Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.

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.

Cell-penetrating peptide drugs prevent adrenergic regulation of pacemaker channels without altering the overall response of the cell to cAMP.

The first crystal structure of an active plant asparaginyl endopeptidase reveals a tetrahedral intermediate state in its active site, which may help to explain why these enzymes have been independently recruited to perform peptide macrocyclization.

A peptide motif targeting tumor-infiltrating macrophage in triple-negative breast cancer delays tumor growth and favors an antitumor immune response.

Genomics and genetics were used to identify specialized metabolites employed by Pseudomonas bacteria to suppress the growth of potato pathogens, which revealed a key role for cyclic lipopeptides.

The cyclic neuropeptide somatostatin binds to human Aβ1-42 through an interface that critically relies on a specific tryptophan, thereby blocking the propensity of Aβ to aggregate, a critical step in the pathobiology of Alzheimer's disease.

A plant immune receptor evolved recognition of caterpillar peptides through key molecular changes.

The atomic resolution cryo-EM structure of somatostatin receptor 2 (SSTR2) provides insights into the mechanism by which SSTRs recognize their ligands and will serve as a platform to develop selective agonists and therapeutics.

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.