2002
Assessment of RET/PTC Oncogene Activation and Clonality in Thyroid Nodules with Incomplete Morphological Evidence of Papillary Carcinoma A Search for the Early Precursors of Papillary Cancer
Fusco A, Chiappetta G, Hui P, Garcia-Rostan G, Golden L, Kinder BK, Dillon DA, Giuliano A, Cirafici AM, Santoro M, Rosai J, Tallini G. Assessment of RET/PTC Oncogene Activation and Clonality in Thyroid Nodules with Incomplete Morphological Evidence of Papillary Carcinoma A Search for the Early Precursors of Papillary Cancer. American Journal Of Pathology 2002, 160: 2157-2167. PMID: 12057919, PMCID: PMC1850819, DOI: 10.1016/s0002-9440(10)61164-9.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAnimalsBase SequenceCarcinoma, PapillaryCloning, MolecularDrosophila ProteinsGene Expression Regulation, NeoplasticGenetic MarkersHumansMembrane ProteinsMiceMolecular Sequence DataNeoplasm InvasivenessNuclear Receptor CoactivatorsOncogene ProteinsOncogene Proteins, FusionPatched ReceptorsPatched-1 ReceptorProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-retRabbitsReceptor Protein-Tyrosine KinasesReceptors, Cell SurfaceReverse Transcriptase Polymerase Chain ReactionThyroid NeoplasmsThyroid NoduleTranscription FactorsConceptsLaser capture microdissectionPapillary cancerRET/PTC1RET immunoreactivityThyroid nodulesCarcinoma featuresMicroscopic fociPapillary carcinomaInvasive papillary cancerCytological alterationsReverse transcriptase-polymerase chain reactionRET activationRET/PTC3 rearrangementsTranscriptase-polymerase chain reactionRET/PTC3Analysis of clonalityRET/PTC oncogene activationPrecursor lesionsEntire lesionTumor fociPolyclonal tumorsAdenomatous nodulesMorphological changesSame tumorMorphological signs
1995
DARPP‐32 (dopamine and cAMP‐regulated phosphoprotein, M r 32,000) is a membrane protein in the bovine parathyroid
Matovcik L, Hemmings H, Kinder B. DARPP‐32 (dopamine and cAMP‐regulated phosphoprotein, M r 32,000) is a membrane protein in the bovine parathyroid. FEBS Letters 1995, 364: 67-74. PMID: 7750546, DOI: 10.1016/0014-5793(95)00359-h.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrain ChemistryCattleDopamine and cAMP-Regulated Phosphoprotein 32Fluorescent Antibody TechniqueIsoenzymesMembrane ProteinsMembranesMicroscopy, ImmunoelectronNerve Tissue ProteinsParathyroid GlandsPhosphoprotein PhosphatasesPhosphoproteinsProtein Phosphatase 1Protein PrenylationSubcellular FractionsTissue DistributionConceptsProtein phosphatase 1 gammaDARPP-32Protein phosphatase-1 inhibitorPhosphatase-1 inhibitorImmunocytochemical localization studiesMembrane proteinsIntracellular membranesPlasma membraneMetabolic labelingProtein presentLocalization studiesBovine parathyroidImmunoblot analysisSoluble formParticulate fractionDistinct formsMembraneCentral nervous systemCellsM NaClNervous systemParathyroid cellsCytoplasmProteinVesicles
1994
Antibodies to an epitope on synapsin I detect a protein associated with the endocytic compartment in non-neuronal cells.
Matovcik LM, Karapetian O, Czernik AJ, Marino CR, Kinder BK, Gorelick FS. Antibodies to an epitope on synapsin I detect a protein associated with the endocytic compartment in non-neuronal cells. European Journal Of Cell Biology 1994, 65: 327-40. PMID: 7536673.Peer-Reviewed Original ResearchConceptsClone 9 cellsEndocytic compartmentsPotential substrate proteinsDependent protein kinase IISynapsin ISmall intracellular vesiclesProtein kinase IIRat liver endosomesSubstrate proteinsPhosphorylation sequenceNon-neuronal cellsCLIP-170Intracellular vesiclesKinase IILarge endosomesPostnuclear supernatantEndosomesSensitive compartmentLiver endosomesProteinConfocal microscopyCell linesVesiclesIntestinal enterocytesCompartments