J. D. Puglisi

This study uses single-molecule techniques and cryo-EM to show how eIF1A and eIF5B remodel initiation complexes to facilitate ribosomal subunit joining during translation initiation.

The paper directly observes yeast 43S ribosomal scanning along mRNA 5'UTRs, revealing its speed and structural regulation mechanisms.

This paper develops a real-time single-molecule RNA sequencing method to visualize telomerase catalysis and structural dynamics at single-nucleotide resolution.

The paper uses single-molecule fluorescence assays to study eukaryotic translation termination dynamics in yeast, revealing a conserved multi-step process involving eRF1 and eRF3.

This paper investigates how SARS-CoV-2 NSP1 inhibits translation initiation by competing with mRNA for binding to the 40S ribosomal subunit, modulated by eIFs.

The paper investigates how eIF5B facilitates the transition from translation initiation to elongation in yeast using single-molecule fluorescence microscopy.

This study investigates RACK1's exchange dynamics on and off the ribosome using fluorescent labeling and biochemical analyses, showing its stable binding and limited conformational changes.

This paper introduces DRRAFTER, a method to model RNA-protein complexes from cryoEM maps, showing it can build accurate RNA coordinates in real-world scenarios.