M. Batchelor

Exploring the dynamics and interactions of the N-myc transactivation domain through solution NMR

This study uses NMR to analyze the structure, dynamics, and interactions of N-myc's transactivation domain, revealing phosphorylation sites and binding interactions.

Loss of the first β-strand of human prion protein generates an aggregation-competent partially "open" form

This study examines the structural and functional changes in a truncated form of human prion protein lacking a conserved membrane region, showing it forms fibrils more readily than the native form.

Syntaxin 6 delays prion protein fibril formation and prolongs presence of toxic aggregation intermediates

This study shows syntaxin-6 inhibits PrP fibril formation but prolongs toxic intermediate aggregates, suggesting it acts as an anti-chaperone in prion disease.

α-Helix stabilization by co-operative side chain charge-reinforced interactions to phosphoserine in a basic kinase-substrate motif

The paper shows phosphorylation stabilizes an α-helix in a kinase-substrate motif through charge-reinforced side chain interactions, with phosphorylation of Ser promoting helix formation and Thr inducing an opposing response.

Brazilin Removes Toxic alpha-Synuclein and Seeding Competent Assemblies from Parkinson Brain by Altering Conformational Equilibrium

This paper shows Brazilin inhibits alpha-synuclein fibril formation and reduces toxicity in Parkinson's disease by altering conformational equilibrium.