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

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.

Assembly of the human enzyme inosine monophosphate dehydrogenase 2 into filaments promotes substrate-dependent resistance to feedback inhibition by downstream products, promoting increased flux during proliferative states.

Protein kinase dysregulation, implicated in various diseases via cell signaling pathways, can be therapeutically and experimentally managed through allosteric modulation, facilitated by a dynamic network of interactions, with computational techniques enabling precise control in live systems.

Nuclear phosphoinositide signaling controls telomeric gene repression and activation essential for switching expression of surface antigen genes and thus antigenic variation.

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.

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.

A minimal subset of two to three residues in cyclic nucleotide binding (CNB) domains controls nucleoside vs. cyclic nucleotide specificity, repurposing PKA of certain pathogens for novel nucleoside signaling pathways or sensing.

Our latest Special Issue brings together research on the allosteric regulation of kinase activity.

Allostery in an intrinsically disordered domain of glucocorticoid receptor is mediated by opposing thermodynamic signals that are directed through the production of different isoforms.