Structural and biochemical analysis of an abundant and conserved protein complex called EMC shows how it is likely to insert nascent membrane proteins into the endoplasmic reticulum membrane.
A conserved viral protein complex that promotes membrane wrapping of nascent herpesvirus particles shows structural similarity to cellular membrane-remodelling proteins, suggesting functional mimicry.
Calcium-driven protein changes, causing glycogenolysis, poor synthesis, and diminished content of glycogen, along with diminished glucose transporters, lead to hyperglycemia in patients prone to calcium leaks from intracellular muscle stores.
Combined simulations and electrophysiological experiments show that the CLC channels and exchangers form physically distinct and evolutionarily conserved pathways through which Cl- and H+ ions move when crossing biological membranes.
The structure of the membrane-integrated components of a unique substrate decarboxylation-driven primary-active sodium pump provides insights into its transport mechanism.
The roles of key telomerase active site residues were elucidated to determine how telomerase selects the correct from the incorrect nucleotide to maintain telomere integrity.
