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
1996
Intersubunit Communication in Tryptophan Synthase by Carbon-13 and Fluorine-19 REDOR NMR †
McDowell L, Lee M, McKay R, Anderson K, Schaefer J. Intersubunit Communication in Tryptophan Synthase by Carbon-13 and Fluorine-19 REDOR NMR †. Biochemistry 1996, 35: 3328-3334. PMID: 8605170, DOI: 10.1021/bi9518297.Peer-Reviewed Original ResearchConceptsProton dipolar decouplingMagic angle spinningLocal electric field gradientsElectric field gradientIsotropic shiftsLigand bindingChemical shiftsNMR spectraConformational gatingEnzyme tryptophan synthaseBeta subunitCarbon-13Dipolar decouplingTryptophan synthaseMother liquorResolved linesConformational rearrangementsBinding of serineNMRLigandField gradientEnzyme complexIntersubunit communicationTyrosine residuesSubunit