• mutations
  • To investigate this hypothesis, we infected cell lines expressing PD-causing point mutations in α-synuclein with MSA patient samples. (pnas.org)
  • Coexpression of the A53T and E46K mutations was unable to rescue MSA prion infection in vitro, establishing that MSA α-synuclein prions are conformationally distinct from the misfolded α-synuclein in PD patients. (pnas.org)
  • pathology
  • Inhibition of MARKs dramatically exacerbated α-synuclein pathology. (jneurosci.org)
  • The analysis of inclusion body constituents gives additional information about pathways also involved in the pathology of synucleinopathies. (mdpi.com)
  • It is not found in Lewy bodies, but it is associated with hippocampal pathology in PD and DLB. (wikipedia.org)
  • mutation
  • MSA prions robustly infected wild-type, A30P, and A53T α-synuclein-YFP cells, but they were unable to replicate in cells expressing the E46K mutation. (pnas.org)
  • variants
  • We showed that PQQ dramatically inhibits the fibril formation of C-terminal truncated alpha-synuclein110119, and 133 as well as the mixtures of full-length alpha-synuclein with these truncated variants. (biomedcentral.com)
  • Conversely, the rate of axonal transport is not determined by lipid affinity and is not sufficient to account for differences in presynaptic localization of α-synuclein-eGFP variants. (biomedcentral.com)
  • fibrils
  • The ability of α-synuclein recombinant fibrils to infect all cell lines tested argues that synthetic α-synuclein prions are not predictive of the disease-causing strains in human patients. (pnas.org)
  • Since the fibrils and precursor oligomers of alpha-synuclein are cytotoxic to the neuron, inhibitors that prevent the formation of oligomers and/or fibrils might open the way to a novel therapeutic approach to PD. (biomedcentral.com)
  • prion
  • This observation indicates that the α-synuclein prion conformation found in PD is different from the strain found in MSA, providing biological evidence that these diseases arise from distinct prion strains. (pnas.org)