Found 1536 with Last Name = 'toure' and Initial = 'b' 
Affinity DataIC50: 1nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
TargetDual specificity mitogen-activated protein kinase kinase 1/2(Homo sapiens (Human))
TBA
Curated by ChEMBL
TBA
Curated by ChEMBL
Affinity DataIC50: <1nMAssay Description:Inhibition of MEK in human KYSE-520 cells assessed as reduction in p-ERK levelsMore data for this Ligand-Target Pair
3D Structure (crystal)
Affinity DataIC50: 2.5nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 3nMAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 3nMT: 2°CAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 3nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 4nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 4nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 4nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 4nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 4nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 5nMAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 5nMT: 2°CAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 5nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 5nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 6nMAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 6nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 6nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 6nMT: 2°CAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 6nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 6nMT: 2°CAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 6nMAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 7nMAssay Description:Allosteric inhibition of 6x-histidine tagged human SHP2 (Met1-L525 residues) expressed in Escherichia coli BL21 Star (DE3) using IRS1_pY1172(dPEG8)pY...More data for this Ligand-Target Pair
Affinity DataIC50: 7nMAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 7nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 7nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 7nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 7nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 7nMT: 2°CAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 7nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 7.5nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 7.5nMpH: 7.5 T: 2°CAssay Description:The IDH1 (R132H) mutant catalyzes the reduced form of NADP+ (NADPH) and α-ketoglutarate (α-KG) to form nicotinamide adenine dinucleotide ph...More data for this Ligand-Target Pair
Affinity DataIC50: 7.86nMpH: 7.5 T: 2°CAssay Description:The IDH1 (R132H) mutant catalyzes the reduced form of NADP+ (NADPH) and α-ketoglutarate (α-KG) to form nicotinamide adenine dinucleotide ph...More data for this Ligand-Target Pair
Affinity DataIC50: 8nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 8nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 8nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 8.12nMpH: 7.5 T: 2°CAssay Description:The IDH1 (R132H) mutant catalyzes the reduced form of NADP+ (NADPH) and α-ketoglutarate (α-KG) to form nicotinamide adenine dinucleotide ph...More data for this Ligand-Target Pair
Affinity DataIC50: 8.35nMpH: 7.5 T: 2°CAssay Description:The IDH1 (R132H) mutant catalyzes the reduced form of NADP+ (NADPH) and α-ketoglutarate (α-KG) to form nicotinamide adenine dinucleotide ph...More data for this Ligand-Target Pair
Affinity DataIC50: <8.60nMT: 2°CAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: <8.60nMAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 9nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 9nMT: 2°CAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 9nMT: 2°CAssay Description:The autoparsylation activity of the TNKS 1/2 or PARP1/2 enzymes was measured by the liquid chromatography-mass spectrometry (LC/MS) detection of nico...More data for this Ligand-Target Pair
Affinity DataIC50: 9nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 9nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 9nMAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 9.30nMAssay Description:SHP2 is allosterically activated through binding of bis-tyrosyl-phorphorylated peptides to its Src Homology 2 (SH2) domains. The latter activation st...More data for this Ligand-Target Pair
Affinity DataIC50: 9.5nMT: 2°CAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 9.5nMAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
Affinity DataIC50: 9.5nMAssay Description:The human tankyrase 1 PARP catalytic domain, TNKS1P, was cloned into a pDONR221 vector using the Invitrogen Gateway Technology. This entry clone was ...More data for this Ligand-Target Pair
