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@ARTICLE{Vasili:281812,
      author       = {Vasili, Eftychia and König, Annekatrin and Al-Azzani,
                      Mohammed and Bosbach, Clara and Gatzemeier, Luisa Maria and
                      Thom, Searlait and Chegão, Ana and Miranda, Hugo Vicente
                      and Steinem, Claudia and Erskine, Daniel and Outeiro, Tiago
                      F},
      title        = {{G}lycation of alpha-synuclein enhances aggregation and
                      neuroinflammatory responses.},
      journal      = {npj Parkinson's Disease},
      volume       = {11},
      number       = {1},
      issn         = {2373-8057},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DZNE-2025-01195},
      pages        = {307},
      year         = {2025},
      abstract     = {The risk of developing Parkinson's disease (PD) is elevated
                      in individuals with type 2 diabetes (T2DM), but the
                      molecular pathways underlying this link remain unclear.
                      Glycation, a non-enzymatic modification of lysine and
                      arginine residues by reducing sugars or reactive
                      dicarbonyls, may disrupt proteostasis and trigger pathology.
                      Here, we investigated how methylglyoxal (MGO)- and
                      ribose-mediated glycation influence aSyn aggregation,
                      neuroinflammation, and detoxification pathways. Using
                      SH-SY5Y cells, primary neurons, primary microglia and
                      MGO-injected aSyn transgenic mice, we found that
                      MGO-glycated aSyn promotes PD associated pathological
                      features, including pS129-positive aSyn aggregates,
                      neuroinflammation, and impairment of the glyoxalase
                      detoxification pathway. Ribose-glycated aSyn, while
                      immunogenic, exerts limited effects on aggregation and
                      seeding. Both glycated species activates microglia and
                      upregulate pro-inflammatory markers. We further developed a
                      novel antibody specific for MGO-glycated aSyn, which
                      selectively detects Lewy body-like deposits in dementia with
                      Lewy bodies (DLB) tissue and MGO-injected mice. These
                      findings implicate MGO-glycation in PD-T2DM comorbidity.},
      cin          = {AG Fischer},
      ddc          = {610},
      cid          = {I:(DE-2719)1410002},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:41131060},
      doi          = {10.1038/s41531-025-01159-w},
      url          = {https://pub.dzne.de/record/281812},
}