Evidence map›Paper›PMID 24290065›Full record

ArticleBioorganic & medicinal chemistry2014

Modeling in vitro inhibition of butyrylcholinesterase using molecular docking, multi-linear regression and artificial neural network approaches.

Fang Zheng, Max Zhan, Xiaoqin Huang, Mohamed Diwan M Abdul Hameed, Chang-Guo Zhan

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
4.5field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  4. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Fang ZhengDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536, United States. Electronic address: fzhen2@email.uky.edu.
Max ZhanDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536, United States.
Xiaoqin HuangDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536, United States.
Mohamed Diwan M Abdul HameedDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536, United States.
Chang-Guo ZhanDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, Lexington, KY 40536, United States. Electronic address: zhan@uky.edu.
University of Kentucky · US

Funding

Long-lasting cocaine-metabolizing enzyme for cocaine addiction treatmentR01DA035552 · NIDA · UNIVERSITY OF KENTUCKY · PI ZHAN, CHANG-GUO · 2013 to 2015
$3.4M
High-activity mutants of cocaine esterase for treatment of drug addictionR01DA025100 · NIDA · UNIVERSITY OF KENTUCKY · PI LANDRY, DONALD W, WOODS, JAMES H · 2008 to 2012
$2.5M
Redesign of Butyrylcholinesterase for Cocaine MetabolismR01DA013930 · NIDA · UNIVERSITY OF KENTUCKY · PI ZHAN, CHANG-GUO · 2003 to 2010
$2.4M
Development of a Cocaine-Metabolizing Enzyme for Drug Overdose TreatmentR01DA032910 · NIDA · UNIVERSITY OF KENTUCKY · PI ZHAN, CHANG-GUO · 2012 to 2015
$1.8M
NIDA NIH HHS R01 DA013930NIDA NIH HHS R01DA013930NIDA NIH HHS R01 DA025100NIDA NIH HHS R01 DA032910NIDA NIH HHS R01DA032910NIDA NIH HHS R01 DA035552NIDA NIH HHS R01DA035552
6 · The paper itself

Abstract

Butyrylcholinesterase (BChE) has been an important protein used for development of anti-cocaine medication. Through computational design, BChE mutants with ∼2000-fold improved catalytic efficiency against cocaine have been discovered in our lab. To study drug-enzyme interaction it is important to build mathematical model to predict molecular inhibitory activity against BChE. This report presents a neural network (NN) QSAR study, compared with multi-linear regression (MLR) and molecular docking, on a set of 93 small molecules that act as inhibitors of BChE by use of the inhibitory activities (pIC₅₀ values) of the molecules as target values. The statistical results for the linear model built from docking generated energy descriptors were: r(2)=0.67, rmsd=0.87, q(2)=0.65 and loormsd=0.90; the statistical results for the ligand-based MLR model were: r(2)=0.89, rmsd=0.51, q(2)=0.85 and loormsd=0.58; the statistical results for the ligand-based NN model were the best: r(2)=0.95, rmsd=0.33, q(2)=0.90 and loormsd=0.48, demonstrating that the NN is powerful in analysis of a set of complicated data. As BChE is also an established drug target to develop new treatment for Alzheimer's disease (AD). The developed QSAR models provide tools for rationalizing identification of potential BChE inhibitors or selection of compounds for synthesis in the discovery of novel effective inhibitors of BChE in the future.

Indexed as

ButyrylcholinesteraseModels, MolecularMolecular Docking SimulationQuantitative Structure-Activity RelationshipButyrylcholinesteraseEnzyme inhibitorMolecular dockingNeural network analysisQSAR

Identifiers

PMID24290065
PMCPMC3919557
OpenAlexW2165554798

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.