Poupak Dadvar , Duangnapa Kovanich , Gert E. Folkers, Klaus Rumpel, Reinout Raijmakers and Albert J. R. Heck
The cover picture shows the structure of an immobilized, clinically used phosphodiesterase-5 (PDE5) inhibitor. On p. 2654 ff., A. J. R. Heck et al. discuss how they used beads functionalized with this inhibitor to affinity enrich and identify interacting proteins directly in mammalain tissue (i.e., rat testis, shown in the background). Mass spectrometric analysis showed that not only the known target, PDE5, but also several members of the PEBP family of proteins, including the Raf kinase inhibitory protein (RKIP), bound to the drug.