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| Content Provider | Royal Society of Chemistry (RSC) |
|---|---|
| Author | Sopko, Richelle Andrews, Brenda J. |
| Copyright Year | 2008 |
| Abstract | Protein phosphorylation is associated with most cell signaling and developmental processes in eukaryotes. Despite the vast extent of the phosphoproteome within the cell, connecting specific kinases with relevant targets remains a significant experimental frontier. The challenge of linking kinases and their substrates reflects the complexity of kinase function. For example, kinases tend to exert their biological effects through supernumerary, redundant phosphorylation, often on multiple protein complex components. Although these types of phosphorylation events are biologically significant, those kinases responsible are often difficult to identify. Recent methods for global analysis of proteinphosphorylation promise to substantially accelerate efforts to map the dynamic phosphorylome. Here, we review both conventional methods to identify kinase targets and more comprehensive genomic and proteomic approaches to connect the kinome and phosphorylome. |
| Starting Page | 920 |
| Ending Page | 933 |
| Page Count | 14 |
| File Format | HTM / HTML PDF |
| ISSN | 1742206X |
| Volume Number | 4 |
| Issue Number | 9 |
| Journal | Molecular BioSystems |
| DOI | 10.1039/b801724g |
| Language | English |
| Publisher | Royal Society of Chemistry |
| Access Restriction | Open |
| Subject Keyword | Kinome Phosphorylation Protein kinase Cell signaling Protein |
| Content Type | Text |
| Resource Type | Article |
| Subject | Molecular Biology Biotechnology |
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