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@ARTICLE{Graewert:618954,
      author       = {Graewert, Melissa A. and Volkova, Maria and Jonasson, Klara
                      and Määttä, Juha A. E. and Gräwert, Tobias and Mamidi,
                      Samara and Kulesskaya, Natalia and Evenäs, Johan and
                      Johnsson, Richard E. and Svergun, Dmitri and Bhattacharjee,
                      Arnab and Huttunen, Henri J.},
      title        = {{S}tructural basis of {CDNF} interaction with the {UPR}
                      regulator {GRP}78},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2024-07265},
      pages        = {8175},
      year         = {2024},
      abstract     = {Cerebral dopamine neurotrophic factor (CDNF) is an
                      unconventional neurotrophic factor that is a
                      disease-modifying drug candidate for Parkinson’s disease.
                      CDNF has pleiotropic protective effects on stressed cells,
                      but its mechanism of action remains incompletely understood.
                      Here, we use state-of-the-art advanced structural techniques
                      to resolve the structural basis of CDNF interaction with
                      GRP78, the master regulator of the unfolded protein response
                      (UPR) pathway. Subsequent binding studies confirm the
                      obtained structural model of the complex, eventually
                      revealing the interaction site of CDNF and GRP78. Finally,
                      mutating the key residues of CDNF mediating its interaction
                      with GRP78 not only results in impaired binding of CDNF but
                      also abolishes the neuroprotective activity of CDNF-derived
                      peptides in mesencephalic neuron cultures. These results
                      suggest that the molecular interaction with GRP78 mediates
                      the neuroprotective actions of CDNF and provide a structural
                      basis for development of next generation CDNF-based
                      therapeutic compounds against neurodegenerative diseases.},
      cin          = {EMBL-User / EMBL},
      ddc          = {500},
      cid          = {I:(DE-H253)EMBL-User-20120814 / I:(DE-H253)EMBL-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / iNEXT-Discovery -
                      Infrastructure for transnational access and discovery in
                      structural biology (871037)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(EU-Grant)871037},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39289391},
      UT           = {WOS:001376977000003},
      doi          = {10.1038/s41467-024-52478-0},
      url          = {https://bib-pubdb1.desy.de/record/618954},
}