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The diffusion coefficients of proteins in the cytoplasm depend on their net charge and the distribution of charge over the protein surface, with positive proteins moving up to 100-fold slower because they bind to ribosomes.

Eukaryotic translation initiation factor 4A is stimulated by the ribosomal pre-initiation complex and promotes the recruitment of mRNAs regardless of their degree of structure.

Bacteria contain large numbers of negatively-charged proteins to avoid the electrostatic interactions with ribosomes that would dramatically reduce protein diffusion.

A 3.2 Å resolution structure of Vps4 provides a detailed model for protein substrate binding and translocation by AAA ATPases.

X-ray crystallographic studies have completed the first atomic resolution description of the kinetic cycle of a potassium channel's pore domain.

The ability of lipid nanodiscs to trap different types of amyloid intermediates, as successfully demonstrated in this study for human-IAPP, could become one of the most powerful approaches to dissect the complicated misfolding pathways of protein aggregation.

Biochemical and mutagenesis analysis reveal the long-anticipated RNA-binding elements of Polycomb Repressive Complex 2 (PRC2), an important chromatin modifier, allowing construction of separation-of-function mutants of PRC2 defective in RNA binding but retaining histone-modifying activity.

Divergence in immunoproteasome substrate specificity and regulation from the constitutive proteasome impacts peptide cleavage quantity and the cellular capacity of the ubiquitin-proteasome system.

Comparative -omic analyses of five knockout mouse strains with disrupted mitochondrial DNA expression at different levels provide a high quality resource of altered gene expression patterns that reveal several common secondary patophysiological changes of mitochondrial dysfunction.

Conventional annotations of coding sequences have missed thousands of short open-reading frames encoding proteins that are conserved and with specific functions.