1992
Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I
Benfenati F, Valtorta F, Rubenstein J, Gorelick F, Greengard P, Czernik A. Synaptic vesicle-associated Ca2+/calmodulin-dependent protein kinase II is a binding protein for synapsin I. Nature 1992, 359: 417-420. PMID: 1328883, DOI: 10.1038/359417a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrainCalcium-Calmodulin-Dependent Protein KinasesChromatography, High Pressure LiquidElectrophoresis, Gel, Two-DimensionalElectrophoresis, Polyacrylamide GelGene Expression Regulation, EnzymologicMolecular Sequence DataPhosphorylationProtein KinasesRatsReceptors, NeurotransmitterSubstrate SpecificitySynapsinsSynaptic VesiclesConceptsDependent protein kinase IIProtein kinase IIC-terminal regionKinase IISynapsin ISynaptic vesicle-associated phosphoproteinsAmino-terminal regionCarboxy-terminal regionKinase functionRegulatory domainProtein componentsMembrane phospholipidsProteinPhosphoproteinVesiclesEnzymeRegionBindingPhospholipidsDomainSynaptic
1991
Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor
Klueppelberg UG, Gates LK, Gorelick FS, Miller LJ. Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor. Journal Of Biological Chemistry 1991, 266: 2403-2408. PMID: 1989991, DOI: 10.1016/s0021-9258(18)52258-4.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCarbacholCell FractionationChromatography, AffinityChromatography, High Pressure LiquidElectrophoresis, Polyacrylamide GelEnzyme ActivationKineticsMalePancreasPhosphorylationProtein Kinase CRatsRats, Inbred StrainsReceptors, CholecystokininSincalideSolubilityTetradecanoylphorbol AcetateConceptsC activationSodium dodecyl sulfate-polyacrylamide gelsDodecyl sulfate-polyacrylamide gelsProtein kinase C activationPlasma membrane glycoproteinsPhosphorylated MrKinase C activationSulfate-polyacrylamide gelsSerine residuesRegulated mannerAffinity-labeled proteinsMembrane glycoproteinsPhosphorylationReceptor proteinProteinNative formATP poolAffinity resinLectin affinity chromatographyConcentration-dependent mannerDirect activationPancreatic cholecystokinin receptorSubsequent solubilizationReceptorsActivation
1990
Regulated phosphorylation of secretory granule membrane proteins of the rat parotid gland
Marino CR, Castle JD, Gorelick FS. Regulated phosphorylation of secretory granule membrane proteins of the rat parotid gland. American Journal Of Physiology 1990, 259: g70-g77. PMID: 1695488, DOI: 10.1152/ajpgi.1990.259.1.g70.Peer-Reviewed Original ResearchConceptsSecretory granule membrane proteinsIntegral membrane proteinsMembrane proteinsGranule membrane proteinProtein phosphorylation eventsGranule membrane fractionExocrine secretory granulesPhosphorylation eventsSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisRat parotid glandRegulated phosphorylationSulfate-polyacrylamide gel electrophoresisSitu phosphorylationIntact cellsMembrane fractionTime-dependent mannerPhosphorylationProteinSecretory granule fractionParotid lobulesGel electrophoresisProtein antiserumSecretory granulesPhosphoprotein