2002
Mechanistic Characterization of Toxoplasma gondiiThymidylate Synthase (TS-DHFR)-Dihydrofolate Reductase EVIDENCE FOR A TS INTERMEDIATE AND TS HALF-SITES REACTIVITY*
Johnson E, Hinz W, Atreya C, Maley F, Anderson K. Mechanistic Characterization of Toxoplasma gondiiThymidylate Synthase (TS-DHFR)-Dihydrofolate Reductase EVIDENCE FOR A TS INTERMEDIATE AND TS HALF-SITES REACTIVITY*. Journal Of Biological Chemistry 2002, 277: 43126-43136. PMID: 12192007, DOI: 10.1074/jbc.m206523200.Peer-Reviewed Original Research
2001
Toxicity of Antiviral Nucleoside Analogs and the Human Mitochondrial DNA Polymerase*
Johnson A, Ray A, Hanes J, Suo Z, Colacino J, Anderson K, Johnson K. Toxicity of Antiviral Nucleoside Analogs and the Human Mitochondrial DNA Polymerase*. Journal Of Biological Chemistry 2001, 276: 40847-40857. PMID: 11526116, DOI: 10.1074/jbc.m106743200.Peer-Reviewed Original Research
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
1999
Using loop length variants to dissect the folding pathway of a four-helix-bundle protein 11Edited by P. E. Wright
Nagi A, Anderson K, Regan L. Using loop length variants to dissect the folding pathway of a four-helix-bundle protein 11Edited by P. E. Wright. Journal Of Molecular Biology 1999, 286: 257-265. PMID: 9931264, DOI: 10.1006/jmbi.1998.2474.Peer-Reviewed Original ResearchMeSH KeywordsEscherichia coliKineticsMutationProtein DenaturationProtein FoldingProtein Structure, SecondaryRecombinant ProteinsConceptsFour-helix bundle proteinWild-type proteinHelix-connecting loopsProtein folding pathwaysMutant proteinsTwo-residue loopSame general mechanismHelix monomersLength variantsFolding pathwaysE. WrightDimeric intermediateProteinGeneral mechanismFoldingPolyglycine linkerPathwayGlycine linkerLinkerLoop lengthAlterations
1998
Structure and Functional Relationships in Human pur H
Beardsley G, Rayl E, Gunn K, Moroson B, Seow H, Anderson K, Vergis J, Fleming K, Worland S, Condon B, Davies J. Structure and Functional Relationships in Human pur H. Advances In Experimental Medicine And Biology 1998, 431: 221-226. PMID: 9598063, DOI: 10.1007/978-1-4615-5381-6_43.Peer-Reviewed Original Research
1997
RNA Dependent DNA Replication Fidelity of HIV-1 Reverse Transcriptase: Evidence of Discrimination between DNA and RNA Substrates †
Kerr S, Anderson K. RNA Dependent DNA Replication Fidelity of HIV-1 Reverse Transcriptase: Evidence of Discrimination between DNA and RNA Substrates †. Biochemistry 1997, 36: 14056-14063. PMID: 9369477, DOI: 10.1021/bi971385+.Peer-Reviewed Original ResearchPre-Steady-State Kinetic Analysis of the Trichodiene Synthase Reaction Pathway †
Cane D, Chiu H, Liang P, Anderson K. Pre-Steady-State Kinetic Analysis of the Trichodiene Synthase Reaction Pathway †. Biochemistry 1997, 36: 8332-8339. PMID: 9204880, DOI: 10.1021/bi963018o.Peer-Reviewed Original ResearchConceptsChemical catalysisReaction pathwaysRapid chemical quench methodsActive siteSteady-state catalytic rateSingle turnover reactionsRate constant kcatEnzyme active siteNerolidyl diphosphateDeuterium isotope effectSingle-turnover experimentsSingle turnover rateState kinetic analysisTurnover reactionsDetection limitCatalytic rateOverall reactionSteady-state releaseIsotope effectRate-limiting stepState kineticsCatalysisReactionQuench methodSynthase reaction
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
1995
Kinetic Characterization of Channel Impaired Mutants of Tryptophan Synthase (∗)
Anderson K, Kim A, Quillen J, Sayers E, Yang X, Miles E. Kinetic Characterization of Channel Impaired Mutants of Tryptophan Synthase (∗). Journal Of Biological Chemistry 1995, 270: 29936-29944. PMID: 8530393, DOI: 10.1074/jbc.270.50.29936.Peer-Reviewed Original ResearchBinding SitesCarbon RadioisotopesGlycerophosphatesIndolesKineticsMacromolecular SubstancesMathematicsModels, TheoreticalMutagenesis, Site-DirectedPoint MutationProtein ConformationRadioisotope Dilution TechniqueRecombinant ProteinsSalmonella typhimuriumSerineStructure-Activity RelationshipTryptophan SynthaseReevaluating glyphosate as a transition-state inhibitor of EPSP synthase: identification of an EPSP synthase.EPSP.glyphosate ternary complex.
Sammons R, Gruys K, Anderson K, Johnson K, Sikorski J. Reevaluating glyphosate as a transition-state inhibitor of EPSP synthase: identification of an EPSP synthase.EPSP.glyphosate ternary complex. Biochemistry 1995, 34: 6433-40. PMID: 7756274, DOI: 10.1021/bi00019a024.Peer-Reviewed Original ResearchConceptsEPSP synthaseTernary complexShikimate 3-phosphateSteady-state kineticsEnzyme active siteTransition-state analogSubstrate turnoverSynthase reactionTransition-state inhibitorsEnzymeAssociated with PEPUncompetitive inhibitorBinding resultsSynthaseActive siteFluorescence titration experimentsShikimateOxonium ionsTurnoverInteraction of glyphosateTitration experimentsCrystallization and preliminary X‐ray investigation of the recombinant Trypanosoma brucei rhodesiense calmodulin
El‐Sayed N, Patton C, Harkins P, Fox R, Anderson K. Crystallization and preliminary X‐ray investigation of the recombinant Trypanosoma brucei rhodesiense calmodulin. Proteins Structure Function And Bioinformatics 1995, 21: 354-357. PMID: 7567957, DOI: 10.1002/prot.340210409.Peer-Reviewed Original ResearchConceptsPreliminary X-ray investigationUnit cell dimensionsMolecular replacement methodX-ray investigationsSpace groupAsymmetric unitCrystal structureCell dimensionsRecombinant calmodulinMolecular massCrystalUnit cellTrypanosoma brucei rhodesienseVapor diffusionReplacement methodM cacodylate bufferCalmodulinStructureExpression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A Binding
Hoffmann K, Kakalis L, Anderson K, Armitage I, Handschumacher R. Expression of Human Cyclophilin‐40 and the Effect of the His141→Trp Mutation on Catalysis and Cyclosporin A Binding. The FEBS Journal 1995, 229: 188-193. PMID: 7744028, DOI: 10.1111/j.1432-1033.1995.0188l.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid IsomerasesBase SequenceBinding SitesCarrier ProteinsCyclophilin DCyclophilinsCyclosporineEnzyme ActivationEscherichia coliHumansMagnetic Resonance SpectroscopyModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPeptidylprolyl IsomeraseProtein BindingRecombinant ProteinsConceptsCyP-40Isomerase activityPeptidyl-prolyl cis-trans isomerase activityHuman cyclophilin-40PGEX-3X expression vectorSite-directed mutagenesisMutant proteinsCyclophilin 40Intrinsic isomerase activityNMR difference spectroscopySuccinyl-AlaExpression vectorHistidine residuesEscherichia coliTryptophan residuesProteinCyclophilinMolecular modellingAla-ProResiduesGel filtrationWeak affinityBindingHigh affinityAffinity matrix
1992
Mechanism and fidelity of HIV reverse transcriptase.
Kati W, Johnson K, Jerva L, Anderson K. Mechanism and fidelity of HIV reverse transcriptase. Journal Of Biological Chemistry 1992, 267: 25988-25997. PMID: 1281479, DOI: 10.1016/s0021-9258(18)35706-5.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding SitesDeoxyribonucleotidesDNAEscherichia coliHIV Reverse TranscriptaseHIV-1KineticsModels, BiologicalMolecular Sequence DataNucleic Acid HeteroduplexesOligodeoxyribonucleotidesOligoribonucleotidesRecombinant ProteinsRNARNA-Directed DNA PolymeraseSubstrate SpecificityTemplates, GeneticConceptsRNA templateRNA/DNA heteroduplexesRNA cleavageDuplex DNAPre-steady state burstRate of DNA polymerizationDNA-dependent polymerasesRNA cleavage productsBinding of dNTPSingle nucleotide incorporationRibonuclease domainRNA-dependentVirus reverse transcriptasePublished crystal structureNucleotide incorporationNucleoside triphosphatesHuman immunodeficiency virus reverse transcriptaseDNTP complexDissociation of DNADNA polymerizationReverse transcriptaseDATPHeteroduplexCleavage productsRNA