The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
A Highly Conserved Motif within the NH2-terminal Coiled-coil Domain of Angiopoietin-like Protein 4 Confers Its Inhibitory Effects on Lipoprotein Lipase by Disrupting the Enzyme Dimerization
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Several studies have reported that ANGPTL3 is a less potent inhibitor than ANGPTL4.
“In fact, several studies have reported that ANGPTL3 is a less potent inhibitor than ANGPTL4 (54, 55, 60, 133, 136),”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [133]
The proposed mechanism of dissociation of LPL dimers into inactive monomers seems less likely given recent evidence that LPL is catalytically active as a monomer.
“One proposed mechanism, the dissociation of LPL dimers into inactive monomers (133), seems less likely given recent evidence that LPL is catalytically active as a monomer (99).”
From Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8 (2021) · cites this paper as [133]
Angptl4 prevents LPL dimerization and thereby prevents LPL activation.
“Angptl4 is primarily expressed in adipose tissue and liver, induced by fasting and secreted into the circulation [4], where it prevents LPL dimerization and thereby preventing LPL activation [5–8].”
From Differential effects of angiopoietin-like 4 in brain and muscle on regulation of lipoprotein lipase activity (2015) · cites this paper as [6]
Angptl4 is a known inhibitor of LPL activity in peripheral tissues.
“Angiopoietin-like (Angptl) 4 is a known inhibitor of LPL activity.”
From Differential effects of angiopoietin-like 4 in brain and muscle on regulation of lipoprotein lipase activity (2015) · cites this paper as [6]
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Chen, B., Lam, K. S. L., Wang, Y., Wu, D., Lam, M. C., Shen, J., Wong, L., Hoo, R. L. C., Zhang, J., & Xu, A. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.01.004 · Cited by 238
Self-citationAngptl3-null Mice Show Low Plasma Lipid Concentrations by Enhanced Lipoprotein Lipase Activity
FUJIMOTO, K., KOISHI, R., SHIMIZUGAWA, T., & ANDO, Y. (2006) · Experimental Animals · doi:10.1538/expanim.55.27 · Cited by 104
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Hepatokines: Linking nonalcoholic fatty liver disease and insulin resistance
Meex, R. C. R., & Watt, M. J. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2017.56 · Cited by 631
Inactivating Variants in ANGPTL4 and Risk of Coronary Artery Disease
Dewey, F. E., Gusarova, V., O’Dushlaine, C., Gottesman, O., Trejos, J., Hunt, C., Van Hout, C. V., Habegger, L., Buckler, D., Lai, K.-M. V., et al. (2016) · New England Journal of Medicine · doi:10.1056/nejmoa1510926 · Cited by 497
Lipoprotein lipase and its regulators: an unfolding story
Wu, S. A., Kersten, S., & Qi, L. (2021) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2020.11.005 · Cited by 225
Angiopoietin-like 3 in lipoprotein metabolism
Kersten, S. (2017) · Nature Reviews Endocrinology · doi:10.1038/nrendo.2017.119 · Cited by 220
Regulation of lipoprotein metabolism by ANGPTL3, ANGPTL4, and ANGPTL8
Sylvers-Davie, K. L., & Davies, B. S. J. (2021) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00195.2021 · Cited by 154
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Metadata
- Authors
- Yau, M.-H., Wang, Y., Lam, K. S. L., Zhang, J., Wu, D., & Xu, A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-05
- Volume
- 284
- Issue
- 18
- Pages
- 11942-11952
- ISSN
- 0021-9258
- Cited by
- 109
- References
- 3
- Language
- en
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