Proline is essential for osteoblast differentiation and bone formation by facilitating the production of proline-enriched osteoblast proteins.

Cryo-electron microscopy structures of full-length P5CS, the proline synthesis enzyme, reveal that filamentation is crucial for the coordinated catalytic reactions between the glutamate kinase and γ-glutamyl phosphate reductase domains.

Loss of FAD stemming from cell autonomous defects in mitochondrial proline catabolism impairs sperm quality male reproductive advantage in C. elegans.

Microbial cells optimally structure their proteomes in order to mutually maximize metabolism and translation, as established by an extensive comparison between data and a low-dimensional model of cellular physiology.

Multi-omic analyses reveal a connection between the integrated stress response and the regulation of redox and amino acid metabolism when the TCA cycle is impaired.

Mammalian cells were engineered to synthesize valine, a metabolic capacity that had been lost from the lineage of higher eukaryotes for >500 million years.

Assays using recombinant HIF prolyl hydroxylases did not support hydroxylation of more than 20 reported non-HIF substrates under conditions where robust HIF hydroxylation was observed.

Time-course phosphoproteomics reveals that selective dephosphorylation is critical for directing the MI/MII transition and that, through its inherent phospho-threonine preference, PP2A-B55 imposes specific phosphoregulated behaviors that distinguish the two meiotic divisions.

Mutations elsewhere in the genome play critical roles in improving fitness during amplification and divergence of a gene encoding a weak-link enzyme whose inefficiency limits growth rate.

This enzymatic method enables highly specific and complete 1:1 protein conjugations with small molecules, solid supports, and other proteins, offering broad applicability across diverse biochemical and biotechnological applications.