2019
Integrated multi-omics approach reveals a role of ALDH1A1 in lipid metabolism in human colon cancer cells
Charkoftaki G, Thompson DC, Golla JP, Garcia-Milian R, Lam TT, Engel J, Vasiliou V. Integrated multi-omics approach reveals a role of ALDH1A1 in lipid metabolism in human colon cancer cells. Chemico-Biological Interactions 2019, 304: 88-96. PMID: 30851239, PMCID: PMC7988342, DOI: 10.1016/j.cbi.2019.02.030.Peer-Reviewed Original Research
2012
The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination
Krishnan N, Lam TT, Fritz A, Rempinski D, O'Loughlin K, Minderman H, Berezney R, Marzluff WF, Thapar R. The Prolyl Isomerase Pin1 Targets Stem-Loop Binding Protein (SLBP) To Dissociate the SLBP-Histone mRNA Complex Linking Histone mRNA Decay with SLBP Ubiquitination. Molecular And Cellular Biology 2012, 32: 4306-4322. PMID: 22907757, PMCID: PMC3486140, DOI: 10.1128/mcb.00382-12.Peer-Reviewed Original ResearchMeSH KeywordsCell CycleCell Line, TumorCell NucleusDown-RegulationHEK293 CellsHeLa CellsHistonesHumansMRNA Cleavage and Polyadenylation FactorsNIMA-Interacting Peptidylprolyl IsomeraseNuclear ProteinsPeptidylprolyl IsomeraseProtein Phosphatase 2RNA InterferenceRNA StabilityRNA-Binding ProteinsRNA, MessengerRNA, Small InterferingUbiquitinationConceptsStem-loop binding proteinHistone mRNADegradation of SLBPMRNA stabilityBinding proteinHistone mRNA stabilityRNA degradation machineryHistone mRNA decayS phaseProtein phosphatase 2AHistone mRNA degradationCore histone mRNAsExosome-mediated degradationDownregulation of Pin1Ubiquitin-proteasome systemMRNA 3' endsProlyl isomerase Pin1Phosphatase 2ADegradation machineryMRNA decayMRNA degradationProteasome systemIsomerase Pin1MRNA complexesUntranslated regionEndothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases
Marin EP, Derakhshan B, Lam TT, Davalos A, Sessa WC. Endothelial Cell Palmitoylproteomic Identifies Novel Lipid-Modified Targets and Potential Substrates for Protein Acyl Transferases. Circulation Research 2012, 110: 1336-1344. PMID: 22496122, PMCID: PMC3428238, DOI: 10.1161/circresaha.112.269514.Peer-Reviewed Original ResearchMeSH KeywordsAcetyltransferasesAcyltransferasesAmino Acid SequenceAnimalsChlorocebus aethiopsCOS CellsEndothelial CellsHEK293 CellsHuman Umbilical Vein Endothelial CellsHumansLipoylationMolecular Sequence DataPlatelet Endothelial Cell Adhesion Molecule-1ProteomicsRNA, Small InterferingSubstrate SpecificitySuperoxide DismutaseSuperoxide Dismutase-1ConceptsProtein acyl transferasesAcyl-biotinyl exchangeProtein S-palmitoylationPlatelet endothelial cell adhesion molecule-1Posttranslational lipid modificationRole of palmitoylationEndothelial cell adhesion molecule-1Acyl transferaseEndothelial cell biologyPalmitoyl proteinsS-palmitoylationPosttranslational attachmentProtein localizationCysteine side chainsCell biologyNuclear localizationPalmitoylationLipid modificationEC biologyThioester bondCell adhesion molecule-1Superoxide dismutase 1Functional roleCell surfacePotential substrates