2018
Chapter 39 Structure-Function Relationships in the Pancreatic Acinar Cell
Gorelick F, Pandol S, Jamieson J. Chapter 39 Structure-Function Relationships in the Pancreatic Acinar Cell. 2018, 869-894. DOI: 10.1016/b978-0-12-809954-4.00039-6.Peer-Reviewed Original ResearchProtein synthesisEnzyme precursorsRodent acinar cellsAcinar cellsZymogen granulesCritical physiologic functionsSecretion of enzymesStructure-function relationshipsMajor cell typesCellular functionsCell biologistsVesicular transportCell signalingGolgi complexHuman acinar cellsPhysiologic functionEndoplasmic reticulumDuct cellsCell organellesPancreatic acinar cellsCell typesEnzyme proteinDigestive enzymesEnzymeMajor physiologic function
2014
Adenylyl cyclases in the digestive system
Sabbatini ME, Gorelick F, Glaser S. Adenylyl cyclases in the digestive system. Cellular Signalling 2014, 26: 1173-1181. PMID: 24521753, PMCID: PMC4441802, DOI: 10.1016/j.cellsig.2014.01.033.Peer-Reviewed Original Research
2012
Chapter 49 Structure–function Relationships in the Pancreatic Acinar Cell
Gorelick F, Jamieson J. Chapter 49 Structure–function Relationships in the Pancreatic Acinar Cell. 2012, 1341-1360. DOI: 10.1016/b978-0-12-382026-6.00049-x.Peer-Reviewed Original ResearchProtein synthesisZymogen granulesAcinar cellsSecretion of enzymesStructure-function relationshipsNascent proteinsVesicular transportCell signalingEnzyme precursorsGolgi complexEndoplasmic reticulumPancreatic acinar cellsDigestive enzymesEnzymeModel systemExport protein synthesisVectorial mannerApical regionProteinCellsHormonal routesGranulesDigestionDietary proteinExocytosis
2011
Environmental and Genetic Stressors and the Unfolded Protein Response in Exocrine Pancreatic Function – A Hypothesis
Pandol SJ, Gorelick FS, Lugea A. Environmental and Genetic Stressors and the Unfolded Protein Response in Exocrine Pancreatic Function – A Hypothesis. Frontiers In Physiology 2011, 2: 8. PMID: 21483727, PMCID: PMC3070477, DOI: 10.3389/fphys.2011.00008.Peer-Reviewed Original ResearchProtein responseER stressProtein synthetic machineryUnfolded protein responseDigestive enzymesProtein synthetic capacityRecent findingsAdaptive UPREndoplasmic reticulum stressGenetic stressorsSynthetic machineryMammalian organsEnvironmental stressorsProtein synthesisKey pathwaysUPRReticulum stressExocrine cellsExocrine pancreasSynthetic capacityEnzymePathwayPathologic pathwaysStressorsMachinery
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