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@ARTICLE{Younas:282557,
      author       = {Younas, Neelam and Zerr, Inga},
      title        = {{O}xidative stress-induced stress granules: a central link
                      to protein aggregation in neurodegenerative diseases.},
      journal      = {Frontiers in neuroscience},
      volume       = {19},
      issn         = {1662-4548},
      address      = {Lausanne},
      publisher    = {Frontiers Research Foundation},
      reportid     = {DZNE-2025-01320},
      pages        = {1686571},
      year         = {2025},
      abstract     = {Intracellular aggregation of proteins such as Tau, TDP43,
                      FUS, prion protein, and α-synuclein is a major hallmark of
                      many major neurodegenerative diseases. Aberrant stress
                      granules (SGs) are emerging as key contributors to the
                      nucleation of toxic protein aggregates in these disorders.
                      SGs are dynamic, membrane less cytoplasmic assemblies that
                      form transiently through liquid-liquid phase separation
                      (LLPS) of RNA binding proteins (RBPs) containing low
                      complexity domains, together with stalled mRNAs, to help
                      cells cope with stress. While physiological SGs facilitate
                      cellular resilience to acute stress and undergo rapid
                      disassembly, chronic or excessive stress leads to persistent
                      SGs, driving pathological protein aggregation characteristic
                      of age related neurodegeneration. The inherent reversible
                      aggregation of RBPs crucial for cellular function
                      paradoxically exposes them to misfolding disorders. Notably,
                      recent findings expand this paradigm by demonstrating that
                      Tau itself participates in SG formation, with Tau-SG
                      interactions potentiating Tau aggregation and disease
                      progression in tauopathies. Despite these insights, the
                      precise cellular stressors and posttranslational
                      modifications (PTMs) governing the shift from physiological
                      granules to pathological aggregates remain poorly defined.
                      Emerging evidence highlights oxidative stress as a central
                      upstream mediator of this transition. In this perspective,
                      we synthesize current understanding of how SG dynamics
                      intersect with oxidative stress to potentiate protein
                      aggregation, proposing molecular mechanisms that bridge SG
                      biology and neurodegenerative disease. Elucidating these
                      pathways is essential for the development of targeted
                      therapeutic interventions for disorders such as Alzheimer's
                      disease and related tauopathies.},
      keywords     = {oxidative stress (Other) / pathological aggregation (Other)
                      / persistent SGs (Other) / stress granules (Other) /
                      tauopathies (Other)},
      cin          = {AG Zerr},
      ddc          = {610},
      cid          = {I:(DE-2719)1440011-1},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41278186},
      pmc          = {pmc:PMC12634546},
      doi          = {10.3389/fnins.2025.1686571},
      url          = {https://pub.dzne.de/record/282557},
}