Simon L. Newstead

This study identifies the binding site of CVN293 on THIK-1 K2P channel and reveals its allosteric inhibition mechanism through cryoEM structures and functional validation.

The paper identifies PQLC2 as a lysosomal pH regulator that affects tau homeostasis through a CRISPRi screen in iPSC-derived neurons.

The paper determines the structure of cornichon receptors bound to an SLC transporter and shows how they couple membrane adaptation with cargo selection during ER export.

The paper identifies equivalent gain-of-function variants in KCNK3 and KCNK9 that cause distinct channelopathies and investigates their functional effects on homomeric and heteromeric TASK channels.

The paper identifies a splice variant-dependent localization of PMCA2 to lysosomes and links it to neurodegenerative diseases.

The paper investigates how PI(3,5)P2 regulates lysosomal pH by inhibiting ClC-7, showing structural changes in ClC-7 upon PI(3,5)P2 binding and linking this to disease mutations.

This study identifies DtpT as the primary dipeptide transporter in Staphylococcus aureus and reveals its role in glutathione uptake, enhancing bacterial survival in macrophages.

The paper presents a cryoEM structure of the human THIK-1 K2P K+ channel, revealing structural features and regulatory mechanisms involving lipids and anaesthetics.

The paper develops a bioinformatic pipeline to predict substrates for orphan SLC proteins using multi-omics data, identifying known substrates and new SLC-drug interactions.

This study presents cryoEM structures of TASK-1 and TASK-3 channels, revealing structural insights into their gating mechanism and pH sensitivity, and how mutations disrupt function in disease.

The paper identifies SLC45A4 as a pain-related gene encoding a neuronal polyamine transporter through GWAS and functional studies.

The paper identifies nanobodies that selectively modulate TREK-2 channel activity and reveals their binding mechanisms through structural analysis.

This study uses molecular dynamics simulations to elucidate the conformational mechanism and proton-substrate coupling in mammalian POTs, revealing key structural differences and functional insights.