Peter Rehling

This study elucidates the mechanism of human tRNA 3'CCA maturation by determining TRNT1 structures and showing a continuous polymerization and translocation mechanism.

This study uses super-resolution microscopy to visualize mitochondrial mRNAs and their interactions with proteins, revealing dynamic changes in mRNA distribution and structure during apoptosis and in disease.

The paper profiles the LAM family of contact site tethers to understand their localization and function, revealing unique and shared roles through proximity labeling.

The paper introduces an AID library for on-demand protein depletion in yeast, enabling systematic study of protein function and uncovering new roles in cell cycle and mitochondrial processes.

This study identifies Yet3 as a protein that recruits sterol biosynthesis enzymes to ER contact sites, enabling on-demand sterol production and influencing organellar structure and function.