Discovery of triterpenoids as potent dual inhibitors of pancreatic lipase and human carboxylesterase 1 [PDF]
Journal of Enzyme Inhibition and Medicinal Chemistry, 2022 Pancreatic lipase (PL) is a well-known key target for the prevention and treatment of obesity. Human carboxylesterase 1A (hCES1A) has become an important target for the treatment of hyperlipidaemia.
Jing Zhang +12 more
doaj +8 more sources
Comparison of the Structure and Activity of Glycosylated and Aglycosylated Human Carboxylesterase 1. [PDF]
PLoS ONE, 2015 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
Victoria Arena de Souza +6 more
doaj +9 more sources
Catalytic Hydrolysis Mechanism of Cocaine by Human Carboxylesterase 1: An Orthoester Intermediate Slows Down the Reaction [PDF]
Molecules, 2019 Human carboxylesterase 1 (hCES1) is a major carboxylesterase in the human body and plays important roles in the metabolism of a wide variety of substances, including lipids and drugs, and therefore is attracting more and more attention from areas ...
Maocai Yan +6 more
doaj +4 more sources
Immobilization of active human carboxylesterase 1 in biomimetic silica nanoparticles. [PDF]
Biotechnol Prog, 2011 AbstractThe encapsulation of proteins in biomimetic silica has recently been shown to successfully maintain enzymes in their active state. Organophosphate (OP) compounds are used as pesticides as well as potent chemical warfare nerve agents. Because these toxicants are life threatening, we sought to generate biomimetic silicas capable of responding to ...
Edwards JS +6 more
europepmc +7 more sources
Hepatocyte‐Specific Expression of Human Carboxylesterase 1 Attenuates Diet‐Induced Steatohepatitis and Hyperlipidemia in Mice [PDF]
Hepatology Communications, 2020 Rodents have at least five carboxylesterase 1 (Ces1) genes, whereas there is only one CES1 gene in humans, raising the question as to whether human CES1 and mouse Ces1 genes share the same functions.
Yanyong Xu +6 more
doaj +2 more sources
Structure-Activity Relationships of Pentacyclic Triterpenoids as Potent and Selective Inhibitors against Human Carboxylesterase 1 [PDF]
Frontiers in Pharmacology, 2017 Human carboxylesterase 1 (hCE1), one of the most important serine hydrolases distributed in liver and adipocytes, plays key roles in endobiotic homeostasis and xenobiotic metabolism.
Li-Wei Zou +14 more
doaj +2 more sources
A structural examination of agrochemical processing by human carboxylesterase 1 [PDF]
Journal of Pesticide Science, 2010 Human carboxylesterase 1 (hCE1) is the primary carboxylesterase expressed in the liver. This critical member of the phase I drug metabolism pathway detoxifies a wide-range of endobiotics, xenobiotics, and agrochemicals. To date, more than a dozen X-ray crystal structures have been elucidated of hCE1 in complex with a broad spectrum of ligands ...
Hemmert, Andrew C., Redinbo, Matthew R.
openaire +4 more sources
Catalytic Reaction Mechanism for Drug Metabolism in Human Carboxylesterase-1: Cocaine Hydrolysis Pathway. [PDF]
Mol Pharm, 2018 Carboxylesterase-1 (CE-1) is a crucial enzyme responsible for metabolism/activation/inactivation of xenobiotics (therapeutic agents, prodrugs, abused drugs, and organophosphorus nerve agents etc.) and also involved in many other biological processes.
Yao J, Chen X, Zheng F, Zhan CG.
europepmc +6 more sources
Anti-Influenza Prodrug Oseltamivir Is Activated by Carboxylesterase Human Carboxylesterase 1, and the Activation Is Inhibited by Antiplatelet Agent Clopidogrel [PDF]
The Journal of Pharmacology and Experimental Therapeutics, 2006 Oseltamivir is the main medicine recommended by the World Health Organization in anticipation of next influenza pandemic. This anti-influenza viral agent is an ester prodrug, and the antiviral activity is achieved by its hydrolytic metabolite: oseltamivir carboxylate.
Shi, Deshi +7 more
openaire +4 more sources
Structure of recombinant human carboxylesterase 1 isolated from whole cabbage looper larvae. [PDF]
Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012 The use of whole insect larvae as a source of recombinant proteins offers a more cost-effective method of producing large quantities of human proteins than conventional cell-culture approaches. Human carboxylesterase 1 has been produced in and isolated from whole Trichoplusia ni larvae.
Greenblatt HM +7 more
europepmc +5 more sources