| dc.creator | McInnes, C. | en |
| dc.creator | Mezna, M. | en |
| dc.creator | Kontopidis, G. | en |
| dc.date.accessioned | 2015-11-23T10:39:14Z | |
| dc.date.available | 2015-11-23T10:39:14Z | |
| dc.date.issued | 2006 | |
| dc.identifier | 10.1016/j.chembiol.2006.07.001 | |
| dc.identifier.issn | 1074-5521 | |
| dc.identifier.uri | http://hdl.handle.net/11615/30854 | |
| dc.description.abstract | Protein kinases exist in inactive and active states, but little attention has been paid to which state is or should be the target in drug discovery efforts. In this issue of Chemistry & Biology, Okram et al. [1] tackle this issue and show that inhibitors can be designed specifically to bind to inactive Abl. | en |
| dc.source | Chemistry & Biology | en |
| dc.source.uri | <Go to ISI>://WOS:000239546800003 | |
| dc.subject | INHIBITOR BINDING | en |
| dc.subject | TYROSINE KINASE | en |
| dc.subject | INACTIVE CDK2 | en |
| dc.subject | MECHANISM | en |
| dc.subject | DESIGN | en |
| dc.subject | STI-571 | en |
| dc.subject | COMPLEX | en |
| dc.subject | Biochemistry & Molecular Biology | en |
| dc.title | Catch the kinase conformer | en |
| dc.type | journalArticle | en |
