Ron O. Dror

This study uses deep mutational pharmacology to show how different residues in the -opioid receptor determine the efficacy of opioids by shaping distinct activation mechanisms.

The paper investigates how BIM1 selectively inhibits CLC-Ka over CLC-Kb by analyzing cryo-EM structures and showing that interactions with a conserved lysine and dynamic gating-loop behavior underlie this selectivity.

The paper reports cryo-EM structures of GerA, revealing how nutrient binding triggers channel opening through allosteric switches and subunit interactions.

The paper identifies and characterizes small molecule allosteric modulators of the AT1R, revealing their conformational mechanisms and effects on G protein and β-arrestin pathways.

The paper provides a mechanistic model for the 2:1 Cl-/H+ exchange in CLC transporters using structural and computational methods.

MedSAGE improves small molecule drug design by generating synthesizable, drug-like molecules with high predicted affinity and selectivity for therapeutic targets.

This study identifies a non-canonical mechanism of GPCR activation where agonists directly rearrange an intracellular loop to regulate signaling, with implications for drug design.

This paper introduces positively tuned GEVIs that enhance spike detection in vivo with standard imaging systems, offering higher temporal resolution than calcium indicators.

The paper identifies 150 transcriptional activation domains in yeast, shows their binding to Mediator, and develops a neural network to predict ADs across species.

This study uses deep mutational scanning to analyze GPCR variants, identifying key residues for signaling and function across multiple GPCR classes.

The paper identifies 138 associations between common protein-altering variants in GPCR genes and various phenotypes using UK Biobank data.