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Biochemical and in vivo physiology imaging reveal that plant pathogens actively imbalance the apoplastic eAdo/eATP levels as a virulence mechanism.

Stable isotope labeling reveals that NAD crosses the inner membrane of mammalian mitochondria via an unknown transporter.

The roles of key telomerase active site residues were elucidated to determine how telomerase selects the correct from the incorrect nucleotide to maintain telomere integrity.

The important oncogene KRasG13C can be targeted by covalently binding nucleotide-analogues, resulting in a locked protein that can no longer induce oncogenic signaling.

Reengineering the nucleotide-binding pocket of an extant ATPase to restore ancestral GTPase activity revealed an ATP-dependent intermediate required for function and suggested why the protein evolved to use ATP.

Random sequence RNA pools display an innate capacity for ligation and recombination, enabling them to “bootstrap” themselves towards higher compositional, informational and structural complexity.

Biochemical and structural analyses reveal direct ubiquitin modification of single-stranded nucleic acids, catalysed by the DTX3L ubiquitin ligase.

Multicellular and socially aggregating prokaryotes contain previously undescribed, chaperone-based systems predicted to mediate defensive biological conflicts, several components of which are thematically similar antecedents of eukaryotic apoptosis pathways.

RNA degradation is completed through specific intermediates, such as diribonucleotides, which must be removed from the cells by a specific enzyme.

Atomic structures suggest a novel mechanism for the regulation of mRNA transcription and capping in dsRNA viruses.