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  • neurons
  • Synuclein is however found predominantly in the presynaptic termini, in both free or membrane-bound forms, with roughly 15% of synuclein being membrane-bound in any moment in neurons. (wikipedia.org)
  • Thus, it is suggested that alpha-synuclein in mitochondria is differentially expressed in different brain regions and the background levels of mitochondrial alpha-synuclein may be a potential factor affecting mitochondrial function and predisposing some neurons to degeneration. (wikipedia.org)
  • cellular
  • The normal cellular function of gamma-synuclein remains unknown. (wikipedia.org)
  • Extra glutamine residues can acquire toxic properties through a variety of ways, including irregular protein folding and degradation pathways, altered subcellular localization, and abnormal interactions with other cellular proteins. (wikipedia.org)
  • absence
  • As of 2014, an increasing number of reports suggest, however, the presence of partial structures or mostly structured oligomeric states in the solution structure of alpha-synuclein even in the absence of lipids. (wikipedia.org)
  • activity
  • This is the primary route cells use to degrade proteins.Decreased proteasome activity is consistent with models in which intracellular protein aggregates form. (wikipedia.org)
  • research
  • Extensive research has been done using the models of nematode (C. elegans), and fruit fly (Drosophila), mice, and non-human primates. (wikipedia.org)
  • Research indicates proteasome enzymes may not be able to correctly cleave these irregular proteins, which could possibly result in a more toxic species. (wikipedia.org)
  • form
  • autophagy-lysosome pathways: a form of programmed cell death (PCD), this becomes the favorable route when a protein is aggregate-prone meaning it is a poor proteasome substrate. (wikipedia.org)