2023
Nucleolar structure connects with global nuclear organization.
Wang C, Ma H, Baserga S, Pederson T, Huang S. Nucleolar structure connects with global nuclear organization. Molecular Biology Of The Cell 2023, 34: ar114. PMID: 37610836, PMCID: PMC10846622, DOI: 10.1091/mbc.e23-02-0062.Peer-Reviewed Original ResearchConceptsNucleolar structureGenomic lociNuclear domainsSpecific genomic lociGlobal nuclear organizationRNA processing factorsRNA polymerase ICajal bodiesNuclear organizationRibosome synthesisNuclear bodiesKnockdown cellsPerinucleolar compartmentPolymerase IIntranuclear locationHeLa cellsNucleolar segregationSpatial organizationNucleoliLociUtp4CellsRPA194SegregationCompositional changes
2001
Fibrillarin and Other snoRNP Proteins Are Targets of Autoantibodies in Xenobiotic-Induced Autoimmunity
Yang J, Baserga S, Turley S, Pollard K. Fibrillarin and Other snoRNP Proteins Are Targets of Autoantibodies in Xenobiotic-Induced Autoimmunity. Clinical Immunology 2001, 101: 38-50. PMID: 11580225, DOI: 10.1006/clim.2001.5099.Peer-Reviewed Original ResearchConceptsSJL/J miceSmall nucleolar ribonucleoproteinSnoRNP proteinsCajal bodiesNucleolar ribonucleoproteinMetaphase chromosomesAmphibian cellsJ miceFibrillarinInterphase cellsProtein componentsNucleolar immunofluorescence patternProteinAnti-nucleolar antibodiesCell linesTarget of autoantibodiesAutoantibody responseAntibody responsePredominant targetImmunofluorescence patternMurineCellsRibonucleoproteinChromosomesMice
1999
Human Nop5/Nop58 is a component common to the box C/D small nucleolar ribonucleoproteins.
Lyman S, Gerace L, Baserga S. Human Nop5/Nop58 is a component common to the box C/D small nucleolar ribonucleoproteins. RNA 1999, 5: 1597-604. PMID: 10606270, PMCID: PMC1369881, DOI: 10.1017/s1355838299991288.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsCell NucleolusCloning, MolecularConserved SequenceHeLa CellsHumansMiceMolecular Sequence DataMolecular WeightNuclear ProteinsRatsRecombinant ProteinsRibonucleoproteinsRibonucleoproteins, Small NucleolarSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSequence Homology, Amino Acid
1998
M Phase Phosphoprotein 10 Is a Human U3 Small Nucleolar Ribonucleoprotein Component
Westendorf J, Konstantinov K, Wormsley S, Shu M, Matsumoto-Taniura N, Pirollet F, Klier F, Gerace L, Baserga S. M Phase Phosphoprotein 10 Is a Human U3 Small Nucleolar Ribonucleoprotein Component. Molecular Biology Of The Cell 1998, 9: 437-449. PMID: 9450966, PMCID: PMC25272, DOI: 10.1091/mbc.9.2.437.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceCell FractionationCell NucleolusChromosomal Proteins, Non-HistoneCloning, MolecularDactinomycinDNA, ComplementaryHeLa CellsHumansIsoelectric PointMitosisMolecular Sequence DataMolecular WeightNuclear ProteinsPhosphoproteinsRibonucleoproteinsRibonucleoproteins, Small NuclearRNA, Small NuclearSequence Analysis, DNASpecies SpecificityConceptsM-phase phosphoproteinsPrenucleolar bodiesBox C/D snoRNAsU3 small nucleolar RNASmall nucleolar RNAsIsolation of cDNAsHuman U3D snoRNAsRRNA processingNucleolar proteinsP80-coilinNovel proteinNucleolar functionU3 snoRNAChromosome surfaceNucleolar RNAsCell fractionationMpp10FibrillarinInterphase cellsCell cycleRibonucleoprotein componentsM phaseProteinSnoRNAs