2001
FYVE Domain Targets Pib1p Ubiquitin Ligase to Endosome and Vacuolar Membranes*
Shin M, Ogburn K, Varban O, Gilbert P, Burd C. FYVE Domain Targets Pib1p Ubiquitin Ligase to Endosome and Vacuolar Membranes*. Journal Of Biological Chemistry 2001, 276: 41388-41393. PMID: 11526110, DOI: 10.1074/jbc.m105665200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceEndosomesGreen Fluorescent ProteinsIntracellular MembranesLigasesLuminescent ProteinsMolecular Sequence DataPhosphatidylinositol 3-KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionUbiquitin-Protein Ligase ComplexesUbiquitin-Protein LigasesVacuolesConceptsPI3K productsVacuolar membraneFYVE domainUbiquitin ligaseK productRING-type ubiquitin ligaseUbiquitin ligase activityFYVE fingerFinger motifEukaryotic cellsYeast SaccharomycesCellular proteinsRING domainLigase activityDeletional analysisFusion proteinStructural domainsHistidine residuesPrimary structurePI3KFluorescence microscopyProteinLigaseBindsMembrane
1999
Phosphatidylinositol 3-Phosphate Recognition by the FYVE Domain
Kutateladze T, Ogburn K, Watson W, de Beer T, Emr S, Burd C, Overduin M. Phosphatidylinositol 3-Phosphate Recognition by the FYVE Domain. Molecular Cell 1999, 3: 805-811. PMID: 10394369, DOI: 10.1016/s1097-2765(01)80013-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBinding SitesConserved SequenceDimerizationHumansLiposomesMembrane ProteinsMolecular Sequence DataMolecular WeightMutationNuclear Magnetic Resonance, BiomolecularPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphatidylinositolsProtein BindingProtein FoldingProtein Structure, SecondarySolubilitySubstrate SpecificityVesicular Transport ProteinsZincZinc FingersConceptsFYVE domainEndosome autoantigen 1Membrane trafficking eventsHeteronuclear magnetic resonance spectroscopyZinc-binding motifSpecific amino acidsTrafficking eventsEndosome fusionCellular signalingAlpha-helixBeta hairpinAmino acidsPhosphoinositidePhosphatidylinositolMotifStructural featuresRing fingerDomainPtdlnsSignalingProteinHairpinHelixBroad rangeLipids
1997
Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component
Cowles C, Snyder W, Burd C, Emr S. Novel Golgi to vacuole delivery pathway in yeast: identification of a sorting determinant and required transport component. The EMBO Journal 1997, 16: 2769-2782. PMID: 9184222, PMCID: PMC1169886, DOI: 10.1093/emboj/16.10.2769.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAmino Acid SequenceBiological TransportCarboxypeptidasesCarrier ProteinsCathepsin ACell CompartmentationFungal ProteinsGolgi ApparatusMembrane ProteinsModels, BiologicalMolecular Sequence DataNuclear ProteinsQa-SNARE ProteinsRecombinant Fusion ProteinsRNA-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsVacuolesVesicular Transport ProteinsConceptsVacuolar protein sorting (vps) mutantsSoluble vacuolar hydrolasesVacuolar membrane proteinSoluble vacuolar proteinsDomain-swapping experimentsNon-permissive conditionsNon-permissive temperatureCytoplasmic tail domainVacuolar deliveryT-SNAREsNovel GolgiTransport intermediatesSorting signalsVacuolar hydrolasesVesicle recognitionVacuolar proteinDouble mutantAmino acid portionVacuolar localizationMembrane proteinsTail domainDelivery pathwayPlasma membraneSelective packagingAlkaline phosphatase
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 determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins.
Görlach M, Burd C, Dreyfuss G. The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins. Journal Of Biological Chemistry 1994, 269: 23074-23078. PMID: 8083209, DOI: 10.1016/s0021-9258(17)31621-6.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBinding SitesElectrophoresis, Polyacrylamide GelGene AmplificationHeterogeneous-Nuclear Ribonucleoprotein Group CHeterogeneous-Nuclear RibonucleoproteinsMolecular Sequence DataRibonucleoproteinsRNA, Heterogeneous NuclearRNA-Binding ProteinsSequence Homology, Amino AcidConceptsRNA-binding domainRNA-binding specificityHnRNP C1Selection/amplificationC proteinMinimal RNA-binding domainHeterogeneous nuclear ribonucleoprotein C proteinsHnRNP C proteinsRandom sequence RNARNA-binding propertiesDeterminant of RNAFilter binding assaysRNP motifGeneral RNASpecificity residesC1-binding siteSequence RNAMotif familyRNA ligandsU residuesContiguous stretchesRNAAmino acidsProteinVariable regionsConserved Structures and Diversity of Functions of RNA-Binding Proteins
Burd C, Dreyfuss G. Conserved Structures and Diversity of Functions of RNA-Binding Proteins. Science 1994, 265: 615-621. PMID: 8036511, DOI: 10.1126/science.8036511.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesHumansMolecular Sequence DataRibonucleoproteinsRNA-Binding ProteinsSequence Homology, Amino AcidThe 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 rateRNA binding specificity of hnRNP A1: significance of hnRNP A1 high‐affinity binding sites in pre‐mRNA splicing.
Burd C, Dreyfuss G. RNA binding specificity of hnRNP A1: significance of hnRNP A1 high‐affinity binding sites in pre‐mRNA splicing. The EMBO Journal 1994, 13: 1197-1204. PMID: 7510636, PMCID: PMC394929, DOI: 10.1002/j.1460-2075.1994.tb06369.x.Peer-Reviewed Original ResearchAnimalsBase SequenceBinding SitesCell NucleusConsensus SequenceDNA PrimersGlobinsHeterogeneous Nuclear Ribonucleoprotein A1Heterogeneous-Nuclear Ribonucleoprotein Group A-BHeterogeneous-Nuclear RibonucleoproteinsIntronsMolecular Sequence DataOligodeoxyribonucleotidesOligoribonucleotidesRecombinant ProteinsRibonucleoproteinsRNARNA PrecursorsRNA SplicingRNA-Binding ProteinsUltraviolet Rays
1993
hnRNP Proteins and the Biogenesis of mRNA
Dreyfuss G, Matunis M, Piñol-Roma S, Burd C. hnRNP Proteins and the Biogenesis of mRNA. Annual Review Of Biochemistry 1993, 62: 289-321. PMID: 8352591, DOI: 10.1146/annurev.bi.62.070193.001445.Peer-Reviewed Original Research
1992
RNA binding characteristics of a 16 kDa glycine‐rich protein from maize
Ludevid M, Freire M, Gómez J, Burd C, Albericio F, Giralt E, Dreyfuss G, Pagès M. RNA binding characteristics of a 16 kDa glycine‐rich protein from maize. The Plant Journal 1992, 2: 999-1003. PMID: 1302645, DOI: 10.1046/j.1365-313x.1992.t01-10-00999.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceHeat-Shock ProteinsMolecular Sequence DataPlant ProteinsPoly APoly CPoly GPoly URNA-Binding ProteinsSeedsZea maysConceptsConsensus sequence-type RNA-binding domainStress responseGlycine-rich proteinRNA-binding domainGuanosine-rich RNAsRNA-binding proteinRNA metabolismProtein bindsLate embryogenesisMature embryosProteinLikely roleRNAMaizeEmbryogenesisEmbryosPlantsBindsMA16MRNASequenceMetabolismAssaysUridineResponse
1991
The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities.
Burd C, Matunis E, Dreyfuss G. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Molecular And Cellular Biology 1991, 11: 3419-3424. PMID: 1675426, PMCID: PMC361068, DOI: 10.1128/mcb.11.7.3419.Peer-Reviewed Original Research
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