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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.

Alkylation stress modify mRNAs and results in translation arrest, which activates the ribosome-rescue pathway of trans translation in bacteria.

Phosphatidylinositol 3-phosphate interacts with PfHsp70-1 and stabilizes the Plasmodium digestive vacuole under febrile temperatures.

LOV2GIVe allows to activate Gi proteins non-invasively with innocuous blue light based on a design principle unrelated to light-activated GPCRs (metazoan opsins), thereby expanding the range of potential experimental applications.

A set of ER-localized membrane proteins whose loss causes developmental diseases in humans, assemble with Sec61 into a translocon that facilitates the biogenesis of hundreds of different multi-pass membrane proteins.

Rigorous biochemical and structural analyses reveal the precise topology of cohesin's association with DNA and suggest a mechanism for how DNA is transported inside the ring.

Protein engineering of a reversibly switchable fluorescent protein enables post-hoc reversible and repeatable marking of elevated calcium concentrations using blue light.

Methods that use puromycin to localize active translation do not actually detect the site of translation.