Chemical complementation: a reaction-independent genetic assay for enzyme catalysis. - Wikidata - wikimedia - TriplyDB

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

http://www.wikidata.org/entity/Q34428979

about

Evolution of efficient pathways for degradation of anthropogenic chemicals.Enabling glycosyltransferase evolution: a facile substrate-attachment strategy for phage-display enzyme evolution.Identification of novel benzoylformate decarboxylases by growth selection High-throughput selection for cellulase catalysts using chemical complementation.Nucleating the assembly of macromolecular complexes.Studying disorders of vertebrate iron and heme metabolism using zebrafish.Design and Applications of Bifunctional Small Molecules: Why Two Heads Are Better Than One.Identification and validation of protein targets of bioactive small molecules Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.The yeast three-hybrid system as an experimental platform to identify proteins interacting with small signaling molecules in plant cells: potential and limitations Gene function: getting specific, generally speaking.Selection of biocatalysts for chemical synthesis.Effective molarity redux: Proximity as a guiding force in chemistry and biology.A Heritable Recombination system for synthetic Darwinian evolution in yeast.A human vitamin D receptor mutant activated by cholecalciferol.Transcriptional regulation improves the throughput of three-hybrid counter selections in Saccharomyces cerevisiae.A fusion of disciplines: chemical approaches to exploit fusion proteins for functional genomics.Rational design of p53, an intrinsically unstructured protein, for the fabrication of novel molecular sensors Selection strategies for improved biocatalysts.A small-molecule switch for Golgi sulfotransferases.Translating cancer research by synthetic biology.Applications of genetically-encoded biosensors for the construction and control of biosynthetic pathways.Protein tango: the toolbox to capture interacting partners.Reporter-based screening and selection of enzymes.Methods for the directed evolution of proteins.Synthesis of orthogonally reactive FK506 derivatives via olefin cross metathesis.A system for the continuous directed evolution of biomolecules.Investigation of the mechanism of resistance to third-generation cephalosporins by class C beta-lactamases by using chemical complementation.Transcription factor logic using chemical complementation.Evolution of a split RNA polymerase as a versatile biosensor platform.Glycosynthases in Biocatalysis

P2860

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P2860

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

http://www.wikidata.org/entity/Q34428979

description

2002 nî lūn-bûn

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2002 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

@ast

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

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Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

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type

label

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

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Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

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Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

@nl

prefLabel

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

@ast

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

@en

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis.

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Chemical complementation: a reaction-independent genetic assay for enzyme catalysis

@en

P2093

Colleen Bleczinski

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

Debleena Sengupta

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

Gilda Salazar-Jimenez

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Hening Lin

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Kathleen Baker

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Virginia W Cornish

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P2860

Searching sequence space by definably random mutagenesis: improving the catalytic potency of an enzyme

Function-based isolation of novel enzymes from a large library.

Using an AraC-based three-hybrid system to detect biocatalysts in vivo.

A method for directed evolution and functional cloning of enzymes.

Screening and selection methods for large-scale analysis of protein function.

beta-Galactosidase containing a human immunodeficiency virus protease cleavage site is cleaved and inactivated by human immunodeficiency virus protease

Combinatorial and computational challenges for biocatalyst design.

Rapid assay processing by integration of dual-color fluorescence cross-correlation spectroscopy: high throughput screening for enzyme activity.

Directed evolution of an aspartate aminotransferase with new substrate specificities

Selection for improved subtiligases by phage display.

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16537-16542

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scholarly article

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10.1073/PNAS.262420099

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26

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99

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2002-12-13T00:00:00Z

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10990093

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12482929

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139179

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