ArticleThe AAPS journal2017
Effectiveness of a Cocaine Hydrolase for Cocaine Toxicity Treatment in Male and Female Rats.
Article in The AAPS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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Who cites it
18 citing papers in PubMed, 25 citations in OpenAlex.
- Observation of aldicarb hydrolysis by a cocaine hydrolase.Bioscience reports · 2026Article
- A cocaine hydrolase engineered from human butyrylcholinesterase as a medical countermeasure for aldicarb poisoning.Chemico-biological interactions · 2025Article
- Development of a Ghrelin Deacylase to Attenuate Drug Reward and Associated Effects of Methamphetamine.ACS pharmacology & translational science · 2025Article
- Treatment of acute organophosphate poisoning by using a cocaine hydrolase engineered from human butyrylcholinesterase.Chemico-biological interactions · 2025Article
- In vitro and in vivo stability of a highly efficient long-acting cocaine hydrolase.Scientific reports · 2024Article
- Long-lasting blocking of interoceptive effects of cocaine by a highly efficient cocaine hydrolase in rats.Scientific reports · 2024Article
- Catalytic activities of a highly efficient cocaine hydrolase for hydrolysis of biologically active cocaine metabolites norcocaine and benzoylecgonine.Scientific reports · 2023Article
- Gender differences in cocaine-induced hyperactivity and dopamine transporter trafficking to the plasma membrane.Addiction biology · 2022Article
- Recovery of dopaminergic system after cocaine exposure and impact of a long-acting cocaine hydrolase.Addiction biology · 2022Article
- Effects of alcohol on metabolism and toxicity of cocaine in rats.Toxicology reports · 2022Article
- Cocaine hydrolase blocks cocaine-induced dopamine transporter trafficking to the plasma membrane.Addiction biology · 2022Article
- Clinical potential of a rationally engineered enzyme for treatment of cocaine dependence: Long-lasting blocking of the psychostimulant, discriminative stimulus, and reinforcing effects of cocaine.Neuropharmacology · 2020Article
- Structure-Based Design and Discovery of a Long-Acting Cocaine Hydrolase Mutant with Improved Binding Affinity to Neonatal Fc Receptor for Treatment of Cocaine Abuse.The AAPS journal · 2020Article
- Reengineering of Albumin-Fused Cocaine Hydrolase CocH1 (TV-1380) to Prolong Its Biological Half-Life.The AAPS journal · 2019Article
- In vivo characterization of toxicity of norcocaethylene and norcocaine identified as the most toxic cocaine metabolites in male mice.Drug and alcohol dependence · 2019Article
- Dimerization of human butyrylcholinesterase expressed in bacterium for development of a thermally stable bioscavenger of organophosphorus compounds.Chemico-biological interactions · 2019Article
- Kinetic characterization of cholinesterases and a therapeutically valuable cocaine hydrolase for their catalytic activities against heroin and its metabolite 6-monoacetylmorphine.Chemico-biological interactions · 2018Article
- Catalytic Reaction Mechanism for Drug Metabolism in Human Carboxylesterase-1: Cocaine Hydrolysis Pathway.Molecular pharmaceutics · 2018Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Development of a truly effective medication for treatment of cocaine abuse has been a grand challenge. There is no FDA-approved therapeutic agent specific for cocaine addiction or overdose. An enzyme therapy using an efficient cocaine-metabolizing enzyme could be a promising treatment strategy for cocaine overdose and addiction. One of our previously designed cocaine hydrolases (CocHs), known as CocH1, was fused with human serum albumin (HSA) to prolong the biological half-life. The fusion protein CocH1-HSA is an investigational new drug (IND) approved by the FDA for clinical trials in cocaine addiction treatment, but not in cocaine overdose/toxicity treatment. In the present study, we aimed to evaluate the pharmacokinetic profile of CocH1-HSA and its effectiveness for cocaine toxicity treatment in male and female rats and demonstrate the clinical potential. The data demonstrate that enzyme CocH1-HSA has very similar pharmacokinetic profile in male and female rats. For both male and female rats, the enzyme can rapidly eliminate cocaine even if the cocaine dose is as high as 180 mg/kg (LD
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Registered trials
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.