Stalling spliceosome assembly at a novel step before Bact complex formation reveals new insights into the extensive RNP rearrangements and compositional changes that accompany the intricate process of spliceosome activation.

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.

Viewing the dynamic interactions of individual spliceosomal subcomplexes with single pre-messenger RNA molecules reveals how nearby flanking splice sites accelerate pre-spliceosome assembly and the splicing of multi-intron pre-mRNAs.

Single molecule fluorescence analysis of spliceosome E complex formation reveals how tuning of U1 binding to the 5' SS facilitates efficient capture of the snRNP by pre-mRNAs.

Competition between minor and major splice sites in SRSF10 controls cell type-dependent expression of all SR-proteins and reveals a global impact of the minor spliceosome on major intron splicing.

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

Interactions with Sm proteins can provide a way in which regulatory factors can modulate alternative splice site choices.

Alternative splicing provides a mechanism to maintain oscillations of the circadian clock.

Transient transcriptome sequencing and kinetic modeling suggest how the kinetics and yield of RNA splicing are encoded in the human genome.