Katarzyna Magiera

TL;DR: The latest work on structural characterization of the checkpoint proteins, their interactions with cognate ligands and with therapeutic antibodies reveals that they all have a similar modular structure, composed of small domains similar in topology to the domains found in antibodies.

TL;DR: NMR and X-ray characterization is presented for the two classes of small-molecule PD-1/PD-L1 inhibitors that carry a number of disadvantages such as the high cost of the antibodies, their limited half-life, and immunogenicity.

TL;DR: Evidence is provided that small molecules are capable of alleviating the PD-1/PD-L1 immune checkpoint-mediated exhaustion of Jurkat T-lymphocytes and the X-ray structures of the complexes of B MS-1001 and BMS-1166 were determined, which revealed features that may be responsible for increased potency of the compounds compared to their predecessors.

TL;DR: Both the imaging and cytotoxic properties of the studied ruthenium complexes are strongly influence by the level of internalization and protein interaction.

TL;DR: The most potent LCA derivative, LCA hydroxyamide (LCAHA), inhibits USP2a, leading to a significant Akt/GSK3β-independent destabilization of cyclin D1, but does not change the expression of p27, which leads to the defects in cell-cycle progression.