RNA molecules cause the proteins involved in the formation of germ granules to coalesce into liquid droplets.

An artificially evolved ribozyme can catalyse the synthesis of RNA by using trinucleotide triphosphates as building blocks.

In rotaviruses, the selective packaging of eleven distinct genomic RNA segments requires virus-encoded protein NSP2 to alter the RNA structures, facilitating their interactions with each other.

Cryo-electron microscopy structures show how coliphage HK022 Nun blocks Escherichia coli RNA polymerase translocation by mediating multiple interactions between the RNA polymerase and nucleic acids.

Ded1p and eIF4A, two RNA helicases that function in eukaryotic translation initiation, interact physically with each other and with the scaffolding protein eIF4G.

A bacteriophage remodels the RNA metabolism machinery of a bacterial host to sequentially clear host transcripts and then stabilize the viral RNA.

The structural architecture of the 4-subunit, RNA-binding human negative elongation factor NELF is derived by a combination of X-ray crystallography and protein crosslinking.

Tertiary folding of the Rev-response element (RRE) in HIV RNA ensures the rapid formation of the Rev-RRE viral ribonucleoprotein particle via a two-step process.

The Dengue virus contains discretely folded RNA structures that confer the ability to resist a powerful host cell enzyme and produce a disease-inducing noncoding RNA.

Motif length plays a critical role in the specification of biological function within a conserved family of RNA-binding proteins.