2010
A new bright green‐emitting fluorescent protein – engineered monomeric and dimeric forms
Ilagan RP, Rhoades E, Gruber DF, Kao H, Pieribone VA, Regan L. A new bright green‐emitting fluorescent protein – engineered monomeric and dimeric forms. The FEBS Journal 2010, 277: 1967-1978. PMID: 20345907, PMCID: PMC2855763, DOI: 10.1111/j.1742-4658.2010.07618.x.Peer-Reviewed Original Research
2009
Novel Internal Regions of Fluorescent Proteins Undergo Divergent Evolutionary Patterns
Gruber DF, DeSalle R, Lienau EK, Tchernov D, Pieribone VA, Kao HT. Novel Internal Regions of Fluorescent Proteins Undergo Divergent Evolutionary Patterns. Molecular Biology And Evolution 2009, 26: 2841-2848. PMID: 19770223, PMCID: PMC2775108, DOI: 10.1093/molbev/msp194.Peer-Reviewed Original ResearchConceptsFluorescent proteinStrong positive selection pressureDivergent evolutionary pressuresDivergent evolutionary patternsMolecular phylogenetic analysisSuperfamily of proteinsPositive selection pressureCyan fluorescent proteinGreen fluorescent proteinRed fluorescent proteinNatural functionMolecular evolutionPhylogenetic analysisEvolutionary patternsEvolutionary pressureSelection pressureProtein sequencesMarine organismsCompact proteinGeographic originNovel regionBiological researchProteinOrganismsInternal region
2002
A protein kinase A–dependent molecular switch in synapsins regulates neurite outgrowth
Kao HT, Song HJ, Porton B, Ming GL, Hoh J, Abraham M, Czernik AJ, Pieribone VA, Poo MM, Greengard P. A protein kinase A–dependent molecular switch in synapsins regulates neurite outgrowth. Nature Neuroscience 2002, 5: 431-437. PMID: 11976703, DOI: 10.1038/nn840.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodiesBucladesineCells, CulturedConserved SequenceCyclic AMP-Dependent Protein KinasesEmbryo, NonmammalianEnzyme ActivatorsEnzyme InhibitorsGenes, ReporterMicroinjectionsMolecular Sequence DataMutagenesis, Site-DirectedNeuritesNeuronsPhosphorylationRNA, MessengerSequence Homology, Amino AcidSynapsinsXenopus laevisConceptsProtein kinase ANeurite outgrowthCAMP/protein kinase APhospho-specific antibodiesSingle amino acid residueX. laevis embryosAmino acid residuesDependent molecular switchPhosphorylation of synapsinCyclic AMPEmbryonic neuronal culturesNeuronal cell lineProtein kinaseConstitutive phosphorylationKinase AMolecular approachesMolecular switchAcid residuesLaevis embryosPKA inhibitorPotential molecular approachPhosphorylationGrowth-promoting actionCell linesSynapsin
1999
Regulation of Synaptotagmin I Phosphorylation by Multiple Protein Kinases
Hilfiker S, Pieribone V, Nordstedt C, Greengard P, Czernik A. Regulation of Synaptotagmin I Phosphorylation by Multiple Protein Kinases. Journal Of Neurochemistry 1999, 73: 921-932. PMID: 10461881, DOI: 10.1046/j.1471-4159.1999.0730921.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein KinasesCasein Kinase IICell DifferentiationClathrinConserved SequenceHumansIsoenzymesMembrane GlycoproteinsMolecular Sequence DataNerve Tissue ProteinsPC12 CellsPeptide MappingPhosphoamino AcidsPhosphorylationProtein Kinase CProtein KinasesProtein Serine-Threonine KinasesRatsSynaptosomesSynaptotagmin ISynaptotagminsConceptsProtein kinase CSynaptotagmin IProtein kinaseKinase IISynaptic vesicle life cycleCasein kinase IIMultiple protein kinasesClathrin-coated vesiclesDependent protein kinase IICalcium-triggered exocytosisProtein kinase IICytoplasmic domainTryptic phosphopeptidesPhosphorylation stateRat synaptotagmin IKinase CCalcium sensorPhosphorylationKinaseSame residuesSynaptic vesiclesPC12 cellsPhorbol esterThr112I phosphorylation
1998
Regulation of iron metabolism in the sanguivore lamprey Lampetra fluviatilis
Andersen Ø, Pantopoulos K, Kao H, Muckenthaler M, Youson J, Pieribone V. Regulation of iron metabolism in the sanguivore lamprey Lampetra fluviatilis. The FEBS Journal 1998, 254: 223-229. PMID: 9660174, DOI: 10.1046/j.1432-1327.1998.2540223.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCloning, MolecularConserved SequenceDNA PrimersDNA, ComplementaryEvolution, MolecularFerritinsHumansIn Vitro TechniquesIronIron Regulatory Protein 1Iron Regulatory Protein 2Iron-Regulatory ProteinsIron-Sulfur ProteinsLampreysMolecular Sequence DataPolymerase Chain ReactionProtein ConformationRatsRNA-Binding ProteinsSequence Homology, Amino AcidSequence Homology, Nucleic AcidConceptsIron-responsive elementFerritin iron-responsive elementLamprey Lampetra fluviatilisSequence identityIRE/IRP regulatory systemEvolution of vertebratesLampetra fluviatilisIron regulatory proteinsNorthern blot analysisVertebrate evolutionMammalian extractsAncient lineageExtant representativesCDNA sequenceH-ferritinFerritin cDNASpecific complexUntranslated regionIRP-1Regulatory systemIRP-2Blot analysisLampreyElectrophoretic mobilityKb
1993
Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones.
Risinger C, Blomqvist AG, Lundell I, Lambertsson A, Nässel D, Pieribone VA, Brodin L, Larhammar D. Evolutionary conservation of synaptosome-associated protein 25 kDa (SNAP-25) shown by Drosophila and Torpedo cDNA clones. Journal Of Biological Chemistry 1993, 268: 24408-24414. PMID: 8226991, DOI: 10.1016/s0021-9258(20)80540-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBiological EvolutionBlotting, NorthernConserved SequenceDNA, ComplementaryDrosophila melanogasterDrosophila ProteinsIn Situ HybridizationMembrane ProteinsMolecular Sequence DataNerve Tissue ProteinsSequence Homology, Amino AcidSynaptosomal-Associated Protein 25TorpedoConceptsVesicle dockingCDNA clonesMembrane fusionSNAP-25Basic molecular machineryDisplay sequence similarityMembrane-spanning regionSynaptic vesicle dockingDegree of conservationAmino acid identityRay Torpedo marmorataEvolutionary conservationTorpedo proteinDrosophila melanogasterMolecular machinerySequence similarityMembrane attachmentAcid identityNeuron-specific proteinCysteine residuesDrosophilaSynaptobrevinProtein 25Situ hybridizationProtein