2010
Chemical Inducers of Targeted Protein Degradation*
Raina K, Crews CM. Chemical Inducers of Targeted Protein Degradation*. Journal Of Biological Chemistry 2010, 285: 11057-11060. PMID: 20147751, PMCID: PMC2856979, DOI: 10.1074/jbc.r109.078105.Peer-Reviewed Original ResearchConceptsProtein degradationTargeted Protein DegradationPost-translational levelSubsequent phenotypic analysisProtein functionSelective gene inactivationCellular proteinsCellular phenotypesRNA interferenceGene inactivationSpecific proteinsChemical inducersPhenotypic analysisChemical inductionGenetic mutationsProteinGenesDegradationMutationsPhenotypeDecreased productionMRNAInducerInactivationInduction
2003
Selective inhibitors of the osteoblast proteasome stimulate bone formation in vivo and in vitro
Garrett IR, Chen D, Gutierrez G, Zhao M, Escobedo A, Rossini G, Harris SE, Gallwitz W, Kim KB, Hu S, Crews CM, Mundy GR. Selective inhibitors of the osteoblast proteasome stimulate bone formation in vivo and in vitro. Journal Of Clinical Investigation 2003, 111: 1771-1782. PMID: 12782679, PMCID: PMC156102, DOI: 10.1172/jci16198.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, NorthernBlotting, WesternBone and BonesBone DevelopmentBone Morphogenetic Protein 2Bone Morphogenetic Protein 4Bone Morphogenetic ProteinsCarrier ProteinsCell DivisionCell LineCysteine EndopeptidasesDNADose-Response Relationship, DrugEnzyme-Linked Immunosorbent AssayGenetic VectorsHumansLuciferasesMiceMice, Inbred ICRMultienzyme ComplexesOrgan Culture TechniquesOsteoblastsPromoter Regions, GeneticProteasome Endopeptidase ComplexProteinsRNA, MessengerSkullTranscription, GeneticTransfectionTransforming Growth Factor betaConceptsUbiquitin-proteasome pathwayBMP-4BMP-2Osteoblast differentiationBMP-6 mRNA expressionUbiquitin-proteasome machineryEffect of nogginCatalytic beta subunitsProteasome inhibitorsBMP-2 gene expressionBone morphogenetic protein-2Drosophila homologueMorphogenetic protein-2Gli3 proteinGene expressionBeta subunitProteolytic processingProtein 2Bone formationDifferent inhibitorsEndogenous inhibitorOsteoblastic cellsProteasomeNogginInhibitor-1
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 brainSequenceSchizosaccharomycesMEK1MEKThreonineProtein
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