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@ARTICLE{Schtzmann:1052089,
      author       = {Schützmann, Marie P. and Hoyer, Wolfgang},
      title        = {{O}ff-pathway oligomers of α-synuclein and {A}β inhibit
                      secondary nucleation of α-synuclein amyloid fibrils},
      journal      = {Journal of molecular biology},
      volume       = {437},
      number       = {10},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2026-00754},
      pages        = {169048 -},
      year         = {2025},
      abstract     = {α-Synuclein (αSyn) is a key culprit in the pathogenesis
                      of synucleinopathies such as Parkinson’s Disease (PD), in
                      which it forms not only insoluble aggregates called amyloid
                      fibrils but also smaller, likely more detrimental species
                      termed oligomers. This property is shared with other
                      amyloidogenic proteins such as the Alzheimer’s
                      Disease-associated amyloid-β (Aβ). We previously found an
                      intriguing interplay between off-pathway Aβ oligomers and
                      Aβ fibrils, in which the oligomers interfere with fibril
                      formation via inhibition of secondary nucleation by blocking
                      secondary nucleation sites on the fibril surface. Here,
                      using ThT aggregation kinetics and atomic force microscopy
                      (AFM), we tested if the same interplay applies to αSyn
                      fibrils. Both homotypic (i.e. αSyn) and heterotypic (i.e.
                      Aβ) off-pathway oligomers inhibited αSyn aggregation in
                      kinetic assays of secondary nucleation. Initially soluble,
                      kinetically trapped Aβ oligomers co-precipitated with
                      αSyn(1–108) fibrils. The resulting co-assemblies were
                      imaged as clusters of curvilinear oligomers by AFM. The
                      results indicate that off-pathway oligomers have a general
                      tendency to bind amyloid fibril surfaces, also in the
                      absence of sequence homology between fibril and oligomer.
                      The interplay between off-pathway oligomers and amyloid
                      fibrils adds another level of complexity to the homo- and
                      hetero-assembly processes of amyloidogenic proteins.},
      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},
      doi          = {10.1016/j.jmb.2025.169048},
      url          = {https://juser.fz-juelich.de/record/1052089},
}