2025
A fluorescence-based assay for measuring aminopropyltransferase activity
Singh P, Choi J, Ben Mamoun C. A fluorescence-based assay for measuring aminopropyltransferase activity. Methods In Enzymology 2025, 715: 363-388. PMID: 40382149, DOI: 10.1016/bs.mie.2025.01.067.Peer-Reviewed Original ResearchConceptsAminopropyl transferaseFluorescence-based assaySpermine synthase activityHigh-throughput chemical screeningSaccharomyces cerevisiaeFormation of spermidinePrincipal polyaminesCellular processesHigh-throughput screeningCellular functionsSubstrate analogsSpermidine synthaseDrug discovery effortsPolyamine biosynthesisLiving cellsChemical screeningEnzymeNeurodegenerative disordersPolycationic alkylaminesSynthase activityDiscovery effortsNovel inhibitorsAPT activityChemical librariesInfectious diseases
2024
A fluorescence-based assay for measuring polyamine biosynthesis aminopropyl transferase–mediated catalysis
Singh P, Choi J, Wang W, Lam T, Lechner P, Vanderwal C, Pou S, Nilsen A, Mamoun C. A fluorescence-based assay for measuring polyamine biosynthesis aminopropyl transferase–mediated catalysis. Journal Of Biological Chemistry 2024, 300: 107832. PMID: 39342998, PMCID: PMC11541840, DOI: 10.1016/j.jbc.2024.107832.Peer-Reviewed Original ResearchAminopropyl transferaseFluorescence-based assayLack of high-throughput assaysHigh-throughput screeningCarbon chain lengthChemical librariesMass spectrometryChain lengthHigh-throughput assayDrug discoveryMass spectrometry analysisSaccharomyces cerevisiaeThin-layer chromatographyFluorescence intensityCellular functionsSpectrometry analysisPolycationic moleculesFluorescent conjugatesIsoindoleAPT activityCatalysisAssayBenzeneAdductsEnzyme
2007
Substrate activity screening (SAS): a general procedure for the preparation and screening of a fragment-based non-peptidic protease substrate library for inhibitor discovery
Patterson AW, Wood WJ, Ellman JA. Substrate activity screening (SAS): a general procedure for the preparation and screening of a fragment-based non-peptidic protease substrate library for inhibitor discovery. Nature Protocols 2007, 2: 424-433. PMID: 17406604, DOI: 10.1038/nprot.2007.28.Peer-Reviewed Original ResearchConceptsSubstrate Activity ScreeningRapid analog synthesisSolid-phase synthesisActivity screeningSimple fluorescence-based assayFragment-based methodsNon-peptidic inhibitorsN-acyl groupAnalog synthesisInhibitor discoveryFluorescence-based assayWeak binding substratesBinding substrateSubstrate librariesAminocoumarinsProtease substratesSynthesisSubstrateGeneral procedureDirect replacementPharmacophoreNovel substratePreparationConversionCys
2005
Substrate Activity Screening: A Fragment-Based Method for the Rapid Identification of Nonpeptidic Protease Inhibitors
Wood WJ, Patterson AW, Tsuruoka H, Jain RK, Ellman JA. Substrate Activity Screening: A Fragment-Based Method for the Rapid Identification of Nonpeptidic Protease Inhibitors. Journal Of The American Chemical Society 2005, 127: 15521-15527. PMID: 16262416, DOI: 10.1021/ja0547230.Peer-Reviewed Original ResearchConceptsSubstrate Activity ScreeningRapid analog synthesisSimple fluorescence-based assayFragment-based methodsSubstrate-based methodLow molecular weightN-acyl groupAnalog synthesisNonpeptidic inhibitorsFluorescence-based assaySubstrate classesMolecular weightActivity screeningAldehyde inhibitorsAminocoumarinsMultiple distinct classesProtease substratesSAS methodNanomolar affinityCleavage efficiencyCysteine protease cathepsin SSubstrateRapid identificationProtease cathepsin SDirect replacement
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