Tuned out
Controlling kinase inhibitors’ residence time via reversible covalent binding is of high interest in drug discovery. Tuning reversible covalent binding kinetics using a pan-kinase inhibitor that reacts with the catalytic lysine enabled exquisite temporal selectivity in vitro and in vivo.
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| Veröffentlicht in: | Nature chemical biology 2022-09, Vol.18 (9), p.917-918 |
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| container_title | Nature chemical biology |
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| creator | Ferguson, Fleur M. |
| description | Controlling kinase inhibitors’ residence time via reversible covalent binding is of high interest in drug discovery. Tuning reversible covalent binding kinetics using a pan-kinase inhibitor that reacts with the catalytic lysine enabled exquisite temporal selectivity in vitro and in vivo. |
| doi_str_mv | 10.1038/s41589-022-01037-z |
| format | Article |
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| identifier | ISSN: 1552-4450 |
| ispartof | Nature chemical biology, 2022-09, Vol.18 (9), p.917-918 |
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| language | eng |
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| source | Springer Online Journals; Nature Journals Online |
| subjects | 631/154/309 631/92/275 631/92/475 631/92/613 Binding Binding sites Biochemical Engineering Biochemistry Biology Bioorganic Chemistry Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Drugs Enzyme inhibitors FDA approval Kinases Lysine News & Views news-and-views Pharmaceuticals Proteins Selectivity |
| title | Tuned out |
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