2018
Structural Basis for MARK1 Kinase Autoinhibition by Its KA1 Domain
Emptage RP, Lemmon MA, Ferguson KM, Marmorstein R. Structural Basis for MARK1 Kinase Autoinhibition by Its KA1 Domain. Structure 2018, 26: 1137-1143.e3. PMID: 30099988, PMCID: PMC6092042, DOI: 10.1016/j.str.2018.05.008.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesCheckpoint Kinase 1Cloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionGenetic VectorsHumansKineticsModels, MolecularMutationPeptidesProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsProtein Serine-Threonine KinasesRecombinant ProteinsStructural Homology, ProteinSubstrate SpecificityThermodynamicsConceptsKA1 domainSer/Thr protein kinaseKinase structureRelated kinasesUBA domainKinase domainProtein kinaseStructural basisC-terminusUnexpected interfaceC-lobeKinaseΑD helixPotential new avenuesAutoinhibitoryData implicateDomain surfaceDomainNew avenuesYeastAutoinhibitionCrystal structureHelixAlzheimer's diseaseVariants
2009
ErbB2/HER2/Neu resembles an autoinhibited invertebrate EGF receptor
Alvarado D, Klein D, Lemmon M. ErbB2/HER2/Neu resembles an autoinhibited invertebrate EGF receptor. The FASEB Journal 2009, 23: 884.3-884.3. DOI: 10.1096/fasebj.23.1_supplement.884.3.Peer-Reviewed Original ResearchReceptor tyrosine kinase ErbB2Human cancersAutoinhibitory interactionsExtracellular regionInterdomain interactionsEGF receptorErbB2 signalingOrphan receptorOncogenic propertiesHuman EGFRErbB receptorsImportant therapeutic targetErbB2Structural studiesTherapeutic targetNovel aspectsReceptorsAutoinhibitoryAutoinhibitionSignalingOverexpressionImportant implicationsRegulationTherapeutic approachesEGFR
1995
P3-52 IDENTIFICATION OF AUTOINHIBITORY AND CALMODULIN-RINDING DOMAINS ON CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE I
Yokokura H, Picciotto M, Nairn A, Hidaka H. P3-52 IDENTIFICATION OF AUTOINHIBITORY AND CALMODULIN-RINDING DOMAINS ON CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE I. Journal Of Pharmacological Sciences 1995, 67: 259. DOI: 10.1016/s0021-5198(19)47002-9.Peer-Reviewed Original Research
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply