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.

This paper identifies a negative allosteric modulator of the μ-opioid receptor that blocks agonist activity and enhances naloxone efficacy, offering potential for safer opioid overdose reversal.

The paper proposes a step-wise activation model for metabotropic glutamate receptor subtype 5, supported by structural and fluorescence imaging data of different activation states.

The paper presents the cryo-EM structure of the glucagon receptor bound to a ligand and G-protein, revealing structural insights into ligand efficacy and activation mechanism.