Cited by 543

The DOI matches its Crossref record; 98 of the 98 references it cites were found in a registry or an index.

Human carboxylesterases: a comprehensive review

Open access

Wang, Dandan, Zou, Liwei, Jin, Qiang, Hou, Jie, Ge, Guangbo, Yang, Ling·2018·Acta Pharmaceutica Sinica B

DOI 10.1016/j.apsb.2018.05.005

Open this paper in CoChat — free account

Abstract

Mammalian carboxylesterases (CEs) are key enzymes from the serine hydrolase superfamily. In the human body, two predominant carboxylesterases (CES1 and CES2) have been identified and extensively studied over the past decade. These two enzymes play crucial roles in the metabolism of a wide variety of endogenous esters, ester-containing drugs and environmental toxicants. The key roles of CES in both human health and xenobiotic metabolism arouse great interest in the discovery of potent CES modulators to regulate endobiotic metabolism or to improve the efficacy of ester drugs. This review covers the structural and catalytic features of CES, tissue distributions, biological functions, genetic polymorphisms, substrate specificities and inhibitor properties of CES1 and CES2, as well as the significance and recent progress on the discovery of CES modulators. The information presented here will help pharmacologists explore the relevance of CES to human diseases or to assign the contribution of certain CES in xenobiotic metabolism. It will also facilitate medicinal chemistry efforts to design prodrugs activated by a given CES isoform, or to develop potent and selective modulators of CES for potential biomedical applications.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1016/j.apsb.2018.05.005

Cites

98 of 98 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Harmonizing the Metabolic Syndrome: A Joint Interim Statement of the International Diabetes Federation Task Force on Epidemiology and Prevention; National Heart, Lung, and Blood Institute; American Heart Association; World Heart Federation; International Atherosclerosis Society; and International Association for the Study of Obesity
Alberti, K. G. M. M., Eckel, R. H., Grundy, S. M., Zimmet, P. Z., Cleeman, J. I., Donato, K. A., Fruchart, J.-C., James, W. P. T., Loria, C. M., & Smith, S. C. (2009) · Circulation · doi:10.1161/circulationaha.109.192644 · Cited by 14,860
Structure-antioxidant activity relationships of flavonoids and phenolic acids
Rice-Evans, C. A., Miller, N. J., & Paganga, G. (1996) · Free Radical Biology and Medicine · doi:10.1016/0891-5849(95)02227-9 · Cited by 9,085
Natural products as sources of new drugs from 1981 to 2014
Newman, D. J., & Cragg, G. M. (2016) · Journal of Natural Products · doi:10.1021/acs.jnatprod.5b01055 · Cited by 5,858
THE MAMMALIAN CARBOXYLESTERASES: From Molecules to Functions
Satoh, T., & Hosokawa, M. (1998) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.38.1.257 · Cited by 758
Butyrylcholinesterase, paraoxonase, and albumin esterase, but not carboxylesterase, are present in human plasma
Li, B., Sedlacek, M., Manoharan, I., Boopathy, R., Duysen, E. G., Masson, P., & Lockridge, O. (2005) · Biochemical Pharmacology · doi:10.1016/j.bcp.2005.09.002 · Cited by 540
Structure, function and regulation of carboxylesterases
Satoh, T., & Hosokawa, M. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2006.07.001 · Cited by 488
The Role of Human Carboxylesterases in Drug Metabolism: Have We Overlooked Their Importance?
Casey Laizure, S., Herring, V., Hu, Z., Witbrodt, K., & Parker, R. B. (2013) · Pharmacotherapy: The Journal of Human Pharmacology and Drug Therapy · doi:10.1002/phar.1194 · Cited by 446
Structure and Catalytic Properties of Carboxylesterase Isozymes Involved in Metabolic Activation of Prodrugs
Hosokawa, M. (2008) · Molecules · doi:10.3390/molecules13020412 · Cited by 382
Structure, Function, and Regulation of Carboxylesterases
Hosokawa, M., & Satoh, T. (2006) · Toxicology of Organophosphate & Carbamate Compounds · doi:10.1016/b978-012088523-7/50017-x · Cited by 374
Human Carboxylesterase Isozymes: Catalytic Properties and Rational Drug Design
Imai, T. (2006) · Drug Metabolism and Pharmacokinetics · doi:10.2133/dmpk.21.173 · Cited by 359
Fluoro ketone inhibitors of hydrolytic enzymes
Gelb, M. H., Svaren, J. P., & Abeles, R. H. (1985) · Biochemistry · doi:10.1021/bi00329a001 · Cited by 343
Carboxylesterases in lipid metabolism: from mouse to human
Lian, J., Nelson, R., & Lehner, R. (2018) · Protein & Cell · doi:10.1007/s13238-017-0437-z · Cited by 300
Current Progress on Esterases: From Molecular Structure to Function
Satoh, T., Taylor, P., Bosron, W. F., Sanghani, S. P., Hosokawa, M., & Du, B. N. L. (2002) · Drug Metabolism and Disposition · doi:10.1124/dmd.30.5.488 · Cited by 295
Human carboxylesterase 2 is commonly expressed in tumor tissue and is correlated with activation of irinotecan.
Xu, G. H., Zhang, W., Ma, M. K., & McLeod, H. L. (2002) · PubMed · Cited by 277
Substrate Specificity of Carboxylesterase Isozymes and Their Contribution to Hydrolase Activity in Human Liver and Small Intestine
Imai, T., Taketani, M., Shii, M., Hosokawa, M., & Chiba, K. (2006) · Drug Metabolism and Disposition · doi:10.1124/dmd.106.009381 · Cited by 275
Genetic Determinants of Dabigatran Plasma Levels and Their Relation to Bleeding
Paré, G., Eriksson, N., Lehr, T., Connolly, S., Eikelboom, J., Ezekowitz, M. D., Axelsson, T., Haertter, S., Oldgren, J., Reilly, P., et al. (2013) · Circulation · doi:10.1161/circulationaha.112.001233 · Cited by 255
Antiplatelet Agents Aspirin and Clopidogrel Are Hydrolyzed by Distinct Carboxylesterases, and Clopidogrel Is Transesterificated in the Presence of Ethyl Alcohol
Tang, M., Mukundan, M., Yang, J., Charpentier, N., LeCluyse, E. L., Black, C., Yang, D., Shi, D., & Yan, B. (2006) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.106.110577 · Cited by 250
Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme
Bencharit, S., Morton, C. L., Xue, Y., Potter, P. M., & Redinbo, M. R. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb919 · Cited by 232
Human liver cocaine esterases: ethanol‐mediated formation of ethylcocaine
Dean, R. A., Christian, C. D., Sample, R. H. B., & Bosron, W. F. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.12.1916095 · Cited by 216
Keynote review: Mammalian carboxylesterases: From drug targets to protein therapeutics
Redinbo, M. R., & Potter, P. M. (2005) · Drug Discovery Today · doi:10.1016/s1359-6446(05)03383-0 · Cited by 213
Structure, bioactivity, and synthesis of methylated flavonoids
Wen, L., Jiang, Y., Yang, J., Zhao, Y., Tian, M., & Yang, B. (2017) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.13350 · Cited by 205
A Highly Selective Ratiometric Two-Photon Fluorescent Probe for Human Cytochrome P450 1A
Dai, Z.-R., Ge, G.-B., Feng, L., Ning, J., Hu, L.-H., Jin, Q., Wang, D.-D., Lv, X., Dou, T.-Y., Cui, J.-N., et al. (2015) · Journal of the American Chemical Society · doi:10.1021/jacs.5b09854 · Cited by 194
Self-citation
Carboxylesterase 1 as a Determinant of Clopidogrel Metabolism and Activation
Zhu, H.-J., Wang, X., Gawronski, B. E., Brinda, B. J., Angiolillo, D. J., & Markowitz, J. S. (2013) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.112.201640 · Cited by 193
Hydrolysis of Capecitabine to 5′-Deoxy-5-fluorocytidine by Human Carboxylesterases and Inhibition by Loperamide
Quinney, S. K., Sanghani, S. P., Davis, W. I., Hurley, T. D., Sun, Z., Murry, D. J., & Bosron, W. F. (2005) · The Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.104.081265 · Cited by 184
Serine hydrolase targets of organophosphorus toxicants
Casida, J. E., & Quistad, G. B. (2005) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.10.036 · Cited by 183
Crystal Structure of Human Carboxylesterase 1 Complexed with the Alzheimer's Drug Tacrine
Bencharit, S., Morton, C. L., Hyatt, J. L., Kuhn, P., Danks, M. K., Potter, P. M., & Redinbo, M. R. (2003) · Chemistry & Biology · doi:10.1016/s1074-5521(03)00071-1 · Cited by 174
Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine
Brzezinski, M. R., Abraham, T. L., Stone, C. L., Dean, R. A., & Bosron, W. F. (1994) · Biochemical Pharmacology · doi:10.1016/0006-2952(94)90461-8 · Cited by 171
Human carboxylesterases and their role in xenobiotic and endobiotic metabolism
Ross, M. K., & Crow, J. A. (2007) · Journal of Biochemical and Molecular Toxicology · doi:10.1002/jbt.20178 · Cited by 169
Human carboxylesterases HCE1 and HCE2: Ontogenic expression, inter-individual variability and differential hydrolysis of oseltamivir, aspirin, deltamethrin and permethrin
Yang, D., Pearce, R. E., Wang, X., Gaedigk, R., Wan, Y.-J. Y., & Yan, B. (2009) · Biochemical Pharmacology · doi:10.1016/j.bcp.2008.10.005 · Cited by 167
Structural insights into CPT-11 activation by mammalian carboxylesterases
Bencharit, S., Morton, C. L., Howard-Williams, E. L., Danks, M. K., Potter, P. M., & Redinbo, M. R. (2002) · Nature Structural Biology · doi:10.1038/nsb790 · Cited by 161
The potential of natural products for targeting PPARα
Rigano, D., Sirignano, C., & Taglialatela‐Scafati, O. (2017) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2017.05.005 · Cited by 160
Hepatic Carboxylesterase 1 Is Essential for Both Normal and Farnesoid X Receptor-Controlled Lipid Homeostasis
Xu, J., Li, Y., Chen, W.-D., Xu, Y., Yin, L., Ge, X., Jadhav, K., Adorini, L., & Zhang, Y. (2013) · Hepatology · doi:10.1002/hep.26714 · Cited by 154
HYDROLYSIS OF IRINOTECAN AND ITS OXIDATIVE METABOLITES, 7-ETHYL-10-[4-N-(5-AMINOPENTANOIC ACID)-1-PIPERIDINO] CARBONYLOXYCAMPTOTHECIN AND 7-ETHYL-10-[4-(1-PIPERIDINO)-1-AMINO]-CARBONYLOXYCAMPTOTHECIN, BY HUMAN CARBOXYLESTERASES CES1A1, CES2, AND A NEWLY EXPRESSED CARBOXYLESTERASE ISOENZYME, CES3
Sanghani, S. P., Quinney, S. K., Fredenburg, T. B., Davis, W. I., Murry, D. J., & BOSRON, W. F. (2004) · Drug Metabolism and Disposition · doi:10.1124/dmd.32.5.505 · Cited by 145
Carboxylesterase 2 prevents liver steatosis by modulating lipolysis, endoplasmic reticulum stress, and lipogenesis and is regulated by hepatocyte nuclear factor 4 alpha in mice
Li, Y., Zalzala, M. H., Jadhav, K. S., Xu, Y., Kasumov, T., Yin, L., & Zhang, Y. (2016) · Hepatology · doi:10.1002/hep.28472 · Cited by 144
Integrated phenotypic and activity-based profiling links Ces3 to obesity and diabetes
Domínguez, E., Galmozzi, A., Chang, J. W., Hsu, K., Pawlak, J., Li, W., Godio, C., Thomas, J. R., Partida, D., Niessen, S., et al. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1429 · Cited by 140
Human Carboxylesterase 2 Reverses Obesity-Induced Diacylglycerol Accumulation and Glucose Intolerance
Ruby, M. A., Massart, J., Hunerdosse, D. M., Schönke, M., Correia, J. C., Louie, S. M., Ruas, J. L., Näslund, E. B., Nomura, D. K., & Zierath, J. R. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.070 · Cited by 138
A Two-Photon Ratiometric Fluorescent Probe for Imaging Carboxylesterase 2 in Living Cells and Tissues
Jin, Q., Feng, L., Wang, D., Dai, Z., Wang, P., Zou, L., Liu, Z., Wang, J., Yu, Y., Ge, G., et al. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b09573 · Cited by 136
Self-citation
Human Carboxylesterases: An Update on CES1, CES2 and CES3
Sanghani, S. P., Sanghani, P. C., Schiel, M. A., & BOSRON, W. F. (2009) · Protein and Peptide Letters · doi:10.2174/092986609789071324 · Cited by 135
The Biotransformation of Prasugrel, a New Thienopyridine Prodrug, by the Human Carboxylesterases 1 and 2
Williams, E. T., Jones, K. O., Ponsler, G. D., Lowery, S. M., Perkins, E. J., Wrighton, S. A., Ruterbories, K. J., Kazui, M., & Farid, N. A. (2008) · Drug Metabolism and Disposition · doi:10.1124/dmd.107.020248 · Cited by 128
Pyrethroids: Mammalian Metabolism and Toxicity
Kaneko, H. (2010) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf102567z · Cited by 124
A highly selective near-infrared fluorescent probe for carboxylesterase 2 and its bioimaging applications in living cells and animals
Jin, Q., Feng, L., Wang, D., Wu, J., Hou, J., Dai, Z., Sun, S., Wang, J., Ge, G., Cui, J., et al. (2016) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2016.04.075 · Cited by 122
Self-citation
A highly selective fluorescent ESIPT probe for the detection of Human carboxylesterase 2 and its biological applications
Feng, L., Liu, Z., Hou, J., Lv, X., Ning, J., Ge, G., Cui, J., & Yang, L. (2014) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2014.10.002 · Cited by 120
Self-citation
Crystal structure of carboxylesterase from Pseudomonas fluorescens, an α/β hydrolase with broad substrate specificity
Kim, K. K., Song, H. K., Shin, D. H., Hwang, K. Y., Choe, S., Yoo, O. J., & Suh, S. W. (1997) · Structure · doi:10.1016/s0969-2126(97)00306-7 · Cited by 120
Characterization of pyrethroid hydrolysis by the human liver carboxylesterases hCE-1 and hCE-2
Nishi, K., Huang, H., Kamita, S. G., Kim, I.-H., Morisseau, C. H. P., & Hammock, B. D. (2005) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2005.11.005 · Cited by 118
Carboxylesterase inhibitors
Hatfield, M. J., & Potter, P. M. (2011) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2011.586339 · Cited by 113
Human Carboxylesterase-2 Hydrolyzes the Prodrug of Gemcitabine (LY2334737) and Confers Prodrug Sensitivity to Cancer Cells
Pratt, S. E., Durland–Busbice, S., Shepard, R. L., Heinz-Taheny, K. M., Iversen, P. W., & Dantzig, A. H. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-1184 · Cited by 104
Carboxylesterases Are Uniquely Expressed among Tissues and Regulated by Nuclear Hormone Receptors in the Mouse
Jones, R., Taylor, A. M., Tong, E. Y., & Repa, J. J. (2012) · Drug Metabolism and Disposition · doi:10.1124/dmd.112.048397 · Cited by 104
New approaches to prevent intestinal toxicity of irinotecan-based regimens
Alimonti, A., Gelibter, A. J., Pavese, I., Satta, F., Cognetti, F., Ferretti, G., Rasio, D., Vecchione, A., & Palma, M. D. (2004) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2004.05.002 · Cited by 103
Carboxylesterase Inhibitors: An Update
Zou, L., Jin, Q., Wang, D., Qian, Q.-K., Hao, D., Ge, G., & Yang, L. (2017) · Current Medicinal Chemistry · doi:10.2174/0929867325666171204155558 · Cited by 102
Self-citation
Metabolic diseases and cancer risk
Faulds, M. H., & Dahlman‐Wright, K. (2011) · Current Opinion in Oncology · doi:10.1097/cco.0b013e32834e0582 · Cited by 95
Natural Products as Leads in Schistosome Drug Discovery
Neves, B. J., Andrade, C. H., & Cravo, P. (2015) · Molecules · doi:10.3390/molecules20021872 · Cited by 95
Discovery of Novel Selective Inhibitors of Human Intestinal Carboxylesterase for the Amelioration of Irinotecan-Induced Diarrhea: Synthesis, Quantitative Structure-Activity Relationship Analysis, and Biological Activity
Wadkins, R. M., Hyatt, J. L., Yoon, K. J. P., Morton, C. L., Lee, R. E., Jr., Damodaran, K., Beroza, P., Danks, M. K., & Potter, P. M. (2004) · Molecular Pharmacology · doi:10.1124/mol.65.6.1336 · Cited by 95
The COOH terminus of several liver carboxylesterases targets these enzymes to the lumen of the endoplasmic reticulum.
Robbi, M., & Beaufay, H. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54952-8 · Cited by 93
Characterization of enzymes involved in formation of ethyl esters of long-chain fatty acids in humans
Diczfalusy, M. A., Björkhem, I., Einarsson, C., Hillebrant, C.-G., & Alexson, S. E. H. (2001) · Journal of Lipid Research · doi:10.1016/s0022-2275(20)31590-x · Cited by 91
A highly selective ratiometric fluorescent probe for in vitro monitoring and cellular imaging of human carboxylesterase 1
Liu, Z., Feng, L., Ge, G., Lv, X., Hou, J., Cao, Y., Cui, J., & Yang, L. (2014) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2014.01.049 · Cited by 87
Self-citation
Activation of the Antiviral Prodrug Oseltamivir Is Impaired by Two Newly Identified Carboxylesterase 1 Variants
Zhu, H., & Markowitz, J. S. (2008) · Drug Metabolism and Disposition · doi:10.1124/dmd.108.024943 · Cited by 87
Fatty Acid Ethyl Esters: Potentially Toxic Products of Myocardial Ethanol Metabolism
Beckemeier, M. E., & Bora, P. S. (1998) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1998.0812 · Cited by 85
Inhibition of carboxylesterase 1 is associated with cholesteryl ester retention in human THP-1 monocyte/macrophages
Crow, J. A., Middleton, B. L., Borazjani, A., Hatfield, M. J., Potter, P. M., & Ross, M. K. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2008.07.005 · Cited by 82
Carboxylesterase 1 gene polymorphism and methylphenidate response in ADHD
Nemoda, Z., Angyal, N., Tárnok, Z., Gádoros, J., & Sasvári‐Székely, M. (2009) · Neuropharmacology · doi:10.1016/j.neuropharm.2009.08.014 · Cited by 81
Protostane Triterpenoids from the Rhizome of Alisma orientale Exhibit Inhibitory Effects on Human Carboxylesterase 2
Mai, Z.-P., Zhou, K., Ge, G., Wang, C., Huo, X., Dong, P., Deng, S., Zhang, B., Zhang, H.-L., Huang, S., et al. (2015) · Journal of Natural Products · doi:10.1021/acs.jnatprod.5b00321 · Cited by 81
Self-citation
Flavonoids: From Structure to Health Issues
Santos‐Buelga, C., & Feliciano, A. S. (2017) · Molecules · doi:10.3390/molecules22030477 · Cited by 78
A practical strategy to design and develop an isoform-specific fluorescent probe for a target enzyme: CYP1A1 as a case study
Dai, Z., Feng, L., Jin, Q., Cheng, H.-L. M., Li, Y., Ning, J., Yu, Y., Ge, G., Cui, J., & Yang, L. (2016) · Chemical Science · doi:10.1039/c6sc03970g · Cited by 77
Self-citation
Design, synthesis, and structure-activity relationship study of glycyrrhetinic acid derivatives as potent and selective inhibitors against human carboxylesterase 2
Zou, L., Li, Y., Wang, P., Zhou, K., Hou, J., Jin, Q., Hao, D., Ge, G., & Yang, L. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.02.020 · Cited by 76
Self-citation
Nuclear receptor-mediated regulation of carboxylesterase expression and activity
Staudinger, J. L., Xu, C., Cui, Y. J., & Klaassen, C. D. (2010) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1517/17425250903483215 · Cited by 72
Crystal Structures of Human Carboxylesterase 1 in Covalent Complexes with the Chemical Warfare Agents Soman and Tabun,
Fleming, C. D., Edwards, C. C., Kirby, S. D., Maxwell, D. M., Potter, P. M., Cerasoli, D. M., & Redinbo, M. R. (2007) · Biochemistry · doi:10.1021/bi700246n · Cited by 72
Developmental neurotoxic effects of two pesticides: Behavior and biomolecular studies on chlorpyrifos and carbaryl
Lee, I., Eriksson, P., Fredriksson, A., Buratovic, S., & Viberg, H. (2015) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2015.08.014 · Cited by 71
A ratiometric fluorescent sensor for highly selective detection of human carboxylesterase 2 and its application in living cells
Liu, Z., Feng, L., Hou, J., Lv, X., Ning, J., Ge, G., Wang, K., Cui, J., & Yang, L. (2014) · Sensors and Actuators B Chemical · doi:10.1016/j.snb.2014.08.066 · Cited by 71
Self-citation
A highly specific ratiometric two-photon fluorescent probe to detect dipeptidyl peptidase IV in plasma and living systems
Zou, L., Wang, P., Qian, X., Feng, L., Yu, Y., Wang, D., Jin, Q., Hou, J., Liu, Z., Ge, G., et al. (2016) · Biosensors and Bioelectronics · doi:10.1016/j.bios.2016.11.068 · Cited by 71
Self-citation
Sacubitril Is Selectively Activated by Carboxylesterase 1 (CES1) in the Liver and the Activation Is Affected by CES1 Genetic Variation
Shi, J., Wang, X., Nguyen, J., Wu, A. H., Bleske, B. E., & Zhu, H. (2016) · Drug Metabolism and Disposition · doi:10.1124/dmd.115.068536 · Cited by 69
Characterization and structure-activity relationship studies of flavonoids as inhibitors against human carboxylesterase 2
Weng, Z.-M., Ge, G., Dou, T., Wang, P., Liu, P., Tian, X.-H., Qiao, N., Yu, Y., Zou, L., Zhou, Q., et al. (2018) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2018.01.011 · Cited by 68
Self-citation
Modulation of Esterified Drug Metabolism by Tanshinones from Salvia miltiorrhiza (“Danshen”)
Hatfield, M. J., Tsurkan, L. G., Hyatt, J. L., Edwards, C. C., Lemoff, A. S., Jeffries, C. T., Yan, B., & Potter, P. M. (2013) · Journal of Natural Products · doi:10.1021/np300628a · Cited by 61
Dose-additive inhibition of chinook salmon acetylcholinesterase activity by mixtures of organophosphate and carbamate insecticides
Scholz, N. L., Truelove, N. K., Labenia, J. S., Baldwin, D. H., & Collier, T. K. (2006) · Environmental Toxicology and Chemistry · doi:10.1897/05-030r1.1 · Cited by 61
Improved, Selective, Human Intestinal Carboxylesterase Inhibitors Designed to Modulate 7-Ethyl-10-[4-(1-piperidino)-1-piperidino]carbonyloxycamptothecin (Irinotecan; CPT-11) Toxicity
Hicks, L. D., Hyatt, J. L., Stoddard, S. V., Tsurkan, L. G., Edwards, C. C., Wadkins, R. M., & Potter, P. M. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm9001296 · Cited by 59
Inhibition of carboxylesterase activity of THP1 monocytes/macrophages and recombinant human carboxylesterase 1 by oxysterols and fatty acids
Crow, J. A., Herring, K. L., Xie, S., Borazjani, A., Potter, P. M., & Ross, M. K. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2009.09.002 · Cited by 54
Urethane dimethacrylate induces cytotoxicity and regulates cyclooxygenase-2, hemeoxygenase and carboxylesterase expression in human dental pulp cells
Chang, H., Chang, M., Wang, H., Huang, G., Lee, Y., Wang, Y., Chan, C., Yeung, S., Tseng, S., & Jeng, J. (2013) · Acta Biomaterialia · doi:10.1016/j.actbio.2013.10.006 · Cited by 53
Inhibition of human carboxylesterases hCE1 and hiCE by cholinesterase inhibitors
Tsurkan, L. G., Hatfield, M. J., Edwards, C. C., Hyatt, J. L., & Potter, P. M. (2012) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2012.10.018 · Cited by 51
An Optimized Two‐Photon Fluorescent Probe for Biological Sensing and Imaging of Catechol‐O‐Methyltransferase
Wang, P., Xia, Y., Zou, L., Qian, X., Dou, T., Jin, Q., Li, S., Yu, Y., Wang, D., Luo, Q., et al. (2017) · Chemistry - A European Journal · doi:10.1002/chem.201701384 · Cited by 51
Self-citation
Identification of a C-reactive Protein Binding Site in Two Hepatic Carboxylesterases Capable of Retaining C-reactive Protein within the Endoplasmic Reticulum
Yue, C. C., Muller‐Greven, J., Dailey, P., Lozanski, G., Anderson, V. E., & Macintyre, S. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.22245 · Cited by 48
The Effect of Ethanol on Oral Cocaine Pharmacokinetics Reveals an Unrecognized Class of Ethanol-Mediated Drug Interactions
Parker, R. B., & Laizure, S. C. (2009) · Drug Metabolism and Disposition · doi:10.1124/dmd.109.030056 · Cited by 44
Structure and Dynamics of Serine Hydrolase-Organophosphate Adducts
Kovach, I. M. (1988) · Journal of enzyme inhibition · doi:10.3109/14756368809040726 · Cited by 44
Association of Oseltamivir Activation with Gender and Carboxylesterase 1 Genetic Polymorphisms
Shi, J., Wang, X., Eyler, R. F., Liang, Y., Liu, L., Mueller, B. A., & Zhu, H. (2016) · Basic & Clinical Pharmacology & Toxicology · doi:10.1111/bcpt.12625 · Cited by 43
Bysspectin A, an unusual octaketide dimer and the precursor derivatives from the endophytic fungus Byssochlamys spectabilis IMM0002 and their biological activities
Wu, Y., Zhang, H., Sun, Z.-H., Dai, J.-G., Hu, Y., Li, R., Lin, P., Xia, G., Wang, L., Qiu, B.-L., et al. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.01.030 · Cited by 43
Self-citation
Structure−Function Analysis of Human Triacylglycerol Hydrolase by Site-Directed Mutagenesis: Identification of the Catalytic Triad and a Glycosylation Site
Alam, M., Vance, D. E., & Lehner, R. S. (2002) · Biochemistry · doi:10.1021/bi0255625 · Cited by 39
Covalent inhibition of recombinant human carboxylesterase 1 and 2 and monoacylglycerol lipase by the carbamates JZL184 and URB597
Crow, J. A., Bittles, V., Borazjani, A., Potter, P. M., & Ross, M. K. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.08.017 · Cited by 38
Planarity and Constraint of the Carbonyl Groups in 1,2-Diones Are Determinants for Selective Inhibition of Human Carboxylesterase 1
Hyatt, J. L., Wadkins, R. M., Tsurkan, L. G., Hicks, L. D., Hatfield, M. J., Edwards, C. C., Ross, C. R., Cantalupo, S. A., Crundwell, G., Danks, M. K., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm0706867 · Cited by 37
Hepatic Carboxylesterase 1 Is Induced by Glucose and Regulates Postprandial Glucose Levels
Xu, J., Yin, L., Xu, Y., Li, Y., Zalzala, M. H., Cheng, G., & Zhang, Y. (2014) · PLoS ONE · doi:10.1371/journal.pone.0109663 · Cited by 35
Fishing for Nature’s Hits: Establishment of the Zebrafish as a Model for Screening Antidiabetic Natural Products
Tabassum, N., Tai, H., Jung, D., & Williams, D. R. (2015) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2015/287847 · Cited by 35
Genomic analysis of the carboxylesterases: Identification and classification of novel forms
Williams, E. T., Wang, H., Wrighton, S. A., Qian, Y., & Perkins, E. J. (2010) · Molecular Phylogenetics and Evolution · doi:10.1016/j.ympev.2010.05.018 · Cited by 34
Serine Hydrolase KIAA1363: Toxicological and Structural Features with Emphasis on Organophosphate Interactions
Nomura, D. K., Durkin, K. A., Chiang, K. P., Quistad, G. B., Cravatt, B. F., & Casida, J. E. (2006) · Chemical Research in Toxicology · doi:10.1021/tx060117m · Cited by 34
Antioxidant sulforaphane and sensitizer trinitrobenzene sulfonate induce carboxylesterase-1 through a novel element transactivated by nuclear factor-E2 related factor-2
Chen, Y.-T., Shi, D., Yang, D., et al. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.06.025 · Cited by 32
Dexamethasone suppresses the expression of multiple rat carboxylesterases through transcriptional repression: Evidence for an involvement of the glucocorticoid receptor
Shi, D., Yang, J., Yang, D., & Yan, B. (2008) · Toxicology · doi:10.1016/j.tox.2008.09.019 · Cited by 31
Purification and Characterization of Human Heart Fatty Acid Ethyl Ester Synthase/Carboxylesterase
Bora, P. S. (1996) · Journal of Molecular and Cellular Cardiology · doi:10.1006/jmcc.1996.0195 · Cited by 31
Liver-Specific Cholesteryl Ester Hydrolase Deficiency Attenuates Sterol Elimination in the Feces and Increases Atherosclerosis in Ldlr −/− Mice
Bie, J., Wang, J., Marqueen, K. E., Osborne, R., Kakiyama, G., Korzun, W. J., Ghosh, S. S., & Ghosh, S. (2013) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.113.301634 · Cited by 31
Regulations of Xenobiotics and Endobiotics on Carboxylesterases: A Comprehensive Review
Xu, Y., Zhang, C., He, W., & Liu, D. (2016) · European Journal of Drug Metabolism and Pharmacokinetics · doi:10.1007/s13318-016-0326-5 · Cited by 29
Allosteric kinetics of human carboxylesterase 1: Species differences and interindividual variability
Takahashi, S., Katoh, M., Saitoh, T., et al. (2008) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.21376 · Cited by 28
The Signal for Retention of the Egasyn-Glucuronidase Complex within the Endoplasmic Reticulum
Zhen, L., Baumann, H., Novák, E. K., et al. (1993) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1993.1368 · Cited by 26
Baboon carboxylesterases 1 and 2: sequences, structures and phylogenetic relationships with human and other primate carboxylesterases
Holmes, R. S., Glenn, J. P., VandeBerg, J. L., & Cox, L. A. (2009) · Journal of Medical Primatology · doi:10.1111/j.1600-0684.2008.00315.x · Cited by 16
Assessment of Induction of Cytochrome P450 by NO-1886 (Ibrolipim), a Lipoprotein Lipase-Promoting Agent, in Primary Cultures of Human Hepatocytes and in Female Rat Liver
Morioka, Y., Nishimura, M., Imai, T., et al. (2006) · Drug Metabolism and Pharmacokinetics · doi:10.2133/dmpk.21.19 · Cited by 13

Fluorescent dyes based on rhodamine derivatives for bioimaging and therapeutics: recent progress, challenges, and prospects
Zeng, S., Liu, X., Kafuti, Y. S., Kim, H., Wang, J., Peng, X., Li, H., & Yoon, J. (2023) · Chemical Society Reviews · doi:10.1039/d2cs00799a · Cited by 341
Remimazolam: non-clinical and clinical profile of a new sedative/anesthetic agent
Kilpatrick, G. J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.690875 · Cited by 262
A Proximal-to-Distal Survey of Healthy Adult Human Small Intestine and Colon Epithelium by Single-Cell Transcriptomics
Burclaff, J., Bliton, R. J., Breau, K. A., Ok, M. T., Gomez-Martinez, I., Ranek, J. S., Bhatt, A. P., Purvis, J. E., Woosley, J. T., & Magness, S. T. (2022) · Cellular and Molecular Gastroenterology and Hepatology · doi:10.1016/j.jcmgh.2022.02.007 · Cited by 242
Insight Into Microbial Applications for the Biodegradation of Pyrethroid Insecticides
Bhatt, P., Huang, Y., Zhan, H., & Chen, S. (2019) · Frontiers in Microbiology · doi:10.3389/fmicb.2019.01778 · Cited by 202
Scalable production of tissue-like vascularized liver organoids from human PSCs
Harrison, S. P., Siller, R., Tanaka, Y., Chollet, M. E., de la Morena-Barrio, M. E., Xiang, Y., Patterson, B., Andersen, E., Bravo-Pérez, C., Kempf, H., et al. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-01074-1 · Cited by 119

See all 543

Authors: Wang, D., Zou, L., Jin, Q., Hou, J., Ge, G., & Yang, L.
Venue: Acta Pharmaceutica Sinica B
Publisher: Elsevier BV
Published: 2018-09
Volume: 8
Issue: 5
Pages: 699-712
ISSN: 2211-3835 (ISSN-L)
DOI: 10.1016/j.apsb.2018.05.005
OpenAlex: W2810653208
Cited by: 543
References: 98
FWCI: 43.90
Type: journal article
Language: en
Open access: gold

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

Human carboxylesterases: a comprehensive review

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources