2014
Temporal resolution of protein signaling (473.1)
Anderson K, Sohl C, Luo B, Mo S, Kim Y, Apetri M, Lew E, Furdui C, Schlessinger J. Temporal resolution of protein signaling (473.1). The FASEB Journal 2014, 28 DOI: 10.1096/fasebj.28.1_supplement.473.1.Peer-Reviewed Original ResearchReceptor tyrosine kinasesProtein signalingMultiple signal transduction pathwaysSpecific tyrosine residuesSignal transduction pathwaysSingle receptor tyrosine kinaseCellular processesTyrosine autophosphorylationOncogenic formsTransduction pathwaysRTK activityPhosphorylation modificationMutant formsReceptor dimerizationTyrosine residuesLigand bindingMolecular mechanismsTyrosine kinaseFunctional understandingOncogenic behaviorMolecular signaturesMultiple developmental disordersEarly dynamic eventsCell proliferationEssential role
2000
Insights into the HER-2 Receptor Tyrosine Kinase Mechanism and Substrate Specificity Using a Transient Kinetic Analysis †
Jan A, Johnson E, Diamonti A, Carraway K, Anderson K. Insights into the HER-2 Receptor Tyrosine Kinase Mechanism and Substrate Specificity Using a Transient Kinetic Analysis †. Biochemistry 2000, 39: 9786-9803. PMID: 10933796, DOI: 10.1021/bi9924922.Peer-Reviewed Original ResearchConceptsReceptor tyrosine kinasesRecombinant proteinsTyrosine kinaseSerine/threonine kinaseProtein kinase familyReceptor-like proteinCatalytic mechanismDegenerate peptide libraryStopped-flow fluorescence studiesIntracellular tyrosine kinase domainTyrosine kinase mechanismTyrosine kinase domainState kinetic analysisThreonine kinaseKinase familyCatalytic subunitKinase domainPhosphorylation stateSubstrate specificityProtein modificationNucleotide interactionsKinase mechanismConformational changesTransient kinetic investigationsHER-2/erbB