The DOI matches its Crossref record; 143 of the 143 references it cites were found in a registry or an index.
Carboxylesterases in lipid metabolism: from mouse to human
Open accessAbstract
Mammalian carboxylesterases hydrolyze a wide range of xenobiotic and endogenous compounds, including lipid esters. Physiological functions of carboxylesterases in lipid metabolism and energy homeostasis in vivo have been demonstrated by genetic manipulations and chemical inhibition in mice, and in vitro through (over)expression, knockdown of expression, and chemical inhibition in a variety of cells. Recent research advances have revealed the relevance of carboxylesterases to metabolic diseases such as obesity and fatty liver disease, suggesting these enzymes might be potential targets for treatment of metabolic disorders. In order to translate pre-clinical studies in cellular and mouse models to humans, differences and similarities of carboxylesterases between mice and human need to be elucidated. This review presents and discusses the research progress in structure and function of mouse and human carboxylesterases, and the role of these enzymes in lipid metabolism and metabolic disorders.
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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
Overweight, obesity, and mortality from cancer in a prospectively studied cohort of U.S. Adults
Calle, E. E., Rodriguez, C., Walker-Thurmond, K., & Thun, M. J. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa021423 · Cited by 7,696
Human Fatty Liver Disease: Old Questions and New Insights
Cohen, J. C., Horton, J. D., & Hobbs, H. H. (2011) · Science · doi:10.1126/science.1204265 · Cited by 2,089 · cited 1×
“NASH can further progress to liver cirrhosis and hepatocellular carcinoma (Cohen et al., 2011; Tiniakos et al., 2010).”
BackgroundGeneration and initial analysis of more than 15,000 full-length human and mouse cDNA sequences
Mammalian Gene Collection (MGC) Program Team* (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242603899 · Cited by 1,749
A C-terminal signal prevents secretion of luminal ER proteins
Munro, S., & Pelham, H. R. B. (1987) · Cell · doi:10.1016/0092-8674(87)90086-9 · Cited by 1,721
Lipid Droplets and Cellular Lipid Metabolism
Walther, T. C., & Farese, R. V. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061009-102430 · Cited by 1,661
Lipid metabolic reprogramming in cancer cells
Beloribi-Djefaflia, S., Vasseur, S., & Guillaumond, F. (2016) · Oncogenesis · doi:10.1038/oncsis.2015.49 · Cited by 1,398
The lipid droplet is an important organelle for hepatitis C virus production
Miyanari, Y., Atsuzawa, K., Usuda, N., Watashi, K., Hishiki, T., Zayas, M., Bartenschlager, R., Wakita, T., Hijikata, M., & Shimotohno, K. (2007) · Nature Cell Biology · doi:10.1038/ncb1631 · Cited by 1,249
Lipid droplets: a unified view of a dynamic organelle
Martin, S., & Parton, R. G. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1912 · Cited by 1,169
Activation of the nuclear receptor FXR improves hyperglycemia and hyperlipidemia in diabetic mice
Zhang, Y., Lee, F. Y., Barrera, G., Lee, H., Vales, C., Gonzalez, F. J., Willson, T. M., & Edwards, P. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0506982103 · Cited by 953
Cited by
Human carboxylesterases: a comprehensive review
Wang, D., Zou, L., Jin, Q., Hou, J., Ge, G., & Yang, L. (2018) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2018.05.005 · Cited by 543
Ghiboub, M., Elfiky, A. M. I., de Winther, M. P. J., Harker, N. R., Tough, D. F., & de Jonge, W. J. (2021) · Journal of Personalized Medicine · doi:10.3390/jpm11050336 · Cited by 28
Human Carboxylesterase 2 in Cocaine Metabolism
Figueiredo, P. R., González, R. D., & Carvalho, A. T. P. (2021) · Molecular Catalysis · doi:10.1016/j.mcat.2021.111938 · Cited by 9
Metadata
- Authors
- Lian, J., Nelson, R., & Lehner, R.
- Venue
- Protein & Cell
- Publisher
- Oxford University Press (OUP)
- Published
- 2017-07-04
- Volume
- 9
- Issue
- 2
- Pages
- 178-195
- ISSN
- 1674-800X (ISSN-L)
- 1674-8018
- OpenAlex
- W2732879716
- Cited by
- 300
- References
- 143
- FWCI
- 10.51
- Type
- journal article
- Language
- en
- Open access
- gold
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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).
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