An outer membrane vesicle pulse-chase assay demonstrates that the Acinetobacter baumannii Mla system is a retrograde lipid transporter.

Structure of MlaFEDB ABC transporter with substrate bound in the outward-open pocket of MlaE provides mechanistic insights into lipid transport within the Gram-negative bacterial cell envelope.

An Acinetobacter baumannii ABC transporter likely facilitates transport of glycerophospholipids from the inner to the outer membrane.

Proprioceptive signals about leg position, movement, and vibration are integrated in downstream circuits in the fly's central nervous system.

Analysis of the E. coli protein DolP reveals the first dual BON-domain structure and identifies phospholipid binding as a new mechanism for protein localisation to the outer membrane division site.

Auxiliary proteins play functional roles in modulating the assembly and activity of a non-canonical ABC transporter that is important for the maintenance of outer membrane lipid asymmetry.

The BPTF PHD finger is inhibited from binding the methylated H3 tails in the context of the nucleosome due to their robust interaction with the nucleosomal DNA, which can be modulated by additional histone PTMs.

Cholinergic system play an important role in waking-to-sleep cycles and in sleep stabilization.

Structure of MlaFB reveals how a small binding protein and the C-terminal tail on an ATPase subunit work together to regulate the assembly and function of an ABC transporter.

Functional and mechanistic analyses of cancer cells containing homozygous deletion of TP53 and FXR2 reveal that inhibition of FXR1 blocks cell proliferation in a collateral lethality manner, opening an avenue to develop therapies targeting such cancers.