Michael I. Wilson

TL;DR: It is shown that the interaction between human pVHL and a specific domain of the HIF-1α subunit is regulated through hydroxylation of a proline residue by an enzyme the authors have termed Hif-α prolyl-hydroxylase (HIF-PH).

TL;DR: Optimize hydrogen bonding to the buried hydroxyprolyl group confers precise discrimination between hydroxylated and unmodified prolyl residues in two functionally independent regions of HIF-1α, providing a new focus for development of therapeutic agents to modulate cellular responses to hypoxia.

TL;DR: The crystal structure of the p40(phox)/p67(Phox) PB1 heterodimer is determined, which reveals that both domains have a beta grasp topology and that they bind in a front-to-back arrangement through conserved electrostatic interactions between an acidic OPCA motif on p40 (phox) and basic residues in p67( phox).

TL;DR: The crystal structure of the PX domain is determined and the presence of similar hydrophobic pairs in the amino‐acid sequences of other membrane‐binding domains and proteins suggests that the same structural motif may be shared by other membranes‐binding proteins, whose physiological functions depend on strong hydrophilic membrane interactions.