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Updated: Dec 30, 2025
Detection of Disease-associated α-synuclein by Enhanced ELISA in the Brain of Transgenic Mice Overexpressing Human A53T Mutated α-synuclein
Published on: May 30, 2015
The biochemical basis of interactions between Glucocerebrosidase and alpha-synuclein in GBA1 mutation carriers
Marco Toffoli1, Laura Smith1, Anthony H V Schapira1
1Department of Clinical and Movement Neurosciences, University College London Queen Square Institute of Neurology, London, UK.
Abstract:
The discovery of genes involved in familial as well as sporadic forms of Parkinson disease (PD) constitutes an important milestone in understanding this disorder's pathophysiology and potential treatment. Among these genes, GBA1 is one of the most common and well-studied, but it is still unclear how mutations in GBA1 translate into an increased risk for developing PD. In this review, we provide an overview of the biochemical and structural relationship between GBA1 and PD to help understand the recent advances in the development of PD therapies intended to target this pathway.
