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@ARTICLE{Chakraborty:274063,
      author       = {Chakraborty, Pijush and Ibáñez de Opakua, Alain and
                      Purslow, Jeffrey and Fromm, Simon A and Chatterjee, Debdeep
                      and Zachrdla, Milan and Zhuang, Shannon and Puri, Sambhavi
                      and Wolozin, Benjamin and Zweckstetter, Markus},
      title        = {{GSK}3β phosphorylation catalyzes the aggregation of tau
                      into {A}lzheimer's disease-like filaments.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {121},
      number       = {52},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {DZNE-2025-00044},
      pages        = {e2414176121},
      year         = {2024},
      abstract     = {The pathological deposition of proteins is a hallmark of
                      several devastating neurodegenerative diseases. These
                      pathological deposits comprise aggregates of proteins that
                      adopt distinct structures named strains. However, the
                      molecular factors responsible for the formation of distinct
                      aggregate strains are unknown. Here, we show that the
                      serine/threonine kinase GSK3β catalyzes the aggregation of
                      the protein tau into Alzheimer's disease (AD)-like
                      filaments. We demonstrate that phosphorylation by GSK3β,
                      but not by several other kinases, promotes the aggregation
                      of full-length tau as well as enhances phase separation into
                      gel-like condensate structures. Cryoelectron microscopy
                      further reveals that the fibrils formed by
                      GSK3β-phosphorylated tau adopt a fold comparable to that of
                      paired helical filaments isolated from the brains of AD
                      patients. Our results elucidate the intricate relationship
                      between posttranslational modification and the formation of
                      tau strains in neurodegenerative diseases.},
      keywords     = {tau Proteins: metabolism / Alzheimer Disease: metabolism /
                      Alzheimer Disease: pathology / Phosphorylation / Humans /
                      Glycogen Synthase Kinase 3 beta: metabolism / Protein
                      Aggregation, Pathological: metabolism / Protein Processing,
                      Post-Translational / Brain: metabolism / Brain: pathology /
                      Cryoelectron Microscopy / Protein Aggregates / Alzheimer's
                      disease (Other) / NMR (Other) / cryo-EM (Other) /
                      phosphorylation (Other) / tau (Other) / tau Proteins (NLM
                      Chemicals) / Glycogen Synthase Kinase 3 beta (NLM Chemicals)
                      / MAPT protein, human (NLM Chemicals) / Protein Aggregates
                      (NLM Chemicals) / GSK3B protein, human (NLM Chemicals)},
      cin          = {AG Zweckstetter},
      ddc          = {500},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39693350},
      pmc          = {pmc:PMC11670061},
      doi          = {10.1073/pnas.2414176121},
      url          = {https://pub.dzne.de/record/274063},
}