B. K. Kobilka

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.

This study uses time-resolved cryo-EM to visualize the conformational changes in a GPCR-G protein complex during activation, revealing the structural pathway of G protein dissociation.

This study shows RAMP2 inhibits GCGR signaling by inducing conformational changes and disorder in the receptor's extracellular domain.

This study investigates how endocannabinoids modulate CB1 receptor signaling by comparing their activation of Gi1 with synthetic cannabinoids and revealing structural differences in ligand binding.

This paper describes a method using calcineurin fusion to improve cryo-EM structure determination of Family A GPCRs by enhancing particle alignment.

This study compares the structural and signaling differences between two μOR agonists, lofentanil and mitragynine pseudoindoxyl, revealing how their distinct binding modes lead to different G protein and β-arrestin activation profiles.

This study identifies membrane phosphoinositides as regulators of GPCR-arrestin complex dynamics, showing they stabilize complexes and enable temporal control of receptor signaling and recycling.

The paper integrates residue-level pharmacology data with structural contact data to uncover allosteric networks that govern ligand efficacy and potency in GPCRs.

The paper presents cryo-EM structures of MC4R-Gs complexes with NDP-α-MSH and setmelanotide, revealing ligand-specific interactions and activation mechanisms.

The paper develops tools for analyzing interatomic interactions in protein structures and simulations, creating a web resource to identify functional interaction patterns in GPCRs, G proteins, kinases, and muscarinic receptors.

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.

This study shows that local membrane charge affects β2AR coupling to Gi and Gs proteins, with negative charges inhibiting Gi coupling and promoting Gs coupling.