The nuclear export receptor Crm1 cooperatively binds its HIV Rev-RRE cargo as a dimer using a species-specific interface that supports viral replication by enhancing nuclear export of HIV RNA.

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.

RNA-binding protein SRSF3 mediates critical changes in RNA processing of pluripotency genes, which reveals functional consequences of regulated RNA processing during stem cell self-renewal and early development.

YTHDC1 facilitates selective clearance of N6-methyladenosine methylated mRNAs from the nucleus to the cytoplasm through binding by nuclear 'reader' proteins and incorporation into the canonical mRNA export pathway.

A pliable hydrophobic interface in the HIV-1 Rev protein enables assembly of diverse oligomeric structures, guided by the RRE scaffold present in HIV-1 mRNAs.

Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.

The structural and functional analysis of the ATP-dependent RNA helicase Prp43 provides insights into the mechanisms of RNA binding and translocation, which could serve as paradigm for all DEAH-box proteins.

The cryo-EM structure of the human transcription-export THO–UAP56 complex reveals mechanisms of mRNA nuclear export licensing.

The THO-Sub2 complex is an asymmetric homodimer that uses the spatial arrangement of two Sub2 helicases to prevent RNA:DNA hybrids.

A multidimensional chemical mapping strategy enables confident determination of the structures of non-coding RNAs at 1-nm resolution, including previously intractable riboswitch and human regulon states.