Structural and functional characterization of an unanticipated mode of allosteric activity regulation in ribonucleotide reductases controlled by an ATP-cone in the radical-generating subunit.

Atomistic simulations reveal how lipids can allosterically modulate membrane receptors.

Internal dynamics play a crucial functional role in MarR (multiple antibiotic resistance repressor) proteins and their role reconciles the distinct allosteric mechanisms proposed previously.

Substrate and effector bound structures of a bacterial ribonucleotide reductase reveal the molecular basis by which substrate preference is modulated by a distal site on the enzyme.

The signaling ligand (p)ppGpp regulates the enzyme HPRT across species by binding to a novel class of conserved motif, yet its specificity is allosterically altered through evolution of enzyme oligomerization.

Specific residues within an enzyme integrate allosteric inputs that originate from distinct ligand-binding pockets.

The molecular chaperone BIP from the endoplasmic reticulum is fine-tuned postranslationally through the thermodynamic and kinetic alterations in its conformational ensemble of functionally and structurally distinct physiological forms.

Understanding the complex auto-regulatory mechanisms for guanine nucleotide exchange factors is critically important for fully appreciating the layers of control for small GTPases.

Using a short peptide to regulate the activity of HCN ion channels illustrates how physiological modulators could inspire new drugs. .

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.