Uncoupling of dynamin polymerization and GTPase activity can be induced with dynamin, which allows in vivo visualization of its activity at endocytic pits.

Numerous chemokine variants bearing no sequence resemblance elicit similar signaling behavior from the viral GPCR US28, suggesting a mechanism for receptor activation that accommodates extensive ligand degeneracy.

Synthetic single domain antibody libraries and a binder selection cascade encompassing ribosome and phage display enable the selection of conformation-specific binders against previously intractable membrane proteins within three weeks.

Conformation-specific nanobodies enable to capture and solve the first GTP-bound active structure of a bacterial homolog of the Parkinson-associated LRRK2 protein, providing insights into the activation mechanism of these proteins.

Opioid drug efficacy and allosteric modulation is measured using an active state sensor of the mu-opioid receptor.

The cryo-electron microscopy structures of inactive and active states of calcium-sensing receptor (CaSR) reveal the activation mechanisms of CaSR.

Development of nanobodies against a model pentameric ligand-gated ion channel demonstrates they can be functionally active as negative or positive allosteric modulators and offers opportunities for future drug development.

A GPCR activated by the same agonist engages different conformational biosensors at different subcellular locations, suggesting that location-based conformations drive spatial encoding of signaling.

The structure of gp41with its membrane anchors highlights the flexible linkage of the transmembrane regions and the fuson peptides, which generates an asymmetric conformation, a potential target of MPER bNAbs.

A large proportion of nanobodies are unstable when expressed intracellularly, but can be reliably stabilized for intracellular expression by applying a generalizable mutagenesis strategy based on positional sequence conservation.