Paul Nimmer

TL;DR: A fluorescence polarization assay based on the interaction between Bcl-x(L) and BH3 domain peptides is developed and optimized and validates the assay not only for investigating the nature of Bcl(L)-peptide interaction, but also for high-throughput screening of B cl-x (L) inhibitors.

TL;DR: The discovery of a potent, highly selective, B cl-2 inhibitor is described using SAR by NMR and structure-based drug design which could serve as a starting point for the development of a Bcl-2 selective anti-cancer agent.

TL;DR: A-1331852 is described, a first-in-class orally active BCL-XL inhibitor that selectively and potently induces apoptosis in B CL-XL-dependent tumor cells.

TL;DR: The NMR solution structure of the disubstituted N,N'-diarylurea bound to Bcl-XL is obtained demonstrating the folded conformation of the urea motif engaged in extensive pi-interactions with the protein.

TL;DR: An in situ glycan‐mediated ligand‐controlled click (“GLiCo‐Click”) chemistry methodology that enables the attachment of small‐molecule chemical probes to their receptor protein through glycans on live cells can be used to demonstrate target receptor engagement and enables the molecular characterization of receptors.