Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines - Wikidata - wikimedia - TriplyDB

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

http://www.wikidata.org/entity/Q27666976

about

Protein design: toward functional metalloenzymes Tailoring D-amino acid oxidase from the pig kidney to R-stereoselective amine oxidase and its use in the deracemization of α-methylbenzylamine Covalent Anchor Positions Play an Important Role in Tuning Catalytic Properties of a Rationally Designed MnSalen-containing Metalloenzyme Library design and screening protocol for artificial metalloenzymes based on the biotin-streptavidin technology.Light-driven electron injection from a biotinylated triarylamine donor to [Ru(diimine)3](2+)-labeled streptavidin.Supramolecular catalysis. Part 2: artificial enzyme mimics.Transition metal catalysis in confined spaces.Artificial concurrent catalytic processes involving enzymes.Genetic Optimization of Metalloenzymes: Enhancing Enzymes for Non-Natural Reactions.Imino Transfer Hydrogenation Reductions.Unravelling novel synergies between organometallic and biological partners: a quantum mechanics/molecular mechanics study of an artificial metalloenzyme.Novel artificial metalloenzymes by in vivo incorporation of metal-binding unnatural amino acids.An (R)-Imine Reductase Biocatalyst for the Asymmetric Reduction of Cyclic Imines Engineering a dirhodium artificial metalloenzyme for selective olefin cyclopropanation.Synthetic cascades are enabled by combining biocatalysts with artificial metalloenzymes.Magnesium catalysis of imine hydroboration.Directed Evolution of Artificial Imine Reductase.Design of artificial metalloproteins/metalloenzymes by tuning noncovalent interactions.Streptavidin as a Scaffold for Light-Induced Long-Lived Charge Separation.Asymmetric transfer hydrogenation by synthetic catalysts in cancer cells.Immobilization of an artificial imine reductase within silica nanoparticles improves its performance.Coordination chemistry within a protein host: regulation of the secondary coordination sphere.Ligand denticity controls enantiomeric preference in DNA-based asymmetric catalysis Artificial metalloenzymes for the diastereoselective reduction of NAD+ to NAD2H Artificial Metalloenzymes Containing an Organometallic Active Site Conformationally Constrained Cyclic Peptides: Powerful Scaffolds for Asymmetric Catalysis Asymmetric Reduction of Cyclic Imines Catalyzed by a Whole-Cell Biocatalyst Containing an (S)-Imine Reductase

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P2860

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

http://www.wikidata.org/entity/Q27666976

description

2011 nî lūn-bûn

@nan

2011 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի մարտին հրատարակված գիտական հոդված

@hy

2011年の論文

@ja

2011年論文

@yue

2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@ast

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@en

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@nl

type

label

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@ast

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@en

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@nl

prefLabel

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@ast

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@en

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@nl

P1433

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P356

P1433

Angewandte Chemie International Edition

P1476

Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines

@en

P2093

Annette Mutschler

http://www.w3.org/2001/XMLSchema#string

Elisa Nogueira

http://www.w3.org/2001/XMLSchema#string

Julien Pierron

http://www.w3.org/2001/XMLSchema#string

Karoline Kersten

http://www.w3.org/2001/XMLSchema#string

Livia Knörr

http://www.w3.org/2001/XMLSchema#string

Malcolm Jeremy Zimbron

http://www.w3.org/2001/XMLSchema#string

Marc Dürrenberger

http://www.w3.org/2001/XMLSchema#string

Thibaud Rossel

http://www.w3.org/2001/XMLSchema#string

Thomas R Ward

http://www.w3.org/2001/XMLSchema#string

Yvonne M Wilson

http://www.w3.org/2001/XMLSchema#string

P2860

Directed evolution drives the next generation of biocatalysts

X-ray structure and designed evolution of an artificial transfer hydrogenase

Directed evolution of hybrid enzymes: Evolving enantioselectivity of an achiral Rh-complex anchored to a protein.

Design of functional metalloproteins.

Asymmetric transfer hydrogenation of ketones with bifunctional transition metal-based molecular catalysts.

Design strategies for the creation of artificial metalloenzymes.

Protein-based hybrid catalysts--design and evolution.

A highly enantioselective access to tetrahydroisoquinoline and beta-carboline alkaloids with simple noyori-type catalysts in aqueous media.

A chemoenzymatic approach to enantiomerically pure amines using dynamic kinetic resolution: application to the synthesis of norsertraline.

Highly efficient and site-selective phosphane modification of proteins through hydrazone linkage: development of artificial metalloenzymes.

P304

3026-9

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1002/ANIE.201007820

http://www.w3.org/2001/XMLSchema#string

P407

P433

13

http://www.w3.org/2001/XMLSchema#string

P478

50

http://www.w3.org/2001/XMLSchema#string

P50

Tilman Schirmer

Tillmann Heinisch

P577

2011-03-21T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

21404391

http://www.w3.org/2001/XMLSchema#string

P921

enantioselectivity