Ambuja Navalkar

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: 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.

TL;DR: The present study suggests that sequence based interaction of small molecules with soluble α-Syn might dictate their inhibition or modulation capacity, which might be helpful in designing modulators of α- synuclein aggregation.

TL;DR: An insight into understanding p53 as a prion-like protein is provided and cancer to be recognized as amyloid or prions-like disease is proposed.