ChEMBL ligand: CHEMBL2012582
bromodomain containing 4/Bromodomain-containing protein 4 in Human [ChEMBL: CHEMBL1163125] [GtoPdb: 1945] [UniProtKB: O60885] There should be some charts here, you may need to enable JavaScript!
bromodomain testis associated/Bromodomain testis-specific protein in Human [ChEMBL: CHEMBL1795185] [GtoPdb: 2729] [UniProtKB: Q58F21] There should be some charts here, you may need to enable JavaScript!
leucine rich repeat kinase 2/Leucine-rich repeat serine/threonine-protein kinase 2 in Human [ChEMBL: CHEMBL1075104] [GtoPdb: 2059] [UniProtKB: Q5S007] There should be some charts here, you may need to enable JavaScript!

DB	Assay description	Assay Type	Standard value	Standard parameter	Original value	Original units	Original parameter	Reference
bromodomain containing 4/Bromodomain-containing protein 4 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1163125] [GtoPdb: 1945] [UniProtKB: O60885]
ChEMBL	Binding affinity to recombinant human N-terminal hexaHis-tagged BRD4 expressed in Escherichia coli BL21 (DE3) cells by ITC analysis	B	6.71	pKd	194	nM	Kd	J Med Chem (2021) 64: 15772-15786 [PMID:34710325]
ChEMBL	Binding affinity to recombinant human N-terminal hexaHis-tagged BRD4 expressed in Escherichia coli BL21 (DE3) cells by MST assay	B	7.16	pKd	69	nM	Kd	J Med Chem (2021) 64: 15772-15786 [PMID:34710325]
ChEMBL	Binding affinity to recombinant human N-terminal hexaHis-tagged BRD4 expressed in Escherichia coli BL21 (DE3) cells by qPCR assay	B	7.18	pKd	66	nM	Kd	J Med Chem (2021) 64: 15772-15786 [PMID:34710325]
bromodomain testis associated/Bromodomain testis-specific protein in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1795185] [GtoPdb: 2729] [UniProtKB: Q58F21]
ChEMBL	Binding affinity to recombinant human N-terminal hexaHis-tagged BRDT expressed in Escherichia coli BL21 (DE3) cells by ITC analysis	B	5.77	pKd	1700	nM	Kd	J Med Chem (2021) 64: 15772-15786 [PMID:34710325]
ChEMBL	Binding affinity to recombinant human N-terminal hexaHis-tagged BRDT expressed in Escherichia coli BL21 (DE3) cells by MST assay	B	6.15	pKd	700	nM	Kd	J Med Chem (2021) 64: 15772-15786 [PMID:34710325]
ChEMBL	Binding affinity to recombinant human N-terminal hexaHis-tagged BRDT expressed in Escherichia coli BL21 (DE3) cells by qPCR assay	B	6.41	pKd	390	nM	Kd	J Med Chem (2021) 64: 15772-15786 [PMID:34710325]
leucine rich repeat kinase 2/Leucine-rich repeat serine/threonine-protein kinase 2 in Human (target type: SINGLE PROTEIN) [ChEMBL: CHEMBL1075104] [GtoPdb: 2059] [UniProtKB: Q5S007]
GtoPdb	Biochemical assay dissociation constant.	-	8.22	pKi	6	nM	Ki	Bioorg Med Chem Lett (2013) 23: 3690-6 [PMID:23721803]
ChEMBL	Inhibition of GST-tagged LRRK2 (1326 to 2527 amino acids) G2019S mutant (unknown origin)	B	8.22	pKi	6	nM	Ki	Bioorg Med Chem Lett (2013) 23: 3690-3696 [PMID:23721803]
ChEMBL	Inhibition of LRRK2 G2019S and A2016T mutant expressed in HEK293 cells using nictide and ATP as substrate	B	5.51	pIC50	3080	nM	IC50	Bioorg Med Chem Lett (2012) 22: 1864-1869 [PMID:22335897]
ChEMBL	Enzyme Assay: Active GST-LRRK2 (1326-2527), GST-LRRK2[G2019S] (1326-2527), GST-LRRK2[A2016T] (1326-2527) and GST-LRRK2[A2016T+G2019S] (1326-2527) enzyme was purified with glutathione sepharose from HEK293 cell lysate 36 h following transient transfection of the appropriate cDNA constructs. Peptide kinase assays, performed in triplicate, were set up in a total volume of 40 μl containing 0.5 μg LRRK2 kinase (which at approximately 10% purity gives a final concentration of 8 nM) in 50 mM Tris/HCl, pH 7.5, 0.1 mM EGTA, 10 mM MgCl2, 20 μM Nictide, 0.1 μM [γ-32P]ATP (˜500 cpm/pmol) and the indicated concentrations of inhibitor dissolved in DMSO. After incubation for 15 min at 30° C., reactions were terminated by spotting 35 μl of the reaction mix onto P81 phosphocellulose paper and immersion in 50 mM phosphoric acid. Samples were washed extensively and the incorporation of [γ-32P]ATP into Nictide was quantified by Cerenkov counting. IC50 values were calculated with GraphPad Prism using non-linear regression analysis.	B	5.51	pIC50	3080	nM	IC50	US-10913744-B2. LRRK2 inhibitors and methods of making and using the same (2021)
ChEMBL	Inhibition of LRRK2 A2016T mutant expressed in HEK293 cells using nictide and ATP as substrate	B	5.61	pIC50	2450	nM	IC50	Bioorg Med Chem Lett (2012) 22: 1864-1869 [PMID:22335897]
ChEMBL	Enzyme Assay: Active GST-LRRK2 (1326-2527), GST-LRRK2[G2019S] (1326-2527), GST-LRRK2[A2016T] (1326-2527) and GST-LRRK2[A2016T+G2019S] (1326-2527) enzyme was purified with glutathione sepharose from HEK293 cell lysate 36 h following transient transfection of the appropriate cDNA constructs. Peptide kinase assays, performed in triplicate, were set up in a total volume of 40 μl containing 0.5 μg LRRK2 kinase (which at approximately 10% purity gives a final concentration of 8 nM) in 50 mM Tris/HCl, pH 7.5, 0.1 mM EGTA, 10 mM MgCl2, 20 μM Nictide, 0.1 μM [γ-32P]ATP (˜500 cpm/pmol) and the indicated concentrations of inhibitor dissolved in DMSO. After incubation for 15 min at 30° C., reactions were terminated by spotting 35 μl of the reaction mix onto P81 phosphocellulose paper and immersion in 50 mM phosphoric acid. Samples were washed extensively and the incorporation of [γ-32P]ATP into Nictide was quantified by Cerenkov counting. IC50 values were calculated with GraphPad Prism using non-linear regression analysis.	B	5.61	pIC50	2450	nM	IC50	US-10913744-B2. LRRK2 inhibitors and methods of making and using the same (2021)
ChEMBL	Inhibition of recombinant catalytic human GST-tagged LLRK2 G2019S mutant (970 to 2527 residues) expressed in baculovirus expression system using LRRKtide as substrate after 1 hr by alexaFluor-ADP-based FRET assay	B	7.7	pIC50	20	nM	IC50	Eur J Med Chem (2017) 138: 328-342 [PMID:28688273]
ChEMBL	Inhibition of recombinant catalytic human GST-tagged LLRK2 (970 to 2527 residues) expressed in baculovirus expression system using LRRKtide as substrate after 1 hr by alexaFluor-ADP-based FRET assay	B	7.7	pIC50	20	nM	IC50	Eur J Med Chem (2017) 138: 328-342 [PMID:28688273]
ChEMBL	Inhibition of wild-type LRRK2 expressed in HEK293 cells using nictide and [gamma32]ATP as substrate	B	7.89	pIC50	13	nM	IC50	Bioorg Med Chem Lett (2012) 22: 1864-1869 [PMID:22335897]
ChEMBL	Inhibition of wild type GST-tagged LRRK2 ((1326 to 2517 amino acids) (unknown origin)	B	7.89	pIC50	13	nM	IC50	Bioorg Med Chem Lett (2013) 23: 3690-3696 [PMID:23721803]
ChEMBL	Inhibition of wild-type GST-tagged LRRK2 (1326 to 2527 aa)(unknown origin) stably expressed in HEK293 cell lysate using [gamma-32P] after 15 mins by Cerenkov counting method	B	7.89	pIC50	13	nM	IC50	Eur J Med Chem (2015) 95: 29-34 [PMID:25791676]
ChEMBL	Inhibition of LRRK2 (1326 to 2527 residues) in HEK293 cell lysate measured after 15 mins in presence of ATP	B	7.89	pIC50	13	nM	IC50	Eur J Med Chem (2023) 256: 115475-115475 [PMID:37201428]
ChEMBL	Enzyme Assay: Active GST-LRRK2 (1326-2527), GST-LRRK2[G2019S] (1326-2527), GST-LRRK2[A2016T] (1326-2527) and GST-LRRK2[A2016T+G2019S] (1326-2527) enzyme was purified with glutathione sepharose from HEK293 cell lysate 36 h following transient transfection of the appropriate cDNA constructs. Peptide kinase assays, performed in triplicate, were set up in a total volume of 40 μl containing 0.5 μg LRRK2 kinase (which at approximately 10% purity gives a final concentration of 8 nM) in 50 mM Tris/HCl, pH 7.5, 0.1 mM EGTA, 10 mM MgCl2, 20 μM Nictide, 0.1 μM [γ-32P]ATP (˜500 cpm/pmol) and the indicated concentrations of inhibitor dissolved in DMSO. After incubation for 15 min at 30° C., reactions were terminated by spotting 35 μl of the reaction mix onto P81 phosphocellulose paper and immersion in 50 mM phosphoric acid. Samples were washed extensively and the incorporation of [γ-32P]ATP into Nictide was quantified by Cerenkov counting. IC50 values were calculated with GraphPad Prism using non-linear regression analysis.	B	7.89	pIC50	13	nM	IC50	US-10913744-B2. LRRK2 inhibitors and methods of making and using the same (2021)
GtoPdb	With 0.1 mM ATP in the assay.	-	7.89	pIC50	13	nM	IC50	Nat Chem Biol (2011) 7: 203-5 [PMID:21378983]
ChEMBL	Inhibitory Effect on LRRK2: After the compound was dissolved in 100% DMSO at 10 mM, it was serially diluted to the range of 1 μM to 10 μM using biochemical LRRK2 assay buffer (50 mM HEPES (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid) pH 7.5, 10 mM MgCl2, 1 mM EGTA (1,2-bis(o-aminophenoxy)ethane-N,N,N′,N′-tetraacetic acid), 2 mM DTT (dithiothreitol), and 0.01% TWEEN-20 (Aldrich)). Purified LRRK2 (CARNA BIOSCIENCES) was added to a black U-bottom 96-well microtiter plate containing 6 μl of the serially diluted compound, followed by incubation at room temperature for 30 minutes. For the kinase reaction, ATP and a substrate solution specific urea-polypeptide (ULIGHT™-poly TK, PerkinElimer) were added. The reaction was carried out at room temperature for 1 hour, and it was detected with an detection solution (brand name: LANCE™) containing EDTA. A LANCE detection solution containing europium-labeled antibody (LRRK2 specific PT66) was added, followed by incubation at room temperature for 50 minutes, to terminate the kinase experiment. The phosphorylated substrate was detected by 665 nm emission measurement.	B	8.09	pIC50	8.2	nM	IC50	US-11370796-B2. Substituted pyrazoles as LRRK2 inhibitors (2022)
ChEMBL	Inhibition of LRRK2 G2019S mutant (1326 to 252 aa) (unknown origin) stably expressed in HEK293 cell lysate using [gamma-32P] after 15 mins by Cerenkov counting method	B	8.1	pIC50	7.9	nM	IC50	Eur J Med Chem (2015) 95: 29-34 [PMID:25791676]
ChEMBL	Inhibition of LRRK2 G2019S mutant expressed in HEK293 cells using nictide and ATP as substrate	B	8.22	pIC50	6	nM	IC50	Bioorg Med Chem Lett (2012) 22: 1864-1869 [PMID:22335897]
ChEMBL	Inhibition of LRRK2 G2019S mutant in HEK293 cell lysate measured after 15 mins in presence of ATP	B	8.22	pIC50	6	nM	IC50	Eur J Med Chem (2023) 256: 115475-115475 [PMID:37201428]
ChEMBL	Inhibition of GST-LRRK2 (1326 to 2527 residues) G2019S mutant (unknown origin) expressed in HEK293 cells incubated for 15 mins by cerenkov counting method	B	8.22	pIC50	6	nM	IC50	J Med Chem (2020) 63: 11330-11361 [PMID:32352776]
ChEMBL	Enzyme Assay: Active GST-LRRK2 (1326-2527), GST-LRRK2[G2019S] (1326-2527), GST-LRRK2[A2016T] (1326-2527) and GST-LRRK2[A2016T+G2019S] (1326-2527) enzyme was purified with glutathione sepharose from HEK293 cell lysate 36 h following transient transfection of the appropriate cDNA constructs. Peptide kinase assays, performed in triplicate, were set up in a total volume of 40 μl containing 0.5 μg LRRK2 kinase (which at approximately 10% purity gives a final concentration of 8 nM) in 50 mM Tris/HCl, pH 7.5, 0.1 mM EGTA, 10 mM MgCl2, 20 μM Nictide, 0.1 μM [γ-32P]ATP (˜500 cpm/pmol) and the indicated concentrations of inhibitor dissolved in DMSO. After incubation for 15 min at 30° C., reactions were terminated by spotting 35 μl of the reaction mix onto P81 phosphocellulose paper and immersion in 50 mM phosphoric acid. Samples were washed extensively and the incorporation of [γ-32P]ATP into Nictide was quantified by Cerenkov counting. IC50 values were calculated with GraphPad Prism using non-linear regression analysis.	B	8.22	pIC50	6	nM	IC50	US-10913744-B2. LRRK2 inhibitors and methods of making and using the same (2021)
ChEMBL	Inhibition of GST-tagged LRRK2 (1326 to 2527 amino acids) G2019S mutant (unknown origin)	B	8.22	pIC50	6	nM	IC50	Bioorg Med Chem Lett (2013) 23: 3690-3696 [PMID:23721803]
ChEMBL	Inhibition of LRRK2 (unknown origin)	B	8.22	pIC50	6	nM	IC50	J Med Chem (2015) 58: 6733-6746 [PMID:25915084]
ChEMBL	Inhibition of recombinant LRRK2 (unknown origin) using gamma-32P-ATP assessed as LRRKtide substrate phosphorylation level by autoradiography	B	8.46	pIC50	3.5	nM	IC50	Bioorg Med Chem Lett (2014) 24: 4630-4637 [PMID:25219901]

ChEMBL data shown on this page come from version 36:

Zdrazil B, Felix E, Hunter F, Manners EJ, Blackshaw J, Corbett S, de Veij M, Ioannidis H, Lopez DM, Mosquera JF, Magarinos MP, Bosc N, Arcila R, Kizilören T, Gaulton A, Bento AP, Adasme MF, Monecke P, Landrum GA, Leach AR. (2024). The ChEMBL Database in 2023: a drug discovery platform spanning multiple bioactivity data types and time periods. Nucleic Acids Res., 52(D1). DOI: 10.1093/nar/gkad1004. [EPMCID:10767899] [PMID:37933841]
Davies M, Nowotka M, Papadatos G, Dedman N, Gaulton A, Atkinson F, Bellis L, Overington JP. (2015) 'ChEMBL web services: streamlining access to drug discovery data and utilities.' Nucleic Acids Res., 43(W1). DOI: 10.1093/nar/gkv352. [EPMCID:25883136]