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@ARTICLE{Leitz:1043722,
      author       = {Leitz, Anna and Kav, Batuhan and Liu, Xiyang and Fatafta,
                      Hebah and Jankowski, Vera and Aggeler, Bastian and Gao,
                      Yingying and Martin, Ina Verena and Vogt, Kristian and
                      Kramann, Rafael and Ostendorf, Tammo and Rauen, Thomas and
                      Strodel, Birgit and Raffetseder, Ute},
      title        = {{G}uanidinylation of the cold shock protein {YB} ‐1:
                      {M}olecular basis, structural changes and {N}otch‐3
                      receptor binding},
      journal      = {Protein science},
      volume       = {34},
      number       = {7},
      issn         = {0961-8368},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {FZJ-2025-03008},
      pages        = {e70188},
      year         = {2025},
      abstract     = {Posttranslational modifications of Y-box binding protein
                      (YB)-1 are the prerequisite for its very different protein
                      functions. Here, we investigate the underlying molecular
                      mechanisms of YB-1 guanidinylation and link increased serum
                      urea levels as well as the activity of glycine
                      amidinotransferase (GATM) with guanidinylation. Computer
                      simulations show changes in stability and conformation of
                      the YB-1 protein induced by these modifications. In
                      particular, the secondary structure of the doubly
                      guanidinylated YB-1 (YB-1-2G) shows a reduced tendency to
                      form β-sheets, and the modified cold shock domain is more
                      exposed to the solvent. Protein-protein docking techniques
                      in conjunction with molecular dynamics simulations confirm
                      the binding between YB-1 and its receptor Notch-3 at EGF
                      domains 17-24 but show no significant differences in the
                      binding behavior of YB-1 and YB-1-2G. This is confirmed in
                      two different types of receptor-ligand binding assays. In
                      addition, we demonstrate for the first time a high-affinity
                      binding of YB-1 to another ligand binding site on the
                      Notch-3 receptor, thereby achieving effective displacement
                      of the canonical ligand Jagged. In conclusion, we identified
                      molecular processes that lead to the guanidinylation of YB-1
                      and revealed their effects on the structure and binding to
                      receptor Notch-3.},
      cin          = {IBI-7},
      ddc          = {610},
      cid          = {I:(DE-Juel1)IBI-7-20200312},
      pnm          = {5241 - Molecular Information Processing in Cellular Systems
                      (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {40563206},
      UT           = {WOS:001516471300001},
      doi          = {10.1002/pro.70188},
      url          = {https://juser.fz-juelich.de/record/1043722},
}