David C. Zappulla

The paper determines the secondary structure of S. pombe telomerase RNA (TER1) and shows it functions as a flexible scaffold for the telomerase RNP.

This paper uses inverse RNA folding to design a full-length yeast telomerase RNA with increased in vitro activity but reduced in vivo abundance.

The paper identifies a 4-base pair core-enclosing helix in telomerase RNA essential for binding TERT and telomerase activity in yeast.

This study shows that repositioning the Sm-binding site in yeast telomerase RNA affects 3′-end formation and highlights the flexibility of the telomerase RNP structure.

The paper introduces a CRISPR-based yeast two-hybrid system to identify RNA-binding proteins, demonstrating its effectiveness in detecting RNA-protein interactions with high sensitivity.