1993
Raf-1 forms a stable complex with Mek1 and activates Mek1 by serine phosphorylation.
Huang W, Alessandrini A, Crews CM, Erikson RL. Raf-1 forms a stable complex with Mek1 and activates Mek1 by serine phosphorylation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 10947-10951. PMID: 8248196, PMCID: PMC47898, DOI: 10.1073/pnas.90.23.10947.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsEnzyme ActivationIn Vitro TechniquesMacromolecular SubstancesMAP Kinase Kinase 1MiceMitogen-Activated Protein Kinase KinasesPhosphorylationPhosphoserineProtein BindingProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-rafRecombinant Proteins
1992
Phorbol 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 esterProteinThreonine
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