Compile Data Set for Download or QSAR
Report error Found 15 Enz. Inhib. hit(s) with all data for entry = 3315
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31274BDBM31274(Chalcone derivative, B)
Affinity DataIC50: 4.90E+4nMpH: 7.4 T: 2°CAssay Description:Interference of the p53-MDM2 binding by test compounds was measured in a 96-well polypropylene round-bottom microtiter plate (Costar, Serocluster). H...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31274BDBM31274(Chalcone derivative, B)
Affinity DataKd:  9.00E+4nMpH: 7.4 T: 2°CAssay Description:NMR measurements consisted of monitoring changes in chemical shifts and line widths of the backbone amide resonances of uniformly 15N-enriched MDM2 s...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31275BDBM31275(Chalcone derivative, B-1)
Affinity DataIC50: 1.17E+5nMpH: 7.4 T: 2°CAssay Description:Interference of the p53-MDM2 binding by test compounds was measured in a 96-well polypropylene round-bottom microtiter plate (Costar, Serocluster). H...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31275BDBM31275(Chalcone derivative, B-1)
Affinity DataKd:  1.50E+5nMpH: 7.4 T: 2°CAssay Description:NMR measurements consisted of monitoring changes in chemical shifts and line widths of the backbone amide resonances of uniformly 15N-enriched MDM2 s...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31273BDBM31273(Chalcone derivative, A)
Affinity DataIC50: 2.06E+5nMpH: 7.4 T: 2°CAssay Description:Interference of the p53-MDM2 binding by test compounds was measured in a 96-well polypropylene round-bottom microtiter plate (Costar, Serocluster). H...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31273BDBM31273(Chalcone derivative, A)
Affinity DataKd:  2.20E+5nMpH: 7.4 T: 2°CAssay Description:NMR measurements consisted of monitoring changes in chemical shifts and line widths of the backbone amide resonances of uniformly 15N-enriched MDM2 s...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31276BDBM31276(Chalcone derivative, C)
Affinity DataKd:  2.44E+5nMpH: 7.4 T: 2°CAssay Description:NMR measurements consisted of monitoring changes in chemical shifts and line widths of the backbone amide resonances of uniformly 15N-enriched MDM2 s...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31282BDBM31282(Chalcone derivative, L)
Affinity DataKd:  2.50E+5nMpH: 7.4 T: 2°CAssay Description:NMR measurements consisted of monitoring changes in chemical shifts and line widths of the backbone amide resonances of uniformly 15N-enriched MDM2 s...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31276BDBM31276(Chalcone derivative, C)
Affinity DataIC50: 2.50E+5nMpH: 7.4 T: 2°CAssay Description:Interference of the p53-MDM2 binding by test compounds was measured in a 96-well polypropylene round-bottom microtiter plate (Costar, Serocluster). H...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31277BDBM31277(Chalcone derivative, D)
Affinity DataIC50: 2.50E+5nMpH: 7.4 T: 2°CAssay Description:Interference of the p53-MDM2 binding by test compounds was measured in a 96-well polypropylene round-bottom microtiter plate (Costar, Serocluster). H...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31278BDBM31278(Chalcone derivative, E)
Affinity DataIC50: 2.50E+5nMpH: 7.4 T: 2°CAssay Description:Interference of the p53-MDM2 binding by test compounds was measured in a 96-well polypropylene round-bottom microtiter plate (Costar, Serocluster). H...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31279BDBM31279(Chalcone derivative, F)
Affinity DataIC50: 2.50E+5nMpH: 7.4 T: 2°CAssay Description:Interference of the p53-MDM2 binding by test compounds was measured in a 96-well polypropylene round-bottom microtiter plate (Costar, Serocluster). H...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31280BDBM31280(Chalcone derivative, G)
Affinity DataIC50: 2.50E+5nMpH: 7.4 T: 2°CAssay Description:Interference of the p53-MDM2 binding by test compounds was measured in a 96-well polypropylene round-bottom microtiter plate (Costar, Serocluster). H...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31281BDBM31281(Chalcone derivative, H)
Affinity DataIC50: 2.50E+5nMpH: 7.4 T: 2°CAssay Description:Interference of the p53-MDM2 binding by test compounds was measured in a 96-well polypropylene round-bottom microtiter plate (Costar, Serocluster). H...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed
TargetE3 ubiquitin-protein ligase Mdm2(Human)
Max Planck Institute

LigandChemical structure of BindingDB Monomer ID 31283BDBM31283(Chalcone derivative, N)
Affinity DataKd:  2.70E+5nMpH: 7.4 T: 2°CAssay Description:NMR measurements consisted of monitoring changes in chemical shifts and line widths of the backbone amide resonances of uniformly 15N-enriched MDM2 s...More data for this Ligand-Target Pair
In Depth
Date in BDB:
8/17/2009
Entry Details Article
PubMed