Günter Krämer

The paper shows that the ribosome coordinates folding and assembly of a complex protein to enable efficient biogenesis.

This study identifies Apj1 and Ydj1 as J-domain proteins that regulate Hsf1 in distinct phases of the heat shock response in yeast.

This paper introduces a new ribosome profiling protocol that is faster, cheaper, and more sensitive, enabling use with minimal RNA input.

The paper reveals a temporal control mechanism driven by coupled ribosomes that enables the formation of intertwined protein dimers by bypassing closed monomeric states.

The paper shows co-translational ribosome pairing enables the formation of coiled-coil homodimers from misfolding-prone subunits through chaperone-like interactions between nascent chains.

The paper identifies NAC's role in promoting co-translational folding by interacting with nascent chains at the ribosomal tunnel exit, expanding its known functions in protein biogenesis.

This study identifies miR-2954 as a male-essential microRNA critical for avian sex chromosome dosage compensation, showing its role in balancing gene expression in males and females.

The paper investigates the distinct physiological roles of NatA and NatB in S. cerevisiae through transcriptome, translatome, and proteome profiling of mutants, revealing specific effects on gene expression and protein folding.

The paper reveals Ebp1's role in neuronal proteostasis by analyzing ribosomal architecture and proteomic changes in the developing mouse neocortex.

The paper identifies amino acid pairs at the ribosome's P- and A-sites that predictably and causally modulate translation-elongation rates in yeast.

This paper introduces selective 40S footprinting to study translation initiation in human cells, revealing that scanning ribosomes remain cap-tethered and only one ribosome scans a 5UTR at a time.

The paper identifies Bfr1 as a regulator of Pmt1 and Pmt2 translation, affecting unfolded protein O-mannosylation in yeast.

The paper develops chemical kinetic methods to measure translation initiation, elongation, and codon-specific rates from ribosome profiling data, finding significant variability in codon translation rates.

The paper identifies a new quality control pathway for integral membrane proteins involving RAC-Ssb that couples translation rate to the unfolded protein response.