Extracellular ATP activates hyaluronan synthase 2 (HAS2) in epidermal keratinocytes via P2Y2, Ca2+ signaling, and MAPK pathways
Deregulation of LIMD1–VHL–HIF-1α–VEGF pathway is associated with different stages of cervical cancer
ApoE isoforms and carboxyl-terminal-truncated apoE4 forms affect neuronal BACE1 levels and Aβ production independently of their cholesterol efflux capacity
A high-resolution crystal structure of the molybdenum insertase Cnx1E from Arabidopsis thaliana reveals two mutually exclusive molybdate binding sites, that have mechanistic implications for the Mo-insertion process into the pterin moiety of the molybdenum cofactor. In this issue of the Biochemical Journal, Kruse et al. found that molybdate is sequentially bound to the entry and the catalytically-productive site, going hand in hand with a distinct backbone conformation shift. In this image, adenylated molybdopterin and the two molybdate ions are shown in front of the Cnx1E active site. (Image provided by J. Krausze, W. A. Sassen and T. Kruse); for details see pages 1739–1753.