Cryo-EM structure of human TMEM120A reveals that it is a coenzyme A-binding protein and is unlikely to function as a mechanosensitive channel as was recently proposed.

Electrophysiological and structural characterizations reveal that a previously proposed ion channel responsible for sensing mechanical pain is insensitive to poking or stretching stimuli for conducting ions and may serve as a coenzyme A-binding protein instead.

The structural basis of how an enzyme differentiates chemically identical molecules unlike its homolog to channel fatty acids towards secondary metabolism is elucidated.

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.

In vitro and in vivo studies uncovered a molecular link between elevated mitochondrial ceramide levels, coenzyme Q depletion, and insulin resistance.

Electrophysiological and structural data do not support a mechanosensitive channel function for TACAN.

Comparative -omic analyses of five knockout mouse strains with disrupted mitochondrial DNA expression at different levels provide a high quality resource of altered gene expression patterns that reveal several common secondary patophysiological changes of mitochondrial dysfunction.

Lower mitochondrial coenzyme Q was a consistent feature across multiple in vitro and in vivo models of insulin resistance and was sufficient to cause insulin resistance through increased mitochondrial oxidants.

Mitochondria can trigger massive endocytosis by releasing coenzyme A into the cytoplasm and thereby promoting the addition of fatty acids to surface membrane proteins.

Many bacteria use a tiny riboswitch aptamer to sense the thiamin precursor HMP-PP to regulate the production of another thiamin precursor HET-P to efficiently biosynthesize this essential coenzyme.