The C2-domain of cytoplasmic phospholipase A₂α is structurally designed to target PC-rich membrane regions to increase the enzymatic efficiency of the catalytic domain, which prefers PCs with polyunsaturated acyl chains.

A near-complete flux balance analysis model of a minimal cell demonstrates the high essentiality of its metabolic genes, agrees well with experimental essentiality data and suggests some further gene removals.

High-throughput analysis of several Saccharomyces cerevisiae contact sites reveals a large data set of potential contact site proteins, including proteins involved in the regulation of lipid distribution within cells.

Phosphate accumulation in zinc-deficient Arabidobsis shoots is regulated by a pathway involving the transcription factor bZIP23, the phospholipid-remodelling enzyme LPCAT1 and the transporter PHT1;1.

The Cryo-EM structural and biochemical analysis provides a framework for understanding the working mechanism of ALDP.

The conformational cycle of an ABC heterodimeric transporter reveals a divergence in the structural mechanism of ABC exporters.

Novel drug-binding sites of TRPC6 could potentially facilitate future design of drugs to treat TRPC6-mediated diseases.

Benzene mapping simulations of envelope protein rafts from six different flaviviruses reveal a conserved cryptic site whose cluster of ionisable residues is likely responsible for orchestrating pH-dependent conformational changes during fusion, thereby representing an attractive target for antiviral development.

Simulations reveal where phosphoinositide lipids bind to voltage-gated sodium channels and how they reduce channel activity.

Channel characteristics of the presequence translocation pore have a direct impact on protein import into the mitochondrial matrix.