ArticleMolecular systems biology2011
Comparative analysis of Erk phosphorylation suggests a mixed strategy for measuring phospho-form distributions.
Article in Molecular systems biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- An ultrasensitive fiveplex activity assay for cellular kinases.Scientific reports · 2019Article
- Estimating the Distribution of Protein Post-Translational Modification States by Mass Spectrometry.Journal of proteome research · 2018Article
- Proteins and Proteoforms: New Separation Challenges.Analytical chemistry · 2018Review
- Nuclear Magnetic Resonance Spectroscopy for the Identification of Multiple Phosphorylations of Intrinsically Disordered Proteins.Journal of visualized experiments : JoVE · 2016Article
- Long-term dynamics of multisite phosphorylation.Molecular biology of the cell · 2016Article
- FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease.Analytical chemistry · 2016Article
- Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase.The Journal of biological chemistry · 2016Article
- Detection and Differentiation of Threonine- and Tyrosine-Monophosphorylated Forms of ERK1/2 by Capillary Isoelectric Focusing-Immunoassay.Scientific reports · 2015Article
- Sensitive targeted quantification of ERK phosphorylation dynamics and stoichiometry in human cells without affinity enrichment.Analytical chemistry · 2015Article
- Paradoxical results in perturbation-based signaling network reconstruction.Biophysical journal · 2014Article
- Complexity of metastasis-associated SDF-1 ligand signaling in breast cancer stem cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Physiological and pathological phosphorylation of tau by Cdk5.Frontiers in molecular neuroscience · 2014Review
- ERK as a model for systems biology of enzyme kinetics in cells.Current biology : CB · 2013Review
- Deciphering post-translational modification codes.FEBS letters · 2013Review
- Unraveling a phosphorylation event in a folded protein by NMR spectroscopy: phosphorylation of the Pin1 WW domain by PKA.Journal of biomolecular NMR · 2013Article
- Monolignol pathway 4-coumaric acid:coenzyme A ligases in Populus trichocarpa: novel specificity, metabolic regulation, and simulation of coenzyme A ligation fluxes.Plant physiology · 2013Article
- Dimerization and bifunctionality confer robustness to the isocitrate dehydrogenase regulatory system in Escherichia coli.The Journal of biological chemistry · 2013Article
- Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.Nature protocols · 2013Article
- Construction of protein phosphorylation networks by data mining, text mining and ontology integration: analysis of the spindle checkpoint.Database : the journal of biological databases and curation · 2013Article
- Cell signaling, post-translational protein modifications and NMR spectroscopy.Journal of biomolecular NMR · 2012Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
Abstract
The functional impact of multisite protein phosphorylation can depend on both the numbers and the positions of phosphorylated sites-the global pattern of phosphorylation or 'phospho-form'-giving biological systems profound capabilities for dynamic information processing. A central problem in quantitative systems biology, therefore, is to measure the 'phospho-form distribution': the relative amount of each of the 2(n) phospho-forms of a protein with n-phosphorylation sites. We compared four potential methods-western blots with phospho-specific antibodies, peptide-based liquid chromatography (LC) and mass spectrometry (MS; pepMS), protein-based LC/MS (proMS) and nuclear magnetic resonance spectroscopy (NMR)-on differentially phosphorylated samples of the well-studied mitogen-activated protein kinase Erk2, with two phosphorylation sites. The MS methods were quantitatively consistent with each other and with NMR to within 10%, but western blots, while highly sensitive, showed significant discrepancies with MS. NMR also uncovered two additional phosphorylations, for which a combination of pepMS and proMS yielded an estimate of the 16-member phospho-form distribution. This combined MS strategy provides an optimal mixture of accuracy and coverage for quantifying distributions, but positional isomers remain a challenging problem.
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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.