Inhibition of BMX (unknown origin)
- Deposit:2020-06-19
- Modify:2022-08-30
Title: Covalent binding design strategy: A prospective method for discovery of potent targeted anticancer agents.
Abstract: Cancer remains the most serious disease that threatens human health. Molecularly targeted cancer therapies, specifically small-molecule protein kinase inhibitors, form an important part of cancer therapy. Targeted covalent modification represents a proven approach to drug discovery with the recent FDA approvals of afatanib, ibrutinib, and osimertinib agents, which were designed to undergo an irreversible hetero-Michael addition reaction with a unique cysteine residue of a specific protein. Covalent inhibitors possess numerous advantages, including increased biochemical efficacy, longer duration of action, the high potential for improved therapeutic index due to lower effective dose, and the potential to inhibit certain drug resistance mechanisms. In this regard, the novel targeted anticancer agents whose activity is presumably dependent upon a hetero-Michael addition reaction with thiols are summarized in this article.
Compounds with activity <= 10uM or explicitly reported as active by ChEMBL are flagged as active in this PubChem assay presentation.
Journal: Eur J Med Chem
Year: 2017
Volume: 142
First Page: 493
Last Page: 505
DOI: 10.1016/j.ejmech.2017.09.024
Target ChEMBL ID: CHEMBL3834
ChEMBL Target Name: Tyrosine-protein kinase BMX
ChEMBL Target Type: SINGLE PROTEIN - Target is a single protein chain
Relationship Type: D - Direct protein target assigned
Confidence: Direct single protein target assigned
- PubChem
- ChEMBLLICENSEAccess to the web interface of ChEMBL is made under the EBI's Terms of Use (http://www.ebi.ac.uk/Information/termsofuse.html). The ChEMBL data is made available on a Creative Commons Attribution-Share Alike 3.0 Unported License (http://creativecommons.org/licenses/by-sa/3.0/).http://www.ebi.ac.uk/Information/termsofuse.html