Jonathan J. Phillips

This paper describes a method to purify and characterize soluble domains of bacterial membrane receptors, demonstrating its effectiveness with the HasR receptor from Pseudomonas aeruginosa.

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.

This study shows that cargo-sensitive TPR switch in kinesin-1 controls its conformational dynamics by dislocating the TPR shoulder, promoting motor domain activation and microtubule binding.

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