AFF4 increases the combined selectivity of HIV Tat and TAR for super elongation complexes 330-fold over P-TEFb alone.

Structure-function analysis of the super elongation complex formed when HIV replicates inside cells reveals that the HIV-1 Tat protein binds to a cleft between P-TEFb, an enzyme that is involved in normal transcription, and AFF4, a protein that is used to build the super elongation complex

Transcription elongation by the elongation factor P-TEFb promotes the epithelial–mesenchymal transition and metastasis of breast cancer cells, implicating inhibition of this factor as a potential treatment for the late stages of this cancer.

CBP/p300 acetylation of histone H3 at promoters and enhancers stimulates transcriptional elongation through recruitment of the super-elongation complex and BRD4.

The previously uncharacterized protein PPP1R35 is a novel centriolar luminal protein critical for centriole elongation by acting in a complex with microcephaly protein RTTN.

Quantitative live imaging assays reveal that multiple enhancers often fail to work in an additive fashion in the patterning of the Drosophila embryo, and sometimes even interfere with one another.

An inorganic tin oxochloride cluster specifically binds to an intrinsically disordered, histidine-rich, low complexity protein region and arrests de novo transcription initiation without affecting reinitiation.

Combined light and electron microscopy reveals a new function for Arp2/3-mediated actin assembly in nuclear envelope rupture, which leads to a separation of nuclear membranes and pores from the lamina.

Single-molecule observations reveal a mechanism that may be used by multiple competing regulatory proteins to control ribosomal RNA production during rapid bacterial cell growth.