I. Iordanov

This paper identifies structural determinants of PKA-C essential for CFTR activation, showing two distinct regions mediate reversible and irreversible activation, and highlights the role of PKA-C myristoylation in this process.

This study presents cryo-EM structures of PKA-C bound to CFTR, revealing mechanisms of phosphorylation and reversible activation through catalytic interactions and conformational flexibility.

The paper estimates the non-hydrolytic closing rate of WT CFTR by comparing it to mutants with disrupted ATP hydrolysis, revealing how specific mutations affect this rate.