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@ARTICLE{Muschol:1017565,
      author       = {Muschol, Martin and Hoyer, Wolfgang},
      title        = {{A}myloid oligomers as on-pathway precursors or off-pathway
                      competitors of fibrils},
      journal      = {Frontiers in molecular biosciences},
      volume       = {10},
      issn         = {2296-889X},
      address      = {Lausanne},
      publisher    = {Frontiers},
      reportid     = {FZJ-2023-04205},
      pages        = {1120416},
      year         = {2023},
      abstract     = {Amyloid Diseases involve the growth of disease specific
                      proteins into amyloid fibrils and their deposition in
                      protein plaques. Amyloid fibril formation is typically
                      preceded by oligomeric intermediates. Despite significant
                      efforts, the specific role fibrils or oligomers play in the
                      etiology of any given amyloid disease remains controversial.
                      In neurodegenerative disease, though, amyloid oligomers are
                      widely considered critical contributors to disease symptoms.
                      Aside from oligomers as inevitable on-pathway precursors of
                      fibril formation, there is significant evidence for
                      off-pathway oligomer formation competing with fibril growth.
                      The distinct mechanisms and pathways of oligomer formation
                      directly affect our understanding under which conditions
                      oligomers emerge in vivo, and whether their formation is
                      directly coupled to, or distinct from, amyloid fibril
                      formation. In this review, we will discuss the basic energy
                      landscapes underlying the formation of on-pathway vs.
                      off-pathway oligomers, their relation to the related amyloid
                      aggregation kinetics, and their resulting implications for
                      disease etiology. We will review evidence on how differences
                      in the local environment of amyloid assembly can
                      dramatically shift the relative preponderance of oligomers
                      vs. fibrils. Finally, we will comment on gaps in our
                      knowledge of oligomer assembly, of their structure, and on
                      how to assess their relevance to disease etiology.},
      cin          = {IBI-7},
      ddc          = {570},
      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)36 / PUB:(DE-HGF)16},
      pubmed       = {36845541},
      UT           = {WOS:000937088500001},
      doi          = {10.3389/fmolb.2023.1120416},
      url          = {https://juser.fz-juelich.de/record/1017565},
}