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@ARTICLE{Santur:893035,
      author       = {Santur, Karoline and Reinartz, Elke and Lien, Yi and
                      Tusche, Markus and Altendorf, Tim and Sevenich, Marc and
                      Tamgüney, Gültekin and Mohrlüder, Jeannine and Willbold,
                      Dieter},
      title        = {{L}igand-{I}nduced {S}tabilization of the {N}ative {H}uman
                      {S}uperoxide {D}ismutase 1},
      journal      = {ACS chemical neuroscience},
      volume       = {12},
      number       = {13},
      issn         = {1948-7193},
      address      = {Washington, DC},
      publisher    = {ACS Publ.},
      reportid     = {FZJ-2021-02515},
      pages        = {2520–2528},
      year         = {2021},
      abstract     = {A common characteristic of familial (fALS) and sporadic
                      amyotrophic lateral sclerosis (sALS) is the accumulation of
                      aberrant proteinaceous species in the motor neurons and
                      spinal cord of ALS patients—including aggregates of the
                      human superoxide dismutase 1 (hSOD1). hSOD1 is an enzyme
                      that occurs as a stable dimeric protein with several
                      post-translational modifications such as the formation of an
                      intramolecular disulfide bond and the acquisition of metal
                      cofactors that are essential for enzyme activity and further
                      contribute to protein stability. Some mutations and/or
                      destabilizing factors promote hSOD1 misfolding, causing
                      neuronal death. Aggregates containing misfolded wild-type
                      hSOD1 have been found in the spinal cords of sALS as well as
                      in non-hSOD1 fALS patients, leading to the hypothesis that
                      hSOD1 misfolding is a common part of the ALS pathomechanism.
                      Therefore, stabilizing the native conformation of SOD1 may
                      be a promising approach to prevent the formation of toxic
                      hSOD1 species and thus ALS pathogenesis. Here, we present
                      the 16-mer peptide S1VL-21 that interferes with hSOD1
                      aggregation. S1VL-21 was identified by phage display
                      selection with the native conformation of hSOD1 as a target.
                      Several methods such as microscale thermophoresis (MST)
                      measurements, aggregation assays, and cell viability assays
                      revealed that S1VL-21 has a micromolar binding affinity to
                      native hSOD1 and considerably reduces the formation of hSOD1
                      aggregates. This present work therefore provides the first
                      important data on a potential lead compound for
                      hSOD1-related drug development for ALS therapy.},
      cin          = {IBI-7},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {551 - Functional Macromolecules and Complexes (POF3-551) /
                      5244 - Information Processing in Neuronal Networks
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF3-551 / G:(DE-HGF)POF4-5244},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34138531},
      UT           = {WOS:000672585800022},
      doi          = {10.1021/acschemneuro.1c00253},
      url          = {https://juser.fz-juelich.de/record/893035},
}