While the pervasiveness of allostery in proteins is commonly accepted, we 
further show the generic nature of allosteric mechanisms by analyzing here 
transmembrane ion-channel viroporin 3a and RNA-dependent RNA polymerase (RdRp) 
from SARS-CoV-2 along with metabolic enzymes isocitrate dehydrogenase 1 (IDH1) 
and fumarate hydratase (FH) implicated in cancers. Using the previously 
developed structure-based statistical mechanical model of allostery (SBSMMA), we 
share our experience in analyzing the allosteric signaling, predicting latent 
allosteric sites, inducing and tuning targeted allosteric response, and 
exploring the allosteric effects of mutations. This, yet incomplete list of 
phenomenology, forms a complex and unique allosteric territory of protein 
function, which should be thoroughly explored. We propose a generic 
computational framework, which not only allows one to obtain a comprehensive 
allosteric control over proteins but also provides an opportunity to approach 
the fragment-based design of allosteric effectors and drug candidates. The 
advantages of allosteric drugs over traditional orthosteric compounds, 
complemented by the emerging role of the allosteric effects of mutations in the 
expansion of the cancer mutational landscape and in the increased mutability of 
viral proteins, leave no choice besides further extensive studies of allosteric 
mechanisms and their biomedical implications.