Brian K. Kobilka

This study discovers μ-opioid receptor positive allosteric modulators (PAMs) and investigates their dynamic mechanism of action to enhance opioid agonist activity while reducing side effects.

This study uses single-molecule imaging to show how agonist-specific dynamics in structured and disordered regions of the 2AAR regulate signaling and function.

The paper shows that AP-7-168 induces β2AR dimerization by acting as a molecular glue, revealing a new allosteric mechanism for GPCR modulation.

This study uses smFRET to show that opioid ligands modulate Gi protein conformational dynamics, with higher-efficacy agonists promoting open, low-nucleotide-affinity states.

This study reveals that membrane phosphoinositides allosterically regulate β-arrestin dynamics, enabling engagement with minimally phosphorylated GPCRs.

This study identifies structural features determining G protein coupling specificity at a class A GPCR using a Gi-biased agonist.