Neurosecretory protein GL, a previously unknown mammalian neuropeptide, is a novel hypothalamic factor which regulates feeding behavior and peripheral lipogenesis in animals.
Inhibition of C. elegans FLD-1 or Human TLCD1/2 prevents saturated fat lipotoxicity by allowing increased levels of membrane phospholipids that contain fluidizing long-chain polyunsaturated fatty acids.
The structure of phage L's Dec demonstrates a new fold within this family of proteins, and shows modulation of capsid binding occurs through two sites, with site 1 being preferred.
Cryo electron microscopy and structure-based mutagenesis reveal that the bacteriophage BPP-1 contains two of the three major recognized viral folds, one of which exhibits a new topology.
To protect their food and themselves against detrimental mould fungi, the eggs of a wasp species synthesize and emit remarkable amounts of gaseous nitrogen oxides that are highly effective antimicrobials.
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.
An unexpected new biological function was discovered for the universally conserved cofactor lipoate, as lipoate-binding proteins proved essential for a novel wide-spread prokaryotic sulfur oxidation pathway.
Combined cell labelling with a bi-cistronic reporter-gene vector and gold nanorods enables short- and long-term cell tracking in vivo via multimodal imaging (multispectral optoacoustic tomography, bioluminescence, fluorescence) with high spatial resolution.
