imageimageABCB1-dependent multidrug resistance is a major cause of reduced efficacy of drug-based therapy. The cryo-EM-derived structures of ABCB1 presented here reveal a previously uncharacterized au...

A study using CRISPR gene editing reduced drug-resistance genes in ovarian cancer cells, making them more sensitive to treatment. #CancerResearch #GeneEditing

Read the full paper: Intrinsic temporal variations of ABCB1 and ABCB8 gene expression in human melanoma cell lines during spheroid formation

Read the full paper: Discovery of novel coumarin-containing triazolo[1,5-a]pyrimidine derivatives as potent ABCB1 inhibitor for modulation of multidrug resistance

Bats possess an extended lifespan compared to most mammals of their size, and have a low cancer incidence. Here the authors show that several bat species exhibit resistance to genotoxic agents that is...

The hallmark of multidrug resistance conferred by the human ABC transporter ABCB1 (hP-gp) is the recognition and efflux of a diverse range of drugs, though the precise mechanism of polyspecificity remains unresolved. In aquatic animals such as zebrafish, Abcb4, a functional homolog of hP-gp, plays a vital role in surviving environmental toxicants. Here, we show that DrAbcb4 exhibits comparable basal and drug-stimulated ATPase activity to hP-gp. Using cryo-EM, we capture five inward-facing DrAbcb4 conformations with varying separations between its two lobes, illustrating its open-and-close motion. The range of separation exceeds that seen in published P-gp structures that appear to be conformationally restricted. This global open-and-close motion is coupled with individual helix movement, resulting in a highly fluid substrate-binding pocket. These dynamic changes, likely underlying the polyspecificity of substrate recognition, predict unconventional protein-ligand interactions that are