1992
The Primary Structure of MEK, a Protein Kinase that Phosphorylates the ERK Gene Product
Crews C, Alessandrini A, Erikson R. The Primary Structure of MEK, a Protein Kinase that Phosphorylates the ERK Gene Product. Science 1992, 258: 478-480. PMID: 1411546, DOI: 10.1126/science.1411546.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCalcium-Calmodulin-Dependent Protein KinasesGene ExpressionMAP Kinase Kinase 1MiceMitogen-Activated Protein Kinase KinasesMolecular Sequence DataPhosphorylationProtein KinasesProtein Serine-Threonine KinasesProteinsProtein-Tyrosine KinasesRNA, MessengerSequence AlignmentConceptsExtracellular signal-regulated kinaseProtein kinaseMAP kinaseGene productsCritical protein kinaseSignal-regulated kinaseComplementary DNA sequenceMEK genesExtracellular signalsERK kinaseMultiple biochemical signalsDNA sequencesBiochemical signalsPrimary structureKinaseAmino acidsEnzymatic activityGenesMurine brainSequenceSchizosaccharomycesMEK1MEKThreonineProteinPhorbol ester stimulates a protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product.
Alessandrini A, Crews CM, Erikson RL. Phorbol ester stimulates a protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 8200-8204. PMID: 1518847, PMCID: PMC49885, DOI: 10.1073/pnas.89.17.8200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBase SequenceCells, CulturedIn Vitro TechniquesMiceMitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesPeptide MappingPhorbol EstersPhosphorylationPhosphothreonineProtein KinasesProtein-Tyrosine KinasesT-LymphocytesConceptsProtein kinase activityProtein kinaseGene productsKinase activityMyelin basic protein kinaseMyelin basic protein kinase activityMultiple extracellular signalsUpstream protein kinaseWild-type proteinIdentification of proteinsAmino acid residuesSame amino acid residuesERK-1 proteinDegree of phosphorylationReversible phosphorylationThreonine sitesThreonine kinaseExtracellular signalsTyrosine sitesAcid residuesKinasePhosphorylationPhorbol esterProteinThreoninePurification of a murine protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product: relationship to the fission yeast byr1 gene product.
Crews CM, Erikson RL. Purification of a murine protein-tyrosine/threonine kinase that phosphorylates and activates the Erk-1 gene product: relationship to the fission yeast byr1 gene product. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 8205-8209. PMID: 1381507, PMCID: PMC49886, DOI: 10.1073/pnas.89.17.8205.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsEnzyme ActivationFungal ProteinsGenesMiceMitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesMolecular Sequence DataPeptide FragmentsPhosphorylationPhosphoserinePhosphothreoninePhosphotyrosineProtein KinasesRecombinant ProteinsSequence AlignmentTyrosineConceptsGene productsProtein kinaseSerine/threonine phosphatase 2AMyelin basic protein kinaseProtein tyrosine phosphatase 1B.MAPK/ERK kinaseSignal transduction mechanismsPossible signal transduction mechanismsERK-1 proteinSte7 genePhosphatase 2AThreonine kinaseERK kinaseERK-1Tyrosine residuesSequence analysisKinaseTransduction mechanismsMEKTrypsin digestionProteinByr1PurificationGenesLesser extentErks: their fifteen minutes has arrived.
Crews CM, Alessandrini A, Erikson RL. Erks: their fifteen minutes has arrived. Molecular Cancer Research 1992, 3: 135-42. PMID: 1504018.Peer-Reviewed Original ResearchConceptsProtein kinaseCell cycleYeast cellsTyrosine kinase signalsERK protein kinasesSea star oocytesSpecific transcriptional factorsAmino acid residuesSpecific differentiation eventsG0-G1 transitionExtracellular signalsKinase signalsPhosphorylation signalsSignal transductionTranscriptional changesS6 kinaseRaf-1Differentiation eventsMitogenic signalsYeast enzymeGene productsMicrotubule reorganizationDownstream targetsTranscriptional factorsEGF receptor
1991
Mouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine.
Crews CM, Alessandrini AA, Erikson RL. Mouse Erk-1 gene product is a serine/threonine protein kinase that has the potential to phosphorylate tyrosine. Proceedings Of The National Academy Of Sciences Of The United States Of America 1991, 88: 8845-8849. PMID: 1717989, PMCID: PMC52607, DOI: 10.1073/pnas.88.19.8845.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBlotting, WesternCalcium-Calmodulin-Dependent Protein KinasesCloning, MolecularMiceMolecular Sequence DataMolecular WeightMyelin Basic ProteinOligonucleotidesPhosphoprotein PhosphatasesPhosphoproteinsPhosphotyrosinePolymerase Chain ReactionProtein KinasesProtein Phosphatase 2Protein Serine-Threonine KinasesRecombinant ProteinsTyrosineConceptsSerine/threonine protein kinaseERK-1Serine/threonine kinaseRibosomal protein S6 kinaseSubstrate phosphorylation sitesThreonine protein kinaseProtein S6 kinaseSame substrate specificityPhosphatase 2AThreonine residuesThreonine kinaseActive kinasePhosphorylation sitesERK1 proteinS6 kinaseProtein kinaseSequence dataBacterial expressionSubstrate specificityGene productsKinase activityPhosphatase 1BKinaseRat cellsProtein
1989
Sequence and expression of chicken and mouse rsk: homologs of Xenopus laevis ribosomal S6 kinase.
Alcorta DA, Crews CM, Sweet LJ, Bankston L, Jones SW, Erikson RL. Sequence and expression of chicken and mouse rsk: homologs of Xenopus laevis ribosomal S6 kinase. Molecular And Cellular Biology 1989, 9: 3850-3859. PMID: 2779569, PMCID: PMC362446, DOI: 10.1128/mcb.9.9.3850.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceChickensDNAGene Expression RegulationIn Vitro TechniquesMiceMolecular Sequence DataProtein BiosynthesisProtein KinasesRibosomal Protein S6Ribosomal Protein S6 KinasesRibosomal ProteinsRNA, MessengerSequence Homology, Nucleic AcidSpecies SpecificityTranscription, GeneticXenopus laevisConceptsRibosomal S6 kinaseMouse cDNAS6 kinaseCatalytic subunitKilobase pairsDistinct kinase domainsCyclic AMP-dependent protein kinaseAMP-dependent protein kinaseAmino acidsFamily of genesXenopus laevis cDNAIsolation of cDNAsPhosphorylase b kinaseExpression of chickenMRNA transcript sizeGenomic organizationXenopus proteinMolecular cloningMouse homologKinase domainProtein kinaseApparent molecular weightTranscript sizeB kinaseKinase gene