VIAF

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Leader 00000nz a2200037n 45 0
001 WKP|Q88998412 (VIAF cluster) (Authority/Source Record)
003 WKP
005 20241121000344.0
008 241121nneanz||abbn n and d
035 ‎‡a (WKP)Q88998412‏
024 ‎‡a 0000-0002-4439-7738‏ ‎‡2 orcid‏
035 ‎‡a (OCoLC)Q88998412‏
100 0 ‎‡a Liam A Wilson‏ ‎‡c researcher‏ ‎‡9 en‏
400 0 ‎‡a Liam A Wilson‏ ‎‡c onderzoeker‏ ‎‡9 nl‏
670 ‎‡a Author's Adaptation of a continuous, calorimetric kinetic assay to study the agmatinase-catalyzed hydrolytic reaction‏
670 ‎‡a Author's Biomimetics for purple acid phosphatases: A historical perspective‏
670 ‎‡a Author's Broad spectrum antibiotic-degrading metallo-β-lactamases are phylogenetically diverse and widespread in the environment‏
670 ‎‡a Author's Enhancement of antibiotic-activity through complexation with metal ions - Combined ITC, NMR, enzymatic and biological studies.‏
670 ‎‡a Author's Kinetic and Structural Characterization of the First B3 Metallo-β-Lactamase with an Active-Site Glutamic Acid‏
670 ‎‡a Author's Mammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases‏
670 ‎‡a Author's Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms‏
909 ‎‡a (orcid) 0000000244397738‏ ‎‡9 1‏
919 ‎‡a biomimeticsforpurpleacidphosphatasesahistoricalperspective‏ ‎‡A Biomimetics for purple acid phosphatases: A historical perspective‏ ‎‡9 1‏
919 ‎‡a structureandmechanismofpotentbifunctionalβlactamandhomoserinelactonedegradingenzymesfrommarinemicroorganisms‏ ‎‡A Structure and mechanism of potent bifunctional β-lactam- and homoserine lactone-degrading enzymes from marine microorganisms‏ ‎‡9 1‏
919 ‎‡a mammalianagmatinasesconstituteunusualmembersinthefamilyofmn2+dependentureahydrolases‏ ‎‡A Mammalian agmatinases constitute unusual members in the family of Mn2+-dependent ureahydrolases‏ ‎‡9 1‏
919 ‎‡a kineticandstructuralcharacterizationofthe1b3metalloβlactamasewithanactivesiteglutamicacid‏ ‎‡A Kinetic and Structural Characterization of the First B3 Metallo-β-Lactamase with an Active-Site Glutamic Acid‏ ‎‡9 1‏
919 ‎‡a enhancementofantibioticactivitythroughcomplexationwithmetalionscombineditcnmrenzymaticandbiologicalstudies‏ ‎‡A Enhancement of antibiotic-activity through complexation with metal ions - Combined ITC, NMR, enzymatic and biological studies.‏ ‎‡9 1‏
919 ‎‡a adaptationofacontinuouscalorimetrickineticassaytostudytheagmatinasecatalyzedhydrolyticreaction‏ ‎‡A Adaptation of a continuous, calorimetric kinetic assay to study the agmatinase-catalyzed hydrolytic reaction‏ ‎‡9 1‏
919 ‎‡a broadspectrumantibioticdegradingmetalloβlactamasesarephylogeneticallydiverseandwidespreadintheenvironment‏ ‎‡A Broad spectrum antibiotic-degrading metallo-β-lactamases are phylogenetically diverse and widespread in the environment‏ ‎‡9 1‏
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