Allostery, or allosteric regulation, is the phenomenon in which protein 
functional activity is altered by the binding of an effector at an allosteric 
site that is topographically distinct from the orthosteric, active site. As one 
of the most direct and efficient ways to regulate protein function, allostery 
has played a fundamental role in innumerable biological processes of all living 
organisms, including enzyme catalysis, signal transduction, cell metabolism, and 
gene transcription. It is thus considered as "the second secret of life". The 
abnormality of allosteric communication networks between allosteric and 
orthosteric sites is associated with the pathogenesis of human diseases. 
Allosteric modulators, by attaching to structurally diverse allosteric sites, 
offer the potential for differential selectivity and improved safety compared 
with orthosteric drugs that bind to conserved orthosteric sites. Harnessing 
allostery has thus been regarded as a novel strategy for drug discovery. Despite 
much progress having been made in the repertoire of allostery since the turn of 
the millennium, the identification of allosteric drugs for therapeutic targets 
and the elucidation of allosteric mechanisms still present substantial 
challenges. These challenges are derived from the difficulties in the 
identification of allosteric sites and mutations, the assessment of allosteric 
protein-modulator interactions, the screening of allosteric modulators, and the 
elucidation of allosteric mechanisms in biological systems. To address these 
issues, we have developed a panel of allosteric services for specific allosteric 
applications over the past decade, including (i) the creation of the Allosteric 
Database, with the aim of providing comprehensive allosteric information such as 
allosteric proteins, modulators, sites, pathways, etc., (ii) the construction of 
the ASBench benchmark of high-quality allosteric sites for the development of 
computational methods for predicting allosteric sites, (iii) the development of 
Allosite and AllositePro for the prediction of the location of allosteric sites 
in proteins, (iv) the development of the Alloscore scoring function for the 
evaluation of allosteric protein-modulator interactions, (v) the development of 
Allosterome for evolutionary analysis of query allosteric sites/modulators 
within the human proteome, (vi) the development of AlloDriver for the prediction 
of allosteric mutagenesis, and (vii) the development of AlloFinder for the 
virtual screening of allosteric modulators and the investigation of allosteric 
mechanisms. Importantly, we have validated computationally predicted allosteric 
sites, mutations, and modulators in the real cases of sirtuin 6, casein kinase 
2α, phosphodiesterase 10A, and signal transduction and activation of 
transcription 3. Furthermore, our developed allosteric methods have been widely 
exploited by other users around the world for allosteric research. Therefore, 
these allosteric services are expected to expedite the discovery of allosteric 
drugs and the investigation of allosteric mechanisms.