2011
Drug Repositioning and Pharmacophore Identification in the Discovery of Hookworm MIF Inhibitors
Cho Y, Vermeire JJ, Merkel JS, Leng L, Du X, Bucala R, Cappello M, Lolis E. Drug Repositioning and Pharmacophore Identification in the Discovery of Hookworm MIF Inhibitors. Cell Chemical Biology 2011, 18: 1089-1101. PMID: 21944748, PMCID: PMC3294498, DOI: 10.1016/j.chembiol.2011.07.011.Peer-Reviewed Original ResearchMeSH KeywordsAncylostomatoideaAnimalsAnti-Inflammatory Agents, Non-SteroidalBinding SitesCatalytic DomainCrystallography, X-RayDiureticsDrug RepositioningFurosemideHigh-Throughput Screening AssaysHookworm InfectionsHumansKineticsMacrophage Migration-Inhibitory FactorsMeclofenamic AcidSmall Molecule LibrariesConceptsNonsteroidal anti-inflammatory drugsMacrophage migration inhibitory factorMigration inhibitory factorAnti-inflammatory drugsIntestinal nematode parasitesSodium meclofenamateHigh-throughput screenMIF inhibitorsAnimal modelsTherapeutic efficacyBioactive compound librariesInhibitory factorHookworm diseaseDiuretic activityPartial protectionTautomerase activityFurosemideDiseaseDrugsFDADrug repositioningSubmicromolar inhibitionInhibitorsNew pharmacophoreDiuretics
2010
Allosteric inhibition of macrophage migration inhibitory factor revealed by ibudilast
Cho Y, Crichlow GV, Vermeire JJ, Leng L, Du X, Hodsdon ME, Bucala R, Cappello M, Gross M, Gaeta F, Johnson K, Lolis EJ. Allosteric inhibition of macrophage migration inhibitory factor revealed by ibudilast. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 11313-11318. PMID: 20534506, PMCID: PMC2895110, DOI: 10.1073/pnas.1002716107.Peer-Reviewed Original ResearchConceptsMacrophage migration inhibitory factorMigration inhibitory factorInhibitory factorPeripheral blood mononuclear cellsBlood mononuclear cellsNeuropathic painOpioid withdrawalMIF receptorBronchial asthmaOcular indicationsMononuclear cellsProinflammatory proteinsAntiinflammatory drugsGlial cellsPossible therapeuticsAntiinflammatory activityChemotactic functionNonselective inhibitorAV411Major receptorTautomerase activityReceptorsAllosteric binding siteAntibody experimentsTreatment
2004
Ancylostoma ceylanicum anticoagulant peptide-1: role of the predicted reactive site amino acid in mediating inhibition of coagulation factors Xa and VIIa
Mieszczanek J, Harrison LM, Cappello M. Ancylostoma ceylanicum anticoagulant peptide-1: role of the predicted reactive site amino acid in mediating inhibition of coagulation factors Xa and VIIa. Molecular And Biochemical Parasitology 2004, 137: 151-159. PMID: 15279961, DOI: 10.1016/j.molbiopara.2004.05.011.Peer-Reviewed Original ResearchConceptsCoagulation factor XaAmino acid sequence similarityFactor XaGastrointestinal blood lossIron deficiency anemiaSite amino acid residuesAmino acid residuesSite amino acidsMechanism of actionBlood lossHookworm infectionSequence similarityDeficiency anemiaLeading causeFactor VIIa/tissue factor complexFactor complexCoagulation inhibitorsPeptide-1Ancylostoma caninum anticoagulant peptide 5Coagulation responseAcid residuesNon-active siteA. ceylanicumAnticoagulantsTissue factor complex
1996
Anticoagulant repertoire of the hookworm Ancylostoma caninum.
Stassens P, Bergum P, Gansemans Y, Jespers L, Laroche Y, Huang S, Maki S, Messens J, Lauwereys M, Cappello M, Hotez P, Lasters I, Vlasuk G. Anticoagulant repertoire of the hookworm Ancylostoma caninum. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 2149-2154. PMID: 8700900, PMCID: PMC39925, DOI: 10.1073/pnas.93.5.2149.Peer-Reviewed Original ResearchConceptsHookworm Ancylostoma caninumReactive site residuesFVIIa/TFBlood coagulation factor VIIaBlood coagulation factor XaMolecular cloningSerine protease inhibitorMammalian hostsCysteine residuesHost hemostasisSite residuesCoagulation factor VIIaHomologous regionsSequence positionsAncylostoma caninumNematode AscarisCatalytic centerBinary complexUnique mechanismCoagulation factor XaProtease inhibitorsResiduesInhibitorsTissue factorThird form