Thermostable variants of cocaine esterase for long-time protection against cocaine toxicity - Wikidata - awgldk - TriplyDB

Thermostable variants of cocaine esterase for long-time protection against cocaine toxicity

Thermostable variants of cocaine esterase for long-time protection against cocaine toxicity

http://www.wikidata.org/entity/Q34873465

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A Thermally Stable Form of Bacterial Cocaine Esterase: A Potential Therapeutic Agent for Treatment of Cocaine Abuse Structural analysis of thermostabilizing mutations of cocaine esterase Subunit Stabilization and Polyethylene Glycolation of Cocaine Esterase Improves In Vivo Residence Time Rational Design, Preparation, and Characterization of a Therapeutic Enzyme Mutant with Improved Stability and Function for Cocaine Detoxification Biologic Approaches to Treat Substance-Use Disorders Rapid Bioinformatic Identification of Thermostabilizing Mutations Modeling of pharmacokinetics of cocaine in human reveals the feasibility for development of enzyme therapies for drugs of abuse A thermostable bacterial cocaine esterase rapidly eliminates cocaine from brain in nonhuman primates Modulating the thermostability of Endoglucanase I from Trichoderma reesei using computational approaches.Design of high-activity mutants of human butyrylcholinesterase against (-)-cocaine: structural and energetic factors affecting the catalytic efficiency.PEGylation of bacterial cocaine esterase for protection against protease digestion and immunogenicity Anti-cocaine vaccine development.Novel pharmacological approaches to treatment of drug overdose and addiction Design, preparation, and characterization of high-activity mutants of human butyrylcholinesterase specific for detoxification of cocaine.Enhancement of proteolytic activity of a thermostable papain-like protease by structure-based rational design.Amelioration of the cardiovascular effects of cocaine in rhesus monkeys by a long-acting mutant form of cocaine esterase.Effects of a long-acting mutant bacterial cocaine esterase on acute cocaine toxicity in rats.Enzyme-therapy approaches for the treatment of drug overdose and addiction.Are pharmacokinetic approaches feasible for treatment of cocaine addiction and overdose?Evaluation of the hydrolytic activity of a long-acting mutant bacterial cocaine in the presence of commonly co-administered drugs.The ability of bacterial cocaine esterase to hydrolyze cocaine metabolites and their simultaneous quantification using high-performance liquid chromatography-tandem mass spectrometry The fate of bacterial cocaine esterase (CocE): an in vivo study of CocE-mediated cocaine hydrolysis, CocE pharmacokinetics, and CocE elimination.Sulfhydryl-specific PEGylation of phosphotriesterase cysteine mutants for organophosphate detoxification.Bacterial cocaine esterase: a protein-based therapy for cocaine overdose and addiction Pharmacokinetic strategies for treatment of drug overdose and addiction.FireProt: Energy- and Evolution-Based Computational Design of Thermostable Multiple-Point Mutants Long-lasting effects of a PEGylated mutant cocaine esterase (CocE) on the reinforcing and discriminative stimulus effects of cocaine in rats.Cell permeable cocaine esterases constructed by chemical conjugation and genetic recombination.Uricases as therapeutic agents to treat refractory gout: Current states and future directions.Repeated administration of a mutant cocaine esterase: effects on plasma cocaine levels, cocaine-induced cardiovascular activity, and immune responses in rhesus monkeys.Plants as a source of butyrylcholinesterase variants designed for enhanced cocaine hydrolase activity.Reply to Curry and Coombs: Benzoic acid is formed predominantly from the benzoyl ester hydrolysis in the presence of cocaine hydrolase.Fundamental reaction mechanism and free energy profile for (-)-cocaine hydrolysis catalyzed by cocaine esterase Cocaine esterase prevents cocaine-induced toxicity and the ongoing intravenous self-administration of cocaine in rats.Recent progress in protein drug design and discovery with a focus on novel approaches to the development of anti-cocaine medications.Amino-acid mutations to extend the biological half-life of a therapeutically valuable mutant of human butyrylcholinesterase.A highly efficient cocaine-detoxifying enzyme obtained by computational design.Flavin-containing reductase: new perspective on the detoxification of nitrobenzodiazepine.Computational design of protein-ligand interfaces: potential in therapeutic development.Stabilizing biocatalysts.

P2860

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P2860

Thermostable variants of cocaine esterase for long-time protection against cocaine toxicity

http://www.wikidata.org/entity/Q34873465

description

2008 nî lūn-bûn

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2008 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

Thermostable variants of cocai ...... ction against cocaine toxicity

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Thermostable variants of cocai ...... ction against cocaine toxicity

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Thermostable variants of cocai ...... ction against cocaine toxicity

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type

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Thermostable variants of cocai ...... ction against cocaine toxicity

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Thermostable variants of cocai ...... ction against cocaine toxicity

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Thermostable variants of cocai ...... ction against cocaine toxicity

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Thermostable variants of cocai ...... ction against cocaine toxicity

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Thermostable variants of cocai ...... ction against cocaine toxicity

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Thermostable variants of cocai ...... ction against cocaine toxicity

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P1433

Molecular Pharmacology

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Thermostable variants of cocai ...... ction against cocaine toxicity

@en

P2093

Chang-Guo Zhan

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

Daquan Gao

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

Diwahar L Narasimhan

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Donald W Landry

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James H Woods

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Remy Brim

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Roger K Sunahara

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P2860

Design of a Novel Globular Protein Fold with Atomic-Level Accuracy

Most efficient cocaine hydrolase designed by virtual screening of transition states

Native protein sequences are close to optimal for their structures

Crystal structure of a bacterial cocaine esterase

Biochemical characterization and structural analysis of a highly proficient cocaine esterase

Design, structure and stability of a hyperthermophilic protein variant

Chemistry, design, and structure-activity relationship of cocaine antagonists

Gene cloning and nucleotide sequencing and properties of a cocaine esterase from Rhodococcus sp. strain MB1

A catalytic antibody against cocaine prevents cocaine's reinforcing and toxic effects in rats

Computational design of receptor and sensor proteins with novel functions.

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318-323

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scholarly article

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10.1124/MOL.108.049486

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2

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75

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Joanne Macdonald

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2008-11-05T00:00:00Z

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23454391

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18987161

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2684895

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