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@ARTICLE{Pesch:1025963,
      author       = {Pesch, Verena and Flores-Fernandez, José Miguel and
                      Reithofer, Sara and Ma, Liang and Özdüzenciler, Pelin and
                      Busch, Yannick and Sriraman, Aishwarya and Wang, YongLiang
                      and Amidian, Sara and Kroepel, Chiara V M and Müller, Laura
                      and Lien, Yi and Rudtke, Olivia and Frieg, Benedikt and
                      Schröder, Gunnar F and Wille, Holger and Tamgüney,
                      Gültekin},
      title        = {{V}accination with structurally adapted fungal protein
                      fibrils induces immunity to {P}arkinson’s disease},
      journal      = {Brain},
      volume       = {147},
      number       = {5},
      issn         = {0006-8950},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {FZJ-2024-03241},
      pages        = {1644-1652},
      year         = {2024},
      abstract     = {The pathological misfolding and aggregation of soluble
                      α-synuclein into toxic oligomers and insoluble amyloid
                      fibrils causes Parkinson's disease, a progressive
                      age-related neurodegenerative disease for which there is no
                      cure. HET-s is a soluble fungal protein that can form
                      assembled amyloid fibrils in its prion state. We engineered
                      HET-s(218-298) to form four different fibrillar vaccine
                      candidates, each displaying a specific conformational
                      epitope present on the surface of α-synuclein fibrils.
                      Vaccination with these four vaccine candidates prolonged the
                      survival of immunized TgM83+/- mice challenged with
                      α-synuclein fibrils by $8\%$ when injected into the brain
                      to model brain-first Parkinson's disease or by $21\%$ and
                      $22\%$ when injected into the peritoneum or gut wall,
                      respectively, to model body-first Parkinson's disease.
                      Antibodies from fully immunized mice recognized α-synuclein
                      fibrils and brain homogenates from patients with Parkinson's
                      disease, dementia with Lewy bodies and multiple system
                      atrophy. Conformation-specific vaccines that mimic epitopes
                      present only on the surface of pathological fibrils but not
                      on soluble monomers, hold great promise for protection
                      against Parkinson's disease, related synucleinopathies and
                      other amyloidogenic protein misfolding disorders.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {38428032},
      UT           = {WOS:001206420100001},
      doi          = {10.1093/brain/awae061},
      url          = {https://juser.fz-juelich.de/record/1025963},
}