2001
Characterization of a Novel Hemoglobin-Glutathione Adduct That Is Elevated in Diabetic Patients
Al-Abed Y, VanPatten S, Li H, Lawson J, FitzGerald G, Manogue K, Bucala R. Characterization of a Novel Hemoglobin-Glutathione Adduct That Is Elevated in Diabetic Patients. Molecular Medicine 2001, 7: 619-623. PMID: 11778651, PMCID: PMC1950073, DOI: 10.1007/bf03401868.Peer-Reviewed Original ResearchConceptsDiabetic patientsDiabetes mellitusPredictor of prognosisBlood glucose levelsNormal patientsGlucose levelsPatientsUseful markerNormal individualsPathologic situationsOxidative stressMellitusAdditional markersΒ-globin chainsLiquid chromatography-mass spectroscopyΒ-chainMarkersHigh levelsPrognosisDiseaseDiagnosis
1999
Detoxification of Methylglyoxal by the Nucleophilic Bidentate, Phenylacylthiazolium Bromide
Ferguson G, VanPatten S, Bucala R, Al-Abed Y. Detoxification of Methylglyoxal by the Nucleophilic Bidentate, Phenylacylthiazolium Bromide. Chemical Research In Toxicology 1999, 12: 617-622. PMID: 10409401, DOI: 10.1021/tx990007y.Peer-Reviewed Original ResearchConceptsEscherichia coli double mutantRapid cell deathE. coli cellsDetoxification of methylglyoxalExponential-phase cellsDouble mutantSensitive bacterial assayColi cellsCell deathPhase cellsE. coliLong-term complicationsPotassium channelsReactive dicarbonylsBacterial assaysDetoxificationEndogenous nucleophilesCellsMethylglyoxalTissue damage
1998
Contribution of advanced glycosylation to the amyloidogenicity of islet amyloid polypeptide
Kapurniotu A, Bernhagen J, Greenfield N, Al‐Abed Y, Teichberg S, Frank R, Voelter W, Bucala R. Contribution of advanced glycosylation to the amyloidogenicity of islet amyloid polypeptide. The FEBS Journal 1998, 251: 208-216. PMID: 9492286, DOI: 10.1046/j.1432-1327.1998.2510208.x.Peer-Reviewed Original ResearchConceptsAmyloid formationIslet amyloid polypeptidePre-formed aggregatesAdvanced glycosylation end productsIAPP amyloid formationAlzheimer's disease amyloid peptideCircular dichroism spectropolarimetryNucleation-dependent polymerization mechanismBeta-sheet conformationIAPP aggregationBiophysical techniquesIAPP aggregatesHigh molecular massFormation of amyloidAmyloid structuresGreen-gold birefringenceProtein amino groupsCharacteristic fibrillar structureIslet amyloid formationSeedsFibrillar amyloid structuresGlycosylationPolymerization mechanismNon-enzymatic additionPeptide aggregation
1996
The subunit structure of human macrophage migration inhibitory factor: evidence for a trimer
Sun H, Swope M, Craig C, Bedarkar S, Bernhagen J, Bucala R, Lolis E. The subunit structure of human macrophage migration inhibitory factor: evidence for a trimer. Protein Engineering Design And Selection 1996, 9: 631-635. PMID: 8875640, DOI: 10.1093/protein/9.8.631.Peer-Reviewed Original Research
1986
Structure of lysine adducts with 16α-hydroxyestrone and cortisol
Bucala R, Ulrich P, Chait B, Bencsath F, Cerami A. Structure of lysine adducts with 16α-hydroxyestrone and cortisol. The Journal Of Steroid Biochemistry And Molecular Biology 1986, 25: 127-133. PMID: 3091937, DOI: 10.1016/0022-4731(86)90291-8.Peer-Reviewed Original ResearchMeSH KeywordsEstroneHydrocortisoneHydroxyestronesLysineMagnetic Resonance SpectroscopyMass SpectrometrySchiff BasesConceptsSchiff baseReduced Schiff baseStructure of lysineCovalent addition productsPresence of NaCNBH3Schiff base adductsHeyns rearrangementNucleophilic additionAddition productsBase adductsEpsilon-amino groupLysine derivativesStructural analysisAdductsLysine residuesReactionNaCNBH3MoietyCarbonylAminesCompoundsSynthesisMoleculesProductsLysine