K. H. Gardner

This study identifies a mechanism by which PASK's nuclear translocation is regulated by the interaction between its PAS-A domain and a PIM motif, which is modulated by metabolic signals.

The paper identifies ligand-binding sites on and within the ARNT PAS-B domain using NMR, MD simulations, and ensemble docking, revealing distinct binding modes for three small molecules.

This paper introduces a method using high-pressure NMR spectroscopy to identify proteins with internal ligand-binding voids by detecting nonlinear chemical shift changes in 1H/15N HSQC experiments.

The paper uses high-pressure NMR to study conformational changes in ARNT PAS-B Y456T, finding that the slipped conformation is smaller and less compressible than the wildtype and involves an unfolded intermediate.

The paper examines the diversity of oligomeric states and regulatory mechanisms in HWE/HisKA2 histidine kinases, identifying monomeric and dimeric forms with distinct functional responses.

This study investigates the structural dynamics of the LOV2 domain in AsLOV2, showing that Q513 and N414 mediate J-helix unfolding linked to optogenetic function.