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@ARTICLE{Margreiter:906017,
      author       = {Margreiter, Michael A and Witzenberger, Monika and Wasser,
                      Yasmine and Davydova, Elena and Janowski, Robert and Metz,
                      Jonas and Habib, Pardes and Sahnoun, Sabri E. M. and
                      Sobisch, Carina and Poma, Benedetta and Palomino-Hernandez,
                      Oscar and Wagner, Mirko and Carell, Thomas and Shah, N. J.
                      and Schulz, Jörg B. and Niessing, Dierk and Voigt, Aaron
                      and Rossetti, Giulia},
      title        = {{S}mall-molecule modulators of {TRMT}2{A} decrease
                      {P}oly{Q} aggregation and {P}oly{Q}-induced cell death},
      journal      = {Computational and structural biotechnology journal},
      volume       = {20},
      issn         = {2001-0370},
      address      = {Gotenburg},
      publisher    = {Research Network of Computational and Structural
                      Biotechnology (RNCSB)},
      reportid     = {FZJ-2022-01182},
      pages        = {443 - 458},
      year         = {2022},
      abstract     = {Polyglutamine (polyQ) diseases are characterized by an
                      expansion of cytosine-adenine-guanine (CAG) trinucleotide
                      repeats encoding for an uninterrupted prolonged polyQ tract.
                      We previously identified TRMT2A as a strong modifier of
                      polyQ-induced toxicity in an unbiased large-scale screen in
                      Drosophila melanogaster. This work aimed at identifying and
                      validating pharmacological TRMT2A inhibitors as treatment
                      opportunities for polyQ diseases in humans. Computer-aided
                      drug discovery was implemented to identify human TRMT2A
                      inhibitors. Additionally, the crystal structure of one
                      protein domain, the RNA recognition motif (RRM), was
                      determined, and Biacore experiments with the RRM were
                      performed. The identified molecules were validated for their
                      potency to reduce polyQ aggregation and polyQ-induced cell
                      death in human HEK293T cells and patient derived
                      fibroblasts. Our work provides a first step towards
                      pharmacological inhibition of this enzyme and indicates
                      TRMT2A as a viable drug target for polyQ diseases.},
      cin          = {INM-4 / INM-11 / JARA-BRAIN / JSC / INM-9},
      ddc          = {570},
      cid          = {I:(DE-Juel1)INM-4-20090406 / I:(DE-Juel1)INM-11-20170113 /
                      I:(DE-Juel1)VDB1046 / I:(DE-Juel1)JSC-20090406 /
                      I:(DE-Juel1)INM-9-20140121},
      pnm          = {5253 - Neuroimaging (POF4-525) / 5111 - Domain-Specific
                      Simulation $\&$ Data Life Cycle Labs (SDLs) and Research
                      Groups (POF4-511)},
      pid          = {G:(DE-HGF)POF4-5253 / G:(DE-HGF)POF4-5111},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:35070167},
      UT           = {WOS:000819903300015},
      doi          = {10.1016/j.csbj.2021.12.029},
      url          = {https://juser.fz-juelich.de/record/906017},
}