2022
De novo mutations in the BMP signaling pathway in lambdoid craniosynostosis
Timberlake AT, Kiziltug E, Jin SC, Nelson-Williams C, Loring E, Allocco A, Marlier A, Banka S, Stuart H, Passos-Buenos M, Rosa R, Rogatto S, Tonne E, Stiegler A, Boggon T, Alperovich M, Steinbacher D, Staffenberg D, Flores R, Persing J, Kahle K, Lifton R. De novo mutations in the BMP signaling pathway in lambdoid craniosynostosis. Human Genetics 2022, 142: 21-32. PMID: 35997807, DOI: 10.1007/s00439-022-02477-2.Peer-Reviewed Original ResearchConceptsDe novo mutationsDamaging de novo mutationsSingle-cell RNA sequencing analysisTranscriptional co-repressorTarget sequence recognitionRNA sequencing analysisTranscription factor NfixNovo mutationsEnrichment of mutationsBMP receptorsCo-repressorParent-offspring triosTranscription factorsGenetic gainImplicating perturbationsOsteoblast precursorsPremature suture fusionSequencing analysisMolecular etiologySequence recognitionMissense mutationsMutationsExome sequencingGenetic etiologyOsteoprogenitor cells
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
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 range