A dynamic SILAC analysis reveals that neuronal proteome turnover is influenced by the cell type as well as the extracellular environment.

Metabolic labelling reveals complex proteome dynamics in tendon, with faster turnover of proteins in the glycoprotein-rich interfascicular matrix compared to the collagen-rich fascicular matrix.

Autophagy is critical for the turnover of inflammatory signaling complexes containing RHIM-domain proteins.

By performing ¹⁵N pulse-labeling of mice, the turnover of hundreds of proteins in eye tissues was measured by mass spectrometry that revealed long-lived metabolic enzymes in the lens.

Dynamic SILAC labeling in combination with mass spectrometry revealed substantial regulation of protein synthesis, degradation, turnover, and abundance during homeostatic scaling in neurons.

The main proteins of clathrin-mediated endocytosis bind and unbind rapidly, continuously turning over about five times during the formation of an endocytic vesicle in yeast.

Palmitate turnover is controlled by distinct enzyme families with different specificities.

The transcription machinery is required for the disassembly of the promoter-proximal H2A.Z nucleosome, contributing to the constitutive histone turnover at yeast promoters.

The site of ubiquinone binding observed in the cryo-EM structure of respiratory complex I during turnover supports a two-state stabilization change mechanism.

The conformational dynamics of multidrug resistance protein 1 (MRP1) are tracked in real time by single-molecule fluorescence resonance energy transfer experiments, which elucidate the rate-limiting mechanism of MRP1's transport cycle.