Allostery is a universal, biological phenomenon in which orthosteric sites are fine‐tuned by
topologically distal allosteric sites triggered by perturbations, such as ligand binding, residue …

The presence of druggable, topographically distinct allosteric sites on a wide range of
receptor families has offered new paradigms for small molecules to modulate receptor …

Peptide‐based drugs offer high specificity, potency, and selectivity. However, their inherent
flexibility and differences in conformational preferences between their free and bound states …

Background Despite being hugely important in biological processes, allostery is poorly
understood and no universal mechanism has been discovered. Allosteric drugs are a largely …

Orthosteric drugs block the active site to obstruct function; allosteric drugs modify the
population of the active state, to modulate function. Available data lead us to propose that …

Machine learning-based protein structure prediction algorithms, such as RosettaFold and
AlphaFold2, have greatly impacted the structural biology field, arousing a fair amount of …

Selective orthosteric inhibition of kinases has been challenging due to the conserved active
site architecture of kinases and emergence of resistance mutants. Simultaneous inhibition of …

Allosteric drug development holds promise for delivering medicines that are more selective
and less toxic than those that target orthosteric sites. To date, the discovery of allosteric …

Understanding molecular mechanisms underlying the complexity of allosteric regulation in
proteins has attracted considerable attention in drug discovery due to the benefits and …

The concept of allostery was elaborated almost 50years ago by Monod and coworkers to
provide a framework for interpreting experimental studies on the regulation of protein …