Thomas Lanyon‐Hogg

Molecular Glue-like Degraders of TEM β-Lactamases by Periplasmic Protease DegP

This study develops molecular glue-like degraders that target TEM β-lactamases for degradation by DegP, showing improved synergy with piperacillin against resistant E. coli.

A potent macrocyclic peptide binder enables effector-free crystallization of the GTPase RAB27A

The paper identifies a macrocyclic peptide binder, IMP2660, that disrupts RAB27A-effector interactions and enables crystallization of RAB27A without an effector, revealing its structural features.

A novel ciprofloxacin analogue enables daptomycin-mediated killing of resistant Staphylococcus aureus by increasing septum formation

The paper shows that IMP-1700, a ciprofloxacin analogue, increases septum formation in S. aureus, enhancing daptomycin's effectiveness against resistant strains.

Discovery of stereoselective targeted covalent inhibitors of the RAB27-effector protein-protein interaction

This paper develops the first cell-active covalent inhibitors of RAB27-effector interactions, showing enantioselectivity and improved potency over a previously reported toxic compound.

YdbL directly modulates YdbH-YnbE bridge formation to maintain Escherichia coli outer membrane homeostasis

This study shows YdbL modulates YdbH-YnbE bridge formation in E. coli to maintain outer membrane homeostasis by interacting with YnbE and preventing its degradation.

Chemical proteomics identifies signal peptidase IB (SpsB) as a target of the SOS response inhibitor OXF-077 and a regulator of quinolone resistance emergence in Staphylococcus aureus

Live-Cell Chemoproteomic Profiling Identifies the Uncharacterised Protein YbaA as a Direct Target of Ciprofloxacin in Escherichia coli

This study identifies YbaA as a new ciprofloxacin-binding protein in E. coli using AfBPP and validates its interaction through genetic and biophysical assays.

Small molecule inhibitors of the NorA multidrug efflux pump potentiate antibiotic activity by binding the outward-open conformation

The paper identifies IMP-2380, a potent NorA inhibitor that enhances antibiotic activity by stabilizing the outward-open conformation of the efflux pump.