Boris Zinshteyn

The paper identifies N6AMT1's role in cytosolic translation of mitochondrial RNAse P subunits, showing its necessity for mitochondrial RNA processing and function.

This study uses time-resolved DMS footprinting to show that rRNA tertiary interactions and protein binding sites in E. coli remain unfolded until late stages of ribosome assembly.

The paper introduces DART, a method to analyze ribosome targeting, revealing thousand-fold differences in 5' UTR-specific translation activity and identifying regulatory elements.

The paper evaluates commercial RNA-seq depletion methods for ribosome footprint profiling and recommends custom biotinylated oligos over nuclease-based approaches due to their impact on data resolution.