2018
Cell-Penetrating Peptide Mediates Intracellular Membrane Passage of Human Papillomavirus L2 Protein to Trigger Retrograde Trafficking
Zhang P, da Silva G, Deatherage C, Burd C, DiMaio D. Cell-Penetrating Peptide Mediates Intracellular Membrane Passage of Human Papillomavirus L2 Protein to Trigger Retrograde Trafficking. Cell 2018, 174: 1465-1476.e13. PMID: 30122350, PMCID: PMC6128760, DOI: 10.1016/j.cell.2018.07.031.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCapsid ProteinsCell-Penetrating PeptidesEndosomesGolgi ApparatusGreen Fluorescent ProteinsHEK293 CellsHeLa CellsHuman papillomavirus 16HumansMutagenesisOncogene Proteins, ViralProtein TransportRecombinant Fusion ProteinsSequence AlignmentVirus AttachmentVirus InternalizationConceptsCell-penetrating peptidesTrans-Golgi networkNormal cell physiologyL2 proteinRetrograde transport pathwayShort protein segmentsHPV L2 proteinTrafficking factorsRetrograde traffickingCationic cell-penetrating peptidesCell physiologyEndosomal membranesProtein segmentsC-terminusBiological roleNon-enveloped virusesRetrograde pathwayL2 capsid proteinsMembrane passageCell penetrating peptideCapsid proteinViral proteinsProteinRetromerTransport pathways
2000
Visualizing protein dynamics in yeast with green fluorescent protein
Burd C. Visualizing protein dynamics in yeast with green fluorescent protein. Methods In Enzymology 2000, 327: 61-69. PMID: 11044974, DOI: 10.1016/s0076-6879(00)27267-4.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinProtein dynamicsUse of GFPFluorescent proteinYeast cell biologyProtein sortingRNA localizationIndividual cellular componentsChromosomal dynamicsProtein localizationKinase signalingCell biologyMutant strainMolecular tagsCellular componentsYeastProteinNucleocytoplasmicBroad arrayLocalizationSignalingBiologySortingMajor impactTags
1998
Phosphatidylinositol(3)-Phosphate Signaling Mediated by Specific Binding to RING FYVE Domains
Burd C, Emr S. Phosphatidylinositol(3)-Phosphate Signaling Mediated by Specific Binding to RING FYVE Domains. Molecular Cell 1998, 2: 157-162. PMID: 9702203, DOI: 10.1016/s1097-2765(00)80125-2.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBiological TransportCell CompartmentationFungal ProteinsGenes, ReporterGreen Fluorescent ProteinsLiposomesLuminescent ProteinsLysosomesPhosphatidylinositol 3-KinasesPhosphatidylinositol PhosphatesPhosphorylationProtein BindingRecombinant Fusion ProteinsSaccharomyces cerevisiaeSignal TransductionVacuolesZinc FingersConceptsFYVE domain-containing proteinsLysosomal protein traffickingDomain-containing proteinsGFP reporter proteinDomain fusion proteinLipid-binding assaysReceptor signaling cascadesFYVE fingerFYVE domainMembrane traffickingProtein traffickingPhosphate signalingInositol ringProtein domainsReporter proteinRING domainDownstream effectorsEndocytic compartmentsSignaling cascadesMolecular linkFusion proteinIntracellular localizationVps34Important regulatorRecruit/
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
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