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@ARTICLE{Zahra:282332,
      author       = {Zahra, Fatima Tu and Kayani, Hooreen and Noreen, Samra and
                      Noor, Aneeqa and Zafar, Saima},
      title        = {{S}ynuclein {P}roteoforms: {R}ole in {H}ealth and
                      {D}isease.},
      journal      = {Molecular neurobiology},
      volume       = {63},
      number       = {1},
      issn         = {0893-7648},
      address      = {Totowa, NJ},
      publisher    = {Humana Press},
      reportid     = {DZNE-2025-01293},
      pages        = {87},
      year         = {2025},
      abstract     = {Synucleins α, β, and γ are inherently disordered
                      proteins that play essential roles in neuronal physiology
                      and are increasingly recognized as key players in
                      neurodegenerative disease mechanisms. The molecular basis of
                      synucleinopathies, including Parkinson's disease, dementia
                      with Lewy bodies, and multiple system atrophy, is the
                      pathological aggregation and misfolding of synucleins.
                      However, the biological significance of the diverse
                      synuclein proteoforms that result from alternative splicing,
                      extensive post-translational modifications, and
                      conformational heterogeneity is still not fully understood.
                      This review systematically incorporates current knowledge of
                      the structural and functional diversity of synuclein
                      proteoforms, highlighting their molecular interactions and
                      aggregation pathways. We investigate the regulatory effects
                      of β and γ-synucleins (β-syn and γ-syn), which have
                      different physiological functions and clinical applications
                      in addition to influencing α-synuclein (α-syn)
                      aggregation. In addition to synucleins' involvement in the
                      central nervous system, recent findings show their role in
                      immune regulation and functions in peripheral tissues,
                      highlighting their systemic relevance. Controversial
                      aspects, such as the mechanisms of prion-like propagation,
                      proteoform-specific toxicity, and differential cellular
                      vulnerability, are thoroughly analyzed. Synuclein
                      proteoforms have been thoroughly characterized due to
                      developments in molecular imaging and proteomic techniques,
                      opening the door for targeted treatment approaches.
                      Developing novel treatments for mitigating the progression
                      of synucleinopathies and enhancing patient outcomes requires
                      an understanding of the complex biology of synuclein
                      proteoforms. The goal of this study is to present a thorough
                      framework that connects translational research and molecular
                      neurobiology in disorders related to synuclein.},
      subtyp        = {Review Article},
      keywords     = {Humans / Animals / Synucleins: metabolism / Synucleins:
                      chemistry / Health / Synucleinopathies: metabolism /
                      alpha-Synuclein: metabolism / Neurodegenerative Diseases:
                      metabolism / Protein Isoforms: metabolism / PTMs (Other) /
                      Protein misfolding (Other) / Proteoforms (Other) / Synuclein
                      (Other) / Synucleinopathies (Other) / Synucleins (NLM
                      Chemicals) / alpha-Synuclein (NLM Chemicals) / Protein
                      Isoforms (NLM Chemicals)},
      cin          = {AG Zerr},
      ddc          = {570},
      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:41258277},
      doi          = {10.1007/s12035-025-05359-6},
      url          = {https://pub.dzne.de/record/282332},
}