2008
Melanopsin Ganglion Cells Use a Membrane-Associated Rhabdomeric Phototransduction Cascade
Graham DM, Wong KY, Shapiro P, Frederick C, Pattabiraman K, Berson DM. Melanopsin Ganglion Cells Use a Membrane-Associated Rhabdomeric Phototransduction Cascade. Journal Of Neurophysiology 2008, 99: 2522-2532. PMID: 18305089, DOI: 10.1152/jn.01066.2007.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiosensing TechniquesCalciumCell LineCell MembraneDiglyceridesEgtazic AcidElectrophysiologyEnzyme InhibitorsFluorescent Antibody TechniqueGTP-Binding ProteinsHeparinIn Vitro TechniquesInositol 1,4,5-Trisphosphate ReceptorsLight Signal TransductionMalePatch-Clamp TechniquesPC12 CellsPhotic StimulationProtein Kinase CRatsRats, Sprague-DawleyRetinal Ganglion CellsReverse Transcriptase Polymerase Chain ReactionRod OpsinsThapsigarginConceptsRhabdomeric photoreceptorsCommon evolutionary originEvolutionary originPlasma membraneInvertebrate eyesG proteinsPhototransduction cascadePhototransduction mechanismPhospholipase C.Single-cell RT-PCRMammalian eyePhotoreceptorsCascadeRT-PCRCircadian rhythmCellsStriking similarityMembranePatch-clamp recordingsPhototransductionOpsinProteinPhotopigmentsMelanopsinGanglion cells
2001
A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization
Zhou D, Chen L, Hernandez L, Shears S, Galán J. A Salmonella inositol polyphosphatase acts in conjunction with other bacterial effectors to promote host cell actin cytoskeleton rearrangements and bacterial internalization. Molecular Microbiology 2001, 39: 248-260. PMID: 11136447, DOI: 10.1046/j.1365-2958.2001.02230.x.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBacterial Proteinscdc42 GTP-Binding ProteinCell MembraneCells, CulturedChlorocebus aethiopsCOS CellsCytoskeletonHumansInositol PhosphatesIntestinesJNK Mitogen-Activated Protein KinasesMAP Kinase Kinase 4Mitogen-Activated Protein Kinase KinasesPhosphoric Monoester HydrolasesPhosphorylationSalmonella InfectionsSalmonella typhimuriumTransfectionConceptsActin cytoskeleton rearrangementCytoskeleton rearrangementBacterial entrySecretion systemBacterial internalizationCellular responsesHost cellsRho GTPases signalingProtein secretion systemHost cell actin cytoskeleton rearrangementsHost cellular functionsSpecialized protein secretion systemCdc42-dependent mannerNon-phagocytic cellsBacterial effectorsAbility of SalmonellaInositol phosphataseCellular functionsDefective mutantsBacterial proteinsCo-ordinated functionSalmonella pathogenicityBacterium's abilitySopBPhospholipase C.
1991
Antibodies to the alpha q subfamily of guanine nucleotide-binding regulatory protein alpha subunits attenuate activation of phosphatidylinositol 4,5-bisphosphate hydrolysis by hormones.
Gutowski S, Smrcka A, Nowak L, Wu D, Simon M, Sternweis P. Antibodies to the alpha q subfamily of guanine nucleotide-binding regulatory protein alpha subunits attenuate activation of phosphatidylinositol 4,5-bisphosphate hydrolysis by hormones. Journal Of Biological Chemistry 1991, 266: 20519-20524. PMID: 1657928, DOI: 10.1016/s0021-9258(18)54955-3.Peer-Reviewed Original ResearchMeSH KeywordsAngiotensin IIAnimalsBlotting, WesternBradykininCell LineElectrophoresis, Polyacrylamide GelGTP-Binding ProteinsHormonesHydrolysisImmune SeraPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol Diacylglycerol-LyasePhosphatidylinositol PhosphatesPhosphoric Diester HydrolasesPrecipitin TestsRatsConceptsAlpha qHormonal regulationNG108-15 cellsBisphosphate hydrolysisPhospholipase CRegulatory protein alphaPhospholipase C activityAlpha 11Attenuate activationG protein alpha subunitsAffinity-purified antibodiesProtein alphaProtein alpha subunitsAntibodiesGuanosine 5'Rat liverGq familyCommon carboxyl terminusC activityPhospholipase C.Alpha subunitDetergent extractsAntiserumActivationPeptides
1989
Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein
Crise B, Ruusala A, Zagouras P, Shaw A, Rose J. Oligomerization of glycolipid-anchored and soluble forms of the vesicular stomatitis virus glycoprotein. Journal Of Virology 1989, 63: 5328-5333. PMID: 2555557, PMCID: PMC251199, DOI: 10.1128/jvi.63.12.5328-5333.1989.Peer-Reviewed Original ResearchMeSH KeywordsAcetylglucosaminidaseAmino Acid SequenceBase SequenceCentrifugation, Density GradientCodonElectrophoresis, Polyacrylamide GelGlycolipidsHeLa CellsHumansKineticsMacromolecular SubstancesMannosyl-Glycoprotein Endo-beta-N-AcetylglucosaminidaseMembrane GlycoproteinsMolecular Sequence DataRestriction MappingSolubilityVesicular stomatitis Indiana virusViral Envelope ProteinsConceptsG proteinsWild-type G proteinAmino acidsC-terminal amino acidsVesicular stomatitis virus glycoproteinMutant proteinsCytoplasmic domainAnchor sequenceExtracellular domainGolgi apparatusEndoplasmic reticulumCell surfaceTrimer formationProteinPhospholipase C.TransmembraneVirus glycoproteinSoluble formStructural informationSequenceGlycoproteinNormal transmembraneRate of transportGlycoprotein formThy-1.1
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