Despite their potential significance in disease processes, dark kinases remain largely unexplored due to limited functional annotations and a lack of molecular probes. To bridge this gap in kinase-focused drug discovery, our cheminformatics team has developed the Dark Kinome Screening Library - a carefully designed selection of over 1,400 drug-like screening compounds to target understudied kinases. Developed using advanced cheminformatics and data-driven approaches, this specialized Screening Set will effectively support high-throughput screening (HTS) projects in drug discovery and provide a valuable tool to investigate the roles of dark kinases in cellular signaling, oncology, immunology, and other therapeutic areas where kinase dysregulation is a key factor.
The compound selection can be customized based on your requirements. Cherry-picking is available.
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Representative screening compounds from the Dark Kinome Screening Library
Key Features:
- The reference set was created using the ChEMBL and PubChem databases. Machine learning algorithms combined with extensive knowledge were sourced from open-access and commercial databases, including PubChem, ChEMBL, Google Patents, SciFinder, and others.
- A 2D fingerprint similarity search applied to our proprietary HTS Compound Collection resulted in over 1,400 screening compounds selected to target key kinases involved in cancer and inflammation.
- Each compound entry includes information on its closest homolog and highest activity, derived from the ChEMBL and PubChem databases.
Kinase Modulators Included in the Library
- BR serine/threonine-protein kinase 2
- Casein kinase 2
- Casein kinase I gamma 1
- Casein kinase II alpha (prime)
- Cyclin-dependent kinase 10
- Dual specificity protein kinase CLK4
- Dual specificity tyrosine-phosphorylation-regulated kinase 4
- Dual-specificity tyrosine-phosphorylation regulated kinase 2
- Homeodomain-interacting protein kinase 4
- Leukocyte tyrosine kinase receptor
- MAP kinase signal-integrating kinase 2
- MAP kinase-interacting serine/threonine-protein kinase MNK1
- Mitogen-activated protein kinase kinase kinase 10
- NUAK family SNF1-like kinase 2
- Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing beta polypeptide
- Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit gamma
- Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit gamma
- Phosphorylase kinase gamma subunit 1
- Phosphorylase kinase gamma subunit 2
- Protein kinase C theta
- Serine/threonine-protein kinase 17A
- Serine/threonine-protein kinase 33
- Serine/threonine-protein kinase c-TAK1
- Serine/threonine-protein kinase EEF2K
- Serine/threonine-protein kinase MARK1
- Serine/threonine-protein kinase NEK6
- Serine/threonine-protein kinase PAK 3
- Serine/threonine-protein kinase TAO1
- Serine/threonine-protein kinase VRK2
Background Information
The human kinome, encompassing over 500 protein and lipid kinases, plays a pivotal role in cellular signaling and regulation. Kinase dysfunction is a known contributor to the development of numerous diseases, including cancer, infectious diseases, and immune disorders. Despite their recognized significance and inherent druggability by allosteric and competitive inhibitors, approximately one-third of kinases remain poorly studied [1]. These understudied kinases, often referred to as "dark kinases," represent an untapped resource for therapeutic development.
Among them, according to the U.S. National Institutes of Health (NIH), there are 162 human protein kinases characterized by limited functional annotations and insufficiency of high-quality molecular probes to facilitate their study. These kinases are underrepresented in functional studies and signaling networks, leaving significant gaps in our understanding of their roles in physiology and disease. Obviously, tackling this problem is to provide immense potential for drug discovery efforts targeting these promising yet overlooked therapeutic candidates [2].
Reference:
- Gomez, Shawn M et al. “Illuminating function of the understudied druggable kinome.” Drug discovery today vol. 29,3 (2024): 103881. doi:10.1016/j.drudis.2024.103881
- Axtman, Alison D. “Characterizing the role of the dark kinome in neurodegenerative disease - A mini review.” Biochimica et biophysica acta. General subjects vol. 1865,12 (2021): 130014. doi:10.1016/j.bbagen.2021.130014