Translationally active polysomes from mammalian cells/tissues are successfully separated with rapidity, high efficiency and exceptional reproducibility by a SEC-based approach, an accessible alternative to the conventional sucrose density gradient analysis.

Examination of the changes in the transcription start site selection in TCL1-driven chronic lymphocytic leukemia and their impact on mRNA translation revealed a marked elevation of intra-genic cryptic promoters, which are predicted to generate multiple N-terminally truncated or modified proteins.

Using mass spectrometry to study protein composition of translating ribosomes under unstressed or stress conditions, aspartate aminotransferase 2 (Aat2) is identified as a metabolic enzyme with a moonlighting function in the yeast integrated stress-response pathway.

Arabidopsis microRNAs and their effector protein ARGONAUTE1 associate with and act on polysomes on the rough endoplasmic reticulum.

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.

A mouse model where the splicing factor SRSF1 was prevented from accumulating in the cytoplasm revealed reduced translation of thousands of mRNAs and postnatal phenotypes particularly affecting multiciliated cells.

Thousands of small Open Reading Frames are translated, and form two distinct classes based on their translational efficiency and bioinformatic indicators.

Arginine methylation regulates mRNA translation of key protooncogenes via an RGG/RG motif-containing protein called Aven.

Identifying the translational targets of the shuttling protein, SRSF1, reveals that it is needed for normal cell division, and suggests that it couples pre-mRNA splicing and translation.

The GC content of human mRNAs is key to P-body localization and protein yield, and has a major impact on their post-transcriptional control.