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 ResearchMeSH KeywordsAnimalsCell DifferentiationCraniosynostosesMiceMutationNFI Transcription FactorsSignal TransductionTranscription FactorsConceptsDe 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
2001
G-Protein Signaling Through Tubby Proteins
Santagata S, Boggon T, Baird C, Gomez C, Zhao J, Shan W, Myszka D, Shapiro L. G-Protein Signaling Through Tubby Proteins. Science 2001, 292: 2041-2050. PMID: 11375483, DOI: 10.1126/science.1061233.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAdaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsCell MembraneCell NucleusCells, CulturedCrystallography, X-RayGene Expression RegulationGTP-Binding Protein alpha Subunits, Gq-G11Heterotrimeric GTP-Binding ProteinsHumansIntercellular Signaling Peptides and ProteinsIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane LipidsMiceModels, BiologicalMolecular Sequence DataNuclear Localization SignalsObesityPhosphatidylinositol 4,5-DiphosphatePhosphatidylinositol PhosphatesPhospholipase C betaPhosphorylationProtein Structure, TertiaryProteinsReceptor, Serotonin, 5-HT2CReceptors, MuscarinicReceptors, SerotoninRecombinant Fusion ProteinsSignal TransductionTranscription FactorsType C PhospholipasesConceptsTubby-like protein 3G protein signalingTubby proteinTubby domainTranscription regulatorsPlasma membranePhospholipase C-betaReceptor-mediated activationHeterotrimeric GTPSignal transductionGene expressionMolecular mechanismsTubbyC betaCarboxyl terminalCell nucleiMaturity-onset obesityProteinX-ray crystallographyProtein 3SignalingRegulatorMembranePhosphatidylinositolTransduction
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