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 ResearchConceptsAGE 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
1985
Nonenzymatic modification of lens crystallins by prednisolone induces sulfhydryl oxidation and aggregate formation: In vitro and in vivo studies
Bucala R, Manabe S, Urban R, Cerami A. Nonenzymatic modification of lens crystallins by prednisolone induces sulfhydryl oxidation and aggregate formation: In vitro and in vivo studies. Experimental Eye Research 1985, 41: 353-363. PMID: 4065253, DOI: 10.1016/s0014-4835(85)80026-9.Peer-Reviewed Original ResearchConceptsSteroid-induced cataractPossible pharmacological strategiesSteroid therapyLens crystallinsPharmacological strategiesLens opacitiesNonenzymatic modificationGlucocorticoid prednisoloneToxic manifestationsTherapeutic levelsPrednisoloneCataractogenic effectVivo studiesGlucocorticoidsCataractLens proteinsSulfhydryl oxidationGel filtration chromatographyPrevious studiesAddition of dithiothreitol