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A poly(A) tail-based regulatory mechanism dynamically controls PABPC1 protein synthesis in cardiomyocytes and thereby titrates cellular translation in response to developmental and hypertrophic cues.

A chemogenetic tool has been developed to map and manipulate neuronal circuits with spatial and temporal precision.

The integrated stress response is able to rapidly shut down the synthesis of proteins in eukaryotic cells.

An RNA-binding protein called PABPC1 has an important role in determining protein synthesis rates and hypertrophy in the heart.

Regulation of conserved Nodal factors by a maternal protein ensures that Nodal signaling is repressed until the appropriate time in embryonic development.

The RNA-binding protein, Zfp36, which is critical for resolving inflammation, inhibits the production of proinflammatory cytokines via modulation of the cytoplasmic poly(A)-binding protein.

A time-resolved analysis of protein and RNA concentrations and interactions during proteostasis stress highlights the dominant role of translation regulation and a shift of energy metabolism.

Translation pauses occur in strategic positions to facilitate the production of properly folded membrane proteins in bacteria.

Measurements of transcript isoform specific translation across the human genome reveal that isoforms from the same gene can differ in protein production by two orders of magnitude.

The SUMO-Ub-Cdc48 pathway is a novel regulatory mechanism of Pol III and a potential therapeutic target for Pol III-related human diseases.