2008
Functional Adhesiveness of the CX3CL1 Chemokine Requires Its Aggregation ROLE OF THE TRANSMEMBRANE DOMAIN*
Hermand P, Pincet F, Carvalho S, Ansanay H, Trinquet E, Daoudi M, Combadière C, Deterre P. Functional Adhesiveness of the CX3CL1 Chemokine Requires Its Aggregation ROLE OF THE TRANSMEMBRANE DOMAIN*. Journal Of Biological Chemistry 2008, 283: 30225-30234. PMID: 18725411, PMCID: PMC2662081, DOI: 10.1074/jbc.m802638200.Peer-Reviewed Original ResearchConceptsBioluminescence resonance energy transferHomogeneous time-resolved fluorescenceTransmembrane domainAdhesive potencyTransmembrane domain residuesLoss of glycosylationConstitutive oligomersDomain residuesBRET signalTruncation experimentsResonance energy transferCell surfacePrimary cellsSpecific signalsNative formAdhesion assaysAdhesive moleculesCell linesCentral roleAggregation roleInhibition of CX3CL1New pathwayTime-resolved fluorescenceCellsAssays
2001
Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding
Saibil H, Horwich A, Fenton W. Allostery and protein substrate conformational change during GroEL/GroES-mediated protein folding. Advances In Protein Chemistry And Structural Biology 2001, 59: 45-72. PMID: 11868280, DOI: 10.1016/s0065-3233(01)59002-6.Peer-Reviewed Original ResearchConceptsProtein foldingATP-dependent protein foldingChloroplasts of eukaryotesDouble-ring complexesCo-chaperonin GroESC-terminal portionChaperonin machineProtein folding reactionChaperonin systemSubstrate polypeptidesChaperonin complexGroEL-GroESHeptameric ringsGroEL subunitStructural biologyBiophysical approachesEquatorial domainATPase mechanismConformational changesSubstrate conformational changesFolding reactionNative formGroESFoldingGroEL
2000
Proper Folding and Endoplasmic Reticulum to Golgi Transport of Tyrosinase Are Induced by Its Substrates, DOPA and Tyrosine*
Halaban R, Cheng E, Svedine S, Aron R, Hebert D. Proper Folding and Endoplasmic Reticulum to Golgi Transport of Tyrosinase Are Induced by Its Substrates, DOPA and Tyrosine*. Journal Of Biological Chemistry 2000, 276: 11933-11938. PMID: 11124258, DOI: 10.1074/jbc.m008703200.Peer-Reviewed Original ResearchConceptsWild-type tyrosinaseEndoplasmic reticulumProper foldingWild-type proteinMelanoma cellsLoss of pigmentationTyrosinase-positive melanoma cellsGolgi transportType proteinAlbino mutantS proteasomeSubsequent retranslocationMutant formsCatalytic stateEnzymatic activityProteolytic degradationNative formReticulumFoldingProteinTumor-derived antigenic peptidesTyrosinase activitySuppress tyrosinase activityCellsMetabolic changes
1998
Chaperone Action in Folding Newly-Translated Cytosolic Proteins in Bacteria and Eukaryotes
Horwich A. Chaperone Action in Folding Newly-Translated Cytosolic Proteins in Bacteria and Eukaryotes. NATO ASI Series 1998, 41-63. DOI: 10.1007/978-3-642-51463-0_4.Peer-Reviewed Original ResearchNon-native conformationsNative statePrimary amino acid sequenceAmino acid sequenceNon-native statesSubstrate proteinsChaperone functionMolecular chaperonesBiogenesis stepsChaperone actionSpecialized proteinsCofactor bindingProtein foldingAction of nucleotidesPathway stepsMutational alterationsCytosolic proteinsAcid sequenceChaperonesSteric informationFolding processSuch hydrophobic interactionsProteinNative formEssential nature[11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL
Horwich A, Burston S, Rye H, Weissman J, Fenton W. [11] Construction of single-ring and two-ring hybrid versions of bacterial chaperonin GroEL. Methods In Enzymology 1998, 290: 141-146. PMID: 9534157, DOI: 10.1016/s0076-6879(98)90013-1.Peer-Reviewed Original ResearchConceptsBacterial chaperonin GroELGreen fluorescent proteinChaperonin GroELDouble-ring assemblyAddition of GroESDouble-ring complexesSingle-ring versionUnliganded GroELBacterial chaperoninsGroEL ringNeighboring subunitProtein foldsGroELEquatorial domainNonnative formsFluorescent proteinGroESNative stateNative formCentral channelCritical signalingSubunitsSignalingForm contactsNormal ATP
1997
Chaperonin-Mediated Folding in the Eukaryotic Cytosol Proceeds through Rounds of Release of Native and Nonnative Forms
Farr G, Scharl E, Schumacher R, Sondek S, Horwich A. Chaperonin-Mediated Folding in the Eukaryotic Cytosol Proceeds through Rounds of Release of Native and Nonnative Forms. Cell 1997, 89: 927-937. PMID: 9200611, DOI: 10.1016/s0092-8674(00)80278-0.Peer-Reviewed Original ResearchConceptsRounds of releaseSubstrate proteinsNonnative formsNative formChaperonin-mediated foldingEukaryotic cytosolic chaperoninATP-dependent foldingIntact Xenopus oocytesCytosolic chaperoninBacterial chaperoninsEukaryotic cytosolChaperoninNative stateXenopus oocytesEssential roleSingle roundFoldingProteinActinTubulinOverall mechanismGroELTransducinCytosolSmall fraction
1992
Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster
Shuai K, Gupta C, Hawley R, Chase J, Stone K, Williams K. Purification and characterization of an endo-exonuclease from adult flies of Drosophila melanogaster. Nucleic Acids Research 1992, 20: 1379-1385. PMID: 1313969, PMCID: PMC312186, DOI: 10.1093/nar/20.6.1379.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAmino AcidsAnimalsChromatography, DEAE-CelluloseChromatography, High Pressure LiquidDNA, Single-StrandedDrosophila melanogasterElectrophoresis, Polyacrylamide GelEndonucleasesExonucleasesHot TemperatureHydrogen-Ion ConcentrationKineticsMolecular Sequence DataMolecular WeightSodium ChlorideSubstrate SpecificityUltracentrifugation
1991
Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor
Klueppelberg UG, Gates LK, Gorelick FS, Miller LJ. Agonist-regulated phosphorylation of the pancreatic cholecystokinin receptor. Journal Of Biological Chemistry 1991, 266: 2403-2408. PMID: 1989991, DOI: 10.1016/s0021-9258(18)52258-4.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCarbacholCell FractionationChromatography, AffinityChromatography, High Pressure LiquidElectrophoresis, Polyacrylamide GelEnzyme ActivationKineticsMalePancreasPhosphorylationProtein Kinase CRatsRats, Inbred StrainsReceptors, CholecystokininSincalideSolubilityTetradecanoylphorbol AcetateConceptsC activationSodium dodecyl sulfate-polyacrylamide gelsDodecyl sulfate-polyacrylamide gelsProtein kinase C activationPlasma membrane glycoproteinsPhosphorylated MrKinase C activationSulfate-polyacrylamide gelsSerine residuesRegulated mannerAffinity-labeled proteinsMembrane glycoproteinsPhosphorylationReceptor proteinProteinNative formATP poolAffinity resinLectin affinity chromatographyConcentration-dependent mannerDirect activationPancreatic cholecystokinin receptorSubsequent solubilizationReceptorsActivation
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