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.

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.

Atomic structures suggest a novel mechanism for the regulation of mRNA transcription and capping in dsRNA viruses.