Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Computational design of a human butyrylcholinesterase mutant for accelerating cocaine hydrolysis based on the transition-state simulation.

Angewandte Chemie (International ed. in English) - 16 Jan 2006

Gao Daquan, Cho Hoon, Yang Wenchao, Pan Yongmei, Yang Guangfu, Tai Hsin-Hsiung, Zhan Chang-Guo

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Butyrylcholinesterase
Share to Catalysis
Share to Cocaine
Share to Enzyme Activation

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Hydrogen Bonding

Share to Hydrolysis

Share to Molecular Structure

Share to Stereoisomerism

Source

Open in PubMed Open full text

Identifiers

PMID: 16355430
DOI: 10.1002/anie.200503025
PMCID: PMC2878656

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Computational design of a human butyrylcholinesterase mutant for accelerating cocaine hydrolysis based on the transition-state simulation.PMID 16355430Read ↗

Computational redesign of human butyrylcholinesterase for anticocaine medication.Semantic proximity Read ↗

Rational design of an enzyme mutant for anti-cocaine therapeutics.Semantic proximity Read ↗

Free energy perturbation simulation on transition states and high-activity mutants of human butyrylcholinesterase for (-)-cocaine hydrolysis.Semantic proximity Read ↗

Free-energy perturbation simulation on transition states and redesign of butyrylcholinesterase.Semantic proximity Read ↗

Molecular dynamics simulation of cocaine binding with human butyrylcholinesterase and its mutants.Semantic proximity Read ↗

Free energy perturbation (FEP) simulation on the transition states of cocaine hydrolysis catalyzed by human butyrylcholinesterase and its mutants.Semantic proximity Read ↗

Substrate selectivity of high-activity mutants of human butyrylcholinesterase.Semantic proximity Read ↗

Amino-acid mutations to extend the biological half-life of a therapeutically valuable mutant of human butyrylcholinesterase.Semantic proximity Read ↗

Predicted Michaelis-Menten complexes of cocaine-butyrylcholinesterase. Engineering effective butyrylcholinesterase mutants for cocaine detoxication.Semantic proximity Read ↗

Computational design of a thermostable mutant of cocaine esterase via molecular dynamics simulations.Semantic proximity Read ↗

Characterization of a high-activity mutant of human butyrylcholinesterase against (-)-cocaine.Semantic proximity Read ↗

Why does the G117H mutation considerably improve the activity of human butyrylcholinesterase against sarin? Insights from quantum mechanical/molecular mechanical free energy calculations.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.