1996
Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis.
Crews C, Lane W, Schreiber S. Didemnin binds to the protein palmitoyl thioesterase responsible for infantile neuronal ceroid lipofuscinosis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 4316-4319. PMID: 8633062, PMCID: PMC39533, DOI: 10.1073/pnas.93.9.4316.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBrainCattleConsensus SequenceDepsipeptidesDNA PrimersGTP-Binding ProteinsHumansInfantMolecular Sequence DataMolecular WeightNeuronal Ceroid-LipofuscinosesPeptides, CyclicPolymerase Chain ReactionProtein BindingRatsSequence Homology, Amino AcidThiolester HydrolasesConceptsPalmitoyl-protein thioesteraseInfantile neuronal ceroid lipofuscinosisNeuronal ceroid lipofuscinosisGTP-dependent bindingProgressive loss of brain functionDidemnin BG alpha s subunitProtein synthesis inhibitory activityProteins in vitroCeroid lipofuscinosisSequence similarityPalmitoyl thioesteraseProtein thioesteraseHuman cDNAEF1-alphaS subunitsBrain lysatesH-rasThioesteraseProteinBiological activityLipofuscinosisCDNADidemninInhibitory activity
1993
Reconstitution of the Raf-1-MEK-ERK signal transduction pathway in vitro.
Macdonald SG, Crews CM, Wu L, Driller J, Clark R, Erikson RL, McCormick F. Reconstitution of the Raf-1-MEK-ERK signal transduction pathway in vitro. Molecular And Cellular Biology 1993, 13: 6615-6620. PMID: 8413257, PMCID: PMC364724, DOI: 10.1128/mcb.13.11.6615.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBaculoviridaeCell LineCloning, MolecularGenes, rasGenes, srcHumansMAP Kinase Kinase 1Mitogen-Activated Protein Kinase KinasesMothsMutagenesis, Site-DirectedPhosphorylationPolymerase Chain ReactionProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-rafProto-Oncogene Proteins p21(ras)Recombinant ProteinsSignal TransductionTransfectionConceptsRaf-1V-SrcV-rasSf9 cellsGlutathione S-transferase fusion proteinS-transferase fusion proteinSerine/threonine kinaseProtein kinase C phosphorylationKinase-inactive versionERK signal transduction pathwayKinase-inactive mutantRaf-1 phosphorylationKinase C phosphorylationSignal transduction pathwaysRaf-1-MEKActivation of MEKTyrosine kinase oncogenesProtein kinase CAutokinase activityFunction upstreamThreonine kinaseDirect substrateMEK activationTransduction pathwaysC phosphorylation
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