Raymond D. Blind

This study identifies the host soluble inositol phosphate pathway as critical for coronavirus replication and demonstrates a multi-target inhibitor that effectively suppresses viral replication in cells and mice.

The paper develops a compound prioritization strategy using a multi-layer perceptron trained on docked poses from multiple docking approaches to identify putative binders for the nuclear receptor LRH-1.

The paper reports 14 co-crystal structures of human IPMK with inhibitors and identifies structural features contributing to inhibitor potency and selectivity.

This study designs, synthesizes, and characterizes a new class of IPMK kinase inhibitors, showing reduced glioblastoma cell growth and a novel InsP5 metabolic signature.

This study shows multiple inositol phosphate species enhance mTOR and mTORC1 kinase activity in vitro by stabilizing an active form of the kinase.

This paper introduces a novel docking score metric, ΔΔG, which correlates with full-length LRH-1 regulation by compounds in cell-based assays.

This study identifies bilirubin as a direct ligand for LRH-1, showing it modulates LRH-1 activity and gene regulation in liver cells.

This study shows IPMK regulates HDAC3 activity and histone H4 acetylation in human cells through inositol phosphate production.