Stephen P. Muench

The paper presents high-resolution cryo-EM structures of LHCII at different pH levels, revealing minimal conformational changes and insights into lutein conformations and energy quenching mechanisms.

This study identifies eight structurally diverse KCNT1 channel inhibitors through virtual screening and experimental validation, offering potential new treatments for KCNT1-associated epilepsy.

This paper develops and tests ideal efficacy photoswitch ligands for TRPC4/5 channels, enabling precise spatiotemporally-controlled modulation in live tissues.

This study develops a pipeline using Adhirons to guide small molecule discovery against viral targets, identifying hits for Crimean-Congo Haemorrhagic Fever Virus and Influenza A Virus.

This study determines the cryo-EM structures of CD163 in complex with haptoglobin-hemoglobin, revealing its trimeric structure and calcium-dependent mechanism for HpHb clearance.

This study presents cryo-EM structures of TRPC5 bound to (-)-englerin A, revealing its binding site and mechanism of activation.

This study identifies two existing drugs that reduce KCNT1 channel activity and seizure activity in Drosophila models, suggesting potential new treatments for KCNT1-epilepsy.

This paper uses time-resolved cryoEM to directly observe the swinging lever mechanism of myosin-5, showing its structural changes during ATP hydrolysis and force generation.

This paper expresses and functionally characterizes the oncogenic RTK FGFR3-TACC3 using cell-free protein expression, achieving significant kinase activity.

This paper isolates and characterizes Affimers, antibody-like proteins, that inhibit influenza A virus H3 subtype infection in vitro and block HA-receptor interactions.

The paper uses site-directed mutagenesis to identify key residues involved in IR-IGF1R hybrid receptor formation, showing mutations reduce hybrid affinity and support rational drug design.

This paper identifies a molecular switch in the RCK2 domain of KNa1.1 channels that mediates sodium-dependent activation through conformational changes involving specific amino acid residues.

The paper reports the cryo-EM structure of human TRPC5 bound to the xanthine inhibitor Pico145, revealing its interaction with a conserved lipid binding site and elucidating the mechanism of TRPC1/4/5 modulation.