2020
Global and Site-Specific Effect of Phosphorylation on Protein Turnover
Wu C, Ba Q, Lu D, Li W, Salovska B, Hou P, Mueller T, Rosenberger G, Gao E, Di Y, Zhou H, Fornasiero EF, Liu Y. Global and Site-Specific Effect of Phosphorylation on Protein Turnover. Developmental Cell 2020, 56: 111-124.e6. PMID: 33238149, PMCID: PMC7855865, DOI: 10.1016/j.devcel.2020.10.025.Peer-Reviewed Original ResearchConceptsProtein turnoverProtein lifetimeCyclin-dependent kinase substrateStable isotope-labeled amino acidsSite-specific phosphorylationPulse-labeling approachIsotope-labeled amino acidsMass spectrometry-based methodCell fitnessKinase substratePhosphorylation sitesPhosphorylated sitesProteomic methodsCell signalingSpectrometry-based methodsLive cellsAmino acidsPhosphositesRich resourceDisease biologyLabeling approachPhosphorylationModification typesGlutamic acidTurnover
2016
Box C/D sRNA stem ends act as stabilizing anchors for box C/D di-sRNPs
Yip WS, Shigematsu H, Taylor DW, Baserga SJ. Box C/D sRNA stem ends act as stabilizing anchors for box C/D di-sRNPs. Nucleic Acids Research 2016, 44: 8976-8989. PMID: 27342279, PMCID: PMC5062973, DOI: 10.1093/nar/gkw576.Peer-Reviewed Original ResearchConceptsBox C/DArchaeal box C/D sRNPsBox C/D sRNAsBox C/D sRNPRibosomal RNA modificationsElectron microscopy modelCryo-EM reconstructionCellular organismsRibosome functionRNA modificationsSRNAsSRNPModification typesStructural techniquesEukaryaPotential interactionsStemArchaeaStructural analysisStem endClose proximityOrganismsNuclear magnetic resonance studiesCatalyseInteraction
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