ABSTRACT Background Protein-protein interactions (PPIs) are intriguing targets for
designing novel small-molecule inhibitors. The role of PPIs in various infectious and …

The heat shock protein 90 (Hsp90) family consists of four highly conserved isoforms: the
mitochondrial TRAP-1, the endoplasmic reticulum-localised Grp94, and the cytoplasmic …

Protein functions are dynamically regulated by allostery, which enables conformational
communication even between faraway residues, and expresses itself in many forms, akin to …

There were several significant milestones in the last century, from the discovery of the Bohr
effect [1] to understanding that every dynamic protein can be inherently allosteric [2, 3]. It …

Allostery is a constitutive, albeit often elusive, feature of biomolecular systems, which heavily
determines their functioning. Its mechanical, entropic, long-range, ligand, and environment …

Modern drug design relies on a detailed understanding of the molecular recognition process
by which biological partners such as a protein and a drug interact and bind to each other …

Focusing on an important biomedical implication of allostery–design of allosteric drugs, we
describe characteristics of allosteric sites, effectors, and their modes of actions …

SARS-CoV-2 has evolved rapidly in the first 3 years of pandemic diffusion. The initial
evolution of the virus appeared to proceed through big jumps in sequence changes rather …

Introduction The 90-kDa heat shock protein (HSP90) functions as a molecular chaperone, it
assumes a significant role in diseases such as cancer, inflammation, neurodegeneration …

The omnipresence and diversity of allosteric regulation in proteins and protein associations
complemented by the potential for the design of allosterically acting biologics and drugs call …