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BioAssay: AID 625124

Binding constant for RET(V804M) kinase domain

We tested the interaction of 72 kinase inhibitors with 442 kinases covering >80% of the human catalytic protein kinome. Our data show that, as a class, type II inhibitors are more selective than type I inhibitors, but that there are important exceptions to this trend. The data further illustrate that selective inhibitors have been developed against the majority of kinases targeted by the more ..
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 Tested Compounds
 Tested Compounds
All(72)
 
 
Active(29)
 
 
Unspecified(43)
 
 
 Tested Substances
 Tested Substances
All(72)
 
 
Active(29)
 
 
Unspecified(43)
 
 
 Related BioAssays
 Related BioAssays
AID: 625124
Data Source: ChEMBL (774604)
BioAssay Type: Confirmatory, Concentration-Response Relationship Observed
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2012-09-09
Modify Date: 2014-12-06

Data Table ( Complete ):           View Active Data    View All Data
Target
Sequence: RecName: Full=Proto-oncogene tyrosine-protein kinase receptor Ret; AltName: Full=Cadherin family member 12; AltName: Full=Proto-oncogene c-Ret; Contains: RecName: Full=Soluble RET kinase fragment; Contains: RecName: Full=Extracellular cell-membrane anchored RET cadherin 120 kDa fragment; Flags: Precursor
Description ..   
Protein Family: Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein
Comment ..   

Gene:RET     Related Protein 3D Structures     More BioActivity Data..
BioActive Compounds: 29
Description:
Title: Comprehensive analysis of kinase inhibitor selectivity.

Abstract: We tested the interaction of 72 kinase inhibitors with 442 kinases covering >80% of the human catalytic protein kinome. Our data show that, as a class, type II inhibitors are more selective than type I inhibitors, but that there are important exceptions to this trend. The data further illustrate that selective inhibitors have been developed against the majority of kinases targeted by the compounds tested. Analysis of the interaction patterns reveals a class of 'group-selective' inhibitors broadly active against a single subfamily of kinases, but selective outside that subfamily. The data set suggests compounds to use as tools to study kinases for which no dedicated inhibitors exist. It also provides a foundation for further exploring kinase inhibitor biology and toxicity, as well as for studying the structural basis of the observed interaction patterns. Our findings will help to realize the direct enabling potential of genomics for drug development and basic research about cellular signaling.
(PMID: 22037378)
Comment
Compounds with activity <= 50uM or explicitly reported as active by ChEMBL are flagged as active in this PubChem assay presentation.
Categorized Comment - additional comments and annotations
From BioAssay Depositor:
Assay Type: Binding
Target Type: Target is a single protein chain
Assay Data Source: Scientific Literature
Assay Test Type: In vitro
Result Definitions
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TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Kd*Kd PubChem standard valueFloatμM
3BEIBinding Efficiency Index(nM)Float
2SEISurface Efficiency Index(nM)Float
4LELigand EfficiencyFloat
5LLELipophilic Ligand EfficiencyFloat
6Kd activity commentKd activity commentString
7Kd standard flagKd standard flagInteger
8Kd qualifierKd qualifierString
9Kd published valueKd published valueFloatnM
10Kd standard valueKd standard valueFloatnM
11Kd binding domainsKd binding domainsString

* Activity Concentration.

Data Table (Concise)
Data Table ( Complete ):     View Active Data    View All Data
Classification
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