A transmembrane protein uses distinct mechanisms to regulate the movement of specific toll-like receptors-key immune system components involved in detecting pathogens-to their final locations inside cells.
A protein complex that enables cells to transport substances across their membranes, and that typically consists of four subunits, can also function as two hemicomplexes, each with two subunits.
Fluorescence resonance energy transfer has been used to explore the interactions between DNA polymerases, sliding clamps and clamp loaders as DNA is replicated in human cells.
A compound that prevents stressors such as UV light and viral infection from downregulating protein synthesis inside cells improves memory performance in mice.
Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.
C-terminal phosphorylation of the lipid phosphatase PTEN drives a reduction in membrane affinity and leads to a more compact conformation that involves a C2 domain-tail interaction.
Skin cells from a patient with retinitis pigmentosa have been used to generate induced pluripotent stem cells, which could potentially form the basis of new treatments for this disease.
