ArticleMolecular pharmacology2009
Thermostable variants of cocaine esterase for long-time protection against cocaine toxicity.
Article in Molecular pharmacology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
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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.
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.
Who cites it
55 citing papers in PubMed, 88 citations in OpenAlex.
- Leucine Aminopeptidase fromBiomolecules · 2026Article
- FireProtDB 2.0: large-scale manually curated database of the protein stability data.Nucleic acids research · 2026Article
- Treatment of acute organophosphate poisoning by using a cocaine hydrolase engineered from human butyrylcholinesterase.Chemico-biological interactions · 2025Article
- A Microbial Cocaine Bioreporter.Sensors (Basel, Switzerland) · 2024Article
- Long-lasting blocking of interoceptive effects of cocaine by a highly efficient cocaine hydrolase in rats.Scientific reports · 2024Article
- The past, present, and future of enzyme-based therapies.Drug discovery today · 2022Review
- FireProtDB: database of manually curated protein stability data.Nucleic acids research · 2021Article
- Efficient Cocaine Degradation by Cocaine Esterase-Loaded Red Blood Cells.Frontiers in physiology · 2020Article
- PEGylation but Not Fc-Fusion Improves in Vivo Residence Time of a Thermostable Mutant of Bacterial Cocaine Esterase.Bioconjugate chemistry · 2019Article
- Catalytic Reaction Mechanism for Drug Metabolism in Human Carboxylesterase-1: Cocaine Hydrolysis Pathway.Molecular pharmaceutics · 2018Article
- Review: Engineering of thermostable enzymes for industrial applications.APL bioengineering · 2018Review
- Clinical Potential of an Enzyme-based Novel Therapy for Cocaine Overdose.Scientific reports · 2017Article
- Glycoengineering of Esterase Activity through Metabolic Flux-Based Modulation of Sialic Acid.Chembiochem : a European journal of chemical biology · 2017Article
- FireProt: web server for automated design of thermostable proteins.Nucleic acids research · 2017Article
- Free energy profiles of cocaine esterase-cocaine binding process by molecular dynamics and potential of mean force simulations.Chemico-biological interactions · 2016Article
- Metabolic Enzymes of Cocaine Metabolite Benzoylecgonine.ACS chemical biology · 2016Article
- Reply to Curry and Coombs: Benzoic acid is formed predominantly from the benzoyl ester hydrolysis in the presence of cocaine hydrolase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- FireProt: Energy- and Evolution-Based Computational Design of Thermostable Multiple-Point Mutants.PLoS computational biology · 2015Article
- Rapid Bioinformatic Identification of Thermostabilizing Mutations.Biophysical journal · 2015Article
- Biologic Approaches to Treat Substance-Use Disorders.Trends in pharmacological sciences · 2015Review
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
Enhancing cocaine metabolism by administration of cocaine esterase (CocE) has been recognized as a promising treatment strategy for cocaine overdose and addiction, because CocE is the most efficient native enzyme for metabolizing the naturally occurring cocaine yet identified. A major obstacle to the clinical application of CocE is the thermoinstability of native CocE with a half-life of only a few minutes at physiological temperature (37 degrees C). Here we report thermostable variants of CocE developed through rational design using a novel computational approach followed by in vitro and in vivo studies. This integrated computational-experimental effort has yielded a CocE variant with a approximately 30-fold increase in plasma half-life both in vitro and in vivo. The novel design strategy can be used to develop thermostable mutants of any protein.
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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.