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@ARTICLE{Linsenmeier:473388,
      author       = {Linsenmeier, Luise and Mohammadi, Behnam and Shafiq, Mohsin
                      and Frontzek, Karl and Bär, Julia and Shrivastava, Amulya
                      N. and Damme, Markus and Song, Feizhi and Schwarz, Alexander
                      and Da Vela, Stefano and Massignan, Tania and Jung,
                      Sebastian and Correia, Angela and Schmitz, Matthias and
                      Puig, Berta and Hornemann, Simone and Zerr, Inga and
                      Tatzelt, Jörg and Biasini, Emiliano and Saftig, Paul and
                      Schweizer, Michaela and Svergun, Dmitri and Amin, Ladan and
                      Mazzola, Federica and Varani, Luca and Thapa, Simrika and
                      Gilch, Sabine and Schätzl, Hermann and Harris, David A. and
                      Triller, Antoine and Mikhaylova, Marina and Aguzzi, Adriano
                      and Altmeppen, Hermann C. and Glatzel, Markus},
      title        = {{L}igands binding to the prion protein induce its
                      proteolytic release with therapeutic potential in
                      neurodegenerative proteinopathies},
      journal      = {Science advances},
      volume       = {7},
      number       = {48},
      issn         = {2375-2548},
      address      = {Washington, DC [u.a.]},
      publisher    = {Assoc.},
      reportid     = {PUBDB-2022-00011},
      pages        = {eabj1826},
      year         = {2021},
      abstract     = {The prion protein (PrPC) is a central player in
                      neurodegenerative diseases, such as prion diseases or
                      Alzheimer’sdisease. In contrast to disease-promoting cell
                      surface PrPC, extracellular fragments act neuroprotective by
                      blockingneurotoxic disease-associated protein conformers.
                      Fittingly, PrPC release by the metalloprotease
                      ADAM10represents a protective mechanism. We used
                      biochemical, cell biological, morphological, and structural
                      methodsto investigate mechanisms stimulating this
                      proteolytic shedding. Shed PrP negatively correlates with
                      prion conversionand is markedly redistributed in murine
                      brain in the presence of prion deposits or amyloid plaques,
                      indicatinga sequestrating activity. PrP-directed ligands
                      cause structural changes in PrPC and increased shedding in
                      cellsand organotypic brain slice cultures. As an exception,
                      some PrP-directed antibodies targeting repetitive epitopesdo
                      not cause shedding but surface clustering, endocytosis, and
                      degradation of PrPC. Both mechanisms may contributeto
                      beneficial actions described for PrP-directed ligands and
                      pave the way for new therapeutic strategiesagainst currently
                      incurable neurodegenerative diseases.},
      cin          = {EMBL-User / EMBL},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project 390688087 -
                      EXC 2049: Comprehensive approaches to neurological and
                      psychiatric disorders "NeuroCure" (390688087)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)390688087},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34818048},
      UT           = {WOS:000722215300013},
      doi          = {10.1126/sciadv.abj1826},
      url          = {https://bib-pubdb1.desy.de/record/473388},
}