Evidence map›Paper›PMID 31661952›Full record

ArticleBioconjugate chemistry2019

PEGylation but Not Fc-Fusion Improves in Vivo Residence Time of a Thermostable Mutant of Bacterial Cocaine Esterase.

Haifeng Huang, Lei Fang, Liu Xue, Ting Zhang, Kyungbo Kim, Shurong Hou, Fang Zheng, Chang-Guo Zhan

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioconjugate chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 35% 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

1 citing paper in PubMed, 4 citations in OpenAlex.

  1. Article
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

8 authors at 1 institution in 1 country.

Haifeng HuangMolecular Modeling and Biopharmaceutical Center, College of Pharmacy , University of Kentucky , Lexington , Kentucky 40536 , United States.
Lei FangDepartment of Pharmaceutical Sciences, College of Pharmacy , University of Kentucky , Lexington , Kentucky 40536 , United States.
Liu XueDepartment of Pharmaceutical Sciences, College of Pharmacy , University of Kentucky , Lexington , Kentucky 40536 , United States.
Ting ZhangMolecular Modeling and Biopharmaceutical Center, College of Pharmacy , University of Kentucky , Lexington , Kentucky 40536 , United States.
Kyungbo KimMolecular Modeling and Biopharmaceutical Center, College of Pharmacy , University of Kentucky , Lexington , Kentucky 40536 , United States.
Shurong HouMolecular Modeling and Biopharmaceutical Center, College of Pharmacy , University of Kentucky , Lexington , Kentucky 40536 , United States.
Fang ZhengMolecular Modeling and Biopharmaceutical Center, College of Pharmacy , University of Kentucky , Lexington , Kentucky 40536 , United States.
Chang-Guo ZhanMolecular Modeling and Biopharmaceutical Center, College of Pharmacy , University of Kentucky , Lexington , Kentucky 40536 , United States.ORCID 0000-0002-4128-7269
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

It is very popular to fuse a protein drug or drug candidate to the Fc domain of immunoglobulin G (IgG) in order to prolong the in vivo half-life. In this study, we have designed, prepared, and tested an Fc-fused thermostable cocaine esterase (CocE) mutant (known as E196-301, with the T172R/G173Q/L196C/I301C substitutions on CocE) expressed in

Indexed as

AnimalsBacterial ProteinsCarboxylic Ester HydrolasesDrug DesignEnzyme StabilityEscherichia coliHalf-LifeImmunoglobulin Fc FragmentsImmunoglobulin GMutant ProteinsPolyethylene GlycolsProteolysisRatsBacterial ProteinsCarboxylic Ester Hydrolasescocaine esteraseImmunoglobulin Fc FragmentsImmunoglobulin GMutant ProteinsPolyethylene Glycols

Identifiers

PMID31661952
PMCPMC7737243
OpenAlexW2982512756

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.