TY - JOUR AU - Lázaro, Diana F. AU - Dias, Mariana Castro AU - Carija, Anita AU - Navarro, Susanna AU - Madaleno, Carolina Silva AU - Tenreiro, Sandra AU - Ventura, Salvador AU - Outeiro, Tiago F. PY - 2016 DA - 2016/12/09 TI - The effects of the novel A53E alpha-synuclein mutation on its oligomerization and aggregation JO - Acta Neuropathologica Communications SP - 128 VL - 4 IS - 1 AB - α-synuclein (aSyn) is associated with both sporadic and familial forms of Parkinson’s disease (PD), the second most common neurodegenerative disorder after Alzheimer’s disease. In particular, multiplications and point mutations in the gene encoding for aSyn cause familial forms of PD. Moreover, the accumulation of aSyn in Lewy Bodies and Lewy neurites in disorders such as PD, dementia with Lewy bodies, or multiple system atrophy, suggests aSyn misfolding and aggregation plays an important role in these disorders, collectively known as synucleinopathies. The exact function of aSyn remains unclear, but it is known to be associated with vesicles and membranes, and to have an impact on important cellular functions such as intracellular trafficking and protein degradation systems, leading to cellular pathologies that can be readily studied in cell-based models. Thus, understanding the molecular effects of aSyn point mutations may provide important insight into the molecular mechanisms underlying disease onset. SN - 2051-5960 UR - https://doi.org/10.1186/s40478-016-0402-8 DO - 10.1186/s40478-016-0402-8 ID - Lázaro2016 ER -