Amberley D. Stephens

α-Synuclein Facilitates Spontaneous Dopamine Release in a Calcium- and Phosphorylation-Dependent Manner

This study shows α-synuclein modulates spontaneous dopamine release via calcium and phosphorylation-dependent mechanisms, independent of full-fusion recycling.

Brain cholesterol metabolites cause significant neurodegeneration in human iPSC-derived neurons

This study shows that 24S-HC and 27-HC, brain cholesterol metabolites, cause neuronal dysfunction in human iPSC-derived neurons by disrupting calcium signaling, organelle function, and alpha-synuclein accumulation.

Local ionic conditions modulate the aggregation propensity and influence the structural polymorphism of alpha-synuclein

This study investigates how Ca2+ and Na+ ions affect alpha-synuclein aggregation and fibril polymorphism, revealing their distinct roles in modulating conformational dynamics and structural outcomes.

Machine learning-based spike sorting reveals how subneuronal concentrations of monomeric Tau cause a loss in excitatory postsynaptic currents in hippocampal neurons

The paper introduces PseudoSort, a machine learning algorithm for spike sorting, and applies it to MEA data from hippocampal neurons exposed to monomeric Tau, revealing its impact on neuronal activity.

α-synuclein fibril and synaptic vesicle interactions lead to vesicle destruction and increased uptake into neurons

This study investigates how monomeric and fibrillar alpha-synuclein interact with synaptic vesicles, showing fibrils disintegrate vesicles and increase neuronal uptake, potentially contributing to Parkinson's disease pathology.

Label-free characterisation of amyloids and alpha-Synuclein polymorphs by exploiting their intrinsic fluorescence property

This paper introduces a label-free method using intrinsic fluorescence lifetime to characterize amyloids and their polymorphs, showing distinct fluorescence lifetimes for different amyloid structures and polymorphic populations.

Local structural dynamics of alpha-synuclein correlate with aggregation in different physiological conditions

The paper measures how different cellular environments affect alpha-synuclein's structure and aggregation, finding that specific regions drive nucleation and fibril elongation.

Intra-mitochondrial proteostasis is directly coupled to alpha-synuclein and Amyloid β 1-42 pathology

This study shows that intra-mitochondrial proteostasis influences alpha-synuclein and Aβ42 aggregation, while mitochondrial stress factors like complex I inhibition do not affect these pathologies.