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Chemical modifications near the tRNA anticodon and specific mRNA–tRNA pairs combine to control the ribosomal three-nucleotide mRNA reading frame, essential for the sequential addition of amino acids into polypeptide chains.

In mitotically aging yeast cells, the cytosol acidifies, the distances between the organellar membranes decrease dramatically, but crowding on the scale of the average size protein is relatively stable.

Protein O-Mannose Kinase enables Like-acetyl-glucosaminyltransferase 1 to elongate matriglycan on α-dystroglycan, thereby allowing matriglycan to function as a scaffold for extracellular matrix proteins and prevent muscular dystrophy.

Inhibition of bacterial protein synthesis by an antimicrobial peptide apidaecin triggers translation arrest at the stop codons, ribosome queuing and pervasive stop codon readthrough.

Activation and autophosphorylation of CaMKII releases the regulatory segment, which can then bind to and destabilize the hub assembly by trapping large fluctuations in the hub architecture.

Phosphorylation of a highly conserved serine residue is a physiological response of Escerichia coli to environmental potassium levels that inhibits transport by KdpFABC to maintain cellular homeostasis.