RESOURCES

Drug-induced Liver Injury (DILI) remains a major obstacle in drug development. Despite the use of various models, DILI continues to lead to drug attrition, post-market withdrawals, and safety warnings. Recent advancements in 3D culture of PHHs as spheroids have shown promise in overcoming these limitations.

Secondary pharmacology screening data are typically included in investigational new drug applications to define clinical candidates’ selectivity profiles and assess off-target activity risks.

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A novel affinity-based screening approach using the Spectral Shift (SpS) technology was developed at Eurofins Discovery for hit finding programs. In the context of kinase drug discovery, conventional approaches focus on activity-based assays targeting the ATP site. Using this direct biophysical measurement, we can identify allosteric binders that would be missed during conventional HTS.

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STAT (signal transducer and activator of transcription) proteins were identified as transcription factors that play a critical role in extracellular signal transduction, in blood and immune cell development and function and in inflammation.

Helicases are specialized enzymes, essential for unwinding DNA-DNA or RNA-DNA duplexes and required for genome maintenance and cellular homeostasis.

SH2 domains are an emerging target class for the development of small molecules which disrupt protein-protein interactions, as well as for the development of targeted protein degraders. We present screening validation data against a panel of 95 wild type and 7 mutant SH2 domain assays for a collection of reported small molecules and peptides which bind to this protein-protein interaction module.

Eurofins Discovery introduces a novel SH2scan^™️ platform, comprised of 102 assays that utilize our well-known competition binding assay technology, for selectivity profiling of SH2 domain-containing targets.

Helicases are specialized enzymes, critical for many vital cellular processes including duplication of genetic information, DNA repair as well as translation.