Featured Publications
A multi-purpose, regenerable, proteome-scale, human phosphoserine resource for phosphoproteomics
Gassaway BM, Li J, Rad R, Mintseris J, Mohler K, Levy T, Aguiar M, Beausoleil SA, Paulo JA, Rinehart J, Huttlin EL, Gygi SP. A multi-purpose, regenerable, proteome-scale, human phosphoserine resource for phosphoproteomics. Nature Methods 2022, 19: 1371-1375. PMID: 36280721, PMCID: PMC9847208, DOI: 10.1038/s41592-022-01638-5.Peer-Reviewed Original ResearchConceptsPhosphorylation site localizationPhosphorylation positionsCellular signalingPosition of phosphorylationProtein phosphorylationComplex biological systemsPhosphorylated isomersData analysis pipelinePhosphoproteomicsAnalysis pipelinePhosphopeptide standardsPhosphorylationPhosphopeptidesCentral roleBiological systemsWeb toolLocalizationSignalingFragmentation spectra
2015
Robust production of recombinant phosphoproteins using cell-free protein synthesis
Oza JP, Aerni HR, Pirman NL, Barber KW, ter Haar CM, Rogulina S, Amrofell MB, Isaacs FJ, Rinehart J, Jewett MC. Robust production of recombinant phosphoproteins using cell-free protein synthesis. Nature Communications 2015, 6: 8168. PMID: 26350765, PMCID: PMC4566161, DOI: 10.1038/ncomms9168.Peer-Reviewed Original ResearchConceptsMEK1 activityMultiple phosphorylated residuesCo-translational incorporationSite-specific protein phosphorylationCell-free protein synthesis platformHigh-throughput technology platformsCell-free protein synthesisSite-specific phosphorylationStructure-function relationshipsRecombinant phosphoproteinsPhosphorylation eventsMEK1 kinasePhosphorylated residuesProtein phosphorylationProtein synthesisEscherichia coliPhosphoproteinRobust productionSynthesis platformStructural consequencesDirect expressionPhosphorylationTechnology platformKinasePhosphoserine
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