Surabhi Mehra

TL;DR: In vitro generated α-Syn liquid-like droplets eventually undergo a liquid-to-solid transition and form an amyloid hydrogel that contains oligomers and fibrillar species and this work provides detailed insights into the phase-separation behaviour of natively unstructured α- Syn and its conversion to a disease-associated aggregated state, which is highly relevant in Parkinson's disease pathogenesis.

TL;DR: The structural and functional aspects of α-Syn and role of potential factors that may contribute to the underlying mechanism of synucleinopathies are focused on to identify novel targets and develop specific therapeutic strategies to combat Parkinson's and other protein aggregation related neurodegenerative diseases.

TL;DR: The present review specifically provides an overview of recent research on α-Syn aggregation pathways and its modulation by several cellular factors potentially relevant to PD pathogenesis.

TL;DR: In vitro studies show that cancer-associated mutation destabilizes the fold of p53 core domain and also accelerates the aggregation and amyloid formation by this protein, suggesting that inhibiting p53 isyloidogenesis could restore p53 tumor suppressor functions.

TL;DR: Biophysical techniques in conjunction with microscopic images revealed the molecular interaction between lipopolysaccharide and α-synuclein that induce rapid nucleation events and characterizes this heteromolecular interaction associated with an alternative pathway in Parkinson's disease progression.