Bookmark and Share
BioActivity Data for Targets
Filters: All Data » Active      
Filter selected
BioActivity Outcomes:
Active(37)
 
 
BioAssay Types:
Literature(37)
 
 
BioActivity Types:
Kd(21)
 
 
IC50(1)
 
 
Substance Types:
Chemical(37)
 
 
Data download

Chemical Probe    Active    Inactive    Inconclusive    Unspecified   

Total Bioassays: 18    Data Row: 37   Total Pages: 2   Display: Page     
Sort: [Click the result table header to sort]
#StructureSubstanceCompoundActivityBioAssayLinks
OutcomeTypeValue [μM]
1
[SID103543178]
[CID23656596]
Kd 0.0002Binding affinity to transthyretin at pH 4.4 [AID303083, Type: Literature]
View
2
[SID103543176]
[CID23656595]
Kd 0.0003Binding affinity to transthyretin at pH 4.4 [AID303083, Type: Literature]
View
3
[SID103543175]
[CID23656591]
Kd 0.0057Binding affinity to transthyretin at pH 4.4 [AID303083, Type: Literature]
View
4
[SID103543174]
[CID23656594]
Kd 0.0139Binding affinity to transthyretin at pH 4.4 [AID303083, Type: Literature]
View
5
[SID103543179]
[CID23656593]
Kd 0.027Binding affinity to transthyretin at pH 4.4 [AID303083, Type: Literature]
View
6
[SID103543182]
[CID22133420]
Kd 0.027Binding affinity to transthyretin at pH 4.4 [AID303083, Type: Literature]
View
7
[SID103543183]
[CID5712018]
Kd 0.042Binding affinity to transthyretin at pH 4.4 [AID303083, Type: Literature]
View
8
[SID103543181]
[CID18433807]
Kd 0.088Binding affinity to transthyretin at pH 4.4 [AID303083, Type: Literature]
View
9
[SID170484819]
[CID5280445]
Kd 0.1Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]
View
10
[SID170484819]
[CID5280445]
Kd 0.1Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]
View
11
[SID170484819]
[CID5280445]
Kd 0.1Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]
View
12
[SID170484819]
[CID5280445]
Kd 0.1Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]
View
13
[SID103543184]
[CID659923]
Kd 0.12Binding affinity to transthyretin at pH 4.4 [AID303083, Type: Literature]
View
14
[SID103210398]
[CID1369]
Kd 1.1Binding affinity to wild type human TTR denominated hormone binding site expressed in Escherichia coli assessed as dissociation constant for first ligand binding event by isothermal direct titrimetric assay [AID456447, Type: Literature]
View
15
[SID103210398]
[CID1369]
Kd 1.1Binding affinity to wild type human TTR denominated hormone binding site expressed in Escherichia coli assessed as dissociation constant for first ligand binding event by equilibrium dialysis [AID456443, Type: Literature]
View
16
[SID103210398]
[CID1369]
Kd 1.8Binding affinity to wild type human TTR denominated hormone binding site expressed in Escherichia coli by equilibrium dialysis [AID456445, Type: Literature]
View
17
[SID103191339]
[CID3371]
IC50 2.9Inhibition of human transthyretin fibril formation at pH 4.4 after 72 hrs [AID329702, Type: Literature]
View
18
[SID103210398]
[CID1369]
Kd 4.3Binding affinity to wild type human TTR denominated hormone binding site expressed in Escherichia coli by isothermal direct titrimetric assay [AID456449, Type: Literature]
View
19
[SID103210398]
[CID1369]
Kd 4.8Binding affinity to wild type human TTR denominated hormone binding site expressed in Escherichia coli assessed as dissociation constant for second ligand binding event by equilibrium dialysis [AID456444, Type: Literature]
View
20
[SID103210398]
[CID1369]
Kd 4.8Binding affinity to wild type human TTR denominated hormone binding site expressed in Escherichia coli assessed as dissociation constant for second ligand binding event by isothermal direct titrimetric assay [AID456448, Type: Literature]
View