Using chemical genetics and ATP analogues to dissect protein kinase function
Protein kinases catalyze the transfer of the γ-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 re...
| Główni autorzy: | , , , |
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| Format: | Journal article |
| Język: | English |
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2007
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| _version_ | 1826300284623650816 |
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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 γ-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. © 2007 by American Chemical Society. |
| first_indexed | 2024-03-07T05:14:49Z |
| format | Journal article |
| id | oxford-uuid:dcd1e5db-4e8b-455b-9812-019a5da097a0 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:14:49Z |
| publishDate | 2007 |
| record_format | dspace |
| spelling | oxford-uuid:dcd1e5db-4e8b-455b-9812-019a5da097a02022-03-27T09:20:20ZUsing chemical genetics and ATP analogues to dissect protein kinase functionJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:dcd1e5db-4e8b-455b-9812-019a5da097a0EnglishSymplectic Elements at Oxford2007Elphick, LLee, SEGouverneur, VMann, DProtein kinases catalyze the transfer of the γ-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. © 2007 by American Chemical Society. |
| 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 |
| work_keys_str_mv | AT elphickl usingchemicalgeneticsandatpanaloguestodissectproteinkinasefunction AT leese usingchemicalgeneticsandatpanaloguestodissectproteinkinasefunction AT gouverneurv usingchemicalgeneticsandatpanaloguestodissectproteinkinasefunction AT mannd usingchemicalgeneticsandatpanaloguestodissectproteinkinasefunction |