2016
Colorimetric detection of proteins based on target-induced activation of aptazyme
Wu D, Gao T, Lei L, Yang D, Mao X, Li G. Colorimetric detection of proteins based on target-induced activation of aptazyme. Analytica Chimica Acta 2016, 942: 68-73. PMID: 27720123, DOI: 10.1016/j.aca.2016.09.010.Peer-Reviewed Original ResearchConceptsTarget proteinsDetection of proteinsCost-effective detectionAntibody-based assaysAptazymesTarget-induced activityGold nanoparticlesConformational changesDNA linkersProteinDetection of analytesProtein assayCross-linked gold nanoparticlesSignal amplificationEconomical synthesisAssayColorimetric detection of proteinDetection limitAssay methodSignal recognitionColorimetric detectionAnalytical performanceDetection methodGrowth factorDetection of vascular endothelial growth factorProximity ligation-induced assembly of DNAzymes for simple and cost-effective colourimetric detection of proteins with high sensitivity
Wei L, Wang X, Wu D, Li C, Yin Y, Li G. Proximity ligation-induced assembly of DNAzymes for simple and cost-effective colourimetric detection of proteins with high sensitivity. Chemical Communications 2016, 52: 5633-5636. PMID: 27032382, DOI: 10.1039/c6cc00205f.Peer-Reviewed Original Research
2000
Protein Phosphatase 2Cα Dephosphorylates Axin and Activates LEF-1-dependent Transcription*
Wu D, Strovel E, Sussman D. Protein Phosphatase 2Cα Dephosphorylates Axin and Activates LEF-1-dependent Transcription*. Journal Of Biological Chemistry 2000, 275: 2399-2403. PMID: 10644691, DOI: 10.1074/jbc.275.4.2399.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsAxin ProteinCOS CellsDishevelled ProteinsDNA-Binding ProteinsEnzyme ActivationJNK Mitogen-Activated Protein KinasesLymphoid Enhancer-Binding Factor 1Mitogen-Activated Protein KinasesPhosphoprotein PhosphatasesPhosphoproteinsPhosphorylationPrecipitin TestsProtein BindingProtein Phosphatase 2Protein Phosphatase 2CProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsSignal TransductionTranscription FactorsTranscriptional ActivationConceptsLEF-1-dependent transcriptionWnt signal transductionSignal transductionExpression of PP2CProtein phosphatase 2CalphaProtein phosphatase 2CαTwo-hybrid systemDishevelled gene familyReporter gene assayGene familyPositive regulatorCytoplasmic proteinsPP2CNegative regulatorAxinWnt-1Gene assayTranscriptionTransductionRegulatorSynergistic responseProteinExpressionDephosphorylationRepression
1999
Dishevelled proteins lead to two signaling pathways. Regulation of LEF-1 and c-Jun N-terminal kinase in mammalian cells.
Li L, Yuan H, Xie W, Mao J, Caruso A, Sussman D, Wu D. Dishevelled proteins lead to two signaling pathways. Regulation of LEF-1 and c-Jun N-terminal kinase in mammalian cells. Journal Of Biological Chemistry 1999, 274: 33178. DOI: 10.1016/s0021-9258(17)46631-2.Peer-Reviewed Original ResearchSuppression of Glycogen Synthase Kinase Activity Is Not Sufficient for Leukemia Enhancer Factor-1 Activation*
Yuan H, Mao J, Li L, Wu D. Suppression of Glycogen Synthase Kinase Activity Is Not Sufficient for Leukemia Enhancer Factor-1 Activation*. Journal Of Biological Chemistry 1999, 274: 30419-30423. PMID: 10521419, DOI: 10.1074/jbc.274.43.30419.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAnimalsAxin ProteinBeta CateninCalcium-Calmodulin-Dependent Protein KinasesCarrier ProteinsCytoskeletal ProteinsDNA-Binding ProteinsEnzyme ActivationGenes, ReporterGlycogen Synthase Kinase 3Glycogen Synthase KinasesLuciferasesLymphoid Enhancer-Binding Factor 1MiceNeoplasm ProteinsPhosphorylationProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRecombinant ProteinsRepressor ProteinsSignal TransductionTrans-ActivatorsTranscription FactorsTranscription, GeneticTransfectionWnt ProteinsWnt1 ProteinZebrafish ProteinsConceptsGlycogen synthase kinase-3LEF-1-dependent transcriptionKinase activityWnt proteinsWnt-1Glycogen synthase kinase activitySynthase kinase activityProtein kinase AktSynthase kinase-3Enhancer factor-1Kinase AktAxinKinase 3MAktPeptide substratesReduced associationAktPhe residueTyr-216Factor 1TranscriptionFRATProteinActivationAdditional mechanismAxin and Frat1 interact with Dvl and GSK, bridging Dvl to GSK in Wnt‐mediated regulation of LEF‐1
Li L, Yuan H, Weaver C, Mao J, Farr G, Sussman D, Jonkers J, Kimelman D, Wu D. Axin and Frat1 interact with Dvl and GSK, bridging Dvl to GSK in Wnt‐mediated regulation of LEF‐1. The EMBO Journal 1999, 18: 4233-4240. PMID: 10428961, PMCID: PMC1171499, DOI: 10.1093/emboj/18.15.4233.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAnimalsAxin ProteinCalcium-Calmodulin-Dependent Protein KinasesDishevelled ProteinsDNA-Binding ProteinsGlycogen Synthase Kinase 3Glycogen Synthase KinasesLymphoid Enhancer-Binding Factor 1PhosphoproteinsProtein BindingProtein ConformationProteinsProto-Oncogene ProteinsRepressor ProteinsSignal TransductionTranscription FactorsWnt ProteinsWnt1 ProteinXenopusXenopus ProteinsZebrafish ProteinsDishevelled Proteins Lead to Two Signaling Pathways REGULATION OF LEF-1 AND c-Jun N-TERMINAL KINASE IN MAMMALIAN CELLS*
Li L, Yuan H, Xie W, Mao J, Caruso A, McMahon A, Sussman D, Wu D. Dishevelled Proteins Lead to Two Signaling Pathways REGULATION OF LEF-1 AND c-Jun N-TERMINAL KINASE IN MAMMALIAN CELLS*. Journal Of Biological Chemistry 1999, 274: 129-134. PMID: 9867820, DOI: 10.1074/jbc.274.1.129.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAnimalsBeta CateninCalcium-Calmodulin-Dependent Protein KinasesCell Cycle ProteinsCOS CellsCytoskeletal ProteinsDishevelled ProteinsDNA-Binding ProteinsEnzyme ActivationJNK Mitogen-Activated Protein KinasesLymphoid Enhancer-Binding Factor 1MiceMitogen-Activated Protein KinasesPhosphoproteinsSignal TransductionTrans-ActivatorsTranscription FactorsTranscription, GeneticUp-RegulationConceptsJNK activationMammalian cellsT-cell factorSmall G proteinsC-Jun N-terminal kinaseDominant negative mutantBeta-catenin levelsDifferent signaling pathwaysCOS-7 cellsN-terminal kinaseC-Jun NDishevelled proteinsDvl proteinsDEP domainDependent transcriptionNegative mutantPathway regulationKinase activityLEF-1Transcription activitySignaling pathwaysG proteinsNovel pathwayCell factorProtein
1996
Identification of a phospholipase C beta2 region that interacts with Gbeta-gamma.
Kuang Y, Wu Y, Smrcka A, Jiang H, Wu D. Identification of a phospholipase C beta2 region that interacts with Gbeta-gamma. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 2964-2968. PMID: 8610151, PMCID: PMC39743, DOI: 10.1073/pnas.93.7.2964.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntigens, CDBlotting, WesternCell LineChlorocebus aethiopsDNA, ComplementaryGlutamic AcidGTP-Binding ProteinsHumansIsoenzymesKidneyMacromolecular SubstancesMammalsMutagenesis, Site-DirectedPoint MutationPolymerase Chain ReactionReceptor, Anaphylatoxin C5aReceptors, ComplementRecombinant Fusion ProteinsRecombinant ProteinsTransfectionType C PhospholipasesConceptsCOS-7 cellsGlutathione S-transferaseGbeta gammaPLC-beta2Fusion proteinBeta gamma subunitsLigand-induced activationAlpha1B-adrenergic receptorMammalian expression plasmidX boxG proteinsY boxExpression plasmidAmino acidsS-transferaseProteinSequenceResiduesCellsActivationBeta2GalphaGbetaC5a receptorCDNA
1995
Different α1-Adrenergic Receptor Sequences Required for Activating Different Gα Subunits of Gq Class of G Proteins (∗)
Wu D, Jiang H, Simon M. Different α1-Adrenergic Receptor Sequences Required for Activating Different Gα Subunits of Gq Class of G Proteins (∗). Journal Of Biological Chemistry 1995, 270: 9828-9832. PMID: 7730363, DOI: 10.1074/jbc.270.17.9828.Peer-Reviewed Original ResearchConceptsG alpha 16G alpha 14Gq classAlpha 16Receptor sequencesDifferent G alpha subunitsAlpha subunitG proteinsG alpha q/11Different Gα subunitsG alpha subunitsAmino acid stretchAlpha q/11Alpha 14N-terminal segmentThird inner loopGα subunitsBBXXB motifRegulatory proteinsC-terminusN-terminusSpecific mutationsSubunitsProteinSpecific interactions