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@ARTICLE{Uechi:281502,
      author       = {Uechi, Hiroyuki and Sridharan, Sindhuja and Nijssen, Jik
                      and Bilstein, Jessica and Iglesias-Artola, Juan M and
                      Kishigami, Satoshi and Casablancas-Antras, Virginia and
                      Poser, Ina and Martinez, Eduardo J and Boczek, Edgar and
                      Wagner, Michael and Tomschke, Nadine and de Jesus Domingues,
                      António M and Pal, Arun and Doeleman, Thom and Kour,
                      Sukhleen and Anderson, Eric Nathaniel and Stein, Frank and
                      Lee, Hyun O and Zhang, Xiaojie and Fritsch, Anatol W and
                      Jahnel, Marcus and Fürsch, Julius and Murthy, Anastasia C
                      and Alberti, Simon and Bickle, Marc and Fawzi, Nicolas L and
                      Nadler, André and David, Della C and Pandey, Udai B and
                      Hermann, Andreas and Stengel, Florian and Davis, Benjamin G
                      and Baldwin, Andrew J and Savitski, Mikhail M and Hyman,
                      Anthony A and Wheeler, Richard J},
      title        = {{S}mall-molecule dissolution of stress granules by redox
                      modulation benefits {ALS} models.},
      journal      = {Nature chemical biology},
      volume       = {21},
      number       = {10},
      issn         = {1552-4450},
      address      = {Basingstoke},
      publisher    = {Nature Publishing Group},
      reportid     = {DZNE-2025-01123},
      pages        = {1577 - 1588},
      year         = {2025},
      abstract     = {Neurodegenerative diseases, such as amyotrophic lateral
                      sclerosis, are often associated with mutations in stress
                      granule proteins. Aberrant stress granule condensate
                      formation is associated with disease, making it a potential
                      target for pharmacological intervention. Here, we identified
                      lipoamide, a small molecule that specifically prevents
                      cytoplasmic condensation of stress granule proteins. Thermal
                      proteome profiling showed that lipoamide stabilizes
                      intrinsically disordered domain-containing proteins,
                      including SRSF1 and SFPQ, which are stress granule proteins
                      necessary for lipoamide activity. SFPQ has
                      redox-state-specific condensate dissolving behavior, which
                      is modulated by the redox-active lipoamide dithiolane ring.
                      In animals, lipoamide ameliorates aging-associated
                      aggregation of a stress granule reporter protein, improves
                      neuronal morphology and recovers motor defects caused by
                      amyotrophic lateral sclerosis-associated FUS and TDP-43
                      mutants. Thus, lipoamide is a well-tolerated small-molecule
                      modulator of stress granule condensation, and dissection of
                      its molecular mechanism identified a cellular pathway for
                      redox regulation of stress granule formation.},
      keywords     = {Amyotrophic Lateral Sclerosis: metabolism / Amyotrophic
                      Lateral Sclerosis: drug therapy / Amyotrophic Lateral
                      Sclerosis: genetics / Amyotrophic Lateral Sclerosis:
                      pathology / Oxidation-Reduction: drug effects / Humans /
                      Animals / Stress Granules: metabolism / Stress Granules:
                      drug effects / Small Molecule Libraries: pharmacology /
                      Small Molecule Libraries: chemistry / Mice / Disease Models,
                      Animal / Small Molecule Libraries (NLM Chemicals)},
      cin          = {AG Hermann / AG David},
      ddc          = {570},
      cid          = {I:(DE-2719)1511100 / I:(DE-2719)1210004},
      pnm          = {353 - Clinical and Health Care Research (POF4-353) / 899 -
                      ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-353 / G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40369342},
      pmc          = {pmc:PMC12463676},
      doi          = {10.1038/s41589-025-01893-5},
      url          = {https://pub.dzne.de/record/281502},
}