Allostery holds critical role in CRISPR-Cas9 specificity enhancement.

Input from computational models has enabled the detection of allosteric communication that modulates the gating mechanism of a bacterial outer-membrane protein.

Structure-function analyses reveal the mechanistic underpinnings of inside-out transmembrane signaling that controls periplasmic proteolysis, and thereby biofilm formation, in bacteria and may be relevant in the context of other signaling proteins with similar control elements.

Rigorous biophysical studies reconcile several conflicting views on how cGAS is activated, and present a new unifying allosteric activation mechanism.

In mGlu heterodimers, an oriented asymmetrical activation revealed complex allosteric interaction between subunits.

Light-sensitive allosteric switch module, a broadly applicable protein engineering method, is used for the regulation of protein activity with tight temporal control and spatial precision.

Mutations along the signaling pathway of the E. coli sensor histidine kinase PhoQ alter signal gain and ligand-sensitivity by altering thermodynamic allosteric coupling between domains.

Structural biology studies reveal the importance of protein dynamics on understanding molecular mechanisms underlying allosteric modulation of G protein-coupled receptors (GPCR) that offer insights into future GPCR research and drug discovery.

A combination of single-molecule and in vivo FRET showed how drugs affect conformation of mGluR2 at different domains.