Featured Publications
A Ribosomopathy Reveals Decoding Defective Ribosomes Driving Human Dysmorphism
Paolini NA, Attwood M, Sondalle SB, dos Santos Vieira C, van Adrichem AM, di Summa FM, O’Donohue M, Gleizes PE, Rachuri S, Briggs JW, Fischer R, Ratcliffe PJ, Wlodarski MW, Houtkooper RH, von Lindern M, Kuijpers TW, Dinman JD, Baserga SJ, Cockman ME, MacInnes AW. A Ribosomopathy Reveals Decoding Defective Ribosomes Driving Human Dysmorphism. American Journal Of Human Genetics 2017, 100: 506-522. PMID: 28257692, PMCID: PMC5339345, DOI: 10.1016/j.ajhg.2017.01.034.Peer-Reviewed Original ResearchMeSH KeywordsAutism Spectrum DisorderCarrier ProteinsCells, CulturedChildChild, PreschoolCodonDevelopmental DisabilitiesExomeFemaleFibroblastsGenetic VariationHearing LossHumansIntellectual DisabilityMaleMicrocephalyMutationMutation, MissenseNuclear ProteinsOxidative StressProtein BiosynthesisRibosomal ProteinsRibosomesSequence AlignmentSequence Analysis, DNAConceptsMRNA translationRibosomal protein gene mutationsRP gene mutationsAmino acid substitutionsDefective ribosomesSubunit biogenesisCodon translationRibosomal subunitPolysome formationGene mutationsProline residuesDe novo missense mutationsAcid substitutionsLoop regionProtein synthesisBone marrow failurePhenylalanine residuesNovo missense mutationMechanistic distinctionsPrimary cellsMissense mutationsRibosomopathiesProtein gene mutationsUnrelated individualsMutationsHuman diseases of the SSU processome
Sondalle SB, Baserga SJ. Human diseases of the SSU processome. Biochimica Et Biophysica Acta 2013, 1842: 758-764. PMID: 24240090, PMCID: PMC4058823, DOI: 10.1016/j.bbadis.2013.11.004.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsNorth American Indian childhood cirrhosisSSU processome componentsSSU processomeBowen-Conradi syndromeHuman diseasesSmall subunit processomeProduction of ribosomesRibosomal protein assemblyLarge ribonucleoproteinRibosome biogenesisFunctional ribosomesEukaryotic cellsProcessomeProtein assembliesCellular machinesRibosomesRNA cleavageProtein synthesisRibonucleoproteinEukaryotesCirhinAssemblyRRNAsRibosomopathiesBiogenesisChemical Derivatization of Peptide Carboxyl Groups for Highly Efficient Electron Transfer Dissociation
Frey BL, Ladror DT, Sondalle SB, Krusemark CJ, Jue AL, Coon JJ, Smith LM. Chemical Derivatization of Peptide Carboxyl Groups for Highly Efficient Electron Transfer Dissociation. Journal Of The American Society For Mass Spectrometry 2013, 24: 1710-1721. PMID: 23918461, PMCID: PMC3827969, DOI: 10.1007/s13361-013-0701-2.Peer-Reviewed Original ResearchConceptsElectron transfer dissociationTransfer dissociationBovine serum albuminTryptic digestCarboxyl groupsLabeling reagentPeptide carboxyl groupsETD-MS/MSComplex peptide mixturesIncreased charge densitySequence coverageAlkyl tertiary aminesHigh sequence coverageAdditional peptide identificationsDerivatization strategyDerivatized peptidesPeptide derivatizationChemical derivatizationPeptide ionsPrecursor ionsPeptide mixturesETD fragmentationPeptide spectral matchesReaction efficiencyTertiary aminesRPSA, a candidate gene for isolated congenital asplenia, is required for pre-rRNA processing and spleen formation in Xenopus
Griffin JN, Sondalle SB, Robson A, Mis EK, Griffin G, Kulkarni SS, Deniz E, Baserga SJ, Khokha MK. RPSA, a candidate gene for isolated congenital asplenia, is required for pre-rRNA processing and spleen formation in Xenopus. Development 2018, 145: dev166181. PMID: 30337486, PMCID: PMC6215398, DOI: 10.1242/dev.166181.Peer-Reviewed Original ResearchConceptsPre-rRNA processingSmall ribosomal subunitCommon disease-associated mutationDisease-associated mutationsRpsA mRNARibosome biogenesisRibosome productionRibosome functionRibosomal subunitCandidate genesHuman mRNAsProtein componentsImpairs expressionSpleen developmentMolecular patterningRPSASpleen anlageMutationsXenopusGenesFirst animal modelUniversal requirementMRNA
2016
The Contributions of the Ribosome Biogenesis Protein Utp5/WDR43 to Craniofacial Development
Sondalle SB, Baserga SJ, Yelick PC. The Contributions of the Ribosome Biogenesis Protein Utp5/WDR43 to Craniofacial Development. Journal Of Dental Research 2016, 95: 1214-1220. PMID: 27221611, PMCID: PMC5076753, DOI: 10.1177/0022034516651077.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsRibosomal proteinsCraniofacial developmentRibosome biogenesis proteinsRibosomal protein functionHuman craniofacial developmentTissue-specific defectsDiverse cell typesHuman ribosomopathiesBiogenesis proteinsTranslational machineryProtein functionDistinct functionsTranslational mechanismsTissue differentiationCell typesWDR43Global defectsProteinExciting researchSurprising similaritiesUnderstanding of rolesRibosomopathiesBiogenesisMachineryMutations