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@PHDTHESIS{Akoury:282307,
      author       = {Akoury, Elias},
      title        = {{M}olecular {M}echanisms of {T}au {P}rotein {A}ggregation
                      {I}nhibition},
      school       = {Georg-August-Universität Göttingen},
      type         = {Dissertation},
      reportid     = {DZNE-2025-01277},
      pages        = {240 p.},
      year         = {2013},
      note         = {Dissertation, Georg-August-Universität Göttingen, 2013},
      abstract     = {Of all neurodegenerative diseases, Alzheimer´s Disease is
                      the most widespread dementia syndrome, exhibiting
                      progressive memory loss and intellectual abilities. One of
                      the pathological hallmarks of this disease is associated to
                      the presence of abundant intracellular deposits of the Tau
                      protein. Accumulation of these stable species is a multistep
                      process that involves the formation of various transients.
                      Understanding this key step may eventually enable to
                      obstruct aggregation. Tau protein is an intrinsically
                      disordered protein, abundant in neuronal axons where it
                      promotes and stabilizes microtubule assembly. Chapter 1
                      discusses the physiological function and pathological
                      consequences of this protein and sheds light on the current
                      Tau-based research implemented in therapeutic strategies.
                      This chapter also reviews the identification of inhibitors
                      of Tau aggregation as potential disease-modifying drugs;
                      with a detailed discussion of two organic compounds we have
                      recently screened, Phthalocyanine Tetrasulfonate and
                      Phenothiazine Methylene Blue. The same chapter then
                      introduces the Heat shock proteins and their role in Tau
                      clearance. The chapters that follow report our research
                      investigation of aggregation inhibitors and chaperonic
                      partners of Tau where we used an integrated approach to
                      detect possible assemblies of pathogenic conformational
                      transitions. Chapter 2 represents the Phthalocyanine
                      tetrasulfonate study and its inhibition of Tau filament
                      formation by conformational modulation. Chapter 3
                      investigates the mechanistic basis of the
                      phenothiazine-driven inhibition of Tau aggregation. Chapter
                      4, examines how the imbalance of Hsp70 family variants
                      fosters Tau accumulation. As a final point, the significance
                      of the biophysical techniques incorporated in the three
                      published manuscripts are briefly discussed in the last part
                      of Chapter 1.},
      cin          = {AG Zweckstetter},
      cid          = {I:(DE-2719)1410001},
      pnm          = {352 - Disease Mechanisms (POF4-352)},
      pid          = {G:(DE-HGF)POF4-352},
      typ          = {PUB:(DE-HGF)11},
      url          = {https://pub.dzne.de/record/282307},
}