Friedrich Förster

@fridof.bsky.social

Structural biologist, Cryo-EM aficionado, signal peptide nerd, teacher, mentor, dad, …

The first cut is the deepest: Cleavable signal peptides direct thousands of different nascent proteins to the endoplasmic reticulum. Oddly, SPs are all different and nevertheless cleaved with exquisite specificity. Our new cryo-EM structures + MD solve this paradox: www.nature.com/articles/s41...

Structural basis of signal peptide recognition by the signal peptidase complex - Nature Communications

Signal peptides are highly variable, yet the signal peptidase complex processes them with remarkable specificity. Here, authors combine cryo-EM, molecular dynamics simulations and modeling to reveal a...

nature.com

In one of our first publications in 2025, with colleagues from St. Louis, Leiden and Boston, we shed light on the molecular mechanisms of motile cilia, structures used by cells to propel themselves through fluid or to move fluid across their surfaces. www.nature.com/articles/s41...

Structural diversity of axonemes across mammalian motile cilia - Nature

Cryoelectron microscopy, cryoelectron tomography and proteomics are used to resolve the 96-nm modular repeat of axonemal doublet microtubules from both sperm flagella and epithelial cilia of the ovidu...

nature.com

My new life in blue starts with sharing a preprint of amazing Max Gemmer’s ex vivo analysis that sheds light on the machinery responsible for inserting many multispanning transmembrane proteins into the ER membrane #teamtomo: www.biorxiv.org/content/10.1...

Exploring the molecular composition of the multipass translocon in its native membrane environment

bioRxiv - the preprint server for biology, operated by Cold Spring Harbor Laboratory, a research and educational institution

biorxiv.org