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Comprehensive structural and compositional characterization of the in vivo 30S ribosomal assembly landscape reveals parallel pathways for 3′-domain formation and a previously unknown role for the assembly factor RimP.

Cryo-EM reveals how the central functional site of the ribosome is assembled and provides a framework to interpret the consequences of mutations linked to leukaemia-associated ribosomopathies.

eIF3, despite being a general translation initiation factor, functions in mRNA-specific regulation, having a profound impact on the synthesis and activation of the MAPK pathway components and ribosomal proteins.

Microbial cells optimally structure their proteomes in order to mutually maximize metabolism and translation, as established by an extensive comparison between data and a low-dimensional model of cellular physiology.

Endoproteolytic cleavage of the ribosomal precursor protein FUBI-eS30 is required for efficient maturation of small ribosomal subunits in the cytoplasm of human cells and involves the nucleolar deubiquitinase USP36.

The Tsr2 carrier protein connects the nuclear import machinery with the ribosome assembly pathway.

Brain region-specific profiling of O-GlcNAcylation interactome in Drosophila mushroom body suggests that hypo-O-GlcNAcylation impacts cognitive function by regulating translational activity.

The interaction between rDNA instability and proteostasis stress, two major aging hallmarks, underlies single-cell aging trajectories in yeast.

Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

Minimal changes allow an ancestral, unfolded peptide to adopt a known fold by repetition, illuminating a possible path for the emergence of folded proteins at the origin of life.