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
2008
Enhancement of ABL Kinase Catalytic Efficiency by a Direct Binding Regulator Is Independent of Other Regulatory Mechanisms*
Cao X, Tanis KQ, Koleske AJ, Colicelli J. Enhancement of ABL Kinase Catalytic Efficiency by a Direct Binding Regulator Is Independent of Other Regulatory Mechanisms*. Journal Of Biological Chemistry 2008, 283: 31401-31407. PMID: 18796434, PMCID: PMC2581583, DOI: 10.1074/jbc.m804002200.Peer-Reviewed Original ResearchConceptsSH2 domainKinase activityTyrosine kinaseAbl family tyrosine kinasesKinase activation mechanismRelief of autoinhibitionUnique protein structureFamily tyrosine kinasesCatalytic site mutationsPhosphorylation of CrkInhibitor-resistant mutantsAbl kinase activityTyrosine kinase activitySH3-SH2ABL tyrosine kinase activityABL2 kinaseABL substratesRegulatory domainPhosphorylation mechanismDownstream effectorsDomain coreInactive conformationAbl SH3Regulatory mechanismsProtein structure
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply