The ATPase Fap7 prefabricates a uS11:eS26 ribosomal protein complex for ribosome assembly.

The Tsr2 carrier protein connects the nuclear import machinery with the ribosome assembly pathway.

Ribosomal proteins Rps27 (eS27) and Rps27l (eS27L) are an ancient pair of duplicated genes that encode functionally interchangeable proteins, yet have been evolutionarily retained because both copies are necessary to achieve protein expression across cell types.

In glioblastoma stem cells, oncogenes on extrachromosomal DNA do not cluster at distances in keeping with coordinated transcription, with amplified gene expression driven by copy number rather increased transcriptional efficiency.

FGF signalling is responsible for priming the developmental enhancer ZRS across the distal limb mesenchyme during development, allowing ETS factors to modulate its activity through balancing histone acetylation.

Cryo-EM and functional studies reveal how combined action of proteins RPS26/eS26 and RIO1 allows late precursors to the human small ribosomal particle to be matured into fully translation-competent 40S subunits.

Mining electron cryomicroscopy data reveals new ribosomal interactions that preclude translation to potentially regulate gene expression.

An ensemble of cryo-EM structures reveals how eukaryotic elongation factor 2 positions the first codon of a viral mRNA for translation.

A conformational change in the Cricket Paralysis Virus IRES upon double translocation in the ribosome uncovers an unexpected similarity with the Hepatitis C Virus IRES.

The RNA helicase Spb4 restructures rRNA helices H62/H63 and primes pre-ribosomal 60S intermediates for large-scale remodelling by the AAA-ATPase Rea1.