Bookmark and Share
BioAssay: AID 370880

Inhibition of human recombinant PILS-AP at 200 uM by HxBPyne probe-based competitive activity based protein profiling assay in presence of 5 uM HxBpane competitor

High-throughput screening (HTS) has become an integral part of academic and industrial efforts aimed at developing new chemical probes and drugs. These screens typically generate several 'hits', or lead active compounds, that must be prioritized for follow-up medicinal chemistry studies. Among primary considerations for ranking lead compounds is selectivity for the intended target, especially more ..
_
   
 Tested Compounds
 Tested Compounds
All(2)
 
 
Inactive(2)
 
 
 Tested Substances
 Tested Substances
All(2)
 
 
Inactive(2)
 
 
 Related BioAssays
 Related BioAssays
AID: 370880
Data Source: ChEMBL (518909)
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2010-05-26
Modify Date: 2013-11-21

Data Table ( Complete ):           All
Target
Sequence: RecName: Full=Endoplasmic reticulum aminopeptidase 1; AltName: Full=ARTS-1; AltName: Full=Adipocyte-derived leucine aminopeptidase; Short=A-LAP; AltName: Full=Aminopeptidase PILS; AltName: Full=Puromycin-insensitive leucyl-specific aminopeptidase; Short=PILS-AP; AltName: Full=Type 1 tumor necrosis factor receptor shedding aminopeptidase regulator
Description ..   
Protein Family: Peptidase M1 Aminopeptidase N family incudes tricorn interacting factor F3, Endoplasmic reticulum aminopeptidase 1 (ERAP1), Aminopeptidase Q (APQ)
Comment ..   

Gene:ERAP1     Related Protein 3D Structures     More BioActivity Data..
Tested Compounds:
Description:
Title: Ranking the selectivity of PubChem screening hits by activity-based protein profiling: MMP13 as a case study.

Abstract: High-throughput screening (HTS) has become an integral part of academic and industrial efforts aimed at developing new chemical probes and drugs. These screens typically generate several 'hits', or lead active compounds, that must be prioritized for follow-up medicinal chemistry studies. Among primary considerations for ranking lead compounds is selectivity for the intended target, especially among mechanistically related proteins. Here, we show how the chemical proteomic technology activity-based protein profiling (ABPP) can serve as a universal assay to rank HTS hits based on their selectivity across many members of an enzyme superfamily. As a case study, four metalloproteinase-13 (MMP13) inhibitors of similar potency originating from a publically supported HTS and reported in PubChem were tested by ABPP for selectivity against a panel of 27 diverse metalloproteases. The inhibitors could be readily separated into two groups: (1) those that were active against several metalloproteases and (2) those that showed high selectivity for MMP13. The latter set of inhibitors was thereby designated as more suitable for future medicinal chemistry optimization. We anticipate that ABPP will find general utility as a platform to rank the selectivity of lead compounds emerging from HTS assays for a wide variety of enzymes.
(PMID: 18364257)
Categorized Comment
ChEMBL Assay Type: Binding

ChEMBL Assay Data Source: Scientific Literature

ChEMBL Target ID: 101611

ChEMBL Target Type: Target is a single protein chain

Result Definitions
TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Activity activity commentActivity activity commentString
2Activity standard flagActivity standard flagInteger
3Activity qualifierActivity qualifierString
4Activity published valueActivity published valueFloat
5Activity standard valueActivity standard valueFloat

Data Table (Concise)
PageFrom: