ArticlePloS one2015
Comparison of the Structure and Activity of Glycosylated and Aglycosylated Human Carboxylesterase 1.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Randomized evaluation of the loss-of-function carboxylesterase 1 (CES1) G143E variant on clopidogrel and ticagrelor pharmacodynamics.Clinical and translational science · 2024Trial
- Experimental and In Silico Approaches to Study Carboxylesterase Substrate Specificity.Journal of xenobiotics · 2026Review
- In Silico Methodology for Human Carboxylesterases 1 and 2 Isoforms Substrate Selectivity Study.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Triazine Thiols Decrease Apolipoprotein B Secretion From Hepatocytes Through Inhibition of Human Carboxylesterase 1.Cellular and molecular gastroenterology and hepatology · 2026Article
- Fluorogenic chemical tools to shed light on CES1-mediated adverse drug interactions.Chemical communications (Cambridge, England) · 2024Article
- Dynamic interchange between two protonation states is characteristic of active sites of cholinesterases.Protein science : a publication of the Protein Society · 2024Article
- In Silico Study of Camptothecin-Based Pro-Drugs Binding to Human Carboxylesterase 2.Biomolecules · 2024Article
- The study of halogen effect on the reactivity of the serine-targeting covalent warheads.Frontiers in chemistry · 2024Article
- The Crystal Structure of Mouse Ces2c, a Potential Ortholog of Human CES2, Shows Structural Similarities in Substrate Regulation and Product Release to Human CES1.International journal of molecular sciences · 2022Article
- Strategies for Glycoengineering Therapeutic Proteins.Frontiers in chemistry · 2022Review
- Carboxylesterase 1 and Precision Pharmacotherapy: Pharmacogenetics and Nongenetic Regulators.Drug metabolism and disposition: the biological fate of chemicals · 2020Review
- Combined Ensemble Docking and Machine Learning in Identification of Therapeutic Agents with Potential Inhibitory Effect on Human CES1.Molecules (Basel, Switzerland) · 2019Article
- Glycoengineering of Esterase Activity through Metabolic Flux-Based Modulation of Sialic Acid.Chembiochem : a European journal of chemical biology · 2017Article
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 1 country.
Funding
Abstract
Human Carboxylesterase 1 (hCES1) is the key liver microsomal enzyme responsible for detoxification and metabolism of a variety of clinical drugs. To analyse the role of the single N-linked glycan on the structure and activity of the enzyme, authentically glycosylated and aglycosylated hCES1, generated by mutating asparagine 79 to glutamine, were produced in human embryonic kidney cells. Purified enzymes were shown to be predominantly trimeric in solution by analytical ultracentrifugation. The purified aglycosylated enzyme was found to be more active than glycosylated hCES1 and analysis of enzyme kinetics revealed that both enzymes exhibit positive cooperativity. Crystal structures of hCES1 a catalytically inactive mutant (S221A) and the aglycosylated enzyme were determined in the absence of any ligand or substrate to high resolutions (1.86 Å, 1.48 Å and 2.01 Å, respectively). Superposition of all three structures showed only minor conformational differences with a root mean square deviations of around 0.5 Å over all Cα positions. Comparison of the active sites of these un-liganded enzymes with the structures of hCES1-ligand complexes showed that side-chains of the catalytic triad were pre-disposed for substrate binding. Overall the results indicate that preventing N-glycosylation of hCES1 does not significantly affect the structure or activity of the enzyme.
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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.