Evidence map›Paper›PMID 29556863›Full record

ArticleThe AAPS journal2018

Development of Fc-Fused Cocaine Hydrolase for Cocaine Addiction Treatment: Catalytic and Pharmacokinetic Properties.

Xiabin Chen, Jing Deng, Wenpeng Cui, Shurong Hou, Jinling Zhang, Xirong Zheng, Xin Ding, Huimei Wei, Ziyuan Zhou, Kyungbo Kim and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The AAPS journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
1.0field-weighted citation impact, top 24% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 18 citations in OpenAlex.

  1. Pooled it
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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

12 authors at 1 institution in 1 country.

Xiabin ChenMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Jing DengMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Wenpeng CuiMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Shurong HouMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Jinling ZhangMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Xirong ZhengMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Xin DingMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Huimei WeiMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Ziyuan ZhouMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Kyungbo KimMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Chang-Guo ZhanMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA. zhan@uky.edu.
Fang ZhengMolecular Modeling and Biopharmaceutical Center (MMBC) and Department of Pharmaceutical Sciences, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA. fzhen2@email.uky.edu.
University of Kentucky · US

Funding

Development of Long-acting Cocaine Hydrolase as a Treatment for Cocaine AbuseUH3DA041115 · NIDA · UNIVERSITY OF KENTUCKY · PI ZHAN, CHANG-GUO · 2017 to 2019
$3.8M
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 Long-acting Cocaine Hydrolase as a Treatment for Cocaine AbuseUH2DA041115 · NIDA · UNIVERSITY OF KENTUCKY · PI ZHAN, CHANG-GUO · 2015 to 2016
$2.2M
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 R01 DA025100NIDA NIH HHS R01 DA032910NIDA NIH HHS R01 DA035552NIDA NIH HHS UH2 DA041115NIDA NIH HHS UH3 DA041115
6 · The paper itself

Abstract

Cocaine abuse is a worldwide public health and social problem without a US Food and Drug Administration (FDA)-approved medication. Accelerating cocaine metabolism that produces biologically inactive metabolites by administration of an efficient cocaine hydrolase (CocH) has been recognized as a promising strategy for cocaine abuse treatment. However, the therapeutic effects of CocH are limited by its short biological half-life (e.g., 8 h or shorter in rats). In this study, we designed and prepared a set of Fc-fusion proteins constructed by fusing Fc(M3) with CocH3 at the N-terminus of CocH3. A linker between the two protein domains was optimized to improve both the biological half-life and catalytic activity against cocaine. It has been concluded that Fc(M3)-G

Indexed as

AnimalsCarboxylic Ester HydrolasesCatalysisCHO CellsCocaine-Related DisordersCricetulusHalf-LifeImmunoglobulin Fc FragmentsMaleProtein EngineeringRats, Sprague-DawleyRecombinant Fusion ProteinsRecombinant ProteinsCarboxylic Ester Hydrolasescocaine hydrolaseImmunoglobulin Fc FragmentsRecombinant Fusion ProteinsRecombinant Proteinscocainedrug abusemetabolic enzymeprotein engineering

Identifiers

PMID29556863
PMCPMC7734446
OpenAlexW2793086096

What OpenQuestion holds

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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.