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
2001
Presidential address: A biography of calcium
Kinder B. Presidential address: A biography of calcium. Surgery 2001, 130: 899-906. PMID: 11742315, DOI: 10.1067/msy.2001.118955.Peer-Reviewed Original Research
1999
Inhibition of protein phosphatase 1 decreases PTH secretion from isolated dispersed parathyroid cells
Matovcik L, Rhee S, Schaefer J, da Cruz e Silva E, Kinder B. Inhibition of protein phosphatase 1 decreases PTH secretion from isolated dispersed parathyroid cells. Molecular And Cellular Endocrinology 1999, 154: 171-177. PMID: 10509811, DOI: 10.1016/s0303-7207(98)00224-x.Peer-Reviewed Original ResearchConceptsParathyroid hormone secretionOkadaic acidPP-1PP-1 activityPTH secretionPlasma membrane markerHormone secretionParathyroid cellsProtein phosphataseBasal PTH secretionTarget of inhibitionSubcellular fractionationPermeabilized cellsBovine cellsMembrane markersSecretory granulesIntact bovineIntact humanSecretionSelective inhibitorCellsPhosphataseOkadaicInhibitionMarkers
1997
Reconstitution of calcium-regulated parathyroid hormone secretion from streptolysin-O-permeabilized parathyroid cells by guanosine 5'-O-(thio)triphosphate.
Matovcik L, Rhee S, Schaefer J, Kinder B. Reconstitution of calcium-regulated parathyroid hormone secretion from streptolysin-O-permeabilized parathyroid cells by guanosine 5'-O-(thio)triphosphate. Endocrinology 1997, 138: 1170-9. PMID: 9048624, DOI: 10.1210/endo.138.3.4971.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsCalciumCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCattleCell Membrane PermeabilityCyclic AMPCytosolEnergy MetabolismGuanine NucleotidesGuanosine 5'-O-(3-Thiotriphosphate)Osmolar ConcentrationParathyroid GlandsParathyroid HormoneParotid GlandStreptolysinsTime FactorsConceptsPTH secretionParathyroid cellsIntracellular Ca2Hormone secretionParathyroid hormone secretionGuanosine 5'Dose-dependent mannerCalcium/calmodulin-dependent protein kinase IIPTH releaseCalmodulin-dependent protein kinase IIExtracellular Ca2Physiological intracellular Ca2Protein kinase IISecretionAmbient Ca2Low Ca2Ca2GTPγSCellsInverse relationshipCytosolic cofactorsKinase IIAddition of GTPγSAbsence of GTPγSDependent regulation
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
1988
Expression of messenger ribonucleic acids encoding a parathyroid hormone-like peptide in normal human and animal tissues with abnormal expression in human parathyroid adenomas.
Ikeda K, Weir E, Mangin M, Dannies P, Kinder B, Deftos L, Brown E, Broadus A. Expression of messenger ribonucleic acids encoding a parathyroid hormone-like peptide in normal human and animal tissues with abnormal expression in human parathyroid adenomas. Endocrinology 1988, 2: 1230-6. PMID: 3216862, DOI: 10.1210/mend-2-12-1230.Peer-Reviewed Original ResearchConceptsPTH-like peptideHuman parathyroid adenomasParathyroid adenomaAbnormal human parathyroid tissueHuman parathyroid tissueNumber of endocrineMedullary carcinoma cellsParathyroid hormone-like peptideExpression of mRNAAutonomous glandsHumoral hypercalcemiaParathyroid tissueHormone-like peptideAdrenal cortexRat brainNonendocrine tissuesAdrenal medullaBone marrowMessenger ribonucleic acidStomach mucosaHuman osteosarcomaOverexpression of transcriptsRat pituitaryNormal humansAbnormal expression
1987
Purification and properties of a multifunctional calcium/calmodulin-dependent protein kinase from rat pancreas
Cohn J, Kinder B, Jamieson J, Delahunt N, Gorelick F. Purification and properties of a multifunctional calcium/calmodulin-dependent protein kinase from rat pancreas. Biochimica Et Biophysica Acta 1987, 928: 320-331. PMID: 3105599, DOI: 10.1016/0167-4889(87)90192-3.Peer-Reviewed Original ResearchConceptsCalmodulin protein kinaseCalcium/calmodulin-dependent protein kinaseCalmodulin-dependent protein kinaseProtein kinaseMultifunctional calcium/calmodulin-dependent protein kinaseTwo-dimensional gel electrophoresisRibosomal proteinsThreonine residuesLarge subunitCellular functionsRibosomal substratesSubstrate specificityKinaseProteolytic degradationSubunitsGel electrophoresisHydrophobic chromatographyAffinity chromatographyPolyacrylamide gelsCalmodulinPurification procedureGel filtrationEnzyme preparationAutophosphorylationTissue