Quantitative dynamics of phosphoproteome: the devil is in the details.
Recent advances in peptide-based (bottom-up) quantitative proteomics and bioinformatics have opened unprecedented opportunities for extensive investigation of cellular proteomes and their dynamics. Here we discuss two approaches currently used to investigate the global dynamics of phosphorylation ba...
| Egile Nagusiak: | , |
|---|---|
| Formatua: | Journal article |
| Hizkuntza: | English |
| Argitaratua: |
2012
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| _version_ | 1826306393804636160 |
|---|---|
| author | Salek, M Acuto, O |
| author_facet | Salek, M Acuto, O |
| author_sort | Salek, M |
| collection | OXFORD |
| description | Recent advances in peptide-based (bottom-up) quantitative proteomics and bioinformatics have opened unprecedented opportunities for extensive investigation of cellular proteomes and their dynamics. Here we discuss two approaches currently used to investigate the global dynamics of phosphorylation based on the isolation of phosphorylated proteins or peptides. We evaluate the accuracy of these methodologies to grasp the global dynamics of phosphorylation, and we raise awareness on ambiguities inherent to these analyses. We conclude that further development of targeted approaches should prevent inaccurate conclusions about the nature of biological regulations and in particular kinase-substrate networks. |
| first_indexed | 2024-03-07T06:47:18Z |
| format | Journal article |
| id | oxford-uuid:fb4d509e-d2f2-4371-bc85-0a3d2c0dc2fe |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T06:47:18Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | oxford-uuid:fb4d509e-d2f2-4371-bc85-0a3d2c0dc2fe2022-03-27T13:12:39ZQuantitative dynamics of phosphoproteome: the devil is in the details.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:fb4d509e-d2f2-4371-bc85-0a3d2c0dc2feEnglishSymplectic Elements at Oxford2012Salek, MAcuto, ORecent advances in peptide-based (bottom-up) quantitative proteomics and bioinformatics have opened unprecedented opportunities for extensive investigation of cellular proteomes and their dynamics. Here we discuss two approaches currently used to investigate the global dynamics of phosphorylation based on the isolation of phosphorylated proteins or peptides. We evaluate the accuracy of these methodologies to grasp the global dynamics of phosphorylation, and we raise awareness on ambiguities inherent to these analyses. We conclude that further development of targeted approaches should prevent inaccurate conclusions about the nature of biological regulations and in particular kinase-substrate networks. |
| spellingShingle | Salek, M Acuto, O Quantitative dynamics of phosphoproteome: the devil is in the details. |
| title | Quantitative dynamics of phosphoproteome: the devil is in the details. |
| title_full | Quantitative dynamics of phosphoproteome: the devil is in the details. |
| title_fullStr | Quantitative dynamics of phosphoproteome: the devil is in the details. |
| title_full_unstemmed | Quantitative dynamics of phosphoproteome: the devil is in the details. |
| title_short | Quantitative dynamics of phosphoproteome: the devil is in the details. |
| title_sort | quantitative dynamics of phosphoproteome the devil is in the details |
| work_keys_str_mv | AT salekm quantitativedynamicsofphosphoproteomethedevilisinthedetails AT acutoo quantitativedynamicsofphosphoproteomethedevilisinthedetails |