Hundreds of cell growth and stress response genes are controlled by a rare small RNA component of an ancient splicing machinery, providing a raison d'être for its previously unexplained evolutionary conservation.

Real-time single-molecule visualization of transcription and splicing in living cells reveals that RNA synthesis and processing can occur through multiple pathways on the same gene.

The complete architecture of human spliceosomal U1 snRNP and its interaction with the 5′ splice site of pre-mRNA are described in atomic detail.

Structural and functional analyses show how the spliceosomal Prp3 protein concomitantly binds double- and single- stranded regions in U4/U6 di-snRNAs and serves to stabilize the U4/U6•U5 tri-snRNP for splicing.

Inhibiting PRMT1 enzymatic activity promotes megakaryocyte terminal differentiation via RBM15-mediated RNA metabolism, which is dysregulated in hematological malignancies.

Prp43 binds to the pre-mRNA and contacts predominantly U2 proteins in the budding yeast spliceosome.

Single molecule experiments reveal competition between spliceosome activation and the discard of the triple small nuclear ribonucleoprotein complex.

The first malacostracan genome sequence will establish the genetically tractable Parhyale hawaiensis as a model organism in this key animal group.

During evolutionary progression of Alu-exons, repressive U-tracts buffer sudden gains in 3' splice site strength and prevent inclusion of cryptic exons.

A protein regulator of alternative pre-mRNA splicing arrests spliceosome assembly at a previously unrecognized step that defines new intermediate stages in the formation of exon complexes.