Clinical attrition of drug candidates is frequently driven by unforeseen safety liabilities, which are often associated with off-target pharmacological interactions.
The Adenosine A2A Receptor (A2AR) was selected as a representative GPCR to establish an integrated fragment‑based discovery workflow capable of screening fragments on the active receptor state.
We present integrated capabilities for SH2 domain-focused drug discovery, emphasizing STAT protein binding affinity and targeted protein degradation (TPD).
Obesity is a chronic, multifactorial disease projected to affect over 50% of the global population by 2035.
WEE1 is a key regulator of the G2/M cell cycle checkpoint, inhibiting CDK1 to allow DNA repair before mitosis.
Per- and polyfluoroalkyl substances (PFAS) are persistent environmental contaminants posing significant health risks, including endocrine disruption, hepatotoxicity, immuno-toxicity, and developmental effects.
Secondary pharmacology data plays a critical role in new drug applications by characterizing the selectivity profiles of clinical candidates and identifying off-target molecular interactions.
Clinical attrition of drug candidates is frequently driven by unforeseen safety liabilities, which are often associated with off-target pharmacological interactions.
Learn about GPCR families and their targets. Discover target-specific coupling status and GPCR phylogenetic relationships. Review the available cell-based assay covering >90% of the GPCRome for: cAMP and calcium detection, β-Arrestin recruitment, ligand binding, GTPγS activation, pharmacochaperone discovery, and receptor internalization.
There are numerous drugs withdrawn from the market, assigned warnings or halted in development due to observations of idiosyncratic adverse drug reactions (IADRs).
Cytochrome P450 (CYP) enzymes play a central role in the metabolism of many therapeutic agents.
Across biopharma, the pursuit and exploration of molecular glues continues unabated due their potential to transform our ability to modulate disease-relevant proteins.