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

Molecular dynamics simulation of cocaine binding with human butyrylcholinesterase and its mutants.

The journal of physical chemistry. B - 17 Mar 2005

Hamza Adel, Cho Hoon, Tai Hsin-Hsiung, Zhan Chang-Guo

Abstract excerpt

Molecular dynamics (MD) simulations were carried out to study cocaine binding with wild-type human butyrylcholinesterase (BChE) and its mutants based on a recently reported X-ray crystal structure of human BChE. For each BChE-cocaine system, we simulated both the nonprereactive and prereactive co...

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

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Computer Simulation

Share to Crystallography, X-Ray

Share to Hydrolysis

Share to Models, Chemical

Source

Open in PubMed Open full text

Identifiers

PMID: 16851561
DOI: 10.1021/jp0447136
PMCID: PMC2882242

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-16851561-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Molecular dynamics simulation of cocaine binding with human butyrylcholinesterase and its mutants.PMID 16851561Read ↗

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

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

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

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

Model of Human Butyrylcholinesterase Tetramer by Homology Modeling and Dynamics SimulationSemantic proximity Read ↗

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

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

Cocaine esterase-cocaine binding process and the free energy profiles by molecular dynamics and potential of mean force simulations.Semantic proximity Read ↗

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