The inward-open and outward-open structures of MjNhaP1 explain the mechanism of electroneutral sodium-proton antiport across the cell membrane.

An archaeal basal transcription factor containing an iron-sulphur cluster sheds light on the evolution of transcription machineries in archaea and eukaryotes.

The regulatory RNA RydC binds to Hfq to make an effector complex for the recognition of targeted mRNA in the regulation of genetic information.

Post-translational installation of thioglycine in methyl-coenzyme M reductase in the methanogenic archaeon Methanosarcina acetivorans is mediated by the tfuA-ycaO locus and stabilizes the protein secondary structure near the active site.

Multiple solution-state structures are used for the DNA double-strand break repair functions of the Mre11-Rad50 protein complex.

Axonal metabolic flux analysis demonstrates that expression of NMNAT1 blocks axonal degeneration in cultured mouse neurons not by altering NAD+ synthesis, but rather by inhibiting injury-induced, SARM1-dependent NAD+ consumption.

The X-ray structure of the PaNhaP provides a unique view of substrate-ion binding and release in electroneutral sodium/proton antiporters.

Adapting bacteria to use an introduced metabolic pathway recapitulates natural mutations and offers a novel bioremediation strategy.

Comparative structural analysis and biochemical characterization unraveled the mechanisms behind enzymatic substrate selectivity, leading to an amplified theanine yield through active mutant protein screening, thus refining strategies for theanine production.

Mutational analysis and biochemical experiments suggest that the conserved β-hairpin-like membrane-reentrant loop of RseP - an S2P family intramembrane cleaving protease - helps to discriminate substrates by directly interacting with their transmembrane segments.