2000
Kinetic Analysis of the Cyclin-dependent Kinase-activating Kinase (Cak1p) from Budding Yeast*
Enke D, Kaldis P, Solomon M. Kinetic Analysis of the Cyclin-dependent Kinase-activating Kinase (Cak1p) from Budding Yeast*. Journal Of Biological Chemistry 2000, 275: 33267-33271. PMID: 10934199, DOI: 10.1074/jbc.m004748200.Peer-Reviewed Original ResearchThe Effects of Changing the Site of Activating Phosphorylation in CDK2 from Threonine to Serine*
Kaldis P, Cheng A, Solomon M. The Effects of Changing the Site of Activating Phosphorylation in CDK2 from Threonine to Serine*. Journal Of Biological Chemistry 2000, 275: 32578-32584. PMID: 10931829, DOI: 10.1074/jbc.m003212200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionCDC2-CDC28 KinasesCyclin-Dependent Kinase 2Cyclin-Dependent Kinase-Activating KinaseCyclin-Dependent KinasesHumansKineticsMutagenesis, Site-DirectedPhosphorylationProtein Serine-Threonine KinasesRecombinant Fusion ProteinsRecombinant ProteinsSerineSubstrate SpecificityThreonineConceptsWild-type Cdk2Cyclin-dependent kinasesThreonine residuesRNA polymerase IIDegradation of cyclinsHeLa cell extractsCell cycle progressionEssential phosphorylationHuman CDK2Efficient phosphorylationActivating PhosphorylationPolymerase IICyclin HTerminal domainHistone H1Cycle progressionCell extractsPhosphorylationCyclinCDK2General defectCAKKinaseSerineThreonine
1999
The CDK-activating Kinase (Cak1p) from Budding Yeast Has an Unusual ATP-binding Pocket*
Enke D, Kaldis P, Holmes J, Solomon M. The CDK-activating Kinase (Cak1p) from Budding Yeast Has an Unusual ATP-binding Pocket*. Journal Of Biological Chemistry 1999, 274: 1949-1956. PMID: 9890950, DOI: 10.1074/jbc.274.4.1949.Peer-Reviewed Original ResearchConceptsProtein kinaseInvariant lysineMajor cyclin-dependent kinaseLoop regionEssential protein kinaseMost protein kinasesAmino acidsATP-binding pocketCyclin-dependent kinasesBudding YeastCak1pMutagenic analysisATP phosphatesSequence differencesLoop motifKinaseCovalent modificationCore sequenceATP analogYeastCatalytic rateInhibitory drugsLysineMutationsATP
1994
Inactivation of a Cdk2 inhibitor during interleukin 2-induced proliferation of human T lymphocytes.
Firpo E, Koff A, Solomon M, Roberts J. Inactivation of a Cdk2 inhibitor during interleukin 2-induced proliferation of human T lymphocytes. Molecular And Cellular Biology 1994, 14: 4889-4901. PMID: 7516474, PMCID: PMC358861, DOI: 10.1128/mcb.14.7.4889.Peer-Reviewed Original ResearchMeSH KeywordsAdultCDC2-CDC28 KinasesCell CycleCells, CulturedCyclin-Dependent Kinase 2Cyclin-Dependent Kinase Inhibitor p21Cyclin-Dependent KinasesCyclinsDNAEnzyme ActivationFlow CytometryHumansInterleukin-2KineticsLymphocyte ActivationProtein Kinase InhibitorsProtein KinasesProtein Serine-Threonine KinasesReceptors, Antigen, T-CellReceptors, Interleukin-2Recombinant ProteinsRNASignal TransductionTime FactorsT-LymphocytesConceptsCyclin-dependent kinasesMitogenic signalsCyclin-cdk2 complexesCDK2 inhibitorsNegative growth signalsG1 cyclin-CDK complexesCell cycle commitmentCyclin-CDK complexesCyclin-Cdk inhibitorT cell antigen receptorCell proliferationAntigen receptor stimulationCell cycle proteinsInhibitors of CDK2Mitogenic growth factorsGrowth signalsSimilar proteinsBiochemical pathwaysCell cycleCDK inhibitorsCdk2 activationCycle proteinsRestriction pointS phaseCommon target