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April 23, 2020Journal of Lipid ResearchOpen Access

ANGPTL4 inactivates lipoprotein lipase by catalyzing the irreversible unfolding of LPL's hydrolase domain

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Authors

KKKristian Kølby KristensenKLKatrine Zinck Leth-EspensenSYStephen G. Young

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Overview

Advances molecular understanding of LPL regulation; leaves open clinical translation for hypertriglyceridemia.

Key Points

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Cite This Study

Kristensen et al. (2020) studied this question.

synapsesocial.com/papers/6a82c2987a209f4aae23bb3ehttps://doi.org/10.1194/jlr.ilr120000780
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Also Consider

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  1. 1ANGPTL4 sensitizes lipoprotein lipase to PCSK3 cleavage by catalyzing its unfolding2021 · 14 citations
  2. 2ANGPTL4: a new mode in the regulation of intravascular lipolysis2021 · 16 citations
  3. 3The angiopoietin-like protein ANGPTL4 catalyzes unfolding of the hydrolase domain in lipoprotein lipase and the endothelial membrane protein GPIHBP1 counteracts this unfolding2016 · 121 citations
  4. 4On the mechanism of angiopoietin-like protein 8 for control of lipoprotein lipase activity2019 · 123 citations
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