2013
An RNA Degradation Machine Sculpted by Ro Autoantigen and Noncoding RNA
Chen X, Taylor DW, Fowler CC, Galan JE, Wang HW, Wolin SL. An RNA Degradation Machine Sculpted by Ro Autoantigen and Noncoding RNA. Cell 2013, 153: 166-177. PMID: 23540697, PMCID: PMC3646564, DOI: 10.1016/j.cell.2013.02.037.Peer-Reviewed Original ResearchConceptsRNA degradation machineDegradation machineY RNAsSingle-particle electron microscopyRing-shaped proteinRibosomal RNA maturationExoribonuclease polynucleotide phosphorylaseRo autoantigenNcRNAs actRRNA decayRNA maturationProtein cofactorsNoncoding RNAsSubstrate specificityDeinococcus radioduransStructured RNAsPolynucleotide phosphorylaseBiochemical assaysRNAOrthologsNcRNAPNPaseProteinSalmonella typhimuriumAtomic model
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
1993
Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins.
O'Brien C, Margelot K, Wolin S. Xenopus Ro ribonucleoproteins: members of an evolutionarily conserved class of cytoplasmic ribonucleoproteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 7250-7254. PMID: 7688474, PMCID: PMC47114, DOI: 10.1073/pnas.90.15.7250.Peer-Reviewed Original ResearchConceptsY RNAsRo proteinSmall ribonucleoproteinHuman Y RNAsSmall RNA moleculesXenopus egg extractsAmino acid sequenceY-RNAsHY3 RNAsVertebrate speciesMammalian cellsRo RNPsSubcellular locationRNA componentCytoplasmic ribonucleoproteinHY5 RNAAdditional proteinsRNA moleculesAcid sequenceHuman RNAEgg extractsEntire proteinConserved stemOocyte cytoplasmRibonucleoprotein
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: 3801-3808. 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 Subset of Yeast snRNA's Contains Functional Binding Sites for the Highly Conserved Sm Antigen
Riedel N, Wolin S, Guthrie C. A Subset of Yeast snRNA's Contains Functional Binding Sites for the Highly Conserved Sm Antigen. Science 1987, 235: 328-331. PMID: 2948278, DOI: 10.1126/science.2948278.Peer-Reviewed Original Research