Premium
Inside Cover: Characterization of Irreversible Kinase Inhibitors by Directly Detecting Covalent Bond Formation: A Tool for Dissecting Kinase Drug Resistance (ChemBioChem 18/2010)
Author(s) -
Klüter Sabine,
Simard Jeffrey R.,
Rode Haridas B.,
Grütter Christian,
Pawar Vijaykumar,
Raaijmakers Hans C. A.,
Barf Tjeerd A.,
Rabiller Matthias,
van Otterlo Willem A. L.,
Rauh Daniel
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201090088
Subject(s) - covalent bond , chemistry , cysteine , protein kinase domain , t790m , kinase , electrophile , epidermal growth factor receptor , residue (chemistry) , stereochemistry , combinatorial chemistry , mutant , biochemistry , enzyme , receptor , organic chemistry , gefitinib , gene , catalysis
The inside cover picture shows a covalent inhibitor bound to the drug resistance mutant T790M of the epidermal growth factor receptor kinase (EFGR). The inhibitor interacts with the hinge region of the kinase domain, and its electrophile modifies the side chain thiol of a cysteine residue of EGFR. For further details, see the paper by D. Rauh et al. on p. 2557 ff.