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 …

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

Allostery is a fundamental mechanism of cellular homeostasis by intra-protein
communication between distinct functional sites. It is an internal process of proteins to steer …

Allostery is a ubiquitous biological regulatory process in which distant binding sites within a
protein or enzyme are functionally and thermodynamically coupled. Allosteric interactions …

Allosteric regulation is a common mechanism employed by complex biomolecular systems
for regulation of activity and adaptability in the cellular environment, serving as an effective …

The ability of Adenosine Triphosphate (ATP) to modulate protein solubility establishes a
critical link between ATP homeostasis and proteinopathies, such as Parkinson's (PD). The …

The last five years have witnessed major developments in the understanding of the allosteric
phenomenon, broadly defined as coupling between remote molecular sites. Such advances …

Genetic alterations in the PRKACA gene coding for the catalytic α subunit of the cAMP-
dependent protein kinase A (PKA-C) are linked to cortisol-secreting adrenocortical …

The exquisite sensitivity of the NMR chemical shift to local environment makes it an ideal
probe to assess atomic level perturbations in proteins of all sizes and structural …

The final two steps of tryptophan biosynthesis are catalyzed by the enzyme tryptophan
synthase (TS), composed of alpha (αTS) and beta (βTS) subunits. Recently, experimental …