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@ARTICLE{Reichelt:599937,
      author       = {Reichelt, Julia and Sachs, Wiebke and Frömbling, Sarah and
                      Fehlert, Julia and Studencka-Turski, Maja and Betz, Anna and
                      Loreth, Desiree and Blume, Lukas and Witt, Susanne and Pohl,
                      Sandra and Brand, Johannes and Czesla, Maire and Knop, Jan
                      and Florea, Bogdan I. and Zielinski, Stephanie and Sachs,
                      Marlies and Hoxha, Elion and Hermans-Borgmeyer, Irm and
                      Zahner, Gunther and Wiech, Thorsten and Krüger, Elke and
                      Meyer-Schwesinger, Catherine},
      title        = {{N}on-functional ubiquitin {C}-terminal hydrolase {L}1
                      drives podocyte injury through impairing proteasomes in
                      autoimmune glomerulonephritis},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {London},
      publisher    = {Nature Publishing Group UK},
      reportid     = {PUBDB-2023-07626},
      pages        = {2114},
      year         = {2023},
      note         = {The authors would like to thank Antonio Virgillio Failla
                      from the UMIF,UKE and Roland Thuenauer from the ALFM, CSSB,
                      DESY for technicalassistance in super resolution
                      microscopy.},
      abstract     = {Little is known about the mechanistic significance of the
                      ubiquitin proteasome system (UPS) in a kidney autoimmune
                      environment. In membranous nephropathy (MN), autoantibodies
                      target podocytes of the glomerular filter resulting in
                      proteinuria. Converging biochemical, structural, mouse
                      pathomechanistic, and clinical information we report that
                      the deubiquitinase Ubiquitin C-terminal hydrolase L1
                      (UCH-L1) is induced by oxidative stress in podocytes and is
                      directly involved in proteasome substrate accumulation.
                      Mechanistically, this toxic gain-of-function is mediated by
                      non-functional UCH-L1, which interacts with and thereby
                      impairs proteasomes. In experimental MN, UCH-L1 becomes
                      non-functional and MN patients with poor outcome exhibit
                      autoantibodies with preferential reactivity to
                      non-functional UCH-L1. Podocyte-specific deletion of UCH-L1
                      protects from experimental MN, whereas overexpression of
                      non-functional UCH-L1 impairs podocyte proteostasis and
                      drives injury in mice. In conclusion, the UPS is
                      pathomechanistically linked to podocyte disease by aberrant
                      proteasomal interactions of non-functional UCH-L1.},
      cin          = {FS-CS / CSSB-CF-PP},
      ddc          = {500},
      cid          = {I:(DE-H253)FS-CS-20210408 / I:(DE-H253)CSSB-CF-PP-20210530},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633)},
      pid          = {G:(DE-HGF)POF4-633},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37055432},
      UT           = {WOS:000978473800001},
      doi          = {10.1038/s41467-023-37836-8},
      url          = {https://bib-pubdb1.desy.de/record/599937},
}