% 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{Hfs:1030668,
      author       = {Höfs, Lennart and Geißler-Lösch, David and Wunderlich,
                      Kristof M. and Szegö, Eva M. and Van den Haute, Chris and
                      Baekelandt, Veerle and Hoyer, Wolfgang and Falkenburger,
                      Björn H.},
      title        = {{E}valuation of the {E}ffect of β-{W}rapin {AS}69 in a
                      {M}ouse {M}odel {B}ased on {A}lpha-{S}ynuclein
                      {O}verexpression},
      journal      = {Biomolecules},
      volume       = {14},
      number       = {7},
      issn         = {2218-273X},
      address      = {Basel},
      publisher    = {MDPI},
      reportid     = {FZJ-2024-05392},
      pages        = {756 -},
      year         = {2024},
      abstract     = {Aggregation of the protein α-Synuclein (αSyn) is a
                      hallmark of Parkinson’s disease (PD), dementia with Lewy
                      bodies (DLB) and multiple systems atrophy, and alleviating
                      the extent of αSyn pathology is an attractive strategy
                      against neurodegeneration. The engineered binding protein
                      β-wrapin AS69 binds monomeric αSyn. AS69 reduces primary
                      and secondary nucleation as well as fibril elongation in
                      vitro. It also mitigates aSyn pathology in a mouse model
                      based on intrastriatal injection of aSyn pre-formed fibrils
                      (PFFs). Since the PFF-based model does not represent all
                      aspects of PD, we tested here whether AS69 can reduce
                      neurodegeneration resulting from αSyn overexpression. Human
                      A53T-αSyn was overexpressed in the mouse Substantia nigra
                      (SN) by using recombinant adeno-associated viral vector
                      (rAAV). AS69 was also expressed by rAAV transduction.
                      Behavioral tests and immunofluorescence staining were used
                      as outcomes. Transduction with rAAV-αSyn resulted in αSyn
                      pathology as reported by phospho-αSyn staining and caused
                      degeneration of dopaminergic neurons in the SN. The
                      co-expression of rAAV-AS69 did not reduce αSyn pathology or
                      the degeneration of dopaminergic neurons. We conclude that
                      αSyn monomer binding by rAAV-AS69 was insufficient to
                      protect from aSyn pathology resulting from αSyn
                      overexpression.},
      cin          = {IBI-7},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {39062470},
      UT           = {WOS:001276686300001},
      doi          = {10.3390/biom14070756},
      url          = {https://juser.fz-juelich.de/record/1030668},
}