Matthias Thoms

TL;DR: Structural characterization of the inhibitory mechanism of Nsp1 may aid structure-based drug design against SARS-CoV-2 and effectively blocks retinoic acid–inducible gene I–dependent innate immune responses that would otherwise facilitate clearance of the infection.

TL;DR: It is shown that Nsp1 from SARS-CoV-2 binds to 40S and 80S ribosomes, resulting in shutdown of capped mRNA translation both in vitro and in cells, which effectively blocks RIG-I-dependent innate immune responses that would otherwise facilitate clearance of the infection.

TL;DR: This work uses sucrose gradient fractionation combined with quantitative proteomics to systematically identify proteins associated with collided ribosomes and uncovers mechanisms through which EDF1 coordinates multiple responses of the ribosomal-mediated quality control pathway and provides novel insights into the intersection of ribosome- mediated quality control with global transcriptional regulation.

TL;DR: Structural and functional insights are presented into the interaction of Saccharomyces cerevisiae Vms1 with 60S subunits in pre- and post-peptidyl-tRNA cleavage states and the ABCF-type ATPase Arb1 in the ribosomal E-site is found, which stabilizes the delocalized A73 of the peptidyl

TL;DR: Five cryo-electron microscopy structures of human 40S subunit precursors are reported, which describe the compositional and conformational progression during the final steps of 40S assembly and provide evidence for principal differences in small ribosomal subunit formation between humans and the model organism Saccharomyces cerevisiae.