Tino Pleiner

This study shows the ER membrane protein complex (EMC) acts as a chaperone to facilitate the assembly of voltage-gated calcium channels during their biogenesis.

This study determines the structural basis of phage terminase recognition by Avs2 and Upx, revealing distinct binding mechanisms despite structural differences.

The paper shows that short disordered peptides can convert proteins into mechanosensors that respond to cellular forces, expanding the known mechanisms of mechanosensing.

The paper studies the biogenesis of ER membrane proteins, identifying the EMC and BOS complex as key players and proposing a model for coordinated insertion.

This study identifies WNK1 as an essential factor for EMC assembly by stabilizing EMC2 and preventing promiscuous interactions.