2022
Enhanced access to the human phosphoproteome with genetically encoded phosphothreonine
Moen J, Mohler K, Rogulina S, Shi X, Shen H, Rinehart J. Enhanced access to the human phosphoproteome with genetically encoded phosphothreonine. Nature Communications 2022, 13: 7226. PMID: 36433969, PMCID: PMC9700786, DOI: 10.1038/s41467-022-34980-5.Peer-Reviewed Original ResearchConceptsUbiquitous post-translational modificationCo-translational insertionKinase activation mechanismProtein interaction platformOrthogonal translation systemProtein-protein interactionsPost-translational modificationsPhospho-amino acidsAminoacyl-tRNA synthetaseHuman phosphoproteomePhosphorylation eventsTRNA pairsFunctional assignmentCellular processesProtein phosphorylationUpstream kinasePhysiological functionsActivation mechanismTranslation systemKinasePhosphorylationInteraction platformPhosphoproteomePhosphothreoninePhospho
2014
Revealing the amino acid composition of proteins within an expanded genetic code
Aerni HR, Shifman MA, Rogulina S, O'Donoghue P, Rinehart J. Revealing the amino acid composition of proteins within an expanded genetic code. Nucleic Acids Research 2014, 43: e8-e8. PMID: 25378305, PMCID: PMC4333366, DOI: 10.1093/nar/gku1087.Peer-Reviewed Original ResearchConceptsNon-standard amino acidsOrthogonal translation systemGenetic codeUAG codonProtein synthesisConventional proteomic analysisRecombinant reporter proteinRelease factor 1Amino acid insertionAmino acid compositionReporter proteinProteomic analysisExtended proteinSurprising diversityUAG readthroughAcid insertionProteomic workflowStop codonNative proteinCodonEscherichia coliAmino acidsMessenger RNAUAGProtein