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@ARTICLE{Cukkemane:1043690,
      author       = {Cukkemane, Abhishek and Dingley, Andrew J. and Mohrlüder,
                      Jeannine and Santiago-Schübel, Beatrix and Weiergräber,
                      Oliver H. and Willbold, Dieter},
      title        = {{A} peptide mimetic therapeutic strategy targeting
                      dysfunction of the scaffold protein {DISC}-1 in psychiatric
                      disorders},
      journal      = {European journal of pharmaceutical sciences},
      volume       = {211},
      issn         = {0928-0987},
      address      = {New York, NY [u.a.]},
      publisher    = {Elsevier},
      reportid     = {FZJ-2025-02988},
      pages        = {107148 -},
      year         = {2025},
      abstract     = {Disrupted in schizophrenia 1 (DISC1) is a scaffold protein
                      that regulates several physiological processes ranging from
                      cellular division to neurodevelopment, and its dysfunction
                      contributes to various neurological disorders including
                      schizophrenia, bipolar and mood disorders, and autism. Thus,
                      deciphering its native functions and pathophysiological
                      roles is crucial. In this report, three disease-associated
                      mutants of the C-region of DISC1, i.e., S713E, S704C, and
                      L807-frameshift, were examined to further elucidate the role
                      of DISC1 in cell division. We demonstrate that the mutations
                      do not render the variants functionally inactive; instead,
                      the interaction sites are presumably lost during the
                      aggregation of the DISC1 C-region into amyloid-type fibrils.
                      The minimal fibrillizing element in the C-region is the
                      intrinsically disordered β-core (716‒761) that houses a
                      segment absent in the splice variant DISC1Δ22aa, which
                      cannot bind proteins of the mitotic spindle complex and thus
                      hampers cellular proliferation. Based on these
                      structure-function relationships, we present a rational drug
                      development strategy using phage display technology and
                      highlight the role of peptide mimetics in curtailing the
                      agglomeration of fibrils.},
      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       = {40449672},
      UT           = {WOS:001504428300002},
      doi          = {10.1016/j.ejps.2025.107148},
      url          = {https://juser.fz-juelich.de/record/1043690},
}