2021
Pregabalin Treatment does not Affect Amyloid Pathology in 5XFAD Mice
Sadleir K, Popovoic J, Zhu W, Reidel C, Do H, Silverman R, Vassar R. Pregabalin Treatment does not Affect Amyloid Pathology in 5XFAD Mice. Current Alzheimer Research 2021, 18: 283-297. PMID: 34259145, PMCID: PMC9527523, DOI: 10.2174/1567205018666210713125333.Peer-Reviewed Original ResearchConceptsVoltagegated calcium channelsPlacebo-treated miceNeuropathic painPregabalin treatmentStatistically significant positive correlationCalcium channelsCalcium influxAb levelsDecreased markersPregabalinSignificant positive correlationCerebral concentrationsEffective treatmentAmyloid depositsCausative roleDystrophyCalcium dysregulationMiceNeuritic dystrophyProgression of amyloid pathologyPathologyImmunofluorescence imagingNeuronal processesPlaqueTreatment
1993
Inactivation of monoamine oxidase B by analogues of the anticonvulsant agent milacemide (2-(n-pentylamino)acetamide).
Nishimura K, Lu X, Silverman R. Inactivation of monoamine oxidase B by analogues of the anticonvulsant agent milacemide (2-(n-pentylamino)acetamide). Journal Of Medicinal Chemistry 1993, 36: 446-8. PMID: 8474100, DOI: 10.1021/jm00056a004.Peer-Reviewed Original ResearchConceptsInactivation of monoamine oxidase BElectron-withdrawing abilityCarboxylic acidsLinear free energy relationshipFree energy relationshipNitriles 2Trifluoromethylated compoundsMonoamine oxidase BTrifluoromethyl groupCyanomethyl groupCarboxamide groupEnergy relationshipCarbethoxy groupOrganic cosolventsNitrileCompoundsInactivation efficiencyAnaloguesPartition ratioIrreversible inactivationSubstituentsCyanomethylSubstrateCarboxamideAcid
1990
Substituted vitamin K epoxide analogues. New competitive inhibitors and substrates of vitamin K1 epoxide reductase.
Ryall R, Nandi D, Silverman R. Substituted vitamin K epoxide analogues. New competitive inhibitors and substrates of vitamin K1 epoxide reductase. Journal Of Medicinal Chemistry 1990, 33: 1790-7. PMID: 2342073, DOI: 10.1021/jm00168a038.Peer-Reviewed Original Research
1985
Purification of a vitamin K epoxide reductase that catalyzes conversion of vitamin K 2,3-epoxide to 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone.
Mukharji I, Silverman R. Purification of a vitamin K epoxide reductase that catalyzes conversion of vitamin K 2,3-epoxide to 3-hydroxy-2-methyl-3-phytyl-2,3-dihydronaphthoquinone. Proceedings Of The National Academy Of Sciences Of The United States Of America 1985, 82: 2713-2717. PMID: 3857611, PMCID: PMC397635, DOI: 10.1073/pnas.82.9.2713.Peer-Reviewed Original ResearchConceptsVitamin K epoxide reductaseVitamin K 2,3-epoxideReduction of vitamin K 2,3-epoxidePolyacrylamide slab gel electrophoresisSlab gel electrophoresisPresence of sodium dodecyl sulfatePurified enzymeChromophore cofactorsIdentical subunitsApparent homogeneityGel electrophoresisNative enzymeDEAE-celluloseDenatured enzymeConcentrations of glycerolGel filtrationCatalyzes conversionS-200EnzymeBovine liver microsomesPBE-94ReductaseSodium dodecyl sulfateDodecyl sulfateMolecular weight
1977
Mechanism of inactivation of gamma-cystathionase by beta,beta,beta-trifluoroalanine.
Silverman R, Abeles R. Mechanism of inactivation of gamma-cystathionase by beta,beta,beta-trifluoroalanine. Biochemistry 1977, 16: 5515-20. PMID: 921947, DOI: 10.1021/bi00644a019.Peer-Reviewed Original Research