Reuven Gordon

The paper investigates how two small molecule activators of PP2A, ATUX-8385 and DBK-776, affect the structural stability of the PR65 scaffold using biophysical and computational methods.

The paper investigates how SMAPs bind to PR65, showing that S2 is a stable binding site while S1 is not, and that binding promotes an extended PR65 conformation favorable for PP2A holoenzyme assembly.

This paper observes conformational dynamics of unmodified IDPs/IDRs at the single-molecule level using nanoaperture optical tweezers, revealing increased conformational variation and phosphorylation-induced compaction.