Species | Target name | Source | Bibliographic reference |
---|---|---|---|
Homo sapiens | ret proto-oncogene | Starlite/ChEMBL | No references |
Homo sapiens | ROS proto-oncogene 1, receptor tyrosine kinase | Starlite/ChEMBL | No references |
Homo sapiens | fms-related tyrosine kinase 3 | Starlite/ChEMBL | No references |
Homo sapiens | anaplastic lymphoma receptor tyrosine kinase | Starlite/ChEMBL | No references |
Species | Potential target | Known druggable target/s | Ortholog Group |
---|---|---|---|
Brugia malayi | Protein kinase domain containing protein | Get druggable targets OG5_132231 | All targets in OG5_132231 |
Loa Loa (eye worm) | TK protein kinase | Get druggable targets OG5_135644 | All targets in OG5_135644 |
Loa Loa (eye worm) | TK/ALK protein kinase | Get druggable targets OG5_132231 | All targets in OG5_132231 |
Echinococcus multilocularis | tyrosine protein kinase | Get druggable targets OG5_135644 | All targets in OG5_135644 |
Loa Loa (eye worm) | hypothetical protein | Get druggable targets OG5_132231 | All targets in OG5_132231 |
Loa Loa (eye worm) | hypothetical protein | Get druggable targets OG5_135644 | All targets in OG5_135644 |
Echinococcus granulosus | tyrosine protein kinase | Get druggable targets OG5_135644 | All targets in OG5_135644 |
Brugia malayi | Protein kinase domain containing protein | Get druggable targets OG5_135644 | All targets in OG5_135644 |
Species | Potential target | Raw | Global | Species |
---|---|---|---|---|
Brugia malayi | hypothetical protein | 0.0034 | 0.0352 | 0.0352 |
Schistosoma mansoni | hypothetical protein | 0.0034 | 0.0352 | 1 |
Loa Loa (eye worm) | hypothetical protein | 0.0034 | 0.0352 | 0.0352 |
Echinococcus granulosus | MAM | 0.0034 | 0.0352 | 0.0352 |
Loa Loa (eye worm) | hypothetical protein | 0.0034 | 0.0352 | 0.0352 |
Brugia malayi | Immunoglobulin I-set domain containing protein | 0.0025 | 0.0022 | 0.0022 |
Onchocerca volvulus | 0.004 | 0.0567 | 1 | |
Loa Loa (eye worm) | TK protein kinase | 0.0294 | 1 | 1 |
Loa Loa (eye worm) | hypothetical protein | 0.0288 | 0.9764 | 0.9764 |
Brugia malayi | Protein kinase domain containing protein | 0.029 | 0.9858 | 0.9858 |
Schistosoma mansoni | hypothetical protein | 0.0034 | 0.0352 | 1 |
Echinococcus multilocularis | tyrosine protein kinase | 0.0294 | 1 | 1 |
Echinococcus granulosus | tyrosine protein kinase | 0.0294 | 1 | 1 |
Loa Loa (eye worm) | TK/KIN16 protein kinase | 0.0025 | 0.0022 | 0.0022 |
Loa Loa (eye worm) | TK/ALK protein kinase | 0.029 | 0.9855 | 0.9855 |
Loa Loa (eye worm) | hypothetical protein | 0.025 | 0.8357 | 0.8357 |
Echinococcus multilocularis | MAM | 0.0034 | 0.0352 | 0.0352 |
Loa Loa (eye worm) | hypothetical protein | 0.0034 | 0.0352 | 0.0352 |
Activity type | Activity value | Assay description | Source | Reference |
---|---|---|---|---|
IC50 (binding) | = 0.51 nM | BindingDB_Patents: Inhibition Assay. A partial protein of only a kinase domain of FLT3 protein was purchased from Carna Biosciences Inc., Japan, and tests were conducted as in Test Example 5. Test Example 5: A partial protein of only a kinase domain of RET protein was purchased from Carna Biosciences Inc., Japan. The phosphorylation activity toward a peptide substrate was investigated using an EZ reader (Caliper). Test compounds were each mixed with a protein solution to give 8 final concentrations from 100 nM to 0.03 nM, followed by addition of a mixed liquid of ATP and substrate peptide (Caliper) and reaction for 30 minutes. The ATP concentration used was 100 µM. A reaction liquid which contained protein but no test compound (in which the solvent DMSO alone was added at 0.8% in place of the test compound) was prepared, followed by reaction in the same manner with or without ATP addition. | ChEMBL. | No reference |
IC50 (binding) | = 0.51 nM | BindingDB_Patents: Inhibition Assay. A partial protein of only a kinase domain of FLT3 protein was purchased from Carna Biosciences Inc., Japan, and tests were conducted as in Test Example 5. Test Example 5: A partial protein of only a kinase domain of RET protein was purchased from Carna Biosciences Inc., Japan. The phosphorylation activity toward a peptide substrate was investigated using an EZ reader (Caliper). Test compounds were each mixed with a protein solution to give 8 final concentrations from 100 nM to 0.03 nM, followed by addition of a mixed liquid of ATP and substrate peptide (Caliper) and reaction for 30 minutes. The ATP concentration used was 100 µM. A reaction liquid which contained protein but no test compound (in which the solvent DMSO alone was added at 0.8% in place of the test compound) was prepared, followed by reaction in the same manner with or without ATP addition. | ChEMBL. | No reference |
IC50 (binding) | = 0.86 nM | BindingDB_Patents: Inhibition Assay. A partial protein of only a kinase domain of ROS protein was purchased from Carna Biosciences Inc., Japan, and tests were conducted as in Test Example 5, except that the ATP concentration in the mixed solution of ATP and substrate peptide (Caliper) was 50 uM. Test Example 5: A partial protein of only a kinase domain of RET protein was purchased from Carna Biosciences Inc., Japan. The phosphorylation activity toward a peptide substrate was investigated using an EZ reader (Caliper). Test compounds were each mixed with a protein solution to give 8 final concentrations from 100 nM to 0.03 nM, followed by addition of a mixed liquid of ATP and substrate peptide (Caliper) and reaction for 30 minutes. The ATP concentration used was 100 µM. A reaction liquid which contained protein but no test compound (in which the solvent DMSO alone was added at 0.8% in place of the test compound) was prepared, followed by reaction in the same manner with or without ATP addition. | ChEMBL. | No reference |
IC50 (binding) | = 0.95 nM | BindingDB_Patents: Inhibition Assay. A partial protein of only a kinase domain of RET protein was purchased from Carna Biosciences Inc., Japan. The phosphorylation activity toward a peptide substrate was investigated using an EZ reader (Caliper). Test compounds were each mixed with a protein solution to give 8 final concentrations from 100 nM to 0.03 nM, followed by addition of a mixed liquid of ATP and substrate peptide (Caliper) and reaction for 30 minutes. The ATP concentration used was 100 µM. A reaction liquid which contained protein but no test compound (in which the solvent DMSO alone was added at 0.8% in place of the test compound) was prepared, followed by reaction in the same manner with or without ATP addition. In the absence of the test compound, the phosphorylation peptide peak without ATP addition and with ATP addition was assumed to be 100% inhibition and 0% inhibition, respectively. | ChEMBL. | No reference |
IC50 (binding) | = 0.95 nM | BindingDB_Patents: Inhibition Assay. A partial protein of only a kinase domain of RET protein was purchased from Carna Biosciences Inc., Japan. The phosphorylation activity toward a peptide substrate was investigated using an EZ reader (Caliper). Test compounds were each mixed with a protein solution to give 8 final concentrations from 100 nM to 0.03 nM, followed by addition of a mixed liquid of ATP and substrate peptide (Caliper) and reaction for 30 minutes. The ATP concentration used was 100 µM. A reaction liquid which contained protein but no test compound (in which the solvent DMSO alone was added at 0.8% in place of the test compound) was prepared, followed by reaction in the same manner with or without ATP addition. In the absence of the test compound, the phosphorylation peptide peak without ATP addition and with ATP addition was assumed to be 100% inhibition and 0% inhibition, respectively. | ChEMBL. | No reference |
IC50 (binding) | = 2.8 nM | BindingDB_Patents: Inhibition Assay. A recombinant retrovirus was created from expression plasmid FLAG-EML4-ALKv1/pMX-iresCD8 in which cDNA for EMLA-ALK fusion protein v1 was integrated, and injected into mouse lymphoid cell line BA/F3 cells. Using a magnetic bead reagent for cell separation and a purification column (anti-CD8 monoclonal antibody immobilized on magnetic beads and a MiniMACS purification column; both are products of MilteDyi Biotec Inc.), cell surface CD8-expressing cells were purified to establish EML4-ALK fusion protein v1-expressing BA/F3 cells. From the cells, EML4-ALK fusion protein v1 was purified and subjected to kinase activity evaluation. EML4-ALK fusion protein v1 was investigated for its phosphorylation activity toward a peptide substrate by using a kinase activity detection kit (HTRF KinEASE-TK; Cisbio Inc.). Test compounds were each added to a reaction solution containing the enzyme protein to give 8 final concentrations from 1000 nM to 0.3 nM, followed by addition of ATP. | ChEMBL. | No reference |
Many chemical entities in TDR Targets come from high-throughput screenings with whole cells or tissue samples, and not all assayed compounds have been tested against a single a single target protein, probably because they get ruled out during screening process. Even if these compounds may have not been of interest in the original screening, they may come as interesting leads for other screening assays. Furthermore, we may be able to propose drug-target associations using chemical similarities and network patterns.