1999
Structure of a Synthetic Glucose Derived Advanced Glycation End Product That Is Immunologically Cross-Reactive with Its Naturally Occurring Counterparts †
Al-Abed Y, Bucala R. Structure of a Synthetic Glucose Derived Advanced Glycation End Product That Is Immunologically Cross-Reactive with Its Naturally Occurring Counterparts †. Bioconjugate Chemistry 1999, 11: 39-45. PMID: 10639083, DOI: 10.1021/bc990061q.Peer-Reviewed Original ResearchConceptsAdvanced glycation end productsAnti-AGE antibodyGlycation end productsLow-density lipoproteinAGE-modified formCertain diabetic complicationsClasses of antibodiesBeta-amyloid peptideDiabetic complicationsPathological sequelaePrognostic informationAGE formationAGE adductsImmunoreactive fractionEnd productsInhibition of formationVivo ageAgeAntibodiesLines of evidenceVivoCross-linking adductsGlucoseTissueComplications
1997
Tobacco smoke is a source of toxic reactive glycation products
Cerami C, Founds H, Nicholl I, Mitsuhashi T, Giordano D, Vanpatten S, Lee A, Al-Abed Y, Vlassara H, Bucala R, Cerami A. Tobacco smoke is a source of toxic reactive glycation products. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 13915-13920. PMID: 9391127, PMCID: PMC28407, DOI: 10.1073/pnas.94.25.13915.Peer-Reviewed Original ResearchConceptsAdvanced glycation end productsTobacco smokeGlycation productsAGE formationSerum AGE levelsIncidence of atherosclerosisPlasma of patientsGlycation end productsRenal insufficiencyCerebrovascular diseaseCigarette smokersHuman smokersHigh prevalenceHigh riskSmokersNonsmokersGlycotoxinsPatientsSpecific fluorescenceSerum proteinsDiseaseCuring of tobaccoAqueous extractSmokeTobaccoBiochemical and Mutational Investigations of the Enzymatic Activity of Macrophage Migration Inhibitory Factor †
Bendrat K, Al-Abed Y, Callaway D, Peng T, Calandra T, Metz C, Bucala R. Biochemical and Mutational Investigations of the Enzymatic Activity of Macrophage Migration Inhibitory Factor †. Biochemistry 1997, 36: 15356-15362. PMID: 9398265, DOI: 10.1021/bi971153a.Peer-Reviewed Original ResearchConceptsEnzymatic activityL-dopachrome methyl esterN-terminal proline residueSite-directed mutagenesisAmino acid residuesDopachrome tautomerase activityNative solution conditionsMutant proteinsProtein domainsStable trimer formationCarboxy terminusBasic residuesN-terminusProline residuesSDS-PAGE analysisBacterial enzymesHomotrimeric structureAcid residuesCatalytic functionEnzymatic mechanismMutational investigationTrimer formationLow protein concentrationsBiochemical analysisInternal histidine
1996
An agent cleaving glucose-derived protein crosslinks in vitro and in vivo
Vasan S, Zhang X, Zhang X, Kapurniotu A, Bernhagen J, Teichberg S, Basgen J, Wagle D, Shih D, Terlecky I, Bucala R, Cerami A, Egan J, Ulrich P. An agent cleaving glucose-derived protein crosslinks in vitro and in vivo. Nature 1996, 382: 275-278. PMID: 8717046, DOI: 10.1038/382275a0.Peer-Reviewed Original ResearchMeSH KeywordsAmyloid beta-PeptidesAnimalsCross-Linking ReagentsDiabetes MellitusGlucoseGlycation End Products, AdvancedImmunoglobulin GRatsSerum AlbuminThiazolesConceptsAGE crosslinksAdvanced glycation pathwayLow-density lipoproteinPotential therapeutic approachPotential pharmacological strategiesFormation of AGEsReactive α-dicarbonylsPharmacological strategiesGlycation pathwayTherapeutic approachesAdvanced glycationNon-enzymatic glycosylationCollagen crosslinkingNormal agingN-phenacylthiazolium bromideConnective tissueCellular receptorsAgeGlycationTissueProtein crosslinksPost-translational modification processMatrix componentsVivo pointAccelerated rate