Bicyclostreptins are peptide natural products in which a macrocyclic β-ether and a heterocyclic sp³–sp³ linkage between a backbone amide nitrogen and an adjacent α-carbon are installed by two radical S-adenosylmethionine metalloenzymes.

Metabokiller is a novel, explainable AI-backed method for carcinogenicity prediction that leverages the biological and chemical properties associated with carcinogens.

Merging the generalized extracellular molecule sensor (GEMS) system with screening designed ankyrin repeat proteins (DARPins) identifies an advanced modular bispecific extracellular receptor (AMBER) for detection of fibrinogen degradation products.

A FRET-based assay using the conserved tryptophans of bacterial quorum-sensing LuxR-type proteins and synthetic fluorophore-acyl-homoserine lactone conjugates enables measurement of ligand-binding affinities either in vitro or in cells.

Bicyclostreptins are peptide natural products in which a macrocyclic β-ether and a heterocyclic sp³–sp³ linkage between a backbone amide nitrogen and an adjacent α-carbon are installed by two radical S-adenosylmethionine metalloenzymes.

A combination of mass spectrometry, pooled genome screens and STRING analysis identifies key uptake mediating interactions between nanoparticle-adsorbed proteins and cells via the low-density lipoprotein receptor.

Metabokiller is a novel, explainable AI-backed method for carcinogenicity prediction that leverages the biological and chemical properties associated with carcinogens.

Merging the generalized extracellular molecule sensor (GEMS) system with screening designed ankyrin repeat proteins (DARPins) identifies an advanced modular bispecific extracellular receptor (AMBER) for detection of fibrinogen degradation products.

A FRET-based assay using the conserved tryptophans of bacterial quorum-sensing LuxR-type proteins and synthetic fluorophore-acyl-homoserine lactone conjugates enables measurement of ligand-binding affinities either in vitro or in cells.

A hypercompact adenine base editor termed TaRGET-ABE was developed by fusing a catalytically inactive transposon-associated transposase B guided by an engineered RNA to deaminases, which achieves efficient A-to-G conversions via adeno-associated viral delivery in mammalian genomes.