Frank Tippmann

This paper introduces a new ribosome profiling protocol that is faster, cheaper, and more sensitive, enabling use with minimal RNA input.

The paper reveals a temporal control mechanism driven by coupled ribosomes that enables the formation of intertwined protein dimers by bypassing closed monomeric states.

The paper shows co-translational ribosome pairing enables the formation of coiled-coil homodimers from misfolding-prone subunits through chaperone-like interactions between nascent chains.

The paper identifies NAC's role in promoting co-translational folding by interacting with nascent chains at the ribosomal tunnel exit, expanding its known functions in protein biogenesis.