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Glutathione (CID 124886) - Compound BioActivity Data
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BioActivity Outcomes:
Active(29)
 
 
Inactive(116)
 
 
Inconclusive(26)
 
 
Unspecified(72)
 
 
Top Targets:
LYZ1(8)
 
 
NR LBD PPAR(8)
 
 
NR LBD AR(7)
 
 
NR LBD ER(7)
 
 
ABCC MRP doma..(6)
 
 
BioAssay Types:
Literature(88)
 
 
 
 
 
Confirmatory(70)
 
 
 
Summary(24)
 
 
Screening(6)
 
 
BioActivity Types:
Potency(88)
 
 
 
Kd(12)
 
 
IC50(4)
 
 
 
Data download

Chemical Probe    Active    Inactive    Inconclusive    Unspecified   

Total Bioassays: 229    Data Row: 243   Total Pages: 13   Display: Page     
Sort: [Click the result table header to sort]
#SubstanceActivityBioAssayTargetLinks
OutcomeTypeValue [μM]
1
[SID103569245]
IC50 0.02Affinity towards recombinant Glutathione S-transferase (GST) Enzyme. [AID75134, Type: Literature]
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2
[SID46392774]
Kd 3Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain A, 28kda Glutathione S-Transferase From Schistosoma Haematobium [gi:34810137]
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3
[SID46392774]
Kd 3Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain B, 28kda Glutathione S-Transferase From Schistosoma Haematobium [gi:34810138]
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4
[SID46392775]
Kd 3Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain A, 28kda Glutathione S-transferase From Schistosoma Haematobium (glutathione Saturated) [gi:34810139]
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5
[SID46392775]
Kd 3Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain B, 28kda Glutathione S-transferase From Schistosoma Haematobium (glutathione Saturated) [gi:34810140]
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6
[SID46393050]
Kd 90Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain A, Crystal Structure Of Mitochondrial Class Kappa Glutathione Transferase [gi:42543493]
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7
[SID46393050]
Kd 90Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain A, Crystal Structure Of Mitochondrial Class Kappa Glutathione Transferase [gi:42543493]
View
8
[SID46393050]
Kd 90Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain B, Crystal Structure Of Mitochondrial Class Kappa Glutathione Transferase [gi:42543494]
View
9
[SID46393050]
Kd 90Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain B, Crystal Structure Of Mitochondrial Class Kappa Glutathione Transferase [gi:42543494]
View
10
[SID46392415]
Kd 668Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain A, Crystal Structure Of A Recombinant Glutathione Transferase, Created By Replacing The Last Seven Residues Of Each Subunit Of The Human Class Pi Isoenzyme With The Additional C-Terminal Helix Of Human Class Alpha Isoenzyme [gi:20664358]
View
11
[SID46392415]
Kd 668Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain A, Crystal Structure Of A Recombinant Glutathione Transferase, Created By Replacing The Last Seven Residues Of Each Subunit Of The Human Class Pi Isoenzyme With The Additional C-Terminal Helix Of Human Class Alpha Isoenzyme [gi:20664358]
View
12
[SID46392415]
Kd 668Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain B, Crystal Structure Of A Recombinant Glutathione Transferase, Created By Replacing The Last Seven Residues Of Each Subunit Of The Human Class Pi Isoenzyme With The Additional C-Terminal Helix Of Human Class Alpha Isoenzyme [gi:20664359]
View
13
[SID46392415]
Kd 668Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain B, Crystal Structure Of A Recombinant Glutathione Transferase, Created By Replacing The Last Seven Residues Of Each Subunit Of The Human Class Pi Isoenzyme With The Additional C-Terminal Helix Of Human Class Alpha Isoenzyme [gi:20664359]
View
14
[SID46392775]
Experimentally measured binding affinity data derived from PDB [AID1811, Type: other]Chain A, 28kda Glutathione S-transferase From Schistosoma Haematobium (glutathione Saturated) [gi:34810139]
View
15
[SID46392415]
Experimentally measured binding affinity data derived from PDB [AID1811, Type: Literature]Chain A, Crystal Structure Of A Recombinant Glutathione Transferase, Created By Replacing The Last Seven Residues Of Each Subunit Of The Human Class Pi Isoenzyme With The Additional C-Terminal Helix Of Human Class Alpha Isoenzyme [gi:20664358]
View
16
[SID46392774]
Experimentally measured binding affinity data derived from PDB [AID1811, Type: other]Chain A, 28kda Glutathione S-Transferase From Schistosoma Haematobium [gi:34810137]
View
17
[SID46393050]
Experimentally measured binding affinity data derived from PDB [AID1811, Type: Literature]Chain A, Crystal Structure Of Mitochondrial Class Kappa Glutathione Transferase [gi:42543493]
View
18
[SID103569245]
Effect on CU2+-mediated superoxide-dependent cytochrome c reduction at 10 to 30 uM [AID390220, Type: Literature]
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19
[SID103569245]
Effect on CU2+-mediated superoxide-dependent cytochrome c reduction at 10 uM preincubated for 30 mins in presence of superoxide dismutase [AID390221, Type: Literature]
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20
[SID103569245]
Effect on CU2+-mediated superoxide-dependent lucigenin reduction by chemiluminescence assay at 10 to 30 uM [AID390222, Type: Literature]
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