Using chemical genetics and ATP analogues to dissect protein kinase function.
Protein kinases catalyze the transfer of the gamma-phosphate of ATP to a protein substrate and thereby profoundly alter the properties of the phosphorylated protein. The identification of the substrates of protein kinases has proven to be a very difficult task because of the multitude of structurall...
| Main Authors: | , , , |
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| Format: | Journal article |
| Sprog: | English |
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2007
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| _version_ | 1826305986632089600 |
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| author | Elphick, L Lee, SE Gouverneur, V Mann, D |
| author_facet | Elphick, L Lee, SE Gouverneur, V Mann, D |
| author_sort | Elphick, L |
| collection | OXFORD |
| description | Protein kinases catalyze the transfer of the gamma-phosphate of ATP to a protein substrate and thereby profoundly alter the properties of the phosphorylated protein. The identification of the substrates of protein kinases has proven to be a very difficult task because of the multitude of structurally related protein kinases present in cells, their apparent redundancy of function, and the lack of absolute specificity of small-molecule inhibitors. Here, we review approaches that utilize chemical genetics to determine the functions and substrates of protein kinases, focusing on the design of ATP analogues and protein kinase binding site mutants. |
| first_indexed | 2024-03-07T06:41:06Z |
| format | Journal article |
| id | oxford-uuid:f94e055d-0d35-4230-b15c-2ac722f7e7de |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:41:06Z |
| publishDate | 2007 |
| record_format | dspace |
| spelling | oxford-uuid:f94e055d-0d35-4230-b15c-2ac722f7e7de2022-03-27T12:57:01ZUsing chemical genetics and ATP analogues to dissect protein kinase function.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:f94e055d-0d35-4230-b15c-2ac722f7e7deEnglishSymplectic Elements at Oxford2007Elphick, LLee, SEGouverneur, VMann, DProtein kinases catalyze the transfer of the gamma-phosphate of ATP to a protein substrate and thereby profoundly alter the properties of the phosphorylated protein. The identification of the substrates of protein kinases has proven to be a very difficult task because of the multitude of structurally related protein kinases present in cells, their apparent redundancy of function, and the lack of absolute specificity of small-molecule inhibitors. Here, we review approaches that utilize chemical genetics to determine the functions and substrates of protein kinases, focusing on the design of ATP analogues and protein kinase binding site mutants. |
| spellingShingle | Elphick, L Lee, SE Gouverneur, V Mann, D Using chemical genetics and ATP analogues to dissect protein kinase function. |
| title | Using chemical genetics and ATP analogues to dissect protein kinase function. |
| title_full | Using chemical genetics and ATP analogues to dissect protein kinase function. |
| title_fullStr | Using chemical genetics and ATP analogues to dissect protein kinase function. |
| title_full_unstemmed | Using chemical genetics and ATP analogues to dissect protein kinase function. |
| title_short | Using chemical genetics and ATP analogues to dissect protein kinase function. |
| title_sort | using chemical genetics and atp analogues to dissect protein kinase function |
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