ArticleCurrent protocols in molecular biology2012
Determining in vivo phosphorylation sites using mass spectrometry.
Article in Current protocols in molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Optimized Workflow for Proteomics and Phosphoproteomics With Limited Tissue Samples.Current protocols · 2024Article
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- Identification of CryAB as a target of NUAK kinase activity in Drosophila muscle tissue.Genetics · 2023Article
- OSGIN1 is a novel TUBB3 regulator that promotes tumor progression and gefitinib resistance in non-small cell lung cancer.Cellular and molecular life sciences : CMLS · 2023Article
- Analysis of intracellular tyrosine phosphorylation in circulating neutrophils as a rapid assay for theFrontiers in pharmacology · 2023Article
- Informal nutrition symposium: leveraging the microbiome (and the metabolome) for poultry production.Poultry science · 2022Article
- The secreted tyrosine kinase VLK is essential for normal platelet activation and thrombus formation.Blood · 2022Article
- Post-translational modification of Streptococcus sanguinis SpxB influences protein solubility and HMolecular oral microbiology · 2021Article
- Fe-NTA Microcolumn Purification of Phosphopeptides from Immunoprecipitation (IP) Eluates for Mass Spectrometry Analysis.Bio-protocol · 2021Article
- Phosphorylation of human phospholipase A1 DDHD1 at newly identified phosphosites affects its subcellular localization.The Journal of biological chemistry · 2021Article
- Immunopharmacology and Quantitative Analysis of Tyrosine Kinase Signaling.Current protocols in immunology · 2020Article
- Sugar starvation-regulated MYBS2 and 14-3-3 protein interactions enhance plant growth, stress tolerance, and grain weight in rice.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Protein phosphatase 2A has an essential role in promoting thymocyte survival during selection.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Article
- Tyrosine Phosphorylation of Mitochondrial Creatine Kinase 1 Enhances a Druggable Tumor Energy Shuttle Pathway.Cell metabolism · 2018Article
- Regulation of Cx37 channel and growth-suppressive properties by phosphorylation.Journal of cell science · 2017Article
- Serial-omics characterization of equine urine.PloS one · 2017Article
- Regulation of Connexin43 Function and Expression by Tyrosine Kinase 2.The Journal of biological chemistry · 2016Article
- A Cross-Species Study of PI3K Protein-Protein Interactions Reveals the Direct Interaction of P85 and SHP2.Scientific reports · 2016Article
- Triomics Analysis of Imatinib-Treated Myeloma Cells Connects Kinase Inhibition to RNA Processing and Decreased Lipid Biosynthesis.Analytical chemistry · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Phosphorylation is the most studied protein post-translational modification (PTM) in biological systems, since it controls cell growth, proliferation, survival, and other processes. High-resolution/high mass accuracy mass spectrometers are used to identify protein phosphorylation sites due to their speed, sensitivity, selectivity, and throughput. The protocols described here focus on two common strategies: (1) identifying phosphorylation sites from individual proteins and small protein complexes, and (2) identifying global phosphorylation sites from whole-cell and tissue extracts. For the first, endogenous or epitope-tagged proteins are typically immunopurified from cell lysates, purified via gel electrophoresis or precipitation, and enzymatically digested into peptides. Samples can be optionally enriched for phosphopeptides using immobilized metal affinity chromatography (IMAC) or titanium dioxide (TiO(2)) and then analyzed by microcapillary liquid chromatography/tandem mass spectrometry (LC-MS/MS). Global phosphorylation site analyses that capture pSer/pThr/pTyr sites from biological sources sites are more resource and time consuming and involve digesting the whole-cell lysate, followed by peptide fractionation by strong cation-exchange chromatography, phosphopeptide enrichment by IMAC or TiO(2), and LC-MS/MS. Alternatively, the protein lysate can be fractionated by SDS-PAGE, followed by digestion, phosphopeptide enrichment, and LC-MS/MS. One can also immunoprecipitate only phosphotyrosine peptides using a pTyr antibody followed by LC-MS/MS.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.