2023
CLIP-Seq analysis enables the design of protective ribosomal RNA bait oligonucleotides against C9ORF72 ALS/FTD poly-GR pathophysiology
Ortega J, Sasselli I, Boccitto M, Fleming A, Fortuna T, Li Y, Sato K, Clemons T, Mckenna E, Nguyen T, Anderson E, Asin J, Ichida J, Pandey U, Wolin S, Stupp S, Kiskinis E. CLIP-Seq analysis enables the design of protective ribosomal RNA bait oligonucleotides against C9ORF72 ALS/FTD poly-GR pathophysiology. Science Advances 2023, 9: eadf7997. PMID: 37948524, PMCID: PMC10637751, DOI: 10.1126/sciadv.adf7997.Peer-Reviewed Original Research
2014
Bacterial noncoding Y RNAs are widespread and mimic tRNAs
Chen X, Sim S, Wurtmann EJ, Feke A, Wolin SL. Bacterial noncoding Y RNAs are widespread and mimic tRNAs. RNA 2014, 20: 1715-1724. PMID: 25232022, PMCID: PMC4201824, DOI: 10.1261/rna.047241.114.Peer-Reviewed Original ResearchConceptsY RNAsStructured RNA degradationRing-shaped proteinNoncoding Y RNAsBacterial physiologyAnimal cellsNucleotide modificationsDeinococcus radioduransPhage speciesRNA degradationTRNARo60 autoantigenRNAOrthologsNcRNAsSpeciesBacteriaExoribonucleaseRNAsRadioduransProteinRo60EnzymePhysiologyPhosphorylase
2012
Nuclear noncoding RNA surveillance: is the end in sight?
Wolin SL, Sim S, Chen X. Nuclear noncoding RNA surveillance: is the end in sight? Trends In Genetics 2012, 28: 306-313. PMID: 22475369, PMCID: PMC3378728, DOI: 10.1016/j.tig.2012.03.005.Peer-Reviewed Original ResearchConceptsRNA surveillance pathwaySurveillance pathwayAberrant RNAsSteady-state transcriptomeYeast counterpartEukaryotic cellsProtein cofactorsMammalian cellsRNA determinantsHuman diseasesSubsequent degradationRNACofactorPathwayKey roleRecent studiesMetazoansExoribonucleasesAccessible endTranscriptomeNcRNAsCellsYeastNucleaseProtein
2000
RNA degradation: Sm-like proteins wRING the neck of mRNA
Pannone B, Wolin S. RNA degradation: Sm-like proteins wRING the neck of mRNA. Current Biology 2000, 10: r478-r481. PMID: 10898971, DOI: 10.1016/s0960-9822(00)00552-2.Peer-Reviewed Original ResearchRo ribonucleoproteins contribute to the resistance of Deinococcus radiodurans to ultraviolet irradiation
Chen X, Quinn A, Wolin S. Ro ribonucleoproteins contribute to the resistance of Deinococcus radiodurans to ultraviolet irradiation. Genes & Development 2000, 14: 777-782. PMID: 10766734, PMCID: PMC316496, DOI: 10.1101/gad.14.7.777.Peer-Reviewed Original Research
1997
The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation.
Van Horn D, Yoo C, Xue D, Shi H, Wolin S. The La protein in Schizosaccharomyces pombe: a conserved yet dispensable phosphoprotein that functions in tRNA maturation. RNA 1997, 3: 1434-43. PMID: 9404894, PMCID: PMC1369584.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAutoantigensCarrier ProteinsCytoskeletal ProteinsFungal ProteinsHumansMolecular Sequence DataPhosphoproteinsPhosphorylationRecombinant Fusion ProteinsRestriction MappingRibonucleoproteinsRNA Processing, Post-TranscriptionalRNA, FungalRNA, TransferRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSchizosaccharomycesSequence Homology, Amino AcidConceptsLa proteinAbundant nuclear phosphoproteinRNA polymerase III transcriptsFission yeast SchizosaccharomycesPre-tRNA maturationS. pombe cellsPolymerase III transcriptsWild-type cellsHuman La proteinYeast SchizosaccharomycesS. pombePombe cellsYeast SaccharomycesTRNA precursorsNuclear phosphoproteinPattern of tRNAS. cerevisiaeLa autoantigenTRNAProteinSchizosaccharomycesPhosphoproteinYeastExhibit alterationsMaturation
1996
A misfolded form of 5S rRNA is complexed with the Ro and La autoantigens.
Shi H, O'Brien C, Van Horn D, Wolin S. A misfolded form of 5S rRNA is complexed with the Ro and La autoantigens. RNA 1996, 2: 769-84. PMID: 8752087, PMCID: PMC1369414.Peer-Reviewed Original ResearchConceptsRRNA precursorRo proteinAlternative helixQuality control pathwaysYeast Saccharomyces cerevisiaeSmall cytoplasmic RNAProtein-protein interactionsOligonucleotide-directed RNase H cleavageWild-type precursorRRNA biosynthesisY RNAsSecondary structure determinantsMutant RNAsSaccharomyces cerevisiaeLa proteinControl pathwaysCytoplasmic RNANuclease digestionInternal mutationsRRNARNAXenopus oocytesProteinSimilar sequencesRo autoantigen
1995
A perinucleolar compartment contains several RNA polymerase III transcripts as well as the polypyrimidine tract-binding protein, hnRNP I.
Matera A, Frey M, Margelot K, Wolin S. A perinucleolar compartment contains several RNA polymerase III transcripts as well as the polypyrimidine tract-binding protein, hnRNP I. Journal Of Cell Biology 1995, 129: 1181-1193. PMID: 7539809, PMCID: PMC2120477, DOI: 10.1083/jcb.129.5.1181.Peer-Reviewed Original ResearchConceptsY RNAsPol III transcriptsPerinucleolar compartmentHnRNP I/PTBRNA polymerase III transcriptsGenomic DNA clonesPolypyrimidine tract-binding proteinHuman Y RNAsRNA polymerase IIIPolymerase III transcriptsTract-binding proteinRNase MRPRo RNPsNuclear subdomainsTranscription sitesNucleolar peripheryRNase PSubcellular organizationDNA clonesPolymerase IIIRNA componentGene locusMacromolecular assembliesRNATranscriptsCaenorhabditis elegans embryos contain only one major species of Ro RNP.
Van Horn D, Eisenberg D, O'Brien C, Wolin S. Caenorhabditis elegans embryos contain only one major species of Ro RNP. RNA 1995, 1: 293-303. PMID: 7489501, PMCID: PMC1369082.Peer-Reviewed Original ResearchConceptsY RNAsRo proteinRo RNPsC. elegans proteinsRNA recognition motifHuman Y RNAsN-terminal extensionPyrimidine-rich internal loopRo autoantigenRNP functionVertebrate proteinsDiscard pathwayVertebrate cellsC. elegansInvertebrate speciesNematode CaenorhabditisVertebrate speciesProtein functionHuman proteinsRNA biosynthesisDefective precursorsRecognition motifRNA moleculesGenetic analysisRNA
1994
A possible role for the 60-kD Ro autoantigen in a discard pathway for defective 5S rRNA precursors.
O'Brien C, Wolin S. A possible role for the 60-kD Ro autoantigen in a discard pathway for defective 5S rRNA precursors. Genes & Development 1994, 8: 2891-2903. PMID: 7995526, DOI: 10.1101/gad.8.23.2891.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAutoantibodiesAutoantigensAutoimmune DiseasesBase SequenceDNA PrimersDNA, ComplementaryFemaleHumansMolecular Sequence DataMolecular WeightMutagenesisNucleic Acid ConformationOocytesOvaryPolymerase Chain ReactionRibonucleoproteinsRNA PrecursorsRNA, Ribosomal, 5SRNA, Small CytoplasmicTranscription, GeneticXenopusConceptsDiscard pathwayRRNA precursorCytoplasmic RNA-protein complexesRNA-protein complexesVariety of vertebratesRo autoantigenRo RNPsRRNA productionProtein bindsMutant RNAsRRNA sequencesMore point mutationsAdditional nucleotidesRo proteinRRNAPoint mutationsTerminal extensionXenopus oocytesProteinRNAPathwayPossible roleVertebratesRNPsNucleotides
1987
Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily.
Krohne G, Wolin S, McKeon F, Franke W, Kirschner M. Nuclear lamin LI of Xenopus laevis: cDNA cloning, amino acid sequence and binding specificity of a member of the lamin B subfamily. The EMBO Journal 1987, 6: 3801-8. PMID: 3428276, PMCID: PMC553852, DOI: 10.1002/j.1460-2075.1987.tb02716.x.Peer-Reviewed Original ResearchConceptsAmino acid sequenceLamin LIAcid sequenceIdentical amino acid positionsLong C-terminal tailDetailed sequence comparisonXenopus laevisC-terminal tailNear-neutral pIAmino acid positionsIntermediate filament proteinsHuman lamin A.Karyoskeletal proteinsLamin BCDNA clonesCoil domainHelical domainSequence comparisonXenopus laminLamin ALamin B.CDNA cloningLamin A.LaminsNuclear envelopeA new lamin in Xenopus somatic tissues displays strong homology to human lamin A.
Wolin S, Krohne G, Kirschner M. A new lamin in Xenopus somatic tissues displays strong homology to human lamin A. The EMBO Journal 1987, 6: 3809-18. PMID: 3428277, PMCID: PMC553853, DOI: 10.1002/j.1460-2075.1987.tb02717.x.Peer-Reviewed Original ResearchConceptsHuman lamin ACDNA clonesXenopus laminSomatic tissuesLamin AMajor lamin proteinsCarboxy-terminal domainAdult somatic cellsHuman lamin A.Major laminsDistinct structural classesLamin proteinsNuclear laminaLamin LIIIEmbryonic developmentSomatic cellsSomatic laminsStrong homologyLamin A.Lamin LILaminsMajor polypeptidesGerm cellsProteinClones
1983
Genes for two small cytoplasmic Ro RNAs are adjacent and appear to be single-copy in the human genome
Wolin S, Steitz J. Genes for two small cytoplasmic Ro RNAs are adjacent and appear to be single-copy in the human genome. Cell 1983, 32: 735-744. PMID: 6187471, DOI: 10.1016/0092-8674(83)90059-4.Peer-Reviewed Original ResearchConceptsHuman genomeRo RNAsSecondary structure homologyRNA polymerase IIISmall cytoplasmic ribonucleoproteinsClass III genesGenomic clonesMammalian cellsPolymerase IIIRNA componentStructure homologySingle copyCytoplasmic ribonucleoproteinHY5 RNAMouse cellsHuman cellsHY1Cell extractsGenesRNAGenomeRNAsHY3CellsMY1Structure and Function of Small Ribonucleoproteins from Eukaryotic Cells
Steitz JA, Berg C, Gottlieb E, Hardin JA, Hashimoto C, Hendrick JP, Hinterberger M, Krikeles M, Lerner MR, Mount SM, Pettersson I, Rinke J, Rosa M, Wolin S. Structure and Function of Small Ribonucleoproteins from Eukaryotic Cells. 1983, 12: 309-317. PMID: 7166547, DOI: 10.1016/b978-0-12-501650-6.50023-7.Peer-Reviewed Original ResearchConceptsSmall ribonucleoproteinLa proteinRNA polymerase III transcription factorSmall RNA-protein complexesDrosophila U1 RNAU1 small nuclearRNA-protein complexesHnRNA splicingEukaryotic cellsSmall cytoplasmicMammalian cellsRRNA precursorTranscription factorsSmall nuclearU1 RNASplice junctionsRibonucleoproteinLa ribonucleoproteinsFurther characterizationProteinRelated diseasesCellsSplicingTRNARNA
1980
Are snRNPs involved in splicing?
Lerner M, Boyle J, Mount S, Wolin S, Steitz J. Are snRNPs involved in splicing? Nature 1980, 283: 220-224. PMID: 7350545, DOI: 10.1038/283220a0.Peer-Reviewed Original ResearchConceptsSmall nuclear RNA speciesProminent nuclear proteinsRNA-protein complexesSmall RNA moleculesSmall nuclear ribonucleoproteinNuclear RNA speciesSnRNA speciesSnRNAs U1RNA speciesU6 RNASnRNA moleculesNuclear proteinsNuclear ribonucleoproteinNucleotide sequenceU1 RNARNA moleculesSnRNPsExtensive complementaritySplice junctionsNuclear locationLines of evidenceAnti-Sm seraCell nucleiHnRNA moleculesMouse Ehrlich
1979
Expression of microtubule networks in normal cells, transformed cells, and their hybrids.
Wolin S, Kucherlapati R. Expression of microtubule networks in normal cells, transformed cells, and their hybrids. Journal Of Cell Biology 1979, 82: 76-85. PMID: 383725, PMCID: PMC2110424, DOI: 10.1083/jcb.82.1.76.Peer-Reviewed Original ResearchConceptsNormal cellsNormal human cellsOrganization of tubulinCellular functionsChromosome movementCell divisionMouse cellsMicrotubule networkMammalian tubulinHuman cellsCellular architectureMicrotubulesCell linesTubulinPhenotypeCells of miceHuman originCellsEase of detectionHybridsExtensive networkImportant roleAntiserumAttachment propertiesExpression