Annmaree K. Warrender

This study characterizes O-acetylserine sulfhydrylase (CysK) enzymes from bacteria without a sulfate reduction pathway, showing their substrate specificity and functional divergence in cysteine synthesis.

The paper identifies a ternary switch in ERα LBD that regulates receptor activity through distinct H12 conformations, revealing an apo state and its destabilization by mutations.

This study investigates the temperature dependence of enzyme catalysis by analyzing MalL and its mutants, showing cooperative conformational transitions and introducing models to explain non-Arrhenius behavior.