about
Structural, kinetic, and docking studies of artificial imine reductases based on biotin-streptavidin technology: an induced lock-and-key hypothesisImproving the Catalytic Performance of an Artificial Metalloenzyme by Computational DesignAn Iron-Based Molecular Redox Switch as a Model for Iron Release from Enterobactin via the Salicylate Binding ModeArtificial metalloenzymes based on biotin-avidin technology for the enantioselective reduction of ketones by transfer hydrogenation.Library design and screening protocol for artificial metalloenzymes based on the biotin-streptavidin technology.Artificial metalloenzymes: proteins as hosts for enantioselective catalysis.Light-driven electron injection from a biotinylated triarylamine donor to [Ru(diimine)3](2+)-labeled streptavidin.Design strategies for the creation of artificial metalloenzymes.From Photodriven Charge Accumulation to Fueling Enzyme Cascades in Molecular Factories.Toward a Broadly Applicable Force Field for d(6)-Piano Stool Complexes.Profluorescent substrates for the screening of olefin metathesis catalysts.Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes.Supramolecular cluster catalysis: benzene hydrogenation catalyzed by a cationic triruthenium cluster under biphasic conditions.Expression and purification of a recombinant avidin with a lowered isoelectric point in Pichia pastoris.Artificial metalloenzymes for enantioselective catalysis based on biotin-avidin.Artificial metalloenzymes: (strept)avidin as host for enantioselective hydrogenation by achiral biotinylated rhodium-diphosphine complexes.Electrophoretic behavior of streptavidin complexed to a biotinylated probe: a functional screening assay for biotin-binding proteins.Burkavidin: a novel secreted biotin-binding protein from the human pathogen Burkholderia pseudomallei.Chemical optimization of artificial metalloenzymes based on the biotin-avidin technology: (S)-selective and solvent-tolerant hydrogenation catalysts via the introduction of chiral amino acid spacers.Tailoring the active site of chemzymes by using a chemogenetic-optimization procedure: towards substrate-specific artificial hydrogenases based on the biotin-avidin technology.Chemically programmed supramolecular assembly of hemoprotein and streptavidin with alternating alignment.Bioorganic and bioinorganic chemistry.High-level secretion of recombinant full-length streptavidin in Pichia pastoris and its application to enantioselective catalysis.Immobilization of an artificial imine reductase within silica nanoparticles improves its performance.Genetic Engineering of an Artificial Metalloenzyme for Transfer Hydrogenation of a Self-Immolative Substrate in Escherichia coli's PeriplasmSynthesis of salicylamide and bipyridine containing ligands for iron(II) and iron(III) coordinationArtificial metalloenzymes for the diastereoselective reduction of NAD+ to NAD2HEvaluation of the Formate Dehydrogenase Activity of Three-Legged Pianostool Complexes in Dilute Aqueous SolutionForewordComputational Insights on an Artificial Imine Reductase Based on the Biotin–Streptavidin TechnologyEfficient Expression and Mutation of Avidin and Streptavidin as Host Proteins for Enantioselective CatalysisOn-cell catalysis by surface engineering of live cells with an artificial metalloenzymeChemical Optimization of Whole-Cell Transfer Hydrogenation Using Carbonic Anhydrase as Host ProteinAqueous olefin metathesis: recent developments and applicationsArtificial Metalloenzymes Based on the Biotin-Streptavidin Technology: Enzymatic Cascades and Directed EvolutionArtificial transfer hydrogenases based on the biotin-(strept)avidin technology: fine tuning the selectivity by saturation mutagenesis of the host proteinDesign of a functional nitric oxide reductase within a myoglobin scaffoldIdentification of two-histidines one-carboxylate binding motifs in proteins amenable to facial coordination to metalsMerging the best of two worlds: artificial metalloenzymes for enantioselective catalysisOsO4·streptavidin: a tunable hybrid catalyst for the enantioselective cis-dihydroxylation of olefins
P50
Q27695716-7CD44EDB-09BA-49FA-8E6A-B3625FC1DF0CQ27701695-E644CF26-CC35-4094-B981-748DAFC2F5F1Q28201676-E2C48D51-5070-4568-B2F4-30B8237ADB68Q33935114-8EEA3EDF-3C72-4A30-803D-0A8D62F8EEBDQ35975143-96EE0A35-8193-4D48-9916-F9275BD596C1Q36075334-4A5CB205-1EBB-4FA0-983F-88BBEBFA8F47Q36076307-CF464A0C-FDDD-4A4B-BDDD-146D01AB6D45Q37673486-4B4EC35B-5B80-4E01-B582-614704BB3499Q38882067-499E41D3-2779-4ABA-9B47-F5068873EC89Q40303821-BC27057B-DD62-4803-A0C3-1DDD04B5DAD9Q42207899-5F0FC0FF-0AA2-425B-A6E5-DC9EF4DBA396Q43413089-8DDBCCC2-166B-4A3F-AEC5-C57D23E88BEBQ44255489-865CE2FC-191F-4E4F-B3FC-DD69A820D5BBQ44765512-41B7D27D-3E59-4C41-BDF7-DC74B5B50515Q45060144-64FBBD3E-A7E2-445D-9DD0-08CAACF361B3Q45135289-AB732536-A110-4994-888B-AA56A709F7ABQ45205551-63F0A584-739A-47DD-B87E-E540A60CF6A0Q46324744-3823271D-6993-46E7-8482-32098AF1903BQ46727310-0546F04A-CEFB-4DCC-A659-DC239C11CE52Q46795538-D4B14CC2-2EFC-498C-B6B5-A89589AF453CQ50253048-ED39929B-D469-4DF0-8FD3-7DB01F90FC4AQ51730881-7B707C57-6AE7-456D-8263-9FD9E38025E2Q54301221-427DE86F-8132-47A7-8685-1D635325DD2FQ54391939-474784DF-F71B-4D0A-B845-F50D739C3AA6Q57037374-D25A0CAF-6D63-4675-80F3-CB2A208AF1E9Q57503243-7FF77336-6AE0-4638-BE2C-50355548F7E0Q57786604-DD2FD26D-ADB2-4DFB-9803-1A98EF5EB129Q57786655-7AE1F3B7-350A-43E1-91FA-FACA394228C3Q58048641-D8F05B40-DABC-48BE-BF51-27F5FACBA159Q58571663-CD703310-7210-4AF2-901D-D30154761824Q60691601-B0418A77-3AD9-4979-8BFE-7404A88A6B0BQ64027810-34A2B611-2E76-445E-8BAE-827AC316DD68Q64070140-4B551259-3877-49D2-9409-4DF3F7899595Q64240918-4C9F1D6D-28A1-48A8-A35B-9AADEB7BB099Q64273919-265B100A-F6FC-47B8-8CC2-53986804D1C5Q79758532-A50C5259-E598-4393-9321-F2A96B6D1A99Q83198042-3183A124-4987-4EA0-A846-437D508F15D1Q83577027-BB11236E-5813-4C30-AD76-6FD736ED7FBBQ84169342-E6F18ECF-D82C-48BA-BE3E-72F3A802528AQ84990743-2F5598DD-2072-4CBF-A542-083D3E5FB380
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Thomas R Ward
@ast
Thomas R Ward
@en
Thomas R Ward
@es
Thomas R Ward
@nl
type
label
Thomas R Ward
@ast
Thomas R Ward
@en
Thomas R Ward
@es
Thomas R Ward
@nl
prefLabel
Thomas R Ward
@ast
Thomas R Ward
@en
Thomas R Ward
@es
Thomas R Ward
@nl
P108
P106
P31
P496
0000-0001-8602-5468