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
2020
The mechanism of β-N-methylamino-l-alanine inhibition of tRNA aminoacylation and its impact on misincorporation
Han N, Bullwinkle T, Loeb K, Faull K, Mohler K, Rinehart J, Ibba M. The mechanism of β-N-methylamino-l-alanine inhibition of tRNA aminoacylation and its impact on misincorporation. Journal Of Biological Chemistry 2020, 295: 1402-1410. DOI: 10.1016/s0021-9258(17)49898-x.Peer-Reviewed Original ResearchAmino acid activationSerine codonsProtein synthesisHuman protein extractsHuman seryl-tRNA synthetaseAminoacyl-tRNA synthetaseSeryl-tRNA synthetaseAmyotrophic lateral sclerosisAlanyl-tRNA synthetaseN-methylaminoNonproteinogenic amino acidsCotranslational incorporationTRNA aminoacylationAlzheimer's diseaseProtein extractsBiochemical assaysAmino acidsExchange assayBMAAAcid activationSynthetaseCodonAminoacylationNeurodegenerative diseasesMultiple different mechanisms