The modulation of protein-protein interactions with small molecules is one of the most rapidly
developing areas in drug discovery. In this review, we discuss advances over the past …

… Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15. …
recruitment to DCAF15 by a sulfonamide molecular glue E7820. Struct Lond Engl. 27:1625–…

… Viruses can hijack the cellular ubiquitin–proteasome system to induce the degradation of
antiviral host factors. Here, a combination of proteomic, biochemical, structural and virological …

… With a total area of 1150 Å2, the DCAF15RBM39 interaction surface is almost twice as large
… Structural complementarity facilitates E7820-mediated degradation of RBM39 by DCAF15. …

… proteins, as shown in DCAF15-DDB1-DDA1 … structure shows that DCAF12 forms a
stable complex with MAGEA3, which was previously characterized as a DCAF12 degradation …

… DCAF15 has been removed for clarity, and only DDB1 from the DDB1/E27 structure is …
with E27, as observed in the DDB1 ΔBPB /DDA1/DCAF15 complex (indicated by the red arrow). …

… via recruitment of the ubiquitin ligase CRL4 DCAF15 (… on DCAF15, facilitating the recruitment
of RBM39 and RBM23 through the second RNA-recognition motif (RRM) present in RBM39 …

… as an MG to facilitate the formation of a new surface of DCAF15 to recruit RBM39, rather than
… The pyrone group on bufalin may also provide a general structural moiety for discovering …

… can facilitate insights into the structure … structure of DDB1-DCAF15:E7820:RBM39 to build
an unambiguous model of the ternary complex [43]. Recently, a series of cryo-EM structures …

… (i) RNA capping controls transcript stability and translational efficiency, facilitating interactions
between the polyA tail and associated binding proteins (pink geometric shapes) with the …