1994
An intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal.
Okamoto T, Murayama Y, Strittmatter SM, Katada T, Asano S, Ogata E, Nishimoto I. An intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal. Journal Of Biological Chemistry 1994, 269: 13756-13759. PMID: 8188651, DOI: 10.1016/s0021-9258(17)36711-x.Peer-Reviewed Original ResearchConceptsIntrinsic guanineHeterotrimeric G-protein familyG proteinsReceptor signalsGi2 alphaG protein familyProto-oncogene productProtein familyC-terminusResidues 338Alpha subunitReceptor polypeptideBasal activityAlpha activationPolypeptideGuanineReceptor stimulationAlphaExchange inhibitorInhibitorsReceptorsTerminusSubunitsProteinGi2
1992
Palmitoylation alters protein activity: blockade of G(o) stimulation by GAP‐43.
Sudo Y, Valenzuela D, Beck‐Sickinger A, Fishman MC, Strittmatter SM. Palmitoylation alters protein activity: blockade of G(o) stimulation by GAP‐43. The EMBO Journal 1992, 11: 2095-2102. PMID: 1534749, PMCID: PMC556676, DOI: 10.1002/j.1460-2075.1992.tb05268.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCattleGAP-43 ProteinGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)KineticsMembrane GlycoproteinsNerve Tissue ProteinsPalmitic AcidPalmitic AcidsPeptide FragmentsPhosphoproteinsProtein BindingConceptsHeterotrimeric G proteinsProtein-protein interactionsMembrane associationFatty acylationGAP-43Cysteine residuesHydrophobicity of proteinsN-terminusAddition of palmitateG proteinsPalmitoylationNeuronal proteinsProteinGAP-43 proteinTerminal peptidesActive poolResiduesPeptidesCysteineMembraneActivityActivationPool
1991
An intracellular guanine nucleotide release protein for G0. GAP-43 stimulates isolated alpha subunits by a novel mechanism.
Strittmatter SM, Valenzuela D, Sudo Y, Linder ME, Fishman MC. An intracellular guanine nucleotide release protein for G0. GAP-43 stimulates isolated alpha subunits by a novel mechanism. Journal Of Biological Chemistry 1991, 266: 22465-22471. PMID: 1834672, DOI: 10.1016/s0021-9258(18)54595-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainCattleGAP-43 ProteinGTP-Binding ProteinsGuanine NucleotidesGuanosine 5'-O-(3-Thiotriphosphate)Guanosine DiphosphateGuanosine TriphosphateKineticsLiposomesMacromolecular SubstancesMembrane GlycoproteinsNADNerve Tissue ProteinsPertussis ToxinPhosphatidylcholinesPhosphoproteinsProtein BindingRatsRecombinant ProteinsVirulence Factors, BordetellaConceptsG proteinsMembrane-associated G proteinsGAP-43Novel mechanismG protein-coupled receptorsG protein-coupled membrane receptorsIntracellular guanine nucleotidesGuanine nucleotidesProtein-coupled receptorsCytosolic faceGTP gamma S bindingRegions of neuronsGTPase activityGDP releaseAlpha s.Alpha subunitAlpha i1Alpha oMembrane receptorsNeuronal proteinsBeta gammaGTP gamma SProteinGamma S bindingGrowth cones
1990
G0 is a major growth cone protein subject to regulation by GAP-43
Strittmatter S, Valenzuela D, Kennedy T, Neer E, Fishman M. G0 is a major growth cone protein subject to regulation by GAP-43. Nature 1990, 344: 836-841. PMID: 2158629, DOI: 10.1038/344836a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBrain ChemistryCell MembraneGAP-43 ProteinGrowth SubstancesGTP-Binding ProteinsGuanosine 5'-O-(3-Thiotriphosphate)Guanosine TriphosphateMembrane GlycoproteinsMolecular Sequence DataMolecular WeightNerve Tissue ProteinsPeptide FragmentsProtein BindingRatsReceptors, Cell SurfaceReceptors, NeurotransmitterSequence Homology, Nucleic AcidSignal TransductionThionucleotidesConceptsTransmembrane receptorsNeuronal growth cone membraneAmino-terminal domainGTP-binding proteinsGrowth cone membraneExtracellular signalsGrowth cone proteinGAP-43Cone membraneGrowth conesCone proteinNeuronal growthProteinS bindingMajor componentG0ReceptorsGTPRegulationIntracellularBindingMembraneDomain