2005
AP2α alters the transcriptional activity and stability of p53
Stabach P, Thiyagarajan M, Woodfield G, Weigel R. AP2α alters the transcriptional activity and stability of p53. Oncogene 2005, 25: 2148-2159. PMID: 16288208, DOI: 10.1038/sj.onc.1209250.Peer-Reviewed Original ResearchMeSH KeywordsBreast NeoplasmsChromatin ImmunoprecipitationColonic NeoplasmsCyclin-Dependent Kinase Inhibitor p21Gene Expression Regulation, NeoplasticGenes, ReporterHumansImmunoprecipitationLiver NeoplasmsPoint MutationPromoter Regions, GeneticProtein BindingTranscription Factor AP-2Transcription, GeneticTranscriptional ActivationTumor Cells, CulturedTumor Suppressor Protein p53ConceptsTranscriptional activityEndogenous p53 target genesEndogenous p21 geneNormal transcriptional activityP53 target genesP53-mediated inductionAmino acids 305Stability of p53Expression of aP2Transcriptional coactivationP21WAF1/CIP1P21 promoterTarget genesCertain genesRegion of p53AP2αReporter assaysP21 geneFunctional partnershipP53 stabilityP53 activityCell growthPoint mutationsAP2Genes
1998
A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles
Stankewich M, Tse W, Peters L, Ch’ng Y, John K, Stabach P, Devarajan P, Morrow J, Lux S. A widely expressed βIII spectrin associated with Golgi and cytoplasmic vesicles. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 14158-14163. PMID: 9826670, PMCID: PMC24343, DOI: 10.1073/pnas.95.24.14158.Peer-Reviewed Original ResearchConceptsBetaIII spectrinGene mapsMembrane skeletonEndoplasmic reticulum marker calnexinPlasma membrane skeletonPleckstrin homology domainTrans-Golgi networkHuman brain cDNASyntenic regionsGene familyProtein 4.1Membrane associationCompartment markersImportant structural componentDa proteinSelf-association siteGolgi membranesHomology searchCDNA endsRapid amplificationUnidentified isoformChromosome 19Liver Golgi membranesGenBank databaseVesicle markersUtilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1
Sinard J, Stewart G, Stabach P, Argent A, Gilligan D, Morrow J. Utilization of an 86bp exon generates a novel adducin isoform (β4) lacking the MARCKS homology domain1The first two authors contributed equally to this work.1. Biochimica Et Biophysica Acta 1998, 1396: 57-66. PMID: 9524222, DOI: 10.1016/s0167-4781(97)00167-x.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAmino Acid SequenceBase SequenceCalmodulin-Binding ProteinsCloning, MolecularExonsHumansIntracellular Signaling Peptides and ProteinsIsomerismMembrane ProteinsMolecular Sequence DataMyristoylated Alanine-Rich C Kinase SubstrateOrgan SpecificityPolymerase Chain ReactionProtein Structure, TertiaryProteinsSequence Homology, Amino AcidSequence Homology, Nucleic AcidTranscription, GeneticConceptsNovel amino acidAmino acidsBeta-adducinNew isoformHuman bone marrow cDNA libraryBone marrow cDNA libraryDifferent reading framesCalcium/calmodulinLysine-rich sequenceNT-2 cellsProtein kinase CGenomic clonesGenomic mapNew amino acidsAlternate exonsActin crossCDNA libraryReading frameSplice consensus sequenceNew exonsNovel isoformConsensus sequenceStop codonKinase CExons