1996
A Yeast Protein Related to a Mammalian Ras-Binding Protein, Vps9p, Is Required for Localization of Vacuolar Proteins
Burd C, Mustol P, Schu P, Emr S. A Yeast Protein Related to a Mammalian Ras-Binding Protein, Vps9p, Is Required for Localization of Vacuolar Proteins. Molecular And Cellular Biology 1996, 16: 2369-2377. PMID: 8628304, PMCID: PMC231225, DOI: 10.1128/mcb.16.5.2369.Peer-Reviewed Original ResearchMeSH KeywordsAllelesAmino Acid SequenceAnimalsCarrier ProteinsCloning, MolecularFungal ProteinsGenes, FungalGenetic Complementation TestGuanine Nucleotide Exchange FactorsHumansMammalsMolecular Sequence DataMutagenesisPolymerase Chain ReactionRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidTemperatureVacuolesVesicular Transport ProteinsConceptsVacuolar protein sortingProtein sortingVacuolar proteinVPS pathwayVacuolar protein sorting (VPS) genesTemperature-sensitive growth defectTemperature-conditional alleleVacuolar protein precursorsFamily of proteinsSecretion of proteinsRab GTPaseRA-binding proteinsTransport vesiclesYeast proteinsHomology domainYeast SaccharomycesGrowth defectHuman proteinsVps9pDNA sequencesGene productsCytosolic proteinsNonpermissive temperatureCarboxypeptidase YIntracellular transport
1994
The mRNA Poly(A)-Binding Protein: Localization, Abundance, and RNA-Binding Specificity
Görlach M, Burd C, Dreyfuss G. The mRNA Poly(A)-Binding Protein: Localization, Abundance, and RNA-Binding Specificity. Experimental Cell Research 1994, 211: 400-407. PMID: 7908267, DOI: 10.1006/excr.1994.1104.Peer-Reviewed Original ResearchConceptsHuman PABPRNA binding specificityQuantitative immunoblotting experimentsMost eukaryotic mRNAsRNA-binding propertiesTranslation of mRNAsConfocal immunofluorescence microscopySelection/amplificationEukaryotic mRNAsOligonucleotide poolRNA sequencesRich sequencesCellular localizationBinding proteinHeLa cellsImmunofluorescence microscopyImmunoblotting experimentsLow turnover rateLow affinityPABPProteinAbundanceMRNAIntracellular concentrationTurnover rate
1989
Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts.
Burd C, Swanson M, Görlach M, Dreyfuss G. Primary structures of the heterogeneous nuclear ribonucleoprotein A2, B1, and C2 proteins: a diversity of RNA binding proteins is generated by small peptide inserts. Proceedings Of The National Academy Of Sciences Of The United States Of America 1989, 86: 9788-9792. PMID: 2557628, PMCID: PMC298587, DOI: 10.1073/pnas.86.24.9788.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCloning, MolecularDNA Transposable ElementsDNA, NeoplasmElectrophoresis, Gel, Two-DimensionalHeLa CellsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear RibonucleoproteinsHumansMolecular Sequence DataProtein BiosynthesisRestriction MappingRibonucleoproteinsRNA, Heterogeneous NuclearSequence Homology, Nucleic AcidSoftwareTransfectionConceptsAmino acid sequenceCS-RBDsHeterogeneous nuclear ribonucleoprotein A2C2 proteinAmino acidsAcid sequenceDiversity of RNAHnRNP protein A1Amino acid identityAuxiliary domainHnRNP proteinsMRNA splicingProtein cDNAAcid identityCarboxyl terminusAmino terminusPrimary structureProtein A1Frame insertsB1 proteinCDNALarge familyProteinRNATerminus