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@ARTICLE{Arshad:276154,
      author       = {Arshad, Hamza and Eid, Shehab and Mehra, Surabhi and
                      Williams, Declan and Kaczmarczyk, Lech and Stuart, Erica and
                      Jackson, Walker Scot and Schmitt-Ulms, Gerold and Watts,
                      Joel C},
      title        = {{T}he brain interactome of a permissive prion replication
                      substrate.},
      journal      = {Neurobiology of disease},
      volume       = {206},
      issn         = {0969-9961},
      address      = {[Amsterdam]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2025-00226},
      pages        = {106802},
      year         = {2025},
      abstract     = {Bank voles are susceptible to prion strains from many
                      different species, yet the molecular mechanisms underlying
                      the ability of bank vole prion protein (BVPrP) to function
                      as a universal prion acceptor remain unclear. Potential
                      differences in molecular environments and protein
                      interaction networks on the cell surface of brain cells may
                      contribute to BVPrP's unusual behavior. To test this
                      hypothesis, we generated knock-in mice that express
                      physiological levels of BVPrP (M109 isoform) and employed
                      mass spectrometry to compare the interactomes of mouse (Mo)
                      PrP and BVPrP following mild in vivo crosslinking of brain
                      tissue. Substantial overlap was observed between the top
                      interactors for BVPrP and MoPrP, with established
                      PrP-interactors such as neural cell adhesion molecules,
                      subunits of Na+/K+-ATPases, and contactin-1 being equally
                      present in the two interactomes. We conclude that the
                      molecular environments of BVPrP and MoPrP in the brains of
                      mice are very similar. This suggests that the unorthodox
                      properties of BVPrP are unlikely to be mediated by
                      differential interactions with other proteins.},
      keywords     = {Bank voles (Other) / Knock-in mice (Other) / Mass
                      spectrometry (Other) / Prion (Other) / Protein-protein
                      interactions (Other)},
      cin          = {AG Jackson},
      ddc          = {570},
      cid          = {I:(DE-2719)1013019},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39800229},
      doi          = {10.1016/j.nbd.2025.106802},
      url          = {https://pub.dzne.de/record/276154},
}