Measuring the equilibrium dimerization of a polytopic membrane protein in lipid bilayers forms the basis of a new system for studying the physical forces that stabilize membrane protein association in membranes.

In parallel to protein-driven processes, characteristic physicochemical properties of the endoplasmic reticulum membrane modulate intracellular fat accumulation and lipid droplet formation.

Lipids with a propensity to form nonbilayer structures must be present for the last step of membrane fusion to take place.

Substrate releasing or inhibitor binding on the intracellular side of a glutamate transporter homologue require movements of the transport domain through the lipid membrane, which undergoes adaptive deformations.

The transmembrane shape of the F₁F_o ATP synthase monomer provides the molecular basis of high curvature at the ridges of mammalian mitochondrial cristae.

A general mechanism for how powerful forces of assembly and protein mobility can emerge from phase transitions is established.

Members of the calcium homeostasis modulator family expressed in the placenta form large channels with unknown activation properties that harbor a lipid bilayer on the inside of a cylindrical pore.

(O-Acyl)-ω-hydroxy fatty acids and their derivatives, produced by the fatty acid ω-hydroxylase Cyp4f39, form a lipid polarity gradient in the lipid layer of the tear film and prevent dry eye.

The structure of the mechanosensitive channel MscS embedded in a lipid bilayer redefines the nature, location and importance of lipid–protein interactions in the gating of mechanosensitive channels.

The amphipathic helix of perilipin 4 relies on the organization of its polar residues to form a remarkably immobile and stable protein layer on the surface of lipid droplets.