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Structural and functional approaches unambiguously revealed physiologically relevant lateral interactions between FtsZ protofilaments.

The in vivo modification of the canonical intermediate filament protein vimentin with O-linked beta-N-acetylglucosamine affects its function in filament assembly, cell migration and host-pathogen interactions.

Variability in bacterial transcription start site selection involves DNA “scrunching” and “anti-scrunching,” which may represent a general mechanism for start site selection in all organisms.

Introduction of single photoswitchable unnatural amino acid into a neuronal receptor provides reversible, rapid and robust control of its activity by light, representing an important contribution to the fast expanding field of optopharmacology.

The N-terminal domain of the chromatin remodeler ISWI contains previously uncharacterized conserved motifs that maintain structure, prevent ATP hydrolysis unless nucleosomes are bound, and confer H4-tail sensitivity without directly competing with the H4 tail.

Biochemical dissections show that the Guided Entry of Tail Anchored proteins (GET) pathway selects ER-destined tail-anchored proteins using at least two distinct molecular mechanisms, each recognizing a distinct physicochemical feature in the substrate.

NusG enhances transcription elongation by stabilizing DNA base pairs immediately upstream of the RNA-DNA hybrid but does not measurably affect the nucleotide incorporation and the forward translocation by RNA polymerase.

An ancient complex comprising the eukaryotic elongation factor-1A and aminoacylated tRNA is shown to be the target of a cyclic heptapeptide and two unrelated natural products with potent anticancer activity.

Cholera intoxication of human colonic epithelial cells is dependent on recognition of protein glycosylation and fucosylation, not exclusively on ganglioside recognition as proposed previously.

Interdomain linker-mediated oligomerization of the endoplasmic reticulum chaperone protein BiP responds to the unfolded protein burden