Evidence map›Paper›PMID 20161378›Full record

ReviewFuture medicinal chemistry2009

Recent progress in protein drug design and discovery with a focus on novel approaches to the development of anti-cocaine medications.

Fang Zheng, Chang-Guo Zhan

Open access · greenAbstract readReview
In one paragraph

Review in Future medicinal chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

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  12. Epigenetics: a link between addiction and social environment.Cellular and molecular life sciences : CMLS · 2017
    Review
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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

2 authors at 1 institution in 1 country.

Fang ZhengDepartment of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 725 Rose Street, Lexington, KY 40536, USA.
Chang-Guo Zhan
University of Kentucky · US

Funding

Development of Esterases for the Treatment of Cocaine Overdose and AbuseR01DA021416 · NIDA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WOODS, JAMES H · 2006 to 2009
$2.8M
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
NIDA NIH HHS R01 DA013930NIDA NIH HHS R01 DA021416NIDA NIH HHS R01 DA025100
6 · The paper itself

Abstract

Cocaine is highly addictive and no anti-cocaine medication is currently available. Accelerating cocaine metabolism, producing biologically inactive metabolites, is recognized as an ideal anti-cocaine medication strategy, especially for the treatment of acute cocaine toxicity. However, currently known wild-type enzymes have either too low a catalytic efficiency against the abused cocaine, in other words (-)-cocaine, or the in vivo half-life is too short. Novel computational strategies and design approaches have been developed recently to design and discover thermostable or high-activity mutants of enzymes based on detailed structures and catalytic/inactivation mechanisms. The structure- and mechanism-based computational design efforts have led to the discovery of high-activity mutants of butyrylcholinesterase and thermostable mutants of cocaine esterase as promising anti-cocaine therapeutics. The structure- and mechanism-based computational strategies and design approaches may be used to design high-activity and/or thermostable mutants of many other proteins that have clear therapeutic potentials and to design completely new therapeutic enzymes.

Indexed as

Binding SitesButyrylcholinesteraseCarboxylic Ester HydrolasesCocaineComputer SimulationDrug DesignDrug Evaluation, PreclinicalHumansButyrylcholinesteraseCarboxylic Ester HydrolasesCocainecocaine esterase

Identifiers

PMID20161378
PMCPMC2780362
OpenAlexW2066330320

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

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.