Allostery is a fundamental and extensive mechanism of intramolecular signal transmission.
Allosteric drugs possess several unique pharmacological advantages over traditional …

At several stages of drug discovery, bioisosteric replacement is a common and efficient
practice to find new bioactive chemotypes or to optimize series of molecules toward drug …

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 …

Currently, there are two types of drugs on the market: orthosteric, which bind at the active
site; and allosteric, which bind elsewhere on the protein surface, and allosterically change …

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

Highlights•Hidden allosteric sites provide valuable avenues for allosteric drug
discovery.•Hidden allosteric sites are invisible in the ligand-unbound crystal structures.• …

The design of bioisosteres represents a creative and productive approach to improve a
molecule, including by enhancing potency, addressing pharmacokinetic challenges …

Publisher Summary This chapter reviews progress in the use of bioisosterism in drug
design. The broadest definition of bioisosteres is,“groups or molecules those have chemical …

Allosteric regulation, induced by perturbations at an allosteric site topographically distinct
from the orthosteric site, is one of the most direct and efficient ways to fine-tune …

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 …