metabolism / Actin
                      (Other) / Co-immunoprecipitation (Other) / Cytoskeleton
                      (Other) / G2L2 (Other) / GAS (Other) / Growth arrest
                      specific 2 like 2 (Other) / Growth arrest specific proteins
                      (Other) / PrPC (Other) / Prion protein oligomers (Other) /
                      Rapidly progressive Alzheimer’s disease (Other) / Tubulin
                      (Other) / rpAD (Other)},
      cin          = {Ext UMG Zerr / AG Zerr / Göttingen common},
      ddc          = {570},
      cid          = {I:(DE-2719)5000037 / I:(DE-2719)1440011-1 /
                      I:(DE-2719)6000014},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33618749},
      pmc          = {pmc:PMC7898440},
      doi          = {10.1186/s13024-021-00422-x},
      url          = {https://pub.dzne.de/record/155621},
}