2008
Disruption of the EGFR E884–R958 ion pair conserved in the human kinome differentially alters signaling and inhibitor sensitivity
Tang Z, Jiang S, Du R, Petri E, El-Telbany A, Chan P, Kijima T, Dietrich S, Matsui K, Kobayashi M, Sasada S, Okamoto N, Suzuki H, Kawahara K, Iwasaki T, Nakagawa K, Kawase I, Christensen J, Hirashima T, Halmos B, Salgia R, Boggon T, Kern J, Ma P. Disruption of the EGFR E884–R958 ion pair conserved in the human kinome differentially alters signaling and inhibitor sensitivity. Oncogene 2008, 28: 518-533. PMID: 19015641, PMCID: PMC2633425, DOI: 10.1038/onc.2008.411.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAMP-Activated Protein Kinase KinasesAnimalsChlorocebus aethiopsCOS CellsErbB ReceptorsErlotinib HydrochlorideFocal Adhesion Kinase 1HumansIndolesLung NeoplasmsMAP Kinase Signaling SystemMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mutation, MissensePiperazinesProtein ConformationProtein Kinase InhibitorsProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-kitProto-Oncogene Proteins c-metProto-Oncogene Proteins c-retQuinazolinesReceptors, Growth FactorSulfonamidesConceptsHuman kinomeEpidermal growth factor receptorKinase substrate recognitionInhibitor sensitivityCancer-associated mutationsSystematic bioinformatics analysisTumor suppressor geneSmall molecule inhibitorsSubstrate recognitionProtein kinaseGrowth factor receptorBioinformatics analysisHomologous residuesDownstream signalingSequence analysisLysine residuesKinomeC-lobeConformational changesFamily inhibitorsMutation cataloguesAdjacent residuesMET inhibitor SU11274Factor receptorMutations
2000
Screening for phasing atoms in protein crystallography
Boggon T, Shapiro L. Screening for phasing atoms in protein crystallography. Structure 2000, 8: r143-r149. PMID: 10903954, DOI: 10.1016/s0969-2126(00)00168-4.Peer-Reviewed Original ResearchSynchrotron X‐ray reciprocal‐space mapping, topography and diffraction resolution studies of macromolecular crystal quality
Boggon T, Helliwell J, Judge R, Olczak A, Siddons D, Snell E, Stojanoff V. Synchrotron X‐ray reciprocal‐space mapping, topography and diffraction resolution studies of macromolecular crystal quality. Acta Crystallographica Section D, Structural Biology 2000, 56: 868-880. PMID: 10930833, DOI: 10.1107/s0907444900005837.Peer-Reviewed Original Research
1999
Implication of Tubby Proteins as Transcription Factors by Structure-Based Functional Analysis
Boggon T, Shan W, Santagata S, Myers S, Shapiro L. Implication of Tubby Proteins as Transcription Factors by Structure-Based Functional Analysis. Science 1999, 286: 2119-2125. PMID: 10591637, DOI: 10.1126/science.286.5447.2119.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAlternative SplicingAmino Acid SequenceAnimalsCell LineCell NucleusCrystallography, X-RayDNAEye ProteinsHumansIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryProteinsRecombinant ProteinsSequence AlignmentTranscription FactorsTranscriptional ActivationConceptsTubby-like proteinsTubby proteinTranscription factorsBipartite transcription factorDisease phenotypeMulticellular organismsProtein familyBiochemical functionsBiological functionsFunctional analysisStructural cluesCore domainUnique familyProteinGenetic mutationsTubbyPhenotypeRetinal degenerationFamilyMammalsOrganismsVital roleCrystal structureMutationsBroad rangeBound‐solvent structures for microgravity‐, ground control‐, gel‐ and microbatch‐grown hen egg‐white lysozyme crystals at 1.8 Å resolution
Dong J, Boggon T, Chayen N, Raftery J, Bi R, Helliwell J. Bound‐solvent structures for microgravity‐, ground control‐, gel‐ and microbatch‐grown hen egg‐white lysozyme crystals at 1.8 Å resolution. Acta Crystallographica Section D, Structural Biology 1999, 55: 745-752. PMID: 10089304, DOI: 10.1107/s0907444998016047.Peer-Reviewed Original ResearchConceptsHen egg white lysozymeX-ray dataAdvanced Protein Crystallization FacilityDifferent crystallization methodsLysozyme crystalsCrystal growth environmentProtein structureHen egg-white lysozyme crystalsEgg white lysozymeCrystallization methodProtein crystalsGelÅ resolutionCrystalsMicrogravity Spacelab (LMS) missionCrystallizationCrystallization FacilityAgarose gelStructureDiffusion methodPhase boundaryPhysics statesOilNumber of methodsLysozymePurification, crystallization and initial X‐ray analysis of the C1 subunit of the astaxanthin protein, V600, of the chondrophore Velella velella
Chayen N, Boggon T, Raftery J, Helliwell J, Zagalsky P. Purification, crystallization and initial X‐ray analysis of the C1 subunit of the astaxanthin protein, V600, of the chondrophore Velella velella. Acta Crystallographica Section D, Structural Biology 1999, 55: 266-268. PMID: 10089420, DOI: 10.1107/s0907444998006908.Peer-Reviewed Original Research