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
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 Acid