Andy Chevigné

This paper identifies abemaciclib, an FDA-approved CDK4/6 inhibitor, as a potent agonist of ACKR3, an atypical chemokine receptor, revealing its ability to modulate chemokine availability and receptor activity.

This study discovers potent, selective macrocyclic peptide ligands for CXCR4, a class A GPCR, demonstrating the feasibility of de novo peptide design for this receptor family.

This study engineers orthogonal chemokine-receptor pairs to enable targeted immune cell migration and collective swarming behavior in engineered T cells.

This study identifies Ephrin B1 as a key mediator of CXCR4 tumorigenic signaling by promoting its intracellular localization and inhibiting surface expression and signaling.

This study shows ACKR3 is released on extracellular vesicles under both basal and ligand-induced conditions, sequestering chemokines and opioid peptides and modulating their signaling.

This study determines the cryo-EM structures of DARC bound to chemokines CCL7 and CXCL8, revealing unique binding mechanisms and the role of tyrosine sulfation and allelic variation in chemokine engagement.

This study reveals an unconventional activation mechanism of the atypical GPCR ACKR3 using engineered nanobodies and cryo-EM, showing that extracellular pocket volume changes, not microswitch conformational shifts, drive receptor activity.

This study reveals an atypical activation mechanism of CXCR7, identifies its role as an opioid receptor, and highlights potential for novel pain therapeutics.

This study characterizes VUF16840 as a selective inverse agonist of ACKR3 that inhibits constitutive and chemokine-induced signaling by stabilizing the inactive conformation of the receptor.

This study shows GPR15LG binds CXCR4, enhancing CXCL12-induced signaling and promoting cell migration in immune and cancer cells.

This study shows that targeting ACKR2 enhances anti-PD-1 immunotherapy efficacy in melanoma by improving the tumor microenvironment and immune cell infiltration.

This paper designs and characterizes the first photoswitchable small-molecule agonist for ACKR3, showing its selectivity and light-controlled activation properties.

This study identifies GPR182/ACKR5 as a scavenger receptor for CXCL17, GPR15L, and endogenous peptides, revealing distinct binding modes and expanding its ligand repertoire beyond classical chemokines.

This study investigates ligand promiscuity and signaling bias in chemokine receptors by analyzing binding modes and determining cryo-EM structures of receptor-ligand complexes.