2014
Highly efficient targeted mutagenesis in axolotl using Cas9 RNA-guided nuclease
Flowers GP, Timberlake AT, Mclean KC, Monaghan JR, Crews CM. Highly efficient targeted mutagenesis in axolotl using Cas9 RNA-guided nuclease. Development 2014, 141: 2165-2171. PMID: 24764077, PMCID: PMC4011087, DOI: 10.1242/dev.105072.Peer-Reviewed Original ResearchMeSH KeywordsAmbystoma mexicanumAnimalsBase SequenceClustered Regularly Interspaced Short Palindromic RepeatsDeoxyribonucleasesEmbryo, NonmammalianGene TargetingGreen Fluorescent ProteinsINDEL MutationMolecular Sequence DataMutagenesis, Site-DirectedRegenerationRNA, Small UntranslatedSequence Homology, Nucleic AcidConceptsUnique regenerative abilityReverse genetics approachUrodele salamandersAxolotl genomeMolecular toolkitCas9 RNADevelopmental phenotypesGenetic approachesNuclease systemLimb regenerationAxolotl Ambystoma mexicanumTransgenic animalsMolecular biologyAmbystoma mexicanumEGFP expressionRegenerative abilityAxolotlRNAMutation frequencySalamandersNucleaseTissue repairIndividual animalsInvaluable insightsVertebrates
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
MEK2 is a kinase related to MEK1 and is differentially expressed in murine tissues.
Brott BK, Alessandrini A, Largaespada DA, Copeland NG, Jenkins NA, Crews CM, Erikson RL. MEK2 is a kinase related to MEK1 and is differentially expressed in murine tissues. Molecular Cancer Research 1993, 4: 921-9. PMID: 8297798.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAnimalsAnimals, NewbornBase SequenceBrainChromosome MappingCloning, MolecularFemaleGene Expression RegulationMaleMAP Kinase Kinase 1MAP Kinase Kinase 2MiceMitogen-Activated Protein Kinase KinasesMolecular Sequence DataNucleic Acid HybridizationProtein Serine-Threonine KinasesProtein-Tyrosine KinasesRecombinant ProteinsRNA, MessengerSequence AnalysisConceptsERK-1Dual-specificity kinaseMurine chromosome 9Substantial sequence homologyErk/MAPMultigene familyLow expression levelsMEK2 proteinsAdult mouse brainSequence homologyAmino terminusDifferent genesERK-2MEK2MEK1Northern analysisChromosome 9Complementary DNAMurine tissuesExpression levelsKinase
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 esterProteinThreonine
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