2002
Synthesis and Characterization of the First Potent Inhibitor of Yapsin 1 IMPLICATIONS FOR THE STUDY OF YAPSIN-LIKE ENZYMES*
Cawley NX, Chino M, Maldonado A, Rodriguez YM, Loh YP, Ellman JA. Synthesis and Characterization of the First Potent Inhibitor of Yapsin 1 IMPLICATIONS FOR THE STUDY OF YAPSIN-LIKE ENZYMES*. Journal Of Biological Chemistry 2002, 278: 5523-5530. PMID: 12468548, DOI: 10.1074/jbc.m207230200.Peer-Reviewed Original ResearchConceptsYapsin 1Aspartyl proteaseN-terminal amino acid sequence analysisYeast expression systemAmino acid sequence analysisSecreted aspartyl proteaseAcid sequence analysisPotent peptidic inhibitorsSingle-step purificationBasic residuesExpression systemSequence analysisApparent homogeneityPeptidic inhibitorsHuman pathogensPeptide sequencesNonmammalian sourcesFirst potent inhibitorPotent inhibitorProteaseEnzymeCandida albicansSequenceInhibitorsPurification
1993
Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe
ZIMMERLY S, DRAINAS D, SYLVERS L, Dieter S. Identification of a 100‐kDa protein associated with nuclear ribonuclease P activity in Schizosaccharomyces pombe. The FEBS Journal 1993, 217: 501-507. PMID: 8223594, DOI: 10.1111/j.1432-1033.1993.tb18270.x.Peer-Reviewed Original ResearchConceptsFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeGlycerol gradient fractionationCross-linking experimentsPrecursor tRNAsSchizosaccharomyces pombeRibonuclease PProtein interactsRNA componentProtein componentsP activityRibonuclease P activityApparent homogeneityDEAE-cellulose chromatographyPhosphocellulose chromatographySpecific fashionProtein
1991
The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase
Ilag L, Jahn D, Eggertsson G, Söll D. The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase. Journal Of Bacteriology 1991, 173: 3408-3413. PMID: 2045363, PMCID: PMC207952, DOI: 10.1128/jb.173.11.3408-3413.1991.Peer-Reviewed Original ResearchMeSH KeywordsAminolevulinic AcidCentrifugation, Density GradientChromatography, High Pressure LiquidCloning, MolecularDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEscherichia coliIntramolecular TransferasesIsomerasesMolecular WeightPyridoxal PhosphatePyridoxamineTransformation, GeneticConceptsGlu-tRNA reductaseTRNA-dependent transformationApparent native molecular massMolecular massGlutamyl-tRNA synthetaseNative molecular massAminoglycoside antibiotic kanamycinHemL geneWild-type DNAAuxotrophic phenotypeC5 pathwaySodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisMap positionGSA aminotransferasePhysical mappingSulfate-polyacrylamide gel electrophoresisRate zonal sedimentationGene productsThird enzymeGlycerol gradientsApparent homogeneityAntibiotic kanamycinEscherichia coliPure protein
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
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